Author: "Patrick Gilon" / Language: english - Searchworks@Jio Institute Digital Library Search Results

40 results on '"Patrick Gilon"'

1. Corrigendum to 'Inter-domain tagging implicates caveolin-1 in insulin receptor trafficking and Erk signaling bias in pancreatic beta-cells' [Mol Metab 2016 May; 5 (5): 366–378]

Author: Tobias Boothe, Gareth E. Lim, Haoning Cen, Søs Skovsø, Micah Piske, Shu Nan Li, Ivan R. Nabi, Patrick Gilon, and James D. Johnson
Subjects: Internal medicine, RC31-1245
Published: 2024
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2. GLP-1 and GIP receptors signal through distinct β-arrestin 2-dependent pathways to regulate pancreatic β cell function

Author: Nour Zaïmia, Joelle Obeid, Annie Varrault, Julia Sabatier, Christophe Broca, Patrick Gilon, Safia Costes, Gyslaine Bertrand, and Magalie A. Ravier
Subjects: CP: Metabolism, CP: Molecular biology, Biology (General), QH301-705.5
Abstract: Summary: Glucagon-like peptide 1 (GLP-1R) and glucose-dependent insulinotropic polypeptide (GIPR) receptors are G-protein-coupled receptors involved in glucose homeostasis. Diabetogenic conditions decrease β-arrestin 2 (ARRB2) levels in human islets. In mouse β cells, ARRB2 dampens insulin secretion by partially uncoupling cyclic AMP (cAMP)/protein kinase A (PKA) signaling at physiological doses of GLP-1, whereas at pharmacological doses, the activation of extracellular signal-related kinase (ERK)/cAMP-responsive element-binding protein (CREB) requires ARRB2. In contrast, GIP-potentiated insulin secretion needs ARRB2 in mouse and human islets. The GIPR-ARRB2 axis is not involved in cAMP/PKA or ERK signaling but does mediate GIP-induced F-actin depolymerization. Finally, the dual GLP-1/GIP agonist tirzepatide does not require ARRB2 for the potentiation of insulin secretion. Thus, ARRB2 plays distinct roles in regulating GLP-1R and GIPR signaling, and we highlight (1) its role in the physiological context and the possible functional consequences of its decreased expression in pathological situations such as diabetes and (2) the importance of assessing the signaling pathways engaged by the agonists (biased/dual) for therapeutic purposes.
Published: 2023
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3. In depth functional characterization of human induced pluripotent stem cell-derived beta cells in vitro and in vivo

Author: Federica Fantuzzi, Sanna Toivonen, Andrea Alex Schiavo, Heeyoung Chae, Mohammad Tariq, Toshiaki Sawatani, Nathalie Pachera, Ying Cai, Chiara Vinci, Enrico Virgilio, Laurence Ladriere, Mara Suleiman, Piero Marchetti, Jean-Christophe Jonas, Patrick Gilon, Décio L. Eizirik, Mariana Igoillo-Esteve, and Miriam Cnop
Subjects: aggregate, beta cell, human induced pluripotent stem cell, insulin secretion, islet, microwell, Biology (General), QH301-705.5
Abstract: In vitro differentiation of human induced pluripotent stem cells (iPSCs) into beta cells represents an important cell source for diabetes research. Here, we fully characterized iPSC-derived beta cell function in vitro and in vivo in humanized mice. Using a 7-stage protocol, human iPSCs were differentiated into islet-like aggregates with a yield of insulin-positive beta cells comparable to that of human islets. The last three stages of differentiation were conducted with two different 3D culture systems, rotating suspension or static microwells. In the latter, homogeneously small-sized islet-like aggregates were obtained, while in rotating suspension size was heterogeneous and aggregates often clumped. In vitro function was assessed by glucose-stimulated insulin secretion, NAD(P)H and calcium fluctuations. Stage 7 aggregates slightly increased insulin release in response to glucose in vitro. Aggregates were transplanted under the kidney capsule of NOD-SCID mice to allow for further in vivo beta cell maturation. In transplanted mice, grafts showed glucose-responsiveness and maintained normoglycemia after streptozotocin injection. In situ kidney perfusion assays showed modulation of human insulin secretion in response to different secretagogues. In conclusion, iPSCs differentiated with equal efficiency into beta cells in microwells compared to rotating suspension, but the former had a higher experimental success rate. In vitro differentiation generated aggregates lacking fully mature beta cell function. In vivo, beta cells acquired the functional characteristics typical of human islets. With this technology an unlimited supply of islet-like organoids can be generated from human iPSCs that will be instrumental to study beta cell biology and dysfunction in diabetes.
Published: 2022
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4. Glucose inhibits glucagon secretion by decreasing [Ca2+]c and by reducing the efficacy of Ca2+ on exocytosis via somatostatin-dependent and independent mechanisms

Author: Bilal Singh, Firas Khattab, and Patrick Gilon
Subjects: Pancreatic islets, KATP channels, Ca2+, Glucagon, Somatostatin, Internal medicine, RC31-1245
Abstract: Objective: The mechanisms by which glucose stimulates insulin secretion from β-cells are well established and involve inhibition of ATP-sensitive K+ (KATP) channels, followed by a rise in [Ca2+]c that triggers exocytosis. However, the mechanisms by which glucose controls glucagon release from α-cells are much less known. In particular, it is debated whether the sugar controls glucagon secretion by changing α-cell [Ca2+]c, and whether KATP channels or paracrine factors are involved. The present study addresses these issues. Methods: We tested the effect of a decrease or an increase of glucose concentration (Gx, with x = concentration in mM) on α-cell [Ca2+]c and glucagon secretion. α-cell [Ca2+]c was monitored using GluCreGCaMP6f mice expressing the Ca2+-sensitive fluorescent protein, GCaMP6f, specifically in α-cells. [Ca2+]c was compared between dispersed α-cells and α-cells within islets to evaluate the potential contribution of an indirect effect of glucose. The same protocols were used for experiments of glucagon secretion from whole islets and [Ca2+]c measurements to test if changes in glucagon release mirror those in α-cell [Ca2+]c. Results: Blockade of KATP channels by sulfonylureas (tolbutamide 100 μM or gliclazide 25 μM) strongly increased [Ca2+]c in both dispersed α-cells and α-cells within islets. By contrast, glucose had no effect on [Ca2+]c in dispersed α-cells, whereas it affected it in α-cells within islets. The effect of glucose was however different in islets expressing (Sst+/+) or not somatostatin (SST) (Sst−/−). Decreasing glucose concentration from G7 to G1 modestly increased α-cell [Ca2+]c, but to a slightly larger extent in Sst+/+ islets than in Sst−/− islets. This G1-induced [Ca2+]c rise was also observed in the continuous presence of sulfonylureas in both Sst+/+ and Sst−/− islets. Increasing glucose concentration from G7 to G20 did not affect α-cell [Ca2+]c in Sst+/+ islets which remained low, whereas it strongly increased it in Sst−/− islets. The observations that this increase was seen only in α-cells within islets but never in dispersed α-cells and that it was abrogated by the gap junction inhibitor, carbenoxolone, point to an indirect effect of G20 and suggest that, in Sst−/− islets, G20-stimulated β-cells entrain α-cells whereas, in Sst+/+ islets, the concomitant release of SST keeps α-cell [Ca2+]c at low levels. The [Ca2+]c lowering effect of endogenous SST is also supported by the observation that SST receptor antagonists (SSTR2/3) increased [Ca2+]c in α-cells from Sst+/+ islets. All these [Ca2+]c changes induced parallel changes in glucagon release. To test if glucose also controls glucagon release independently of [Ca2+]c changes, additional experiments were performed in the continuous presence of 30 mM K+ and the KATP channel opener diazoxide (250 μM). In these conditions, α-cell [Ca2+]c within islets was elevated and its steady-state level was unaffected by glucose. However, decreasing the glucose concentration from G7 to G1 stimulated glucagon release whereas increasing it from G1 to G15 inhibited it. These effects were also evident in Sst−/− islets, and opposite to those on insulin secretion. Conclusions: We propose a model according to which glucose controls α-cell [Ca2+]c and glucagon secretion through multiple mechanisms. Increasing the glucose concentration modestly decreases [Ca2+]c in α-cells independently of their KATP channels and partly via SST. The involvement of SST increases with the glucose concentration, and one major effect of SST is to keep α-cell [Ca2+]c at low levels by counteracting the effect of an entrainment of α-cells by β-cells when β-cells become stimulated by glucose. All these [Ca2+]c changes induce parallel changes in glucagon release. Glucose also decreases the efficacy of Ca2+ on exocytosis by an attenuating pathway that is opposite to the well-established amplifying pathway controlling insulin release in β-cells.
Published: 2022
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5. Chemerin as an Inducer of β Cell Proliferation Mediates Mitochondrial Homeostasis and Promotes β Cell Mass Expansion

Author: Min Li, Ruifan Zhang, Qian Ge, Lingzhi Yue, Dan Ma, Firas Khattab, Wenhua Xie, Yewei Cui, Patrick Gilon, Xueya Zhao, Xi Li, and Rui Cheng
Subjects: chemerin, β cell, adipokine, insulin secretion, mitochondrial homeostasis, type 2 diabetes, Biology (General), QH301-705.5, Chemistry, QD1-999
Abstract: Loss of the β cell population is a crucial feature of type 2 diabetes. Restoring the β cell mass by stimulating β cell proliferation and preventing its apoptosis was proposed as a therapeutic approach to treating diabetes. Therefore, researchers have been increasingly interested in identifying exogenous factors that can stimulate β cell proliferation in situ and in vitro. Adipokine chemerin, which is secreted from adipose tissue and the liver, has been identified as a chemokine that plays a critical role in the regulation of metabolism. In this study, we demonstrate that chemerin as a circulating adipokine promotes β cell proliferation in vivo and in vitro. Chemerin serum levels and the expression of the main receptors within islets are highly regulated under a variety of challenging conditions, including obesity and type 2 diabetes. As compared to their littermates, mice overexpressing chemerin had a larger islet area and increased β cell mass with both a normal and high-fat diet. Moreover, in chemerin-overexpressed mice, we observed improved mitochondrial homeostasis and increased insulin synthesis. In summary, our findings confirm the potential role of chemerin as an inducer of β cell proliferation, and they provide novel insights into the helpful strategy to expand β cell population.
Published: 2023
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6. KATP channel blockers control glucagon secretion by distinct mechanisms: A direct stimulation of α-cells involving a [Ca2+]c rise and an indirect inhibition mediated by somatostatin

Author: Bilal Singh, Firas Khattab, Heeyoung Chae, Lieven Desmet, Pedro L. Herrera, and Patrick Gilon
Subjects: Pancreatic islets, Sulfonylureas, Ca2+, Glucagon, Somatostatin, Internal medicine, RC31-1245
Abstract: Objective: Glucagon is secreted by pancreatic α-cells in response to hypoglycemia and its hyperglycemic effect helps to restore normal blood glucose. Insulin and somatostatin (SST) secretions from β- and δ-cells, respectively, are stimulated by glucose by mechanisms involving an inhibition of their ATP-sensitive K+ (KATP) channels, leading to an increase in [Ca2+]c that triggers exocytosis. Drugs that close KATP channels, such as sulfonylureas, are used to stimulate insulin release in type 2 diabetic patients. α-cells also express KATP channels. However, the mechanisms by which sulfonylureas control glucagon secretion are still largely debated and were addressed in the present study. In particular, we studied the effects of KATP channel blockers on α-cell [Ca2+]c and glucagon secretion in the presence of a low (1 mM) or a high (15 mM) glucose concentration and evaluated the role of SST in these effects. Methods: Using a transgenic mouse model expressing the Ca2+-sensitive fluorescent protein, GCaMP6f, specifically in α-cells, we measured [Ca2+]c in α-cells either dispersed or within whole islets (by confocal microscopy). By measuring [Ca2+]c in α-cells within islets and glucagon secretion using the same perifusion protocols, we tested whether glucagon secretion correlated with changes in [Ca2+]c in response to sulfonylureas. We studied the role of SST in the effects of sulfonylureas using multiple approaches including genetic ablation of SST, or application of SST-14 and SST receptor antagonists. Results: Application of the sulfonylureas, tolbutamide, or gliclazide, to a medium containing 1 mM or 15 mM glucose increased [Ca2+]c in α-cells by a direct effect as in β-cells. At low glucose, sulfonylureas inhibited glucagon secretion of islets despite the rise in α-cell [Ca2+]c that they triggered. This glucagonostatic effect was indirect and attributed to SST because, in the islets of SST-knockout mice, sulfonylureas induced a stimulation of glucagon secretion which correlated with an increase in α-cell [Ca2+]c. Experiments with exogenous SST-14 and SST receptor antagonists indicated that the glucagonostatic effect of sulfonylureas mainly resulted from an inhibition of the efficacy of cytosolic Ca2+ on exocytosis. Although SST-14 was also able to inhibit glucagon secretion by decreasing α-cell [Ca2+]c, no decrease in [Ca2+]c occurred during sulfonylurea application because it was largely counterbalanced by the direct stimulatory effect of these drugs on α-cell [Ca2+]c. At high glucose, i.e., in conditions where glucagon release was already low, sulfonylureas stimulated glucagon secretion because their direct stimulatory effect on α-cells exceeded the indirect effect by SST. Our results also indicated that, unexpectedly, SST-14 poorly decreased the efficacy of Ca2+ on exocytosis in β-cells. Conclusions: Sulfonylureas exert two opposite actions on α-cells: a direct stimulation as in β-cells and an indirect inhibition by SST. This suggests that any alteration of SST paracrine influence, as described in diabetes, will modify the effect of sulfonylureas on glucagon release. In addition, we suggest that δ-cells inhibit α-cells more efficiently than β-cells.
Published: 2021
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7. SGLT2 is not expressed in pancreatic α- and β-cells, and its inhibition does not directly affect glucagon and insulin secretion in rodents and humans

Author: Heeyoung Chae, Robert Augustin, Eva Gatineau, Eric Mayoux, Mohammed Bensellam, Nancy Antoine, Firas Khattab, Bao-Khanh Lai, Davide Brusa, Birgit Stierstorfer, Holger Klein, Bilal Singh, Lucie Ruiz, Michael Pieper, Michael Mark, Pedro L. Herrera, Fiona M. Gribble, Frank Reimann, Anne Wojtusciszyn, Christophe Broca, Nano Rita, Lorenzo Piemonti, and Patrick Gilon
Subjects: Gliflozins, SGLT2 inhibitor, Glucagon, Insulin, Diabetes, Internal medicine, RC31-1245
Abstract: Objective: Sodium-glucose cotransporter 2 (SGLT2) inhibitors (SGLT2i), or gliflozins, are anti-diabetic drugs that lower glycemia by promoting glucosuria, but they also stimulate endogenous glucose and ketone body production. The likely causes of these metabolic responses are increased blood glucagon levels, and decreased blood insulin levels, but the mechanisms involved are hotly debated. This study verified whether or not SGLT2i affect glucagon and insulin secretion by a direct action on islet cells in three species, using multiple approaches. Methods: We tested the in vivo effects of two selective SGLT2i (dapagliflozin, empagliflozin) and a SGLT1/2i (sotagliflozin) on various biological parameters (glucosuria, glycemia, glucagonemia, insulinemia) in mice. mRNA expression of SGLT2 and other glucose transporters was assessed in rat, mouse, and human FACS-purified α- and β-cells, and by analysis of two human islet cell transcriptomic datasets. Immunodetection of SGLT2 in pancreatic tissues was performed with a validated antibody. The effects of dapagliflozin, empagliflozin, and sotagliflozin on glucagon and insulin secretion were assessed using isolated rat, mouse and human islets and the in situ perfused mouse pancreas. Finally, we tested the long-term effect of SGLT2i on glucagon gene expression. Results: SGLT2 inhibition in mice increased the plasma glucagon/insulin ratio in the fasted state, an effect correlated with a decline in glycemia. Gene expression analyses and immunodetections showed no SGLT2 mRNA or protein expression in rodent and human islet cells, but moderate SGLT1 mRNA expression in human α-cells. However, functional experiments on rat, mouse, and human (29 donors) islets and the in situ perfused mouse pancreas did not identify any direct effect of dapagliflozin, empagliflozin or sotagliflozin on glucagon and insulin secretion. SGLT2i did not affect glucagon gene expression in rat and human islets. Conclusions: The data indicate that the SGLT2i-induced increase of the plasma glucagon/insulin ratio in vivo does not result from a direct action of the gliflozins on islet cells.
Published: 2020
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8. Identification of islet-enriched long non-coding RNAs contributing to β-cell failure in type 2 diabetes

Author: Anna Motterle, Sonia Gattesco, Marie-Line Peyot, Jonathan Lou S. Esguerra, Ana Gomez-Ruiz, D. Ross Laybutt, Patrick Gilon, Frédéric Burdet, Mark Ibberson, Lena Eliasson, Marc Prentki, and Romano Regazzi
Subjects: Diabetes, Insulin, Pancreatic islet, Obesity, Gene expression, Internal medicine, RC31-1245
Abstract: Objective: Non-coding RNAs constitute a major fraction of the β-cell transcriptome. While the involvement of microRNAs is well established, the contribution of long non-coding RNAs (lncRNAs) in the regulation of β-cell functions and in diabetes development remains poorly understood. The aim of this study was to identify novel islet lncRNAs differently expressed in type 2 diabetes models and to investigate their role in β-cell failure and in the development of the disease. Methods: Novel transcripts dysregulated in the islets of diet-induced obese mice were identified by high throughput RNA-sequencing coupled with de novo annotation. Changes in the level of the lncRNAs were assessed by real-time PCR. The functional role of the selected lncRNAs was determined by modifying their expression in MIN6 cells and primary islet cells. Results: We identified about 1500 novel lncRNAs, a number of which were differentially expressed in obese mice. The expression of two lncRNAs highly enriched in β-cells, βlinc2, and βlinc3, correlated to body weight gain and glycemia levels in obese mice and was also modified in diabetic db/db mice. The expression of both lncRNAs was also modulated in vitro in isolated islet cells by glucolipotoxic conditions. Moreover, the expression of the human orthologue of βlinc3 was altered in the islets of type 2 diabetic patients and was associated to the BMI of the donors. Modulation of the level of βlinc2 and βlinc3 by overexpression or downregulation in MIN6 and mouse islet cells did not affect insulin secretion but increased β-cell apoptosis. Conclusions: Taken together, the data show that lncRNAs are modulated in a model of obesity-associated type 2 diabetes and that variations in the expression of some of them may contribute to β-cell failure during the development of the disease.
Published: 2017
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9. Steviol glycosides enhance pancreatic beta-cell function and taste sensation by potentiation of TRPM5 channel activity

Author: Koenraad Philippaert, Andy Pironet, Margot Mesuere, William Sones, Laura Vermeiren, Sara Kerselaers, Sílvia Pinto, Andrei Segal, Nancy Antoine, Conny Gysemans, Jos Laureys, Katleen Lemaire, Patrick Gilon, Eva Cuypers, Jan Tytgat, Chantal Mathieu, Frans Schuit, Patrik Rorsman, Karel Talavera, Thomas Voets, and Rudi Vennekens
Subjects: Science
Abstract: Steviol glycosides are sweet-tasting compounds isolated from a South American shrub and are increasingly used as sweeteners in foods and beverages. Philippaertet al. demonstrate that steviol glycosides potentiate Ca2+-dependent TRPM5 activity and promote glucose-induced insulin secretion and glucose tolerance.
Published: 2017
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10. Inter-domain tagging implicates caveolin-1 in insulin receptor trafficking and Erk signaling bias in pancreatic beta-cells

Author: Tobias Boothe, Gareth E. Lim, Haoning Cen, Søs Skovsø, Micah Piske, Shu Nan Li, Ivan R. Nabi, Patrick Gilon, and James D. Johnson
Subjects: Internal medicine, RC31-1245
Abstract: Objective: The role and mechanisms of insulin receptor internalization remain incompletely understood. Previous trafficking studies of insulin receptors involved fluorescent protein tagging at their termini, manipulations that may be expected to result in dysfunctional receptors. Our objective was to determine the trafficking route and molecular mechanisms of functional tagged insulin receptors and endogenous insulin receptors in pancreatic beta-cells. Methods: We generated functional insulin receptors tagged with pH-resistant fluorescent proteins between domains. Confocal, TIRF and STED imaging revealed a trafficking pattern of inter-domain tagged insulin receptors and endogenous insulin receptors detected with antibodies. Results: Surprisingly, interdomain-tagged and endogenous insulin receptors in beta-cells bypassed classical Rab5a- or Rab7-mediated endocytic routes. Instead, we found that removal of insulin receptors from the plasma membrane involved tyrosine-phosphorylated caveolin-1, prior to trafficking within flotillin-1-positive structures to lysosomes. Multiple methods of inhibiting caveolin-1 significantly reduced Erk activation in vitro or in vivo, while leaving Akt signaling mostly intact. Conclusions: We conclude that phosphorylated caveolin-1 plays a role in insulin receptor internalization towards lysosomes through flotillin-1-positive structures and that caveolin-1 helps bias physiological beta-cell insulin signaling towards Erk activation. Author Video: Author Video Watch what authors say about their articles Keywords: Insulin receptor internalization, Insulin resistance, Pancreatic islet beta-cells, Autocrine insulin signaling
Published: 2016
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11. Can Tea Extracts Exert a Protective Effect Against Diabetes by Reducing Oxidative Stress and Decreasing Glucotoxicity in Pancreatic β-Cells?

Author: Heeyoung Chae and Patrick Gilon
Subjects: Diseases of the endocrine glands. Clinical endocrinology, RC648-665
Published: 2015
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12. How stable is repression of disallowed genes in pancreatic islets in response to metabolic stress?

Author: Katleen Lemaire, Mikaela Granvik, Anica Schraenen, Lotte Goyvaerts, Leentje Van Lommel, Ana Gómez-Ruiz, Peter In 't Veld, Patrick Gilon, and Frans Schuit
Subjects: Medicine, Science
Abstract: The specific phenotype of mature differentiated beta cells not only depends on the specific presence of genes that allow beta cell function but also on the selective absence of housekeeping genes ("disallowed genes") that would interfere with this function. Recent studies have shown that both histone modifications and DNA methylation via the de novo methyltransferase DNMT3A are involved in repression of disallowed genes in neonatal beta cells when these cells acquire their mature phenotype. It is unknown, however, if the environmental influence of advanced age, pregnancy and the metabolic stress of high fat diet or diabetes could alter the repression of disallowed genes in beta cells. In the present study, we show that islet disallowed genes-which are also deeply repressed in FACS-purified beta cells-remain deeply repressed in animals of advanced age and in pregnant females. Moreover, the stability of this repression was correlated with strong and stable histone repression marks that persisted in islets isolated from 2 year old mice and with overall high expression of Dnmt3a in islets. Furthermore, repression of disallowed genes was unaffected by the metabolic stress of high fat diet. However, repression of about half of the disallowed genes was weakened in 16 week-old diabetic db/db mice. In conclusion, we show that the disallowed status of islet genes is stable under physiological challenging conditions (advanced age, pregnancy, high fat diet) but partially lost in islets from diabetic animals.
Published: 2017
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13. The mitochondrial Ca2+ uniporter MCU is essential for glucose-induced ATP increases in pancreatic β-cells.

Author: Andrei I Tarasov, Francesca Semplici, Magalie A Ravier, Elisa A Bellomo, Timothy J Pullen, Patrick Gilon, Israel Sekler, Rosario Rizzuto, and Guy A Rutter
Subjects: Medicine, Science
Abstract: Glucose induces insulin release from pancreatic β-cells by stimulating ATP synthesis, membrane depolarisation and Ca(2+) influx. As well as activating ATP-consuming processes, cytosolic Ca(2+) increases may also potentiate mitochondrial ATP synthesis. Until recently, the ability to study the role of mitochondrial Ca(2+) transport in glucose-stimulated insulin secretion has been hindered by the absence of suitable approaches either to suppress Ca(2+) uptake into these organelles, or to examine the impact on β-cell excitability. Here, we have combined patch-clamp electrophysiology with simultaneous real-time imaging of compartmentalised changes in Ca(2+) and ATP/ADP ratio in single primary mouse β-cells, using recombinant targeted (Pericam or Perceval, respectively) as well as entrapped intracellular (Fura-Red), probes. Through shRNA-mediated silencing we show that the recently-identified mitochondrial Ca(2+) uniporter, MCU, is required for depolarisation-induced mitochondrial Ca(2+) increases, and for a sustained increase in cytosolic ATP/ADP ratio. By contrast, silencing of the mitochondrial Na(+)-Ca(2+) exchanger NCLX affected the kinetics of glucose-induced changes in, but not steady state values of, cytosolic ATP/ADP. Exposure to gluco-lipotoxic conditions delayed both mitochondrial Ca(2+) uptake and cytosolic ATP/ADP ratio increases without affecting the expression of either gene. Mitochondrial Ca(2+) accumulation, mediated by MCU and modulated by NCLX, is thus required for normal glucose sensing by pancreatic β-cells, and becomes defective in conditions mimicking the diabetic milieu.
Published: 2012
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14. GLP-1R agonists demonstrate potential to treat Wolfram syndrome in human preclinical models

Author: Vyron Gorgogietas, Bahareh Rajaei, Chae Heeyoung, Bruno J. Santacreu, Sandra Marín-Cañas, Paraskevi Salpea, Toshiaki Sawatani, Anyishai Musuaya, María N. Arroyo, Cristina Moreno-Castro, Khadija Benabdallah, Celine Demarez, Sanna Toivonen, Cristina Cosentino, Nathalie Pachera, Maria Lytrivi, Ying Cai, Lode Carnel, Cris Brown, Fumihiko Urano, Piero Marchetti, Patrick Gilon, Decio L. Eizirik, Miriam Cnop, Mariana Igoillo-Esteve, and UCL - SSS/IREC/EDIN - Pôle d'endocrinologie, diabète et nutrition
Subjects: Mice, Knockout, Wolfram syndrome, GLP-1R agonists, Endocrinology, Diabetes and Metabolism, Induced Pluripotent Stem Cells, iPSC-derived neurons, Mice, Optic Atrophy, Insulin-Secreting Cells, Internal Medicine, Humans, Animals, Exenatide, Human pancreatic beta cells, iPSC-derived beta cells
Abstract: Aims/hypothesis Wolfram syndrome is a rare autosomal recessive disorder caused by pathogenic variants in the WFS1 gene. It is characterised by insulin-dependent diabetes mellitus, optic nerve atrophy, diabetes insipidus, hearing loss and neurodegeneration. Considering the unmet treatment need for this orphan disease, this study aimed to evaluate the therapeutic potential of glucagon-like peptide 1 receptor (GLP-1R) agonists under wolframin (WFS1) deficiency with a particular focus on human beta cells and neurons. Methods The effect of the GLP-1R agonists dulaglutide and exenatide was examined in Wfs1 knockout mice and in an array of human preclinical models of Wolfram syndrome, including WFS1-deficient human beta cells, human induced pluripotent stem cell (iPSC)-derived beta-like cells and neurons from control individuals and individuals affected by Wolfram syndrome, and humanised mice. Results Our study shows that the long-lasting GLP-1R agonist dulaglutide reverses impaired glucose tolerance in WFS1-deficient mice, and that exenatide and dulaglutide improve beta cell function and prevent apoptosis in different human WFS1-deficient models including iPSC-derived beta cells from people with Wolfram syndrome. Exenatide improved mitochondrial function, reduced oxidative stress and prevented apoptosis in Wolfram syndrome iPSC-derived neural precursors and cerebellar neurons. Conclusions/interpretation Our study provides novel evidence for the beneficial effect of GLP-1R agonists on WFS1-deficient human pancreatic beta cells and neurons, suggesting that these drugs may be considered as a treatment for individuals with Wolfram syndrome. Graphical abstract
Published: 2023

15. Massive lactic acidosis and ketoacidosis with glucagon deficiency in a chronic alcoholic patient

Author: Patrick Gilon, Philippe Boudou, Fabrizio Andreelli, Michel Djibré, Pascal Ferré, Soraya Fellahi, Fidaa Ibrahim, Mathieu Boissan, and UCL - SSS/IREC/EDIN - Pôle d'endocrinologie, diabète et nutrition
Subjects: 2. Zero hunger, 0303 health sciences, medicine.medical_specialty, business.industry, Endocrinology, Diabetes and Metabolism, Chronic alcoholic, 030209 endocrinology & metabolism, General Medicine, medicine.disease, Glucagon Deficiency, Gastroenterology, 3. Good health, Ketoacidosis, 03 medical and health sciences, 0302 clinical medicine, Endocrinology, Internal medicine, Lactic acidosis, Internal Medicine, medicine, business, 030304 developmental biology
Abstract: A non-diabetic chronic alcoholic and undernourished male patient [body mass index (BMI): 16.6 kg/m2] was admitted to our hospital emergency department. He had fasted for the previous 3 days. His blood lactate and ketone body concentrations were massively elevated (18 mmol/L and 14 mmol/L, respectively). Ethanolaemia was negative. Massive metabolic acidosis was noted with a pH of 7.04. Renal function remained normal, but there was mild hepatocellular deficiency and no acute pancreatitis. The patient was hypoglycaemic at admission with a blood glucose level of 3.0 mmol/L, and low concentrations of insulin, C-peptide and insulin-like growth factor (IGF)-1, as well as very low glucagon concentrations (5.2 ng/L; normal range: 8–74 ng/L) despite the prevailing glycaemia. In contrast, cortisol, sex hormone-binding globulin (SHBG) and growth hormone (GH) concentrations were elevated. [...]
Published: 2021

16. LDHA is enriched in human islet alpha cells and upregulated in type 2 diabetes

Author: Anne Wojtusciszyn, Eva Gatineau, Blaz Lupse, Amin Ardestani, Huan Liu, Paulina Karen Mendoza Sanchez, Patrick Gilon, Ralf Dringen, Mona Khazaei, Shirin Geravandi, Kathrin Maedler, and UCL - SSS/IREC/EDIN - Pôle d'endocrinologie, diabète et nutrition
Subjects: medicine.medical_specialty, endocrine system, LDH, medicine.medical_treatment, Biophysics, Biochemistry, Glucagon, Article, LDHA, chemistry.chemical_compound, Downregulation and upregulation, Lactate dehydrogenase, Internal medicine, Insulin Secretion, medicine, Humans, Secretion, RNA, Messenger, Molecular Biology, Cells, Cultured, geography, geography.geographical_feature_category, L-Lactate Dehydrogenase, Chemistry, Pancreatic islets, Insulin, Beta-cell, Diabetes, Cell Biology, Islet, Up-Regulation, Endocrinology, medicine.anatomical_structure, Glucose, Diabetes Mellitus, Type 2, Glucagon-Secreting Cells, Lactate, Beta cell, Islets
Abstract: The lactate dehydrogenase isoform A (LDHA) is a key metabolic enzyme that preferentially catalyzes the conversion of pyruvate to lactate. Whereas LDHA is highly expressed in many tissues, its expression is turned off in the differentiated adult β-cell within the pancreatic islets. The repression of LDHA under normal physiological condition and its inappropriate upregulation under a diabetogenic environment is well-documented in rodent islets/β-cells but little is known about LDHA expression in human islet cells and whether its abundance is altered under diabetic conditions. Analysis of public single-cell RNA-seq (sc-RNA seq) data as well as cell type-specific immunolabeling of human pancreatic islets showed that LDHA was mainly localized in human α-cells while it is expressed at a very low level in β-cells. Furthermore, LDHA, both at mRNA and protein, as well as lactate production is upregulated in human pancreatic islets exposed to chronic high glucose treatment. Microscopic analysis of stressed human islets and autopsy pancreases from individuals with type 2 diabetes (T2D) showed LDHA upregulation mainly in human α-cells. Pharmacological inhibition of LDHA in isolated human islets enhanced insulin secretion under physiological conditions but did not significantly correct the deregulated secretion of insulin or glucagon under diabetic conditions.
Published: 2021

17. Inhibition of aquaporin-1 prevents myocardial remodeling by blocking the transmembrane transport of hydrogen peroxide

Author: Ramona Bella, Luc Bertrand, Andrea J. Yool, Alessandra Ghigo, Lauriane Y. M. Michel, Christophe Beauloye, Simonetta Geninatti-Crich, Virginie Montiel, Patrick Gilon, Dimitri Gilis, Pak Hin Chow, Malte Tiburcy, Charlotte Farah, Sandrine Horman, Olivier Devuyst, Hrag Esfahani, Huguette Debaix, Caroline Bouzin, Wolfram H. Zimmermann, Thomas Michel, Flavia Dei Zotti, Marianne Rooman, Jean-Louis Vanoverschelde, H. Llewelyn Roderick, Davide Brusa, Olaf Bergmann, Jean-Philippe Deglasse, Emma L. Robinson, Jean-Luc Balligand, Delphine De Mulder, Benjamin Steinhorn, Jean-Christophe Jonas, UCL - SSS/IREC/FATH - Pôle de Pharmacologie et thérapeutique, UCL - SSS/IREC/CARD - Pôle de recherche cardiovasculaire, UCL - SSS/IREC/NEFR - Pôle de Néphrologie, UCL - SSS/IREC/EDIN - Pôle d'endocrinologie, diabète et nutrition, UCL - (SLuc) Service de médecine interne générale, UCL - (SLuc) Service de néphrologie, UCL - (SLuc) Service de pathologie cardiovasculaire, and UCL - (SLuc) Service de soins intensifs
Subjects: 0301 basic medicine, Gene isoform, Induced Pluripotent Stem Cells, Aquaporin, 030204 cardiovascular system & hematology, 03 medical and health sciences, Mice, 0302 clinical medicine, Myocyte, Animals, Humans, Myocytes, Cardiac, Induced pluripotent stem cell, Aquaporin 1, Kinase, Chemistry, Myocardium, RNA, General Medicine, Hydrogen Peroxide, Membrane transport, Sciences biomédicales, 3. Good health, Cell biology, IREC/2IP, 030104 developmental biology
Abstract: Pathological remodeling of the myocardium has long been known to involve oxidant signaling, but strategies using systemic antioxidants have generally failed to prevent it. We sought to identify key regulators of oxidant-mediated cardiac hypertrophy amenable to targeted pharmacological therapy. Specific isoforms of the aquaporin water channels have been implicated in oxidant sensing, but their role in heart muscle is unknown. RNA sequencing from human cardiac myocytes revealed that the archetypal AQP1 is a major isoform. AQP1 expression correlates with the severity of hypertrophic remodeling in patients with aortic stenosis. The AQP1 channel was detected at the plasma membrane of human and mouse cardiac myocytes from hypertrophic hearts, where it colocalized with NADPH oxidase-2 and caveolin-3. We show that hydrogen peroxide (H 2 O 2 ), produced extracellularly, is necessary for the hypertrophic response of isolated cardiac myocytes and that AQP1 facilitates the transmembrane transport of H 2 O 2 through its water pore, resulting in activation of oxidant-sensitive kinases in cardiac myocytes. Structural analysis of the amino acid residues lining the water pore of AQP1 supports its permeation by H 2 O 2 .Deletion of Aqp1 or selective blockade of the AQP1 intrasubunit pore inhibited H 2 O 2 transport in mouse and human cells and rescued the myocyte hypertrophy in human induced pluripotent stem cell–derived engineered heart muscle. Treatment of mice with a clinically approved AQP1 inhibitor, Bacopaside, attenuated cardiac hypertrophy. We conclude that cardiac hypertrophy is mediated by the transmembrane transport of H 2 O 2 by the water channel AQP1 and that inhibitors of AQP1 represent new possibilities for treating hypertrophic cardiomyopathies., info:eu-repo/semantics/published
Published: 2020

18. Somatostatin is Only Partly Required for the Glucagonostatic Effect of Glucose but is Necessary for the Glucagonostatic Effect of KATP Channel Blockers

Author: Bao-Khanh Lai, Jean-Christophe Jonas, Christophe Beauloye, Nancy Antoine, Patrick Gilon, Panpan Cheng, Paola Gallo, Susumu Seino, Ana Gómez-Ruiz, Victor J. Seghers, Heeyoung Chae, UCL - SSS/IREC/EDIN - Pôle d'endocrinologie, diabète et nutrition, UCL - SSS/IREC/CARD - Pôle de recherche cardiovasculaire, and UCL - SSS/IREC - Institut de recherche expérimentale et clinique
Subjects: 0301 basic medicine, medicine.medical_specialty, endocrine system, Endocrinology, Diabetes and Metabolism, 030209 endocrinology & metabolism, Glucagon, 03 medical and health sciences, Paracrine signalling, fluids and secretions, 0302 clinical medicine, Endocrinology, Internal medicine, parasitic diseases, medicine, Internal Medicine, Somatostatin receptor 2, Receptor, geography, geography.geographical_feature_category, Chemistry, fungi, Glucagon secretion, Islet, Diabetes and Metabolism, 030104 developmental biology, Somatostatin, medicine.anatomical_structure, Pancreas, hormones, hormone substitutes, and hormone antagonists
Abstract: The mechanisms of control of glucagon secretion are largely unknown. In particular, the paracrine role of somatostatin is unclear. We studied its role in the control of glucagon secretion by glucose and KATP channel blockers, using perifused islets and the in situ perfused pancreas. The involvement of somatostatin was evaluated by comparing glucagon release of control tissue or tissue without paracrine influence of somatostatin (pertussis toxin-treated islets, or islets or pancreas from Sst-/- mice). We show that removal of the paracrine influence of somatostatin suppresses the ability of KATP channel blockers or KATP channel ablation to inhibit glucagon release, suggesting that, in control islets, the glucagonostatic effect of KATP channel blockers/ablation is fully mediated by somatostatin. By contrast, the glucagonostatic effect of glucose in control islets is mainly independent of somatostatin for low glucose concentrations (0-7 mmol/l) but starts to involve somatostatin for high concentrations of the sugar (15-30 mmol/l). This demonstrates that the glucagonostatic effect of glucose only partially depends on somatostatin. RT-qPCR and pharmacological experiments indicate that the glucagonostatic effect of somatostatin is mediated by two types of somatostatin receptors, SSTR2 and SSTR3. These results suggest that alterations of the paracrine influence of somatostatin will affect glucagon release.
Published: 2018

19. Can Tea Extracts Exert a Protective Effect Against Diabetes by Reducing Oxidative Stress and Decreasing Glucotoxicity in Pancreatic β-Cells?

Author: Patrick Gilon, Heeyoung Chae, and UCL - SSS/IREC/EDIN - Pôle d'endocrinologie, diabète et nutrition
Subjects: medicine.medical_specialty, lcsh:RC648-665, business.industry, Endocrinology, Diabetes and Metabolism, Insulin, medicine.medical_treatment, Type 2 Diabetes Mellitus, Type 2 diabetes, medicine.disease, medicine.disease_cause, lcsh:Diseases of the endocrine glands. Clinical endocrinology, Proinflammatory cytokine, Endocrinology, Insulin resistance, Editorial, Internal medicine, Diabetes mellitus, Free radical oxygen, medicine, Islet Studies and Transplantation, business, Oxidative stress
Abstract: Glucose is the main physiological stimulus of pancreatic β-cells. However, chronic exposure of β-cells to elevated glucose concentrations induces glucotoxicity. In animal models of type 2 diabetes, it has been shown that several days of hyperglycemia impairs glucose-stimulated insulin secretion and increases β-cell apoptosis. In patients with type 2 diabetes, the multiple disorders caused by chronic hyperglycemia in β-cells include elevated basal insulin secretion, increased sensitivity to glucose, diminished response to insulinotropic stimuli and substantial depletion of insulin hoarding [1,2]. These defects associated with insulin resistance lead to a progressive loss of β-cell mass and function and to the onset of diabetes. It is crucial to study the mechanisms by which glucotoxicity induces β-cell failure to develop therapeutic strategies for protecting and recovering a functional β-cell mass. Several mechanisms might explain the glucotoxicity due to prolonged hyperglycemia, such as β-cell exhaustion, oxidative stress induced by free radical oxygen species, endoplasmic reticulum (ER) stress, inflammation caused by proinflammatory cytokines and chemokines, loss of neogenesis, proliferation of β-cells, and so on [3,4,5,6,7,8,9,10]. However, the precise mechanisms of glucotoxicity and its contribution to the pathology of type 2 diabetes mellitus (T2DM) are still not fully understood.
Published: 2015

20. TALK-1 channels control β cell endoplasmic reticulum Ca2+ homeostasis

Author: Matthew T. Dickerson, Sarah C. Milian, Prasanna K. Dadi, Patrick Gilon, David A. Jacobson, Kelli L. Jordan, and Nicholas C. Vierra
Subjects: 0301 basic medicine, medicine.medical_specialty, Biology, Endoplasmic Reticulum, Biochemistry, Article, 03 medical and health sciences, Diabetes mellitus genetics, Mice, 0302 clinical medicine, Potassium Channels, Tandem Pore Domain, Internal medicine, Insulin-Secreting Cells, medicine, Diabetes Mellitus, Animals, Homeostasis, Humans, Nuclear membrane, Molecular Biology, Mice, Knockout, Endoplasmic reticulum, HEK 293 cells, Cell Biology, Potassium channel, Cell biology, Cytosol, 030104 developmental biology, medicine.anatomical_structure, Endocrinology, HEK293 Cells, Unfolded protein response, Calcium, 030217 neurology & neurosurgery
Abstract: Ca2+ handling by the endoplasmic reticulum (ER) serves critical roles controlling pancreatic β-cell function and becomes perturbed during the pathogenesis of diabetes. ER Ca2+ homeostasis is determined by ion movements across the ER membrane, including K+ flux through K+ channels. Here, we demonstrated that K+ flux through ER-localized TALK-1 channels facilitated Ca2+ release from the ER in mouse and human β-cells. We found that β-cells from mice lacking TALK-1 exhibited reduced basal cytosolic Ca2+ and increased ER Ca2+ concentrations, suggesting reduced ER Ca2+ leak. These changes in Ca2+ homeostasis were presumably due to TALK-1-mediated ER K+ flux, because we recorded K+ currents mediated by functional TALK-1 channels on the nuclear membrane, which is continuous with the ER. Moreover, overexpression of K+-impermeable TALK-1 channels in HEK293 cells did not reduce ER Ca2+ stores. Reduced ER Ca2+ content in β-cells is associated with ER stress and islet dysfunction in diabetes, and islets from TALK-1-deficient mice fed a high-fat diet showed reduced signs of ER stress, suggesting that TALK-1 activity exacerbated ER stress. Our data establish TALK-1 channels as key regulators of β-cell ER Ca2+, and suggest that TALK-1 may be a therapeutic target to reduce ER Ca2+ handling defects in β-cells during the pathogenesis of diabetes.
Published: 2017

21. Sodium-myoinositol cotransporter-1, SMIT1, mediates the production of reactive oxygen species induced by hyperglycemia in the heart

Author: Hermann Koepsell, Evangelos-Panagiotis Daskalopoulos, Gerard T. Berry, Magali Balteau, Sylvain Battault, Christophe Beauloye, Louis Hue, Jean-Louis Vanoverschelde, Sanda Despa, Audrey Ginion, Florin Despa, Jean-Luc Balligand, Sandrine Horman, Laura Ferté, Luc Bertrand, Patrick Gilon, Anne Van Steenbergen, Christophe de Meester de Ravenstein, UCL - SSS/IREC - Institut de recherche expérimentale et clinique, UCL - SSS/IREC/CARD - Pôle de recherche cardiovasculaire, UCL - SSS/IREC/FATH - Pôle de Pharmacologie et thérapeutique, UCL - (SLuc) Service de pathologie cardiovasculaire, and UCL - (SLuc) Service de médecine interne générale
Subjects: Male, 0301 basic medicine, Gene isoform, medicine.medical_specialty, Sodium, chemistry.chemical_element, 030204 cardiovascular system & hematology, Carbohydrate metabolism, Article, Gene Knockout Techniques, Mice, 03 medical and health sciences, chemistry.chemical_compound, Sodium-Glucose Transporter 1, 0302 clinical medicine, Internal medicine, Diabetic cardiomyopathy, medicine, Animals, Humans, Heat-Shock Proteins, chemistry.chemical_classification, Reactive oxygen species, Multidisciplinary, NADPH oxidase, Symporters, biology, urogenital system, Myocardium, medicine.disease, Rats, Disease Models, Animal, ddc:580, 030104 developmental biology, Endocrinology, chemistry, Hyperglycemia, Galactose, NADPH Oxidase 2, biology.protein, Reactive Oxygen Species, Cotransporter, hormones, hormone substitutes, and hormone antagonists
Abstract: Hyperglycemia (HG) stimulates the production of reactive oxygen species in the heart through activation of NADPH oxidase 2 (NOX2). This production is independent of glucose metabolism but requires sodium/glucose cotransporters (SGLT). Seven SGLT isoforms (SGLT1 to 6 and sodium-myoinositol cotransporter-1, SMIT1) are known, although their expression and function in the heart remain elusive. We investigated these 7 isoforms and found that only SGLT1 and SMIT1 were expressed in mouse, rat and human hearts. In cardiomyocytes, galactose (transported through SGLT1) did not activate NOX2. Accordingly, SGLT1 deficiency did not prevent HG-induced NOX2 activation, ruling it out in the cellular response to HG. In contrast, myo-inositol (transported through SMIT1) reproduced the toxic effects of HG. SMIT1 overexpression exacerbated glucotoxicity and sensitized cardiomyocytes to HG, whereas its deletion prevented HG-induced NOX2 activation. In conclusion, our results show that heart SMIT1 senses HG and triggers NOX2 activation. This could participate in the redox signaling in hyperglycemic heart and contribute to the pathophysiology of diabetic cardiomyopathy.
Published: 2017
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22. Mechanisms of Control of the Free Ca2+ Concentration in the Endoplasmic Reticulum of Mouse Pancreatic β-Cells

Author: Magalie A. Ravier, Rui Cheng-Xue, Patrick Gilon, Jean-Christophe Jonas, Leticia Prates Roma, Frans Schuit, and Dorothée Daro
Subjects: medicine.medical_specialty, Endocrinology, Diabetes and Metabolism, medicine.medical_treatment, Vasodilator Agents, chemistry.chemical_element, Biology, Calcium, Endoplasmic Reticulum, Sarcoplasmic Reticulum Calcium-Transporting ATPases, Mice, Internal medicine, Ca2 concentration, Insulin-Secreting Cells, Internal Medicine, medicine, Diazoxide, Animals, Insulin, Promoter Regions, Genetic, Mice, Knockout, geography, geography.geographical_feature_category, Endoplasmic reticulum, Islet, Endocrinology, Glucose, chemistry, Mrna level, Islet Studies, Gene Expression Regulation, Unfolded protein response, Genetic Engineering, Gene Deletion, medicine.drug
Abstract: OBJECTIVE Sarco-endoplasmic reticulum Ca2+-ATPase 2b (SERCA2b) and SERCA3 pump Ca2+ in the endoplasmic reticulum (ER) of pancreatic β-cells. We studied their role in the control of the free ER Ca2+ concentration ([Ca2+]ER) and the role of SERCA3 in the control of insulin secretion and ER stress. RESEARCH DESIGN AND METHODS β-Cell [Ca2+]ER of SERCA3+/+ and SERCA3−/− mice was monitored with an adenovirus encoding the low Ca2+-affinity sensor D4 addressed to the ER (D4ER) under the control of the insulin promoter. Free cytosolic Ca2+ concentration ([Ca2+]c) and [Ca2+]ER were simultaneously recorded. Insulin secretion and mRNA levels of ER stress genes were studied. RESULTS Glucose elicited synchronized [Ca2+]ER and [Ca2+]c oscillations. [Ca2+]ER oscillations were smaller in SERCA3−/− than in SERCA3+/+ β-cells. Stimulating cell metabolism with various [glucose] in the presence of diazoxide induced a similar dose-dependent [Ca2+]ER rise in SERCA3+/+ and SERCA3−/− β-cells. In a Ca2+-free medium, glucose moderately raised [Ca2+]ER from a highly buffered cytosolic Ca2+ pool. Increasing [Ca2+]c with high [K] elicited a [Ca2+]ER rise that was larger but more transient in SERCA3+/+ than SERCA3−/− β-cells because of the activation of a Ca2+ release from the ER in SERCA3+/+ β-cells. Glucose-induced insulin release was larger in SERCA3−/− than SERCA3+/+ islets. SERCA3 ablation did not induce ER stress. CONCLUSIONS [Ca2+]c and [Ca2+]ER oscillate in phase in response to glucose. Upon [Ca2+]c increase, Ca2+ is taken up by SERCA2b and SERCA3. Strong Ca2+ influx triggers a Ca2+ release from the ER that depends on SERCA3. SERCA3 deficiency neither impairs Ca2+ uptake by the ER upon cell metabolism acceleration and insulin release nor induces ER stress.
Published: 2011

23. Calcium signaling in pancreatic beta-cells in health and in Type 2 diabetes

Author: Patrick Gilon, Heeyoung Chae, Guy A. Rutter, Magalie A. Ravier, Université Catholique de Louvain = Catholic University of Louvain (UCL), Institut de Génomique Fonctionnelle (IGF), and Université de Montpellier (UM)-Université Montpellier 1 (UM1)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Montpellier 2 - Sciences et Techniques (UM2)-Centre National de la Recherche Scientifique (CNRS)
Subjects: SERCA, Insulin/metabolism, Physiology, [SDV]Life Sciences [q-bio], Biology, Endoplasmic Reticulum, symbols.namesake, Islets of Langerhans, Insulin-Secreting Cells, Diabetes Mellitus, Insulin, Glucose/metabolism, Humans, Secretion, beta-Cells, Molecular Biology, ComputingMilieux_MISCELLANEOUS, Calcium signaling, Endoplasmic Reticulum/genetics/pathology, Ryanodine receptor, Endoplasmic reticulum, Diabetes, Cell Biology, Golgi apparatus, Calcium/*metabolism, Calcium Signaling/*genetics, Type 2/*genetics/metabolism/pathology, Cell biology, Insulin-Secreting Cells/metabolism/pathology, Cytosol, Glucose, Diabetes Mellitus, Type 2, Biochemistry, symbols, Calcium, Homeostasis
Abstract: Changes in cytosolic free Ca(2+) concentration ([Ca(2+)]c) play a crucial role in the control of insulin secretion from the electrically excitable pancreatic β-cell. Secretion is controlled by the finely tuned balance between Ca(2+) influx (mainly through voltage-dependent Ca(2+) channels, but also through voltage-independent Ca(2+) channels like store-operated channels) and efflux pathways. Changes in [Ca(2+)]c directly affect [Ca(2+)] in various organelles including the endoplasmic reticulum (ER), mitochondria, the Golgi apparatus, secretory granules and lysosomes, as imaged using recombinant targeted probes. Because most of these organelles have specific Ca(2+) influx and efflux pathways, they mutually influence free [Ca(2+)] in the others. In this article, we review the mechanisms of control of [Ca(2+)] in various compartments and particularly the cytosol, the endoplasmic reticulum ([Ca(2+)]ER), acidic stores and mitochondrial matrix ([Ca(2+)]mito), focusing chiefly on the most important physiological stimulus of β-cells, glucose. We also briefly review some alterations of β-cell Ca(2+) homeostasis in Type 2 diabetes.
Published: 2014

24. UCP2 regulates the glucagon response to fasting and starvation

Author: Alexandre B. Hardy, Michael B. Wheeler, Pedro Luis Herrera, Kacey J. Prentice, Bradford B. Lowell, Sobia Sultan, Patrick Gilon, Emma M. Allister, Dong Kong, Herbert Y. Gaisano, and Christine A. Robson-Doucette
Subjects: Male, Glucagon-Secreting Cells/drug effects/metabolism/secretion, Endocrinology, Diabetes and Metabolism, Adenosine Triphosphate/metabolism, RNA, Messenger/metabolism, Islets of Langerhans/drug effects/metabolism/physiopathology/secretion, medicine.disease_cause, Ion Channels, Hypoglycemia/blood/etiology, Tissue Culture Techniques, Mice, Adenosine Triphosphate, 0302 clinical medicine, Uncoupling Protein 2, ddc:576.5, Original Research, Membrane Potential, Mitochondrial, Mice, Knockout, Online Letters to the Editor, 0303 health sciences, geography.geographical_feature_category, Glucagon secretion, Fasting, Islet, Up-Regulation, Calcium Signaling/drug effects, Mitochondrial Proteins/biosynthesis/genetics/metabolism, hormones, hormone substitutes, and hormone antagonists, medicine.medical_specialty, endocrine system, Mice, 129 Strain, Oxidative Stress/drug effects, Fasting/adverse effects, 030209 endocrinology & metabolism, Oxidative phosphorylation, Biology, Hypoglycemia, Glucagon, Mitochondrial Proteins, Islets of Langerhans, 03 medical and health sciences, Downregulation and upregulation, Reactive Oxygen Species/metabolism, Internal medicine, Internal Medicine, medicine, Animals, Humans, Secretion, Calcium Signaling, RNA, Messenger, Caloric Restriction/adverse effects, Glucagon/genetics/metabolism/secretion, Caloric Restriction, 030304 developmental biology, geography, Uncoupling Agents, Membrane Potential, Mitochondrial/drug effects, medicine.disease, Oxidative Stress, Endocrinology, Islet Studies, Glucagon-Secreting Cells, Uncoupling Agents/pharmacology, Ion Channels/biosynthesis/genetics/metabolism, Reactive Oxygen Species, Oxidative stress
Abstract: Glucagon is important for maintaining euglycemia during fasting/starvation, and abnormal glucagon secretion is associated with type 1 and type 2 diabetes; however, the mechanisms of hypoglycemia-induced glucagon secretion are poorly understood. We previously demonstrated that global deletion of mitochondrial uncoupling protein 2 (UCP2−/−) in mice impaired glucagon secretion from isolated islets. Therefore, UCP2 may contribute to the regulation of hypoglycemia-induced glucagon secretion, which is supported by our current finding that UCP2 expression is increased in nutrient-deprived murine and human islets. Further to this, we created α-cell–specific UCP2 knockout (UCP2AKO) mice, which we used to demonstrate that blood glucose recovery in response to hypoglycemia is impaired owing to attenuated glucagon secretion. UCP2-deleted α-cells have higher levels of intracellular reactive oxygen species (ROS) due to enhanced mitochondrial coupling, which translated into defective stimulus/secretion coupling. The effects of UCP2 deletion were mimicked by the UCP2 inhibitor genipin on both murine and human islets and also by application of exogenous ROS, confirming that changes in oxidative status and electrical activity directly reduce glucagon secretion. Therefore, α-cell UCP2 deletion perturbs the fasting/hypoglycemic glucagon response and shows that UCP2 is necessary for normal α-cell glucose sensing and the maintenance of euglycemia.
Published: 2013

25. Physiological ER Stress: The Model of Insulin-Secreting Pancreatic β-Cells

Author: Patrick Gilon, Mohammed Bensellam, Jean-Christophe Jonas, and UCL - SSS/IREC/EDIN - Pôle d'endocrinologie, diabète et nutrition
Subjects: endocrine system, Biochemistry, Downregulation and upregulation, Endoplasmic reticulum, Unfolded protein response, Glucose homeostasis, Integrated stress response, Blood sugar regulation, Secretion, Biology, Proinsulin
Abstract: Endoplasmic reticulum (ER) stress and the consecutive activation of the Unfolded Protein Response (UPR) contribute to the pathogenesis of several diseases including diabetes, neurodegenerative diseases and inflammation. However, the UPR also plays a crucial adaptive role in the acquisition and maintenance of the phenotype of cells that secrete large amounts of proteins. After a brief overview of this physiological role of the UPR in immunoglobulin-secreting plasmocytes and pancreatic acinar cells, this chapter will mainly focus on insulin-secreting pancreatic b-cells that play a critical role in glucose homeostasis. Upon their stimulation with glucose and other nutrients, these cells display a rise in mitochondrial metabolism, ATP production and Ca2+ pumping in the ER, in parallel to the stimulation of protein (preferentially proinsulin) biosynthesis. These metabolic and functional features give rise to a peculiar pattern of acute regulation of the UPR by nutrients. At low non-stimulatory glucose concentrations, when intracellular ATP, [Ca2+]ER and protein synthesis are low, the IRE1-XBP1 branch of the UPR is at its lowest level of activation while the PERK-eIF2α-ATF4 branch of the UPR is maximally activated, with strong upregulation of Integrated Stress Response (ISR) genes. Upon glucose stimulation, the rise in ATP and [Ca2+]ER leads to PERK-eIF2α dephosphorylation, inhibition of the ISR and derepression of protein synthesis. Consequent activation of the IRE1-XBP1 branch of the UPR upregulates the expression of chaperones, foldases, ER to Golgi transport and ER-associated degradation machinery that help the b-cell coping with the large increase in proinsulin biosynthesis. This opposite glucose regulation of the PERK and IRE1 arms of the UPR is rapid and dynamic, suggesting its importance in the physiological adaptation of the b-cell to changes in nutrient supply.
Published: 2012

26. The mitochondrial Ca2+ uniporter MCU is essential for glucose-induced ATP increases in pancreatic β-cells

Author: Rosario Rizzuto, Francesca Semplici, Timothy J. Pullen, Magalie A. Ravier, Guy A. Rutter, Israel Sekler, Elisa A. Bellomo, Patrick Gilon, Andrei I. Tarasov, UCL - SSS/IREC/EDIN - Pôle d'endocrinologie, diabète et nutrition, Medical Research Council (MRC), and Biotechnology and Biological Sciences Research Council (BBSRC)
Subjects: Anatomy and Physiology, B-CELL, lcsh:Medicine, Mitochondrion, Biochemistry, ESSENTIAL COMPONENT, CALCIUM UNIPORTER, chemistry.chemical_compound, Mice, Endocrinology, 0302 clinical medicine, Adenosine Triphosphate, Insulin-Secreting Cells, Molecular Cell Biology, Signaling in Cellular Processes, Insulin, lcsh:Science, Energy-Producing Organelles, Cells, Cultured, 0303 health sciences, Multidisciplinary, Voltage-dependent calcium channel, ATP synthase, biology, Cellular Structures, Signaling Cascades, Calcium Imaging, Cell biology, Electrophysiology, ISLETS, Carbohydrate Metabolism, Medicine, Science & Technology - Other Topics, Female, Metabolic Pathways, ATP–ADP translocase, FATTY-ACIDS, Intracellular, Research Article, Signal Transduction, Cell Physiology, General Science & Technology, Endocrine System, Neuroimaging, Gastroenterology and Hepatology, CYTOSOLIC CA2+, Bioenergetics, Signaling Pathways, CYTOPLASMIC CA2+, 03 medical and health sciences, INDUCED INSULIN-SECRETION, MD Multidisciplinary, Calcium-Mediated Signal Transduction, OSCILLATIONS, Animals, Calcium Signaling, Gene Silencing, Gestational Diabetes, Uniporter, Biology, Pancreas, 030304 developmental biology, Diabetic Endocrinology, SENSITIVE K+ CHANNEL, Science & Technology, MULTIDISCIPLINARY SCIENCES, lcsh:R, Diabetes Mellitus Type 1, Diabetes Mellitus Type 2, Hormones, Cytosol, Metabolism, Glucose, Subcellular Organelles, chemistry, Calcium Signaling Cascade, biology.protein, lcsh:Q, Calcium, Calcium Channels, Adenosine triphosphate, 030217 neurology & neurosurgery, Neuroscience
Abstract: Glucose induces insulin release from pancreatic β-cells by stimulating ATP synthesis, membrane depolarisation and Ca(2+) influx. As well as activating ATP-consuming processes, cytosolic Ca(2+) increases may also potentiate mitochondrial ATP synthesis. Until recently, the ability to study the role of mitochondrial Ca(2+) transport in glucose-stimulated insulin secretion has been hindered by the absence of suitable approaches either to suppress Ca(2+) uptake into these organelles, or to examine the impact on β-cell excitability. Here, we have combined patch-clamp electrophysiology with simultaneous real-time imaging of compartmentalised changes in Ca(2+) and ATP/ADP ratio in single primary mouse β-cells, using recombinant targeted (Pericam or Perceval, respectively) as well as entrapped intracellular (Fura-Red), probes. Through shRNA-mediated silencing we show that the recently-identified mitochondrial Ca(2+) uniporter, MCU, is required for depolarisation-induced mitochondrial Ca(2+) increases, and for a sustained increase in cytosolic ATP/ADP ratio. By contrast, silencing of the mitochondrial Na(+)-Ca(2+) exchanger NCLX affected the kinetics of glucose-induced changes in, but not steady state values of, cytosolic ATP/ADP. Exposure to gluco-lipotoxic conditions delayed both mitochondrial Ca(2+) uptake and cytosolic ATP/ADP ratio increases without affecting the expression of either gene. Mitochondrial Ca(2+) accumulation, mediated by MCU and modulated by NCLX, is thus required for normal glucose sensing by pancreatic β-cells, and becomes defective in conditions mimicking the diabetic milieu.
Published: 2012

27. Tissue-specific disallowance of housekeeping genes: The other face of cell differentiation

Author: Lieven Thorrez, Ilaria Laudadio, Katrijn Van Deun, Roel Quintens, Nico Hendrickx, Mikaela Granvik, Katleen Lemaire, Anica Schraenen, Leentje Van Lommel, Stefan Lehnert, Cristina Aguayo-Mazzucato, Rui Cheng-Xue, Patrick Gilon, Iven Van Mechelen, Susan Bonner-Weir, Frédéric Lemaigre, Frans Schuit, UCL - SSS/IREC/EDIN - Pôle d'endocrinologie, diabète et nutrition, and UCL - SSS/IREC - Institut de recherche expérimentale et clinique
Subjects: MicroRNAs - genetics, metabolism, Epigenomics, Male, Monocarboxylic Acid Transporters, Cellular differentiation, Messenger, Lactate Dehydrogenases - genetics, metabolism, Biology, Inbred C57BL, RNA, Messenger - genetics, metabolism, Islets of Langerhans, Mice, Monocarboxylic Acid Transporters - genetics, metabolism, Histone methylation, Genetics, Animals, Female, Lactate Dehydrogenases, Liver, Mice, Inbred C57BL, MicroRNAs, Oligonucleotide Array Sequence Analysis, Organ Specificity, Pancreas, RNA, Messenger, Rats, Symporters, Cell Differentiation, Gene Expression Regulation, Developmental, Developmental, Pancreas - cytology, metabolism, Epigenetics, Islets of Langerhans - cytology, metabolism, Psychological repression, Gene, Genetics (clinical), Microarray analysis techniques, Research, Symporters - genetics, metabolism, Housekeeping gene, Gene Expression Regulation, RNA, Liver - cytology, metabolism
Abstract: We report on a hitherto poorly characterized class of genes that are expressed in all tissues, except in one. Often, these genes have been classified as housekeeping genes, based on their nearly ubiquitous expression. However, the specific repression in one tissue defines a special class of ‘‘disallowed genes.’’ In this paper, we used the intersection-union test to screen for such genes in a multi-tissue panel of genome-wide mRNA expression data. We propose that disallowed genes need to be repressed in the specific target tissue to ensure correct tissue function. We provide mechanistic data of repression with two metabolic examples, exercise-induced inappropriate insulin release and interference with ketogenesis in liver. Developmentally, this repression is established during tissue maturation in the early postnatal period involving epigenetic changes in histone methylation. In addition, tissue-specific expression of microRNAs can further diminish these repressed mRNAs. Together, we provide a systematic analysis of tissue-specific repression of housekeeping genes, a phenomenon that has not been studied so far on a genome-wide basis and, when perturbed, can lead to human disease. [Supplemental material is available online at http://www.genome.org. The microarray data have been submitted to the NCBI Gene Expression Omnibus (http://www.ncbi.nlm.nih.gov/geo/) under accession nos. GSE24207 and GSE24940.]
Published: 2011

28. Loss of high-frequency glucose-induced Ca2+ oscillations in pancreatic islets correlates with impaired glucose tolerance in Trpm5-/- mice

Author: Patrick Gilon, Katleen Lemaire, Robert F. Margolskee, Rudi Vennekens, Roel Quintens, Barbara Colsoul, Karel Talavera, Thomas Voets, Leentje Van Lommel, Anica Schraenen, Frans Schuit, Bernd Nilius, Andrei Segal, Grzegorz Owsianik, Zaza Kokrashvili, UCL - SSS/IREC - Institut de recherche expérimentale et clinique, and UCL - SSS/IREC/EDIN - Pôle d'endocrinologie, diabète et nutrition
Subjects: medicine.medical_specialty, medicine.medical_treatment, Intracellular Space, TRPM Cation Channels, Biology, Calcium in biology, Gene Expression Regulation - drug effects, Membrane Potentials, Impaired glucose tolerance, Islets of Langerhans, Mice, Insulin - secretion, Internal medicine, Cations, Insulin Secretion, medicine, Insulin, Glucose homeostasis, Animals, TRPM Cation Channels - deficiency, genetics, metabolism, Intracellular Space - drug effects, metabolism, Calcium Signaling, TRPM5, Membrane Potentials - drug effects, Membrane potential, Multidisciplinary, Pancreatic islets, Islets of Langerhans - cytology, drug effects, metabolism, secretion, Biological Sciences, Glucose Tolerance Test, medicine.disease, Calcium Signaling - drug effects, Glucose, Endocrinology, medicine.anatomical_structure, Phenotype, Gene Expression Regulation, Glucose - pharmacology, Beta cell, Ion Channel Gating - drug effects, Ion Channel Gating
Abstract: Glucose homeostasis is critically dependent on insulin release from pancreatic β-cells, which is strictly regulated by glucose-induced oscillations in membrane potential (V m ) and the cytosolic calcium level ([Ca 2+ ] cyt ). We propose that TRPM5, a Ca 2+ -activated monovalent cation channel, is a positive regulator of glucose-induced insulin release. Immunofluorescence revealed expression of TRPM5 in pancreatic islets. A Ca 2+ -activated nonselective cation current with TRPM5-like properties is significantly reduced in Trpm 5 −/− cells. Ca 2+ -imaging and electrophysiological analysis show that glucose-induced oscillations of V m and [Ca 2+ ] cyt have on average a reduced frequency in Trpm5 −/− islets, specifically due to a lack of fast oscillations. As a consequence, glucose-induced insulin release from Trpm5 −/− pancreatic islets is significantly reduced, resulting in an impaired glucose tolerance in Trpm5 −/− mice.
Published: 2010

29. Increased glucose sensitivity of both triggering and amplifying pathways of insulin secretion in rat islets cultured for 1 wk in high glucose

Author: Jean-Christophe Jonas, Myriam Khaldi, Yves Guiot, Patrick Gilon, Jean-Claude Henquin, and UCL - MD/FSIO - Département de physiologie et pharmacologie
Subjects: Male, medicine.medical_specialty, Physiology, Cell Survival, Endocrinology, Diabetes and Metabolism, medicine.medical_treatment, Stimulation, Biology, Endoplasmic Reticulum, mitochondrial activity, Drug Administration Schedule, Ion Channels, Mitochondrial Proteins, glucose toxicity, chemistry.chemical_compound, Islets of Langerhans, Organ Culture Techniques, Physiology (medical), Internal medicine, Insulin Secretion, medicine, Diazoxide, Animals, Insulin, Uncoupling Protein 2, Calcium Signaling, RNA, Messenger, Rats, Wistar, Pancreatic hormone, geography, Analysis of Variance, geography.geographical_feature_category, Dose-Response Relationship, Drug, pancreatic beta-cell, Membrane Transport Proteins, cytosolic calcium concentration, Islet, Insulin oscillation, Rats, Endocrinology, Glucose, L-Glucose, chemistry, Blood sugar regulation, Insulin Resistance, medicine.drug, Signal Transduction
Abstract: Chronic hyperglycemia has been shown to induce either a lack of response or an increased sensitivity to glucose in pancreatic β-cells. We reinvestigated this controversial issue in a single experimental model by culturing rat islets for 1 wk in 10 or 30 mmol/l glucose (G10, Controls; or G30, High-glucose islets) before testing the effect of stepwise glucose stimulation from G0.5 to G20 on key β-cell stimulus-secretion coupling events. Compared with Controls, the glucose sensitivity of High-glucose islets was markedly increased, leading to maximal stimulation of oxidative metabolism and both triggering and amplifying pathways of insulin secretion in G6 rather than G20, hence to loss of glucose effect above G6. This enhanced glucose sensitivity occurred despite an approximately twofold increase in islet uncoupling protein 2 mRNA expression. Besides this increased glucose sensitivity, the maximal glucose stimulation of insulin secretion in High-glucose islets was reduced by ∼50%, proportionally to the reduction of insulin content. In High-glucose islets, changes in45Ca2+influx induced by glucose and diazoxide were qualitatively similar but quantitatively smaller than in Control islets and, paradoxically, did not lead to detectable changes in the intracellular Ca2+concentration measured by microspectrofluorimetry (fura PE 3). In conclusion, after 1 wk of culture in G30, the loss of glucose stimulation of insulin secretion in the physiological range of glucose concentrations (G5–G10) results from the combination of an increased sensitivity to glucose of both triggering and amplifying pathways of insulin secretion and an ∼50% reduction in the maximal glucose stimulation of insulin secretion.
Published: 2004

30. 40(th) EASD Annual Meeting of the European Association for the Study of Diabetes : Munich, Germany, 5-9 September 2004

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Butler, Francisco Javier Ampudia-Blasco, O N Kong, Attali J-R., C A Hedman, K Oshinyemi, Nicolle Müller, I C Cranston, N Okumus, M V Vlaiculescu, Balasubramanian Ravikumar, W W Cheatham, K Mukasa, K B Biswas, Annunziata Lapolla, Phil McEwan, G Mader, Gilles Chassot, Dragi Anevski, Werner A. Scherbaum, M Donath, C Hesselmann, R A Gandhi, David E. Moller, Ezio Bonifacio, C Garcia, V Ifandi, P Hornnes, Nieuwenhoven Fav., C Puech, S Pérez-Del-Pulgar, Kim S-R., G Hines, C Rubio Terrés, Michael Gaster, N. Hosszufalusi, A Scholze, Andrew A. Young, Stavros Liatis, F Hariri, S Tan, Paul Valensi, Allan E. Karlsen, J Kim, E. Moberg, J Kaiser, L Berman, G Nelson, A Altkrüger, P Kothare, D B Cook, S Doran, G. van Dijk, Shahnaz Shahinfar, Kim C-S., P Stahl, M Manousaki, S Sigrist, S K Lim, M. P. Stern, A Guberti, C Rezzani, J McKenney, Karl Thomaseth, Sofia Carlsson, M Julia, R Brillante, I Rubesova, T Darkow, E Matsumoto, Wendy M. 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Liu, H, Jeong, I, Chae, M, Choi, M, Yoo, H, Kim, C, Yun, M, Na, M, Kang, Y, Kong, O, Son, S, Kim, I, Tanaka, N, Hosoi, M, Matsuyama, Y, Fukumoto, M, Yamakita, T, Yoshioka, K, Ishii, T, Sato, T, Fujii, S, Aoki, T, Shibata, T, Mizutani, N, Suzuki, J, Fowelin, J, Samuelsson, P, Brandrup wogsen, G, Okumura, K, Tokmakova, A, Staroverova, D, Antcieferov, M, Shutichina, I, Kuntchevich, G, Vriesendorp, T, Morélis, Q, Legemate, D, Schaper, F, Mainas, E, Gkioulmpasanis, I, Panagiotou, I, Vassilikos, G, Skorda, L, Sidira, M, Christoforidou, M, Alaveras, A, Artikis, V, Evdemon, E, Lechleitner, M, Koch, T, Ebenbichler, C, Sturm, W, Moretti, L, Moruzzo, D, Boldrini, E, Pandolfo, C, Kameyama, M, Iwasa, R, Cho, M, Nam, J, Huh, K, Kaplar, M, Paragh, G, Erdei, A, Csongradi, E, Garai, I, Varga, J, Galuska, L, Udvardy, M, Higa, M, Kaneko, Y, Hiroi, N, Koziarska, D, Nowacki, P, Majkowska, L, Luzniak, P, Wojciechowska luźniak, A, Tushuizen, M, Nieuwland, R, Snoeck, D, Sturk, A, Diamant, M, Aguiar, L, Bahia, L, Villela, N, Laflor, C, Conde, C, Bottino, D, Dorigo, D, Bouskela, E, Pu, S, Luo, Z, Lam, K, Dan, Q, Xu, A, Shen, J, Cheng, K, Xu, J, Thamer, C, Stefan, N, Haap, M, Heller, E, Tschritter, O, De Prado, A, Ortiz, A, Ybarra, J, Gich, I, Pou, J, Ehren, M, Roggenland, D, Reinsen, B, Klein, H, Rittig, K, Stock, J, Kocher, B, Balletshofer, B, Shon, H, Chung, D, Nakatani, Y, Matsuhisa, M, Kaneto, H, Hatazaki, M, Yoshiuchi, K, Katakami, N, Kawamori, D, Ohtoshi, K, Sakamoto, K, Matsuoka, T, Ozawa, K, Ogawa, S, Hori, M, Yamasaki, Y, Zitouni, K, Harry, D, Nourooz zadeh, J, Earle, K, Olesen, P, Franco, L, Corvaja, C, Semplicini, A, Ceylan işık, A, Arı, N, Rösen, P, Lee, I, Park, K, Jung, E, Shin, D, Jo, S, Obuobie, K, Prakash, P, Hanna, F, Lazarus, J, Varadhan, L, Gurushankar, J, James, D, Sheikh, S, Gaede, P, Zou, D, Vilarrasa, N, Perez maraver, M, Mena, E, Perez, D, Setti, G, Buckingham, R, Urbančič, V, Stefanovska, A, Bernjak, A, Ažman juvan, K, Kocijančič, A, Glowania, A, Filters, T, Fosmark, D, Torjesen, P, Kilhovd, B, Berg, T, Sandvik, L, Hanssen, K, Mentink, C, Donchenko, G, Stepanenko, S, Maingrette, F, Deng, H, Lindenmair, A, Freudenthaler, A, Baumgartner parzer, S, Nizheradze, K, Khoruzhenko, A, Tronko, N, Sheu, W, Ou, H, Shen, H, Lin, T, Wu, H, Yang, C, Mogylnytska, L, Schmoelzer, I, Davies, J, Band, M, Struthers, A, Prázný, M, Škrha, J, Kasalová, Z, Neelotpol, S, Jahan, P, Kauschke, S, Harrop, C, Schäfer, A, Widder, J, Eigenthaler, M, Walter, U, Uchimura, I, Ikebukuro, M, Kaibara, M, Hirata, M, Helal, R, Pervin, F, Yang, X, Jansson, P, Nagaev, I, Jack, M, Carvalho, E, Sunnerhagen, K, Cam, M, Cushman, S, Smith, U, Creely, S, Farmer, J, Gustafson, B, Kusminski, C, Krusinova, E, Wohl, P, Klementova, M, Lanska, V, Mcdougall, C, Kelly, I, Abbas, Z, Lutale, J, Archibald, L, Karunajeewa, H, Stingemore, N, Stuccio, G, Mcgechie, D, Muller, L, Hak, E, Goudzwaard, W, Montorsi, F, Homering, M, Sprenger, K, Goldstein, I, Asnaghi, V, Ferrari, G, Rastaldi, M, Gabellini, D, Dell'Antonio, G, Maestroni, A, Ruggieri, D, Luzi, L, Piemonti, L, Zerbini, G, Anafaroglu, I, Tutuncu, N, Sultana, M, Siddiqua, N, Iwasaki, T, Nakajima, A, Yoneda, M, Mukasa, K, Tanaka, S, and Sekihara, H
Subjects: 0303 health sciences, medicine.medical_specialty, business.industry, EASD, Endocrinology, Diabetes and Metabolism, Human physiology, medicine.disease, 03 medical and health sciences, 0302 clinical medicine, Diabetes mellitus, Family medicine, Internal Medicine, Medicine, business, 030217 neurology & neurosurgery, 030304 developmental biology
Published: 2004

31. Altered cAMP and Ca2+ signaling in mouse pancreatic islets with glucagon-like peptide-1 receptor null phenotype

Author: Jean-Claude Henquin, Louise A. Scrocchi, Karen Moens, Dominique Delmeire, Daisy Flamez, Frans Schuit, Patrick Gilon, A Van Breusegem, Daniel J. Drucker, and UCL - MD/FSIO - Département de physiologie et pharmacologie
Subjects: Male, medicine.medical_specialty, endocrine system, Endocrinology, Diabetes and Metabolism, medicine.medical_treatment, Biology, Glucagon-Like Peptide-1 Receptor, chemistry.chemical_compound, Islets of Langerhans, Mice, Gastric inhibitory polypeptide, Internal medicine, Internal Medicine, medicine, Cyclic AMP, Receptors, Glucagon, Animals, Receptor, Cells, Cultured, Mice, Knockout, geography, geography.geographical_feature_category, Insulin, Pancreatic islets, Diazoxide, Islet, Glucagon-like peptide-1, Acetylcholine, Peptide Fragments, Endocrinology, medicine.anatomical_structure, Glucose, Phenotype, Gastrointestinal hormone, L-Glucose, chemistry, Calcium, Female, hormones, hormone substitutes, and hormone antagonists, Signal Transduction
Abstract: 1-Cells from rodents and humans express different receptors recognizing hormones of the secretin-glucagon family, which--when activated--synergize with glucose in the control of insulin release. We have recently reported that isolated islets from mice homozygous for a GLP-1 receptor null mutation (GLP-1R(-/-)) exhibit a well-preserved insulin-secretory response to glucose. This observation can be interpreted in two different ways: 1) the presence of GLP-1R is not essential for the secretory response of isolated islets to glucose alone; 2) beta-cells in GLP-1R(-/-) pancreases underwent compensatory changes in response to the null mutation. To explore these possibilities, we studied islets from control GLP-IR(+/+) mice in the absence or presence of 1 pmol/l exendin (9-39)amide, a specific and potent GLP-1R antagonist. Exendin (9-39)amide (15-min exposure) reduced glucose-induced insulin secretion from both perifused and statically incubated GLP-1R(+/+) islets by 50% (P < 0.05), and reduced islet cAMP production in parallel (P < 0.001). Furthermore, GLP-1R(-/-) islets exhibited: 1) reduced cAMP accumulation in the presence of 20 mmol/l glucose (knockout islets versus control islets, 12 +/- 1 vs. 27 +/- 3 fmol x islet(-1) x 15 min(-1); P < 0.001) and exaggerated acceleration of cAMP production by 10 nmol/l glucose-dependent insulinotropic peptide (GIP) (increase over 20 mmol/l glucose by GIP in knockout islets versus control islets: 66 +/- 5 vs. 14 +/- 3 fmol x islet(-1) x 15 min(-1); P < 0.001); 2) increased mean cytosolic [Ca2+] ([Ca2+]c) at 7, 10, and 15 mmol/l glucose in knockout islets versus control islets; and 3) signs of asynchrony of [Ca2+]c oscillations between different islet subregions. In conclusion, disruption of GLP-1R signaling is associated with reduced basal but enhanced GIP-stimulated cAMP production and abnormalities in basal and glucose-stimulated [Ca2+]c. These abnormalities suggest that GLP-1R signaling is an essential upstream component of multiple beta-cell signaling pathways.
Published: 1999

32. Influence of cell number on the characteristics and synchrony of Ca2+ oscillations in clusters of mouse pancreatic islet cells

Author: Jean-Christophe Jonas, Françoise C. Jonkers, Patrick Gilon, Jean-Claude Henquin, and UCL - MD/FSIO - Département de physiologie et pharmacologie
Subjects: Time Factors, Physiology, Stimulation, Cell Count, Mice, Inbred Strains, Biology, Islets of Langerhans, Mice, Oscillometry, medicine, Animals, Heptanol, Cells, Cultured, Cell Aggregation, Syncytium, geography, geography.geographical_feature_category, Pancreatic islets, Osmolar Concentration, Gap junction, Original Articles, Anatomy, Intracellular Membranes, Islet, medicine.anatomical_structure, Cytoplasm, Biophysics, Calcium, Female, Intracellular
Abstract: 1. The cytoplasmic Ca2+ concentration ([Ca2+]i) was measured in single cells and cell clusters of different sizes prepared from mouse pancreatic islets. 2. During stimulation with 15 mM glucose, 20 % of isolated cells were inert, whereas 80 % showed [Ca2+]i oscillations of variable amplitude, duration and frequency. Spectral analysis identified a major frequency of 0.14 min-1 and a less prominent one of 0.27 min-1. 3. In contrast, practically all clusters (2-50 cells) responded to glucose, and no inert cells were identified within the clusters. As compared to single cells, mean [Ca2+]i was more elevated, [Ca2+]i oscillations were more regular and their major frequency was slightly higher (but reached a plateau at approximately 0.25 min-1). In some cells and clusters, faster oscillations occurred on top of the slow ones, between them or randomly. 4. Image analysis revealed that the regular [Ca2+]i oscillations were well synchronized between all cells of the clusters. Even when the Ca2+ response was irregular, slow and fast [Ca2+]i oscillations induced by glucose were also synchronous in all cells. 5. In contrast, [Ca2+]i oscillations resulting from mobilization of intracellular Ca2+ by acetylcholine were restricted to certain cells only and were not synchronized. 6. Heptanol and 18alpha-glycyrrhetinic acid, two agents widely used to block gap junctions, altered glucose-induced Ca2+ oscillations, but control experiments showed that they also exerted effects other than a selective uncoupling of the cells. 7. The results support theoretical models predicting an increased regularity of glucose-dependent oscillatory events in clusters as compared to isolated islet cells, but contradict the proposal that the frequency of the oscillations increases with the number of coupled cells. Islet cell clusters function better as electrical than biochemical syncytia. This may explain the co-ordination of [Ca2+]i oscillations driven by depolarization-dependent Ca2+ influx during glucose stimulation.
Published: 1999

33. Uptake and release of Ca2+ by the endoplasmic reticulum contribute to the oscillations of the cytosolic Ca2+ concentration triggered by Ca2+ influx in the electrically excitable pancreatic B-cell

Author: Abdelilah Arredouani, Jesper Gromada, Philippe Gailly, Patrick Gilon, Jean-Claude Henquin, UCL - MD/FSIO - Département de physiologie et pharmacologie, UCL - (SLuc) Service de neurologie, and UCL - (SLuc) Service d'endocrinologie et de nutrition
Subjects: medicine.medical_specialty, SERCA, Thapsigargin, Endoplasmic Reticulum, Biochemistry, Membrane Potentials, Bursting, chemistry.chemical_compound, Islets of Langerhans, Mice, Cytosol, Internal medicine, medicine, Animals, Inositol, Molecular Biology, Ion transporter, Cells, Cultured, Membrane potential, Ion Transport, Endoplasmic reticulum, Cell Biology, Endocrinology, Glucose, chemistry, Biophysics, Calcium, Female, Cyclopiazonic acid
Abstract: The role of intracellular Ca2+ pools in oscillations of the cytosolic Ca2+ concentration ([Ca2+]c) triggered by Ca2+ influx was investigated in mouse pancreatic B-cells. [Ca2+]c oscillations occurring spontaneously during glucose stimulation or repetitively induced by pulses of high K+ (in the presence of diazoxide) were characterized by a descending phase in two components. A rapid decrease in [Ca2+]c coincided with closure of voltage-dependent Ca2+ channels and was followed by a slower phase independent of Ca2+ influx. Blocking the SERCA pump with thapsigargin or cyclopiazonic acid accelerated the rising phase of [Ca2+]c oscillations and increased their amplitude, which suggests that the endoplasmic reticulum (ER) rapidly takes up Ca2+. It also suppressed the slow [Ca2+]c recovery phase, which indicates that this phase corresponds to the slow release of Ca2+ that was taken up by the ER during the upstroke of the [Ca2+]c transient. Glucose promoted the buffering capacity of the ER and amplified the slow [Ca2+]c recovery phase. The slow phase induced by high K+ pulses was not affected by modulators of Ca2+- or inositol 1,4,5-trisphosphate-induced Ca2+ release, did not involve a depolarization-induced Ca2+ release, and was also observed at the end of a rapid rise in [Ca2+]c triggered from caged Ca2+. It is attributed to passive leakage of Ca2+ from the ER. We suggest that the ER displays oscillations of the Ca2+ concentration ([Ca2+]ER) concomitant and parallel to [Ca2+]c. The observation that thapsigargin depolarizes the membrane of B-cells supports the proposal that the degree of Ca2+ filling of the ER modulates the membrane potential. Therefore, [Ca2+]ER oscillations occurring during glucose stimulation are likely to influence the bursting behavior of B-cells and eventually [Ca2+]c oscillations.
Published: 1999

34. SERCA2 Deficiency Impairs Pancreatic β-Cell Function in Response to Diet-Induced Obesity.

Author: Xin Tong, Tatsuyoshi Kono, Anderson-Baucum, Emily K., Wataru Yamamoto, Patrick Gilon, Djamel Lebeche, Day, Richard N., Shull, Gary E., Evans-Molina, Carmella, Tong, Xin, Kono, Tatsuyoshi, Yamamoto, Wataru, Gilon, Patrick, and Lebeche, Djamel
Subjects: ENDOPLASMIC reticulum, TYPE 2 diabetes, B cells, OBESITY, ANIMAL models in research, HOMEOSTASIS, CALCIUM metabolism, ANIMAL experimentation, ANIMALS, BLOOD sugar, CARRIER proteins, CELL physiology, CYTOPLASM, DIET, INSULIN, INSULIN resistance, ISLANDS of Langerhans, MICE, RESEARCH funding, PHYSIOLOGY
Abstract: The sarcoendoplasmic reticulum (ER) Ca(2+) ATPase 2 (SERCA2) pump is a P-type ATPase tasked with the maintenance of ER Ca(2+) stores. Whereas β-cell SERCA2 expression is reduced in diabetes, the role of SERCA2 in the regulation of whole-body glucose homeostasis has remained uncharacterized. To this end, SERCA2 heterozygous mice (S2HET) were challenged with a high-fat diet (HFD) containing 45% of kilocalories from fat. After 16 weeks of the HFD, S2HET mice were hyperglycemic and glucose intolerant, but adiposity and insulin sensitivity were not different between HFD-fed S2HET mice and HFD-fed wild-type controls. Consistent with a defect in β-cell function, insulin secretion, glucose-induced cytosolic Ca(2+) mobilization, and the onset of steady-state glucose-induced Ca(2+) oscillations were impaired in HFD-fed S2HET islets. Moreover, HFD-fed S2HET mice exhibited reduced β-cell mass and proliferation, altered insulin production and proinsulin processing, and increased islet ER stress and death. In contrast, SERCA2 activation with a small molecule allosteric activator increased ER Ca(2+) storage and rescued tunicamycin-induced β-cell death. In aggregate, these data suggest a critical role for SERCA2 and the regulation of ER Ca(2+) homeostasis in the β-cell compensatory response to diet-induced obesity. [ABSTRACT FROM AUTHOR]
Published: 2016
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35. Direct glucocorticoid inhibition of insulin secretion : an in vitro study of dexamethasone effects in mouse islets

Author: Cécile Lambillotte, Jean-Claude Henquin, Patrick Gilon, UCL - MD/FSIO - Département de physiologie et pharmacologie, and UCL - (SLuc) Service d'endocrinologie et de nutrition
Subjects: Male, medicine.medical_specialty, medicine.medical_treatment, Inositol Phosphates, Tolbutamide, Pancreatic islets, Mice, Inbred Strains, Biology, Carbohydrate metabolism, Pertussis toxin, Arginine, Dexamethasone, Islets of Langerhans, Mice, Glucocorticoid receptor, Receptors, Glucocorticoid, Internal medicine, Insulin Secretion, Phorbol Esters, medicine, Cyclic AMP, Animals, Insulin, Virulence Factors, Bordetella, Cytoplasmic calcium, Glucocorticoids, Cells, Cultured, B-Lymphocytes, Dose-Response Relationship, Drug, Insulin secretion, General Medicine, Insulin oscillation, Endocrinology, Glucose, Bucladesine, Pertussis Toxin, Stimulus-secretion coupling, Potassium, Calcium, Oxidation-Reduction, Glucocorticoid, NADP, medicine.drug, Research Article
Abstract: The direct effects of glucocorticoids on pancreatic beta cell function were studied with normal mouse islets. Dexamethasone inhibited insulin secretion from cultured islets in a concentration-dependent manner: maximum of approximately 75% at 250 nM and IC50 at approximately 20 nM dexamethasone. This inhibition was of slow onset (0, 20, and 40% after 1, 2, and 3 h) and only slowly reversible. It was prevented by a blocker of nuclear glucocorticoid receptors, by pertussis toxin, by a phorbol ester, and by dibutyryl cAMP, but was unaffected by an increase in the fuel content of the culture medium. Dexamethasone treatment did not affect islet cAMP levels but slightly reduced inositol phosphate formation. After 18 h of culture with or without 1 microM dexamethasone, the islets were perifused and stimulated by a rise in the glucose concentration from 3 to 15 mM. Both phases of insulin secretion were similarly decreased in dexamethasone-treated islets as compared with control islets. This inhibition could not be ascribed to a lowering of insulin stores (higher in dexamethasone-treated islets), to an alteration of glucose metabolism (glucose oxidation and NAD(P)H changes were unaffected), or to a lesser rise of cytoplasmic Ca2+ in beta cells (only the frequency of the oscillations was modified). Dexamethasone also inhibited insulin secretion induced by arginine, tolbutamide, or high K+. In this case also the inhibition was observed despite a normal rise of cytoplasmic Ca2+. In conclusion, dexamethasone inhibits insulin secretion through a genomic action in beta cells that leads to a decrease in the efficacy of cytoplasmic Ca2+ on the exocytotic process.
Published: 1997

36. Two sites of glucose control of insulin release with distinct dependence on the energy state in pancreatic B-cells

Author: Jean-Claude Henquin, Philippe Detimary, Myriam Nenquin, Patrick Gilon, UCL - MD/FSIO - Département de physiologie et pharmacologie, UCL - MD/NOPS - Département de neurologie et de psychiatrie, UCL - (SLuc) Service de psychiatrie adulte, and UCL - (SLuc) Service d'endocrinologie et de nutrition
Subjects: medicine.medical_specialty, Azides, medicine.medical_treatment, Biology, Biochemistry, Membrane Potentials, chemistry.chemical_compound, Islets of Langerhans, Mice, Tolbutamide, Adenosine Triphosphate, Internal medicine, Insulin Secretion, medicine, Diazoxide, Animals, Insulin, Molecular Biology, Membrane potential, Cell Biology, Adenosine Diphosphate, Adenosine diphosphate, Endocrinology, Membrane repolarization, Glucose, chemistry, Biophysics, Calcium, Female, Oligomycins, Azide, Energy Metabolism, Adenosine triphosphate, Dinitrophenols, Research Article, medicine.drug
Abstract: The energy state of pancreatic B-cells may influence insulin release at several steps of stimulus-secretion coupling. By closing ATP-sensitive K+ channels (K(+)-ATP channels), a rise in the ATP/ADP ratio may regulate the membrane potential, and hence Ca2+ influx. It may also modulate the effectiveness of Ca2+ on its intracellular targets. To assess the existence of these two roles and determine their relative importance for insulin release, we tested the effects of azide, a mitochondrial poison, on mouse B-cell function under various conditions. During stimulation by glucose alone, when K(+)-ATP channels are controlled by cellular metabolism, azide caused parallel, concentration-dependent (0.5-5 mM), membrane repolarization, decrease in cytosolic Ca2+ concentration [Ca2+]i and inhibition of insulin release. When K(+)-ATP channels were closed pharmacologically (by tolbutamide in high glucose), azide did not repolarize the membrane or decrease [Ca2+]i, and was much less effective in inhibiting insulin release. A similar resistance to azide was observed when K(+)-ATP channels were opened by diazoxide, and high K+ was used to depolarize the membrane and raise [Ca2+]i. In contrast, azide similarly decreased ATP levels and increased ADP levels, thereby lowering the ATP/ADP ratio under all conditions. In conclusion, lowering the ATP/ADP ratio in B-cells can inhibit insulin release even when [Ca2+]i remains high. However, this distal step is much more resistant to a decrease in the energy state of B-cells than is the control of membrane potential by K(+)-ATP channels. Generation of the signal triggering insulin release, high [Ca2+]i, through metabolic control of membrane potential requires a higher global ATP/ADP ratio than does activation of the secretory process itself.
Published: 1994

37. Mechanisms by which glucose can control insulin release independently from its action on adenosine triphosphate-sensitive K+ channels in mouse B cells

Author: Jean-Claude Henquin, Philippe Detimary, Patrick Gilon, Zhi-Yong Gao, M. Gembal, UCL - MD/FSIO - Département de physiologie et pharmacologie, UCL - MD/NOPS - Département de neurologie et de psychiatrie, and UCL - (SLuc) Service de psychiatrie adulte
Subjects: Male, medicine.medical_specialty, Potassium Channels, medicine.medical_treatment, Inositol Phosphates, Mice, Inbred Strains, Biology, chemistry.chemical_compound, Islets of Langerhans, Mice, Adenosine Triphosphate, Internal medicine, Insulin Secretion, medicine, Diazoxide, Cyclic AMP, Animals, Insulin, Inositol, Inositol phosphate, Cells, Cultured, Phorbol 12,13-Dibutyrate, Protein Kinase C, Membrane potential, chemistry.chemical_classification, Forskolin, Terpenes, Colforsin, General Medicine, Keto Acids, Cell biology, Adenosine Diphosphate, Adenosine diphosphate, Kinetics, Endocrinology, Glucose, chemistry, Potassium, Tetradecanoylphorbol Acetate, Diterpenes, Adenosine triphosphate, medicine.drug, Research Article
Abstract: Glucose stimulation of insulin release involves closure of ATP-sensitive K+ channels (K(+)-ATP channels), depolarization, and Ca2+ influx in B cells. However, by using diazoxide to open K(+)-ATP channels, and 30 mM K to depolarize the membrane, we could demonstrate that another mechanism exists, by which glucose can control insulin release independently from changes in K(+)-ATP channel activity and in membrane potential (Gembal et al. 1992. J. Clin. Invest. 89:1288-1295). A similar approach was followed here to investigate, with mouse islets, the nature of this newly identified mechanism. The membrane potential-independent increase in insulin release produced by glucose required metabolism of the sugar and was mimicked by other metabolized secretagogues. It also required elevated levels of cytoplasmic Cai2+, but was not due to further changes in Cai2+. It could not be ascribed to acceleration of phosphoinositide metabolism, or to activation of protein kinases A or C. Thus, glucose did not increase inositol phosphate levels and hardly affected cAMP levels. Moreover, increasing inositol phosphates by vasopressin or cAMP by forskolin, and activating protein kinase C by phorbol esters did not mimic the action of glucose on release, and down-regulation of protein kinase C did not prevent these effects. On the other hand, it correlated with an increase in the ATP/ADP ratio in islet cells. We suggest that the membrane potential-independent control of insulin release exerted by glucose involves changes in the energy state of B cells.
Published: 1993

38. Evidence that glucose can control insulin release independently from its action on ATP-sensitive K+ channels in mouse B cells

Author: Marek Gembal, Patrick Gilon, Jean-Claude Henquin, and UCL - MD/FSIO - Département de physiologie et pharmacologie
Subjects: medicine.medical_specialty, Potassium Channels, medicine.medical_treatment, chemistry.chemical_element, Calcium, Biology, Membrane Potentials, Islets of Langerhans, Mice, Adenosine Triphosphate, Internal medicine, Insulin Secretion, medicine, Diazoxide, Animals, Insulin, Cells, Cultured, Membrane potential, Calcium metabolism, Depolarization, General Medicine, Potassium channel, Cytosol, Endocrinology, Glucose, chemistry, Research Article, medicine.drug
Abstract: Glucose stimulation of insulin release involves closure of ATP-sensitive K+ channels, depolarization, and Ca2+ influx in B cells. Mouse islets were used to investigate whether glucose can still regulate insulin release when it cannot control ATP-sensitive K+ channels. Opening of these channels by diazoxide (100-250 mumol/liter) blocked the effects of glucose on B cell membrane potential (intracellular microelectrodes), free cytosolic Ca2+ (fura-2 method), and insulin release, but it did not prevent those of high K (30 mmol/liter). K-induced insulin release in the presence of diazoxide was, however, dose dependently increased by glucose, which was already effective at concentrations (2-6 mmol/liter) that are subthreshold under normal conditions (low K and no diazoxide). This effect was not accompanied by detectable changes in B cell membrane potential. Measurements of 45Ca fluxes and cytosolic Ca2+ indicated that glucose slightly increased Ca2+ influx during the first minutes of depolarization by K, but not in the steady state when its effect on insulin release was the largest. In conclusion, there exists a mechanism by which glucose can control insulin release independently from changes in K(+)-ATP channel activity, in membrane potential, and in cytosolic Ca2+. This mechanism may serve to amplify the secretory response to the triggering signal (closure of K(+)-ATP channels--depolarization--Ca2+ influx) induced by glucose.
Published: 1992

39. Immunocytochemical and autoradiographic studies of the endocrine cells interacting with GABA in the rat stomach

Author: Jérôme Mallefet, Michel Geffard, Patrick Gilon, Ghislaine Campistron, C. De Vriendt, Claude Remacle, S. Pauwels, UCL - MD/FSIO - Département de physiologie et pharmacologie, and UCL - SC/BIOL - Département de biologie
Subjects: medicine.medical_specialty, Histology, Immunocytochemistry, Enteroendocrine cell, Peptide hormone, Biology, Internal medicine, Gastrins, medicine, Endocrine system, Animals, Molecular Biology, Antrum, gamma-Aminobutyric Acid, Gastrin, Rats, Inbred Strains, Cell Biology, General Medicine, Immunohistochemistry, Rats, Medical Laboratory Technology, Microscopy, Electron, Endocrinology, Somatostatin, APUD Cells, nervous system, Gastric Mucosa, Autoradiography, Anatomy, General Agricultural and Biological Sciences, Hormone
Abstract: There are now increasing evidences suggesting that GABA is able of direct interaction with certain endocrine cells. In the present study, highly specific anti-GABA-glutaraldehyde antibodies and 3H-GABA uptake were used at the light and electron microscope levels to investigate the occurrence of cells containing endogenous GABA or taking up exogenous GABA in the mucosal antrum and corpus of the rat stomach. Only certain endocrine cell types of both regions were immunostained or grain-labelled. However, the morphology of their secretory granules did not allow to identify the nature of their hormone with certainty but suggested that somatostatin-like cells could interact with GABA. The combination of gastrin and somatostatin immunodetection with 3H-GABA uptake autoradiography at the light microscope level, revealed that a subpopulation of somatostatin-like cells and other still unidentified endocrine cells are able to take up GABA, while the gastrin-like cells are not. These results reinforce the hypothesis that certain endocrine cell types of the diffuse endocrine system of the digestive tract are able to directly interact with GABA.
Published: 1990

40. Placental lactogens induce serotonin biosynthesis in a subset of mouse beta cells during pregnancy

Author: Mikaela Granvik, G. de Faudeur, N. Binart, Frans Schuit, Katleen Lemaire, L. Van Lommel, J. Mallet, G. Vodjdani, Patrick Gilon, Nico Hendrickx, Anica Schraenen, P. In't Veld, UCL - SSS/IREC/EDIN - Pôle d'endocrinologie, diabète et nutrition, and UCL - SSS/IREC - Institut de recherche expérimentale et clinique
Subjects: endocrine system, Serotonin, medicine.medical_specialty, Insulin-Secreting Cells - classification, drug effects, metabolism, Tryptophan hydroxylase, Endocrinology, Diabetes and Metabolism, Gestational Age, Biology, Gene Expression Regulation, Enzymologic, Article, Mice, Islets of Langerhans, Downregulation and upregulation, Pregnancy, Insulin-Secreting Cells, Internal medicine, Tph2, Tph1, medicine, Internal Medicine, Animals, Tryptophan Hydroxylase - genetics, metabolism, Placental lactogen, Receptor, Cells, Cultured, Mice, Knockout, Fetus, Placental Lactogen - pharmacology, physiology, Serotonin - biosynthesis, Prolactin receptor, Pregnancy - metabolism, Embryo, Mammalian, medicine.disease, Prolactin, Up-Regulation, Mice, Inbred C57BL, Endocrinology, Beta cell heterogeneity, Gene Expression Regulation, Enzymologic - drug effects, Female, Up-Regulation - drug effects, Beta cell
Abstract: Aims/hypothesis Upregulation of the functional beta cell mass is required to match the physiological demands of mother and fetus during pregnancy. This increase is dependent on placental lactogens (PLs) and prolactin receptors, but the mechanisms underlying these events are only partially understood. We studied the mRNA expression profile of mouse islets during pregnancy to gain a better insight into these changes. Methods RNA expression was measured ex vivo via microarrays and quantitative RT-PCR. In vivo observations were extended by in vitro models in which ovine PL was added to cultured mouse islets and MIN6 cells. Results mRNA encoding both isoforms of the rate-limiting enzyme of serotonin biosynthesis, tryptophan hydroxylase (TPH), i.e. Tph1 and Tph2, were strongly induced (fold change 25- to 200-fold) during pregnancy. This induction was mimicked by exposing islets or MIN6 cells to ovine PLs for 24 h and was dependent on janus kinase 2 and signal transducer and activator of transcription 5. Parallel to Tph1 mRNA and protein induction, islet serotonin content increased to a peak level that was 200-fold higher than basal. Interestingly, only a subpopulation of the beta cells was serotonin-positive in vitro and in vivo. The stored serotonin pool in pregnant islets and PL-treated MIN6 cells was rapidly released (turnover once every 2 h). Conclusions/interpretation A very strong lactogen-dependent upregulation of serotonin biosynthesis occurs in a subpopulation of mouse islet beta cells during pregnancy. Since the newly formed serotonin is rapidly released, this lactogen-induced beta cell function may serve local or endocrine tasks, the nature of which remains to be identified. Electronic supplementary material The online version of this article (doi:10.1007/s00125-010-1913-7) contains supplementary material, which is available to authorised users.
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