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1. A high‐fat diet supplemented with medium‐chain triglycerides ameliorates hepatic steatosis by reducing ceramide and diacylglycerol accumulation in mice

Author

Stephanie Mourad, Abdualrahman Mohammed Abdualkader, Xiaobei Li, Shailee Jani, Rolando B. Ceddia, and Rami Al Batran

Subjects
ceramide, diacylglycerol, hepatic steatosis, inflammation, medium‐chain triglycerides, Physiology, QP1-981
Abstract

Abstract Non‐alcoholic fatty liver disease (NAFLD) is projected to be the most common chronic liver disease worldwide and is closely linked to obesity, insulin resistance and type 2 diabetes. Currently, no pharmacological treatments are available to treat NAFLD, and lifestyle modification, including dietary interventions, is the only remedy. Therefore, we conducted a study to determine whether supplementation with medium‐chain triglycerides (MCTs), containing a mixture of C8 and C10 (60/40), attenuates NAFLD in obese and insulin‐resistant mice. To achieve that, we fed C57BL/6 male mice a high‐fat diet (HFD) for 12 weeks to induce obesity and hepatic steatosis, after which obese mice were assigned randomly either to remain on the HFD or to transition to an HFD supplemented with MCTs (HFD + MCTs) or a low‐fat diet (LFD) for 6 weeks as another dietary intervention model. Another group of mice was kept on an LFD throughout the study and used as a lean control group. Obese mice that transitioned to HFD + MCTs exhibited improvement in glucose and insulin tolerance tests, and the latter improvement was independent of changes in adiposity when compared with HFD‐fed mice. Additionally, supplementation with MCTs significantly reduced hepatic steatosis, improved liver enzymes and decreased hepatic expression of inflammation‐related genes to levels similar to those observed in obese mice transitioned to an LFD. Importantly, HFD + MCTs markedly lowered hepatic ceramide and diacylglycerol content and prevented protein kinase C‐ε translocation to the plasma membrane. Our study demonstrated that supplementation with MCTs formulated mainly from C8 and C10 effectively ameliorated NAFLD in obese mice.

Published
2024
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4. An obesogenic diet impairs uncoupled substrate oxidation and promotes whitening of the brown adipose tissue in rats

Author

Daniel Da Eira, Shailee Jani, and Rolando B. Ceddia

Subjects
Glycerol, Tyrosine 3-Monooxygenase, Physiology, Fatty Acids, Thermogenesis, Rats, Diet, Phosphoenolpyruvate, Mitochondrial Proteins, Adipocytes, Brown, Glucose, Adipose Tissue, Brown, Glycerol Kinase, Animals, Obesity, Uncoupling Protein 1, Triglycerides
Abstract

Brown adipose tissue (BAT) is rich in mitochondria containing uncoupling protein 1 (UCP1), and dissipates energy through thermogenesis. However, even though BAT mass and its UCP1 content increase in rodents chronically fed a high-fat sucrose-enriched (HFS) diet, marked expansion of adiposity still occurs in these animals, suggesting insufficient BAT-mediated HFS diet-induced thermogenesis. Thus, the objective of this study was to investigate the metabolic and molecular mechanisms that regulate BAT thermogenesis in HFS-induced obesity. To accomplish this, rats were fed either a standard chow or HFS diet for 8 weeks. Subsequently, glucose and fatty acid metabolism and the molecular mechanisms underlying these processes were assessed in freshly isolated primary BAT adipocytes. Despite increasing BAT mass and its UCP1 content, the HFS diet reduced uncoupled glucose and palmitate oxidation in BAT adipocytes. It also markedly diminished tyrosine hydroxylase content and lipolysis in these cells. Conversely, glucose uptake, lactate production, glycerol incorporation into lipids, palmitate incorporation into triacylglycerol (TAG), phosphoenolpyruvate carboxykinase and glycerol kinase levels, and lipoprotein lipase and cluster of differentiation 36 gene expression were increased. In summary, a HFS diet enhanced glyceroneogenesis and shifted BAT metabolism toward TAG synthesis by impairing UCP1-mediated substrate oxidation and by enhancing fatty acid esterification in intact brown adipocytes. These adaptive metabolic responses to chronic HFS feeding attenuated BAT thermogenic capacity and favoured the development of obesity. KEY POINTS: Despite increasing brown adipose tissue (BAT) mass and levels of thermogenic proteins such as peroxisome proliferator-activated receptor γ coactivator 1α, carnitine palmitoyltransferase 1B and uncoupling protein 1 (UCP1), an obesogenic high-fat sucrose-enriched (HFS) diet attenuated uncoupled glucose and fatty acid oxidation in brown adipocytes. Brown adipocytes diverted glycerol and fatty acids toward triacylglycerol (TAG) synthesis by elevating the cellular machinery that promotes fatty acid uptake along with phosphoenolpyruvate carboxykinase and glycerol kinase levels. The HFS diet increased glucose uptake that supported lactate production and provided substrate for glyceroneogenesis and TAG synthesis in brown adipocytes. Impaired UCP-1-mediated thermogenic capacity and enhanced TAG storage in BAT adipocytes were consistent with reduced adipose triglyceride lipase and tyrosine hydroxylase levels in HFS diet-fed animals.

Published
2022
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8. Enalapril and treadmill running reduce adiposity, but only the latter causes adipose tissue browning in mice

Author

Tiago Fernandes, Antonio Claudio Lucas da Nóbrega, Rolando B. Ceddia, Eliete Dalla Corte Frantz, Beatriz Alexandre-Santos, Edilamar Menezes de Oliveira, Isabele Gomes Giori, D'Angelo Carlo Magliano, Carlos Adam Conte-Junior, and Carla Paulo Vieira

Subjects
Male, 0301 basic medicine, medicine.medical_specialty, Physiology, Adipose Tissue, White, Clinical Biochemistry, Subcutaneous Fat, Adipose tissue, White adipose tissue, Diet, High-Fat, Running, Renin-Angiotensin System, Mice, 03 medical and health sciences, 0302 clinical medicine, Adipose Tissue, Brown, Enalapril, Physical Conditioning, Animal, Internal medicine, Renin–angiotensin system, Browning, Animals, Medicine, Aerobic exercise, Obesity, Receptor, Adiposity, business.industry, Cell Biology, Mice, Inbred C57BL, 030104 developmental biology, Endocrinology, 030220 oncology & carcinogenesis, CAMUNDONGOS, Adipocyte hypertrophy, business, Biomarkers, medicine.drug
Abstract

This study investigated whether regulation of the renin-angiotensin system (RAS) by enalapril and/or aerobic exercise training (AET) causes browning of the subcutaneous white adipose tissue (sWAT). C57BL/6 mice were fed either a standard chow or a high-fat (HF) diet for 16 weeks. At Week 8, HF-fed animals were divided into sedentary (HF), enalapril (HF-E), AET (HF-T), and enalapril plus AET (HF-ET) groups. Subsequently, sWAT was extracted for morphometry, determination of RAS expression, and biomarkers of WAT browning. The HF group displayed adipocyte hypertrophy and induction of the classical RAS axis. Conversely, all interventions reduced adiposity and induced the counterregulatory RAS axis. However, only AET raised plasma irisin, increased peroxisome proliferator-activated receptor-γ coactivator-1α, and uncoupling protein-1 levels, and the expression of PR-domain containing 16 in sWAT. Therefore, we concluded that AET-induced sWAT browning was independent of the counterregulatory axis shifting of RAS in HF diet-induced obesity.

Published
2020
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9. Double Imprinted Nanoparticles for Sequential Membrane‐to‐Nuclear Drug Delivery

Author

Pankaj Singla, Thomas Broughton, Mark V. Sullivan, Saweta Garg, Rolando Berlinguer‐Palmini, Priyanka Gupta, Katie J Smith, Ben Gardner, Francesco Canfarotta, Nicholas W. Turner, Eirini Velliou, Shoba Amarnath, and Marloes Peeters

Subjects
biomimetic 3D cancer models, breast cancer, chemotherapy, imprinted nanoparticles, precision nanomedicine, targeted drug delivery, Science
Abstract

Abstract Efficient and site‐specific delivery of therapeutics drugs remains a critical challenge in cancer treatment. Traditional drug nanocarriers such as antibody‐drug conjugates are not generally accessible due to their high cost and can lead to serious side effects including life‐threatening allergic reactions. Here, these problems are overcome via the engineering of supramolecular agents that are manufactured with an innovative double imprinting approach. The developed molecularly imprinted nanoparticles (nanoMIPs) are targeted toward a linear epitope of estrogen receptor alfa (ERα) and loaded with the chemotherapeutic drug doxorubicin. These nanoMIPs are cost‐effective and rival the affinity of commercial antibodies for ERα. Upon specific binding of the materials to ERα, which is overexpressed in most breast cancers (BCs), nuclear drug delivery is achieved via receptor‐mediated endocytosis. Consequentially, significantly enhanced cytotoxicity is elicited in BC cell lines overexpressing ERα, paving the way for precision treatment of BC. Proof‐of‐concept for the clinical use of the nanoMIPs is provided by evaluating their drug efficacy in sophisticated three‐dimensional (3D) cancer models, which capture the complexity of the tumor microenvironment in vivo without requiring animal models. Thus, these findings highlight the potential of nanoMIPs as a promising class of novel drug compounds for use in cancer treatment.

Published
2024
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10. Enalapril and treadmill running reduce adiposity, but only the latter causes adipose tissue browning in mice

Author

Giori, Isabele G., primary, Magliano, D'Angelo C., additional, Alexandre‐Santos, Beatriz, additional, Fernandes, Tiago, additional, Oliveira, Edilamar M., additional, Vieira, Carla P., additional, Conte‐Junior, Carlos A., additional, Ceddia, Rolando B., additional, Nobrega, Antonio C. L., additional, and Frantz, Eliete D. C., additional

Published
2020
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11. Impact of Exercise Training and Enalapril, either alone or in Combination, on White Adipose Tissue Renin‐Angiotensin System in a Diet‐Induced Obesity Model

Author

Antonio Claudio Lucas da Nóbrega, Carlos Adam Conte-Junior, Eliete Dalla Corte Frantz, Fernanda Marques Freitas, Matheus Pereira Machado, Beatriz Alexandre, Mariana Sodré Boêta Andrade, Carla Paulo Vieira, Rolando B. Ceddia, Agatha Cristie Menezes, and Isabele Gomes Giori

Subjects
0301 basic medicine, medicine.medical_specialty, business.industry, White adipose tissue, medicine.disease, Biochemistry, Obesity, 03 medical and health sciences, 030104 developmental biology, Endocrinology, Internal medicine, Renin–angiotensin system, Genetics, medicine, Enalapril, business, Molecular Biology, Biotechnology, medicine.drug
Published
2018
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12. Regulation of Visceral and Subcutaneous Adipocyte Lipolysis by Acute AICAR-induced AMPK Activation

Author

Rolando B. Ceddia, Mandeep Pinky Gaidhu, and Nicole M. Anthony

Subjects
Male, medicine.medical_specialty, Epinephrine, Intra-Abdominal Fat, Lipolysis, Endocrinology, Diabetes and Metabolism, Subcutaneous Fat, Medicine (miscellaneous), AMP-Activated Protein Kinases, chemistry.chemical_compound, Endocrinology, AMP-activated protein kinase, Adipocyte, Internal medicine, Adipocytes, medicine, Animals, Hypoglycemic Agents, Enzyme Inhibitors, Phosphorylation, Rats, Wistar, Protein kinase A, Nutrition and Dietetics, biology, Acetyl-CoA carboxylase, AMPK, Ribonucleotides, Sterol Esterase, Aminoimidazole Carboxamide, Rats, Pyrimidines, chemistry, biology.protein, Pyrazoles, Acetyl-CoA Carboxylase
Abstract

This study investigated the role of adenosine monophosphate-activated protein kinase (AMPK) in the regulation of lipolysis in visceral (VC) and subcutaneous (SC) rat adipocytes and the molecular mechanisms involved in this process. VC (epididymal and retroperitoneal) and SC (inguinal) adipocytes were isolated from male Wistar rats (160-180 g). Adipocytes were incubated either in the absence or in the presence of the AMPK agonist 5-aminoimidazole-4-carboxamide-1-beta-d-ribofuranoside (AICAR, 0-500 micromol/l). AMPK and acetyl-CoA carboxylase (ACC) phosphorylation, basal and epinephrine-stimulated (100 nmol/l) glycerol release, and hormone-sensitive lipase (HSL) phosphorylation and activity were determined. AICAR-induced (500 micromol/l) AMPK activation inhibited basal glycerol release by approximately 42, 41, and 44% in epididymal, retroperitoneal, and inguinal adipocytes, respectively. Epinephrine-stimulated glycerol release was almost completely prevented by AICAR treatment in adipocytes from all fat depots. The AMPK inhibitor compound C (20 micromol/l) prevented AICAR-induced phosphorylation of AMPK and significantly increased basal (approximately 1.3-, 1.4-, and 1.7-fold) and epinephrine-stimulated (approximately 1.3-, 1.2-, 1.4-fold) glycerol release in epididymal, retroperitoneal, and inguinal adipocytes, respectively. AICAR increased phosphorylation of HSL(Ser565) and inhibited epinephrine-induced phosphorylation of HSL(Ser563) and HSL(Ser660). This was also accompanied by a 73% reduction in epinephrine-stimulated HSL activity. Compound C prevented the phosphorylation of HSL(Ser565) induced by AICAR and partially prevented the inhibitory effect of this drug on basal and epinephrine-stimulated lipolysis in adipocytes in VC and SC fat depots. In summary, despite different fat depots eliciting distinct rates of lipolysis, acute AICAR-induced AMPK activation suppressed HSL phosphorylation/activation and exerted similar antilipolytic effects on both VC and SC adipocytes.

Published
2009
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14. Prolonged exposure to palmitate impairs fatty acid oxidation despite activation of AMP-activated protein kinase in skeletal muscle cells

Author

S. Habib, Mandy So, Michael U. Musheev, M. Mirpourian, Rolando B. Ceddia, Aurelio da Silva Pimenta, Sergiu Fediuc, Rui Curi, and Mandeep Pinky Gaidhu

Subjects
medicine.medical_specialty, Time Factors, Carboxy-Lyases, Cell Survival, Physiology, Glucose uptake, Muscle Fibers, Skeletal, Clinical Biochemistry, Palmitic Acid, AMP-Activated Protein Kinases, Protein Serine-Threonine Kinases, Carbohydrate metabolism, Cell Line, AMP-activated protein kinase, Multienzyme Complexes, Internal medicine, medicine, Animals, Insulin, Myocyte, Phosphorylation, Muscle, Skeletal, Glycogen synthase, Beta oxidation, Carnitine O-Palmitoyltransferase, Dose-Response Relationship, Drug, biology, Fatty Acids, Skeletal muscle, Cell Biology, Metabolism, Rats, Enzyme Activation, Glucose, medicine.anatomical_structure, Endocrinology, biology.protein, Oxidation-Reduction, Glycogen, Acetyl-CoA Carboxylase
Abstract

The aim of this study was to investigate the chronic effects of palmitate on fatty acid (FA) oxidation, AMPK/ACC phosphorylation/activation, intracellular lipid accumulation, and the molecular mechanisms involved in these processes in skeletal muscle cells. Exposure of L6 myotubes for 8 h to 200, 400, 600, and 800 microM of palmitate did not affect cell viability but significantly reduced FA oxidation by approximately 26.5%, approximately 43.5%, approximately 50%, and approximately 47%, respectively. Interestingly, this occurred despite significant increases in AMPK ( approximately 2.5-fold) and ACC ( approximately 3-fold) phosphorylation and in malonyl-CoA decarboxylase activity ( approximately 38-60%). Low concentrations of palmitate (50-100 microM) caused an increase ( approximately 30%) in CPT-1 activity. However, as the concentration of palmitate increased, CPT-1 activity decreased by approximately 32% after exposure for 8 h to 800 microM of palmitate. Although FA uptake was reduced ( approximately 35%) in cells exposed to increasing palmitate concentrations, intracellular lipid accumulation increased in a dose-dependent manner, reaching values approximately 2.3-, approximately 3-, and 4-fold higher than control in muscle cells exposed to 400, 600, and 800 microM palmitate, respectively. Interestingly, myotubes exposed to 400 microM of palmitate for 1 h increased basal glucose uptake and glycogen synthesis by approximately 40%. However, as time of incubation in the presence of palmitate progressed from 1 to 8 h, these increases were abolished and a time-dependent inhibition of insulin-stimulated glucose uptake ( approximately 65%) and glycogen synthesis ( approximately 30%) was observed in myotubes. These findings may help explain the dysfunctional adaptations that occur in glucose and FA metabolism in skeletal muscle under conditions of chronically elevated circulating levels of non-esterified FAs, such as in obesity and Type 2 Diabetes.

Published
2008
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15. The database of the PREDICTS (Projecting Responses of Ecological Diversity In Changing Terrestrial Systems) project

Author

Hudson, Lawrence N., Newbold, Tim, Contu, Sara, Hill, Samantha L. L., Lysenko, Igor, De Palma, Adriana, Phillips, Helen R. P., Alhusseini, Tamera I., Bedford, Felicity E., Bennett, Dominic J., Booth, Hollie, Burton, Victoria J., Chng, Charlotte W. T., Choimes, Argyrios, Correia, David L. P., Day, Julie, Echeverria-Londono, Susy, Emerson, Susan R., Gao, Di, Garon, Morgan, Harrison, Michelle L. K., Ingram, Daniel J., Jung, Martin, Kemp, Victoria, Kirkpatrick, Lucinda, Martin, Callum D., Pan, Yuan, Pask-Hale, Gwilym D., Pynegar, Edwin L., Robinson, Alexandra N., Sanchez-Ortiz, Katia, Senior, Rebecca A., Simmons, Benno I., White, Hannah J., Zhang, Hanbin, Aben, Job, Abrahamczyk, Stefan, Adum, Gilbert B., Aguilar-Barquero, Virginia, Aizen, Marcelo A., Albertos, Belen, Alcala, E. L., del Mar Alguacil, Maria, Alignier, Audrey, Ancrenaz, Marc, Andersen, Alan N., Arbelaez-Cortes, Enrique, Armbrecht, Inge, Arroyo-Rodriguez, Victor, Aumann, Tom, Axmacher, Jan C., Azhar, Badrul, Azpiroz, Adrian B., Baeten, Lander, Bakayoko, Adama, Baldi, Andras, Banks, John E., Baral, Sharad K., Barlow, Jos, Barratt, Barbara I. P., Barrico, Lurdes, Bartolommei, Paola, Barton, Diane M., Basset, Yves, Batary, Peter, Bates, Adam J., Baur, Bruno, Bayne, Erin M., Beja, Pedro, Benedick, Suzan, Berg, Ake, Bernard, Henry, Berry, Nicholas J., Bhatt, Dinesh, Bicknell, Jake E., Bihn, Jochen H., Blake, Robin J., Bobo, Kadiri S., Bocon, Roberto, Boekhout, Teun, Bohning-Gaese, Katrin, Bonham, Kevin J., Borges, Paulo A. V., Borges, Sergio H., Boutin, Celine, Bouyer, Jeremy, Bragagnolo, Cibele, Brandt, Jodi S., Brearley, Francis Q., Brito, Isabel, Bros, Vicenc, Brunet, Jorg, Buczkowski, Grzegorz, Buddle, Christopher M., Bugter, Rob, Buscardo, Erika, Buse, Joern, Cabra-Garcia, Jimmy, Caceres, Nilton C., Cagle, Nicolette L., Calvino-Cancela, Maria, Cameron, Sydney A., Cancello, Eliana M., Caparros, Rut, Cardoso, Pedro, Carpenter, Dan, Carrijo, Tiago F., Carvalho, Anelena L., Cassano, Camila R., Castro, Helena, Castro-Luna, Alejandro A., Cerda, Rolando B., Cerezo, Alexis, Chapman, Kim Alan, Chauvat, Matthieu, Christensen, Morten, Clarke, Francis M., Cleary, Daniel F. R., Colombo, Giorgio, Connop, Stuart P., Craig, Michael D., Cruz-Lopez, Leopoldo, Cunningham, Saul A., D'Aniello, Biagio, D'Cruze, Neil, da Silva, Pedro Giovani, Dallimer, Martin, Danquah, Emmanuel, Darvill, Ben, Dauber, Jens, Davis, Adrian L. V., Dawson, Jeff, de Sassi, Claudio, de Thoisy, Benoit, Deheuvels, Olivier, Dejean, Alain, Devineau, Jean-Louis, Diekoetter, Tim, Dolia, Jignasu V., Dominguez, Erwin, Dominguez-Haydar, Yamileth, Dorn, Silvia, Draper, Isabel, Dreber, Niels, Dumont, Bertrand, Dures, Simon G., Dynesius, Mats, Edenius, Lars, Eggleton, Paul, Eigenbrod, Felix, Elek, Zoltan, Entling, Martin H., Esler, Karen J., De Lima, Ricardo F., Faruk, Aisyah, Farwig, Nina, Fayle, Tom M., Felicioli, Antonio, Felton, Annika M., Fensham, Roderick J., Fernandez, Ignacio C., Ferreira, Catarina C., Ficetola, Gentile F., Fiera, Cristina, Filgueiras, Bruno K. C., Firincioglu, Huseyin K., Flaspohler, David, Floren, Andreas, Fonte, Steven J., Fournier, Anne, Fowler, Robert E., Franzen, Markus, Fraser, Lauchlan H., Fredriksson, Gabriella M., Freire-, Geraldo B., Jr., Frizzo, Tiago L. M., Fukuda, Daisuke, Furlani, Dario, Gaigher, Rene, Ganzhorn, Joerg U., Garcia, Karla P., Garcia-R, Juan C., Garden, Jenni G., Garilleti, Ricardo, Ge, Bao-Ming, Gendreau-Berthiaume, Benoit, Gerard, Philippa J., Gheler-Costa, Carla, Gilbert, Benjamin, Giordani, Paolo, Giordano, Simonetta, Golodets, Carly, Gomes, Laurens G. L., Gould, Rachelle K., Goulson, Dave, Gove, Aaron D., Granjon, Laurent, Grass, Ingo, Gray, Claudia L., Grogan, James, Gu, Weibin, Guardiola, Moises, Gunawardene, Nihara R., Gutierrez, Alvaro G., Gutierrez-Lamus, Doris L., Haarmeyer, Daniela H., Hanley, Mick E., Hanson, Thor, Hashim, Nor R., Hassan, Shombe N., Hatfield, Richard G., Hawes, Joseph E., Hayward, Matt W., Hebert, Christian, Helden, Alvin J., Henden, John-Andre, Henschel, Philipp, Hernandez, Lionel, Herrera, James P., Herrmann, Farina, Herzog, Felix, Higuera-Diaz, Diego, Hilje, Branko, Hofer, Hubert, Hoffmann, Anke, Horgan, Finbarr G., Hornung, Elisabeth, Horvath, Roland, Hylander, Kristoffer, Isaacs-Cubides, Paola, Ishida, Hiroaki, Ishitani, Masahiro, Jacobs, Carmen T., Jaramillo, Victor J., Jauker, Birgit, Jimenez Hernandez, F., Johnson, McKenzie F., Jolli, Virat, Jonsell, Mats, Juliani, S. Nur, Jung, Thomas S., Kapoor, Vena, Kappes, Heike, Kati, Vassiliki, Katovai, Eric, Kellner, Klaus, Kessler, Michael, Kirby, Kathryn R., Kittle, Andrew M., Knight, Mairi E., Knop, Eva, Kohler, Florian, Koivula, Matti, Kolb, Annette, Kone, Mouhamadou, Koroesi, Adam, Krauss, Jochen, Kumar, Ajith, Kumar, Raman, Kurz, David J., Kutt, Alex S., Lachat, Thibault, Lantschner, Victoria, Lara, Francisco, Lasky, Jesse R., Latta, Steven C., Laurance, William F., Lavelle, Patrick, Le Feon, Violette, LeBuhn, Gretchen, Legare, Jean-Philippe, Lehouck, Valerie, Lencinas, Maria V., Lentini, Pia E., Letcher, Susan G., Li, Qi, Litchwark, Simon A., Littlewood, Nick A., Liu, Yunhui, Lo-Man-Hung, Nancy, Lopez-Quintero, Carlos A., Louhaichi, Mounir, Lovei, Gabor L., Lucas-Borja, Manuel Esteban, Luja, Victor H., Luskin, Matthew S., MacSwiney G, M. Cristina, Maeto, Kaoru, Magura, Tibor, Mallari, Neil Aldrin, Malone, Louise A., Malonza, Patrick K., Malumbres-Olarte, Jagoba, Mandujano, Salvador, Maren, Inger E., Marin-Spiotta, Erika, Marsh, Charles J., Marshall, E. J. P., Martinez, Eliana, Pastur, Guillermo Martinez, Mateos, David Moreno, Mayfield, Margaret M., Mazimpaka, Vicente, McCarthy, Jennifer L., McCarthy, Kyle P., McFrederick, Quinn S., McNamara, Sean, Medina, Nagore G., Medina, Rafael, Mena, Jose L., Mico, Estefania, Mikusinski, Grzegorz, Milder, Jeffrey C., Miller, James R., Miranda-Esquivel, Daniel R., Moir, Melinda L., Morales, Carolina L., Muchane, Mary N., Muchane, Muchai, Mudri-Stojnic, Sonja, Munira, A. Nur, Muonz-Alonso, Antonio, Munyekenye, B. F., Naidoo, Robin, Naithani, A., Nakagawa, Michiko, Nakamura, Akihiro, Nakashima, Yoshihiro, Naoe, Shoji, Nates-Parra, Guiomar, Gutierrez, Dario A. Navarrete, Navarro-Iriarte, Luis, Ndang'ang'a, Paul K., Neuschulz, Eike L., Ngai, Jacqueline T., Nicolas, Violaine, Nilsson, Sven G., Noreika, Norbertas, Norfolk, Olivia, Noriega, Jorge Ari, Norton, David A., Noeske, Nicole M., Nowakowski, A. Justin, Numa, Catherine, O'Dea, Niall, O'Farrell, Patrick J., Oduro, William, Oertli, Sabine, Ofori-Boateng, Caleb, Oke, Christopher Omamoke, Oostra, Vicencio, Osgathorpe, Lynne M., Eduardo Otavo, Samuel, Page, Navendu V., Paritsis, Juan, Parra-H, Alejandro, Parry, Luke, Pe'er, Guy, Pearman, Peter B., Pelegrin, Nicolas, Pelissier, Raphael, Peres, Carlos A., Peri, Pablo L., Persson, Anna S., Petanidou, Theodora, Peters, Marcell K., Pethiyagoda, Rohan S., Phalan, Ben, Philips, T. Keith, Pillsbury, Finn C., Pincheira-Ulbrich, Jimmy, Pineda, Eduardo, Pino, Joan, Pizarro-Araya, Jaime, Plumptre, A. J., Poggio, Santiago L., Politi, Natalia, Pons, Pere, Poveda, Katja, Power, Eileen F., Presley, Steven J., Proenca, Vania, Quaranta, Marino, Quintero, Carolina, Rader, Romina, Ramesh, B. R., Ramirez-Pinilla, Martha P., Ranganathan, Jai, Rasmussen, Claus, Redpath-Downing, Nicola A., Reid, J. Leighton, Reis, Yana T., Rey Benayas, Jose M., Carlos Rey-Velasco, Juan, Reynolds, Chevonne, Ribeiro, Danilo Bandini, Richards, Miriam H., Richardson, Barbara A., Richardson, Michael J., Macip Rios, Rodrigo, Robinson, Richard, Robles, Carolina A., Roembke, Joerg, Romero-Duque, Luz Piedad, Ros, Matthias, Rosselli, Loreta, Rossiter, Stephen J., Roth, Dana S., Roulston, T'ai H., Rousseau, Laurent, Rubio, Andre V., Ruel, Jean-Claude, Sadler, Jonathan P., Safian, Szabolcs, Saldana-Vazquez, Romeo A., Sam, Katerina, Samnegard, Ulrika, Santana, Joana, Santos, Xavier, Savage, Jade, Schellhorn, Nancy A., Schilthuizen, Menno, Schmiedel, Ute, Schmitt, Christine B., Schon, Nicole L., Schuepp, Christof, Schumann, Katharina, Schweiger, Oliver, Scott, Dawn M., Scott, Kenneth A., Sedlock, Jodi L., Seefeldt, Steven S., Shahabuddin, Ghazala, Shannon, Graeme, Sheil, Douglas, Sheldon, Frederick H., Shochat, Eyal, Siebert, Stefan J., Silva, Fernando A. B., Simonetti, Javier A., Slade, Eleanor M., Smith, Jo, Smith-Pardo, Allan H., Sodhi, Navjot S., Somarriba, Eduardo J., Sosa, Ramon A., Soto Quiroga, Grimaldo, St-Laurent, Martin-Hugues, Starzomski, Brian M., Stefanescu, Constanti, Steffan-Dewenter, Ingolf, Stouffer, Philip C., Stout, Jane C., Strauch, Ayron M., Struebig, Matthew J., Su, Zhimin, Suarez-Rubio, Marcela, Sugiura, Shinji, Summerville, Keith S., Sung, Yik-Hei, Sutrisno, Hari, Svenning, Jens-Christian, Teder, Tiit, Threlfall, Caragh G., Tiitsaar, Anu, Todd, Jacqui H., Tonietto, Rebecca K., Torre, Ignasi, Tothmeresz, Bela, Tscharntke, Teja, Turner, Edgar C., Tylianakis, Jason M., Uehara-Prado, Marcio, Urbina-Cardona, Nicolas, Vallan, Denis, Vanbergen, Adam J., Vasconcelos, Heraldo L., Vassilev, Kiril, Verboven, Hans A. F., Verdasca, Maria Joao, Verdu, Jose R., Vergara, Carlos H., Vergara, Pablo M., Verhulst, Jort, Virgilio, Massimiliano, Van Vu, Lien, Waite, Edward M., Walker, Tony R., Wang, Hua-Feng, Wang, Yanping, Watling, James I., Weller, Britta, Wells, Konstans, Westphal, Catrin, Wiafe, Edward D., Williams, Christopher D., Willig, Michael R., Woinarski, John C. Z., Wolf, Jan H. D., Wolters, Volkmar, Woodcock, Ben A., Wu, Jihua, Wunderle, Joseph M., Jr., Yamaura, Yuichi, Yoshikura, Satoko, Yu, Douglas W., Zaitsev, Andrey S., Zeidler, Juliane, Zou, Fasheng, Collen, Ben, Ewers, Rob M., Mace, Georgina M., Purves, Drew W., Scharlemann, Joern P. W., Purvis, Andy, Hudson, Lawrence N., Newbold, Tim, Contu, Sara, Hill, Samantha L. L., Lysenko, Igor, De Palma, Adriana, Phillips, Helen R. P., Alhusseini, Tamera I., Bedford, Felicity E., Bennett, Dominic J., Booth, Hollie, Burton, Victoria J., Chng, Charlotte W. T., Choimes, Argyrios, Correia, David L. P., Day, Julie, Echeverria-Londono, Susy, Emerson, Susan R., Gao, Di, Garon, Morgan, Harrison, Michelle L. K., Ingram, Daniel J., Jung, Martin, Kemp, Victoria, Kirkpatrick, Lucinda, Martin, Callum D., Pan, Yuan, Pask-Hale, Gwilym D., Pynegar, Edwin L., Robinson, Alexandra N., Sanchez-Ortiz, Katia, Senior, Rebecca A., Simmons, Benno I., White, Hannah J., Zhang, Hanbin, Aben, Job, Abrahamczyk, Stefan, Adum, Gilbert B., Aguilar-Barquero, Virginia, Aizen, Marcelo A., Albertos, Belen, Alcala, E. L., del Mar Alguacil, Maria, Alignier, Audrey, Ancrenaz, Marc, Andersen, Alan N., Arbelaez-Cortes, Enrique, Armbrecht, Inge, Arroyo-Rodriguez, Victor, Aumann, Tom, Axmacher, Jan C., Azhar, Badrul, Azpiroz, Adrian B., Baeten, Lander, Bakayoko, Adama, Baldi, Andras, Banks, John E., Baral, Sharad K., Barlow, Jos, Barratt, Barbara I. P., Barrico, Lurdes, Bartolommei, Paola, Barton, Diane M., Basset, Yves, Batary, Peter, Bates, Adam J., Baur, Bruno, Bayne, Erin M., Beja, Pedro, Benedick, Suzan, Berg, Ake, Bernard, Henry, Berry, Nicholas J., Bhatt, Dinesh, Bicknell, Jake E., Bihn, Jochen H., Blake, Robin J., Bobo, Kadiri S., Bocon, Roberto, Boekhout, Teun, Bohning-Gaese, Katrin, Bonham, Kevin J., Borges, Paulo A. V., Borges, Sergio H., Boutin, Celine, Bouyer, Jeremy, Bragagnolo, Cibele, Brandt, Jodi S., Brearley, Francis Q., Brito, Isabel, Bros, Vicenc, Brunet, Jorg, Buczkowski, Grzegorz, Buddle, Christopher M., Bugter, Rob, Buscardo, Erika, Buse, Joern, Cabra-Garcia, Jimmy, Caceres, Nilton C., Cagle, Nicolette L., Calvino-Cancela, Maria, Cameron, Sydney A., Cancello, Eliana M., Caparros, Rut, Cardoso, Pedro, Carpenter, Dan, Carrijo, Tiago F., Carvalho, Anelena L., Cassano, Camila R., Castro, Helena, Castro-Luna, Alejandro A., Cerda, Rolando B., Cerezo, Alexis, Chapman, Kim Alan, Chauvat, Matthieu, Christensen, Morten, Clarke, Francis M., Cleary, Daniel F. R., Colombo, Giorgio, Connop, Stuart P., Craig, Michael D., Cruz-Lopez, Leopoldo, Cunningham, Saul A., D'Aniello, Biagio, D'Cruze, Neil, da Silva, Pedro Giovani, Dallimer, Martin, Danquah, Emmanuel, Darvill, Ben, Dauber, Jens, Davis, Adrian L. V., Dawson, Jeff, de Sassi, Claudio, de Thoisy, Benoit, Deheuvels, Olivier, Dejean, Alain, Devineau, Jean-Louis, Diekoetter, Tim, Dolia, Jignasu V., Dominguez, Erwin, Dominguez-Haydar, Yamileth, Dorn, Silvia, Draper, Isabel, Dreber, Niels, Dumont, Bertrand, Dures, Simon G., Dynesius, Mats, Edenius, Lars, Eggleton, Paul, Eigenbrod, Felix, Elek, Zoltan, Entling, Martin H., Esler, Karen J., De Lima, Ricardo F., Faruk, Aisyah, Farwig, Nina, Fayle, Tom M., Felicioli, Antonio, Felton, Annika M., Fensham, Roderick J., Fernandez, Ignacio C., Ferreira, Catarina C., Ficetola, Gentile F., Fiera, Cristina, Filgueiras, Bruno K. C., Firincioglu, Huseyin K., Flaspohler, David, Floren, Andreas, Fonte, Steven J., Fournier, Anne, Fowler, Robert E., Franzen, Markus, Fraser, Lauchlan H., Fredriksson, Gabriella M., Freire-, Geraldo B., Jr., Frizzo, Tiago L. M., Fukuda, Daisuke, Furlani, Dario, Gaigher, Rene, Ganzhorn, Joerg U., Garcia, Karla P., Garcia-R, Juan C., Garden, Jenni G., Garilleti, Ricardo, Ge, Bao-Ming, Gendreau-Berthiaume, Benoit, Gerard, Philippa J., Gheler-Costa, Carla, Gilbert, Benjamin, Giordani, Paolo, Giordano, Simonetta, Golodets, Carly, Gomes, Laurens G. L., Gould, Rachelle K., Goulson, Dave, Gove, Aaron D., Granjon, Laurent, Grass, Ingo, Gray, Claudia L., Grogan, James, Gu, Weibin, Guardiola, Moises, Gunawardene, Nihara R., Gutierrez, Alvaro G., Gutierrez-Lamus, Doris L., Haarmeyer, Daniela H., Hanley, Mick E., Hanson, Thor, Hashim, Nor R., Hassan, Shombe N., Hatfield, Richard G., Hawes, Joseph E., Hayward, Matt W., Hebert, Christian, Helden, Alvin J., Henden, John-Andre, Henschel, Philipp, Hernandez, Lionel, Herrera, James P., Herrmann, Farina, Herzog, Felix, Higuera-Diaz, Diego, Hilje, Branko, Hofer, Hubert, Hoffmann, Anke, Horgan, Finbarr G., Hornung, Elisabeth, Horvath, Roland, Hylander, Kristoffer, Isaacs-Cubides, Paola, Ishida, Hiroaki, Ishitani, Masahiro, Jacobs, Carmen T., Jaramillo, Victor J., Jauker, Birgit, Jimenez Hernandez, F., Johnson, McKenzie F., Jolli, Virat, Jonsell, Mats, Juliani, S. Nur, Jung, Thomas S., Kapoor, Vena, Kappes, Heike, Kati, Vassiliki, Katovai, Eric, Kellner, Klaus, Kessler, Michael, Kirby, Kathryn R., Kittle, Andrew M., Knight, Mairi E., Knop, Eva, Kohler, Florian, Koivula, Matti, Kolb, Annette, Kone, Mouhamadou, Koroesi, Adam, Krauss, Jochen, Kumar, Ajith, Kumar, Raman, Kurz, David J., Kutt, Alex S., Lachat, Thibault, Lantschner, Victoria, Lara, Francisco, Lasky, Jesse R., Latta, Steven C., Laurance, William F., Lavelle, Patrick, Le Feon, Violette, LeBuhn, Gretchen, Legare, Jean-Philippe, Lehouck, Valerie, Lencinas, Maria V., Lentini, Pia E., Letcher, Susan G., Li, Qi, Litchwark, Simon A., Littlewood, Nick A., Liu, Yunhui, Lo-Man-Hung, Nancy, Lopez-Quintero, Carlos A., Louhaichi, Mounir, Lovei, Gabor L., Lucas-Borja, Manuel Esteban, Luja, Victor H., Luskin, Matthew S., MacSwiney G, M. Cristina, Maeto, Kaoru, Magura, Tibor, Mallari, Neil Aldrin, Malone, Louise A., Malonza, Patrick K., Malumbres-Olarte, Jagoba, Mandujano, Salvador, Maren, Inger E., Marin-Spiotta, Erika, Marsh, Charles J., Marshall, E. J. P., Martinez, Eliana, Pastur, Guillermo Martinez, Mateos, David Moreno, Mayfield, Margaret M., Mazimpaka, Vicente, McCarthy, Jennifer L., McCarthy, Kyle P., McFrederick, Quinn S., McNamara, Sean, Medina, Nagore G., Medina, Rafael, Mena, Jose L., Mico, Estefania, Mikusinski, Grzegorz, Milder, Jeffrey C., Miller, James R., Miranda-Esquivel, Daniel R., Moir, Melinda L., Morales, Carolina L., Muchane, Mary N., Muchane, Muchai, Mudri-Stojnic, Sonja, Munira, A. Nur, Muonz-Alonso, Antonio, Munyekenye, B. F., Naidoo, Robin, Naithani, A., Nakagawa, Michiko, Nakamura, Akihiro, Nakashima, Yoshihiro, Naoe, Shoji, Nates-Parra, Guiomar, Gutierrez, Dario A. Navarrete, Navarro-Iriarte, Luis, Ndang'ang'a, Paul K., Neuschulz, Eike L., Ngai, Jacqueline T., Nicolas, Violaine, Nilsson, Sven G., Noreika, Norbertas, Norfolk, Olivia, Noriega, Jorge Ari, Norton, David A., Noeske, Nicole M., Nowakowski, A. Justin, Numa, Catherine, O'Dea, Niall, O'Farrell, Patrick J., Oduro, William, Oertli, Sabine, Ofori-Boateng, Caleb, Oke, Christopher Omamoke, Oostra, Vicencio, Osgathorpe, Lynne M., Eduardo Otavo, Samuel, Page, Navendu V., Paritsis, Juan, Parra-H, Alejandro, Parry, Luke, Pe'er, Guy, Pearman, Peter B., Pelegrin, Nicolas, Pelissier, Raphael, Peres, Carlos A., Peri, Pablo L., Persson, Anna S., Petanidou, Theodora, Peters, Marcell K., Pethiyagoda, Rohan S., Phalan, Ben, Philips, T. Keith, Pillsbury, Finn C., Pincheira-Ulbrich, Jimmy, Pineda, Eduardo, Pino, Joan, Pizarro-Araya, Jaime, Plumptre, A. J., Poggio, Santiago L., Politi, Natalia, Pons, Pere, Poveda, Katja, Power, Eileen F., Presley, Steven J., Proenca, Vania, Quaranta, Marino, Quintero, Carolina, Rader, Romina, Ramesh, B. R., Ramirez-Pinilla, Martha P., Ranganathan, Jai, Rasmussen, Claus, Redpath-Downing, Nicola A., Reid, J. Leighton, Reis, Yana T., Rey Benayas, Jose M., Carlos Rey-Velasco, Juan, Reynolds, Chevonne, Ribeiro, Danilo Bandini, Richards, Miriam H., Richardson, Barbara A., Richardson, Michael J., Macip Rios, Rodrigo, Robinson, Richard, Robles, Carolina A., Roembke, Joerg, Romero-Duque, Luz Piedad, Ros, Matthias, Rosselli, Loreta, Rossiter, Stephen J., Roth, Dana S., Roulston, T'ai H., Rousseau, Laurent, Rubio, Andre V., Ruel, Jean-Claude, Sadler, Jonathan P., Safian, Szabolcs, Saldana-Vazquez, Romeo A., Sam, Katerina, Samnegard, Ulrika, Santana, Joana, Santos, Xavier, Savage, Jade, Schellhorn, Nancy A., Schilthuizen, Menno, Schmiedel, Ute, Schmitt, Christine B., Schon, Nicole L., Schuepp, Christof, Schumann, Katharina, Schweiger, Oliver, Scott, Dawn M., Scott, Kenneth A., Sedlock, Jodi L., Seefeldt, Steven S., Shahabuddin, Ghazala, Shannon, Graeme, Sheil, Douglas, Sheldon, Frederick H., Shochat, Eyal, Siebert, Stefan J., Silva, Fernando A. B., Simonetti, Javier A., Slade, Eleanor M., Smith, Jo, Smith-Pardo, Allan H., Sodhi, Navjot S., Somarriba, Eduardo J., Sosa, Ramon A., Soto Quiroga, Grimaldo, St-Laurent, Martin-Hugues, Starzomski, Brian M., Stefanescu, Constanti, Steffan-Dewenter, Ingolf, Stouffer, Philip C., Stout, Jane C., Strauch, Ayron M., Struebig, Matthew J., Su, Zhimin, Suarez-Rubio, Marcela, Sugiura, Shinji, Summerville, Keith S., Sung, Yik-Hei, Sutrisno, Hari, Svenning, Jens-Christian, Teder, Tiit, Threlfall, Caragh G., Tiitsaar, Anu, Todd, Jacqui H., Tonietto, Rebecca K., Torre, Ignasi, Tothmeresz, Bela, Tscharntke, Teja, Turner, Edgar C., Tylianakis, Jason M., Uehara-Prado, Marcio, Urbina-Cardona, Nicolas, Vallan, Denis, Vanbergen, Adam J., Vasconcelos, Heraldo L., Vassilev, Kiril, Verboven, Hans A. F., Verdasca, Maria Joao, Verdu, Jose R., Vergara, Carlos H., Vergara, Pablo M., Verhulst, Jort, Virgilio, Massimiliano, Van Vu, Lien, Waite, Edward M., Walker, Tony R., Wang, Hua-Feng, Wang, Yanping, Watling, James I., Weller, Britta, Wells, Konstans, Westphal, Catrin, Wiafe, Edward D., Williams, Christopher D., Willig, Michael R., Woinarski, John C. Z., Wolf, Jan H. D., Wolters, Volkmar, Woodcock, Ben A., Wu, Jihua, Wunderle, Joseph M., Jr., Yamaura, Yuichi, Yoshikura, Satoko, Yu, Douglas W., Zaitsev, Andrey S., Zeidler, Juliane, Zou, Fasheng, Collen, Ben, Ewers, Rob M., Mace, Georgina M., Purves, Drew W., Scharlemann, Joern P. W., and Purvis, Andy

Abstract

The PREDICTS project-Projecting Responses of Ecological Diversity In Changing Terrestrial Systems (www.predicts.org.uk)-has collated from published studies a large, reasonably representative database of comparable samples of biodiversity from multiple sites that differ in the nature or intensity of human impacts relating to land use. We have used this evidence base to develop global and regional statistical models of how local biodiversity responds to these measures. We describe and make freely available this 2016 release of the database, containing more than 3.2 million records sampled at over 26,000 locations and representing over 47,000 species. We outline how the database can help in answering a range of questions in ecology and conservation biology. To our knowledge, this is the largest and most geographically and taxonomically representative database of spatial comparisons of biodiversity that has been collated to date; it will be useful to researchers and international efforts wishing to model and understand the global status of biodiversity.

Published
2017

16. Insulin reduces apoptosis and increases DNA synthesis and cell size via distinct signalling pathways in Drosophila Kc cells

Author

G. Bikopoulos, A. J. Hilliker, Gary Sweeney, and Rolando B. Ceddia

Subjects
Cell division, medicine.medical_treatment, Apoptosis, Wortmannin, Phosphatidylinositol 3-Kinases, chemistry.chemical_compound, medicine, Animals, Insulin, Cells, Cultured, Cell Size, biology, Cell growth, Kinase, DNA, Original Articles, Cell Biology, General Medicine, Molecular biology, Cell biology, Androstadienes, Insulin receptor, Bromodeoxyuridine, chemistry, Caspases, biology.protein, Drosophila, Mitogen-Activated Protein Kinases, Signal transduction, Cell Division, Signal Transduction
Abstract

During development of Drosophila, cell proliferation and size are known to be regulated by insulin. Here we use Drosophila Kc cells to examine the molecular basis for the control of cell growth by insulin. Growing cells in the presence of insulin increased cell number above control levels at 16, 24, 48 and 72 h. We have demonstrated a novel anti-apoptotic effect of insulin (approximately 50%) in these cells, measured by caspase 3-like activity, which contributed to the increase in cell number. The anti-apoptotic effect was observed both in control cells and those in which apoptosis was induced by ultraviolet irradiation. An approximately 2-fold stimulation of bromodeoxyuridine incorporation demonstrated that insulin also increased Kc cell proliferation by stimulating new DNA synthesis. The ability of insulin to increase cell number, stimulate bromodeoxyuridine incorporation and reduce caspase 3-like activity was prevented by PD98059, which inhibits activation of the Drosophila extracellular signal regulated kinase (DERK) pathway, and was unaffected by wortmannin, an inhibitor of Drosophila phosphatidylinositol 3-kinase (DPI3K). Insulin also increased cell size approximately 2-fold and this was prevented by wortmannin and rapamycin, an inhibitor of Drosphilia target of rapamycin (DTOR). In summary, we show that DERK plays an important role in mediating the effect of insulin to reduce apoptosis and increase DNA synthesis whereas the DPI3K/DTOR/Dp70S6 kinase pathway mediates effects of insulin on cell size in Drosophila Kc cells.

Published
2004
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17. Creatine supplementation increases glucose oxidation and AMPK phosphorylation and reduces lactate production in L6 rat skeletal muscle cells

Author

Rolando B. Ceddia and Gary Sweeney

Subjects
medicine.medical_specialty, Basal rate, biology, Glycogen, Physiology, Glucose uptake, Glucose transporter, Creatine, Phosphocreatine, chemistry.chemical_compound, Endocrinology, chemistry, Internal medicine, medicine, biology.protein, Glycogen synthase, GLUT4
Abstract

Recent observations have suggested that creatine supplementation might have a beneficial effect on glucoregulation in skeletal muscle. However, conclusive studies on the direct effects of creatine on glucose uptake and metabolism are lacking. The objective of this study was to investigate the effects of creatine supplementation on basal and insulin-stimulated glucose transporter (GLUT4) translocation, glucose uptake, glycogen content, glycogen synthesis, lactate production, glucose oxidation and AMP-activated protein kinase (AMPK) phosphorylation in L6 rat skeletal muscle cells. Four treatment groups were studied: control, insulin (100 nM), creatine (0.5 mM) and creatine + insulin. After 48 h of creatine supplementation the creatine and phosphocreatine contents of L6 myoblasts increased by approximately 9.3- and approximately 5.1-fold, respectively, but the ATP content of the cells was not affected. Insulin significantly increased 2-deoxyglucose uptake ( approximately 1.9-fold), GLUT4 translocation ( approximately 1.8-fold), the incorporation of D-[U-(14)C]glucose into glycogen ( approximately 2.3-fold), lactate production ( approximately 1.5-fold) and (14)CO(2) production ( approximately 1.5-fold). Creatine neither altered the glycogen and GLUT4 contents of the cells nor the insulin-stimulated rates of 2-DG uptake, GLUT4 translocation, glycogen synthesis and glucose oxidation. However, creatine significantly reduced by approximately 42% the basal rate of lactate production and increased by approximately 40% the basal rate of (14)CO(2) production. This is in agreement with the approximately 35% increase in citrate synthase activity and also with the approximately 2-fold increase in the phosphorylation of both alpha-1 and alpha-2 isoforms of AMPK after creatine supplementation. We conclude that 48 h of creatine supplementation does not alter insulin-stimulated glucose uptake and glucose metabolism; however, it activates AMPK, shifts basal glucose metabolism towards oxidation and reduces lactate production in L6 rat skeletal muscle cells.

Published
2004
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18. Insulin stimulates glucose metabolism via the pentose phosphate pathway inDrosophilaKc cells

Author

Gary Sweeney, George J. Bikopoulos, Rolando B. Ceddia, and Arthur J. Hilliker

Subjects
medicine.medical_treatment, Glucose uptake, Biophysics, Deoxyglucose, Carbohydrate metabolism, Pentose phosphate pathway, Tritium, Biochemistry, Cell Line, Pentose Phosphate Pathway, Cell growth, Structural Biology, Genetics, medicine, Animals, Insulin, Carbon Radioisotopes, Lactic Acid, Molecular Biology, Glucose metabolism, biology, Cell Biology, Metabolism, Carbon Dioxide, Citric acid cycle, Insulin receptor, 6-Aminonicotinamide, Drosophila melanogaster, Glucose, biology.protein, Drosophila, Glycogen, Intracellular
Abstract

Drosophila melanogaster has become a prominent and convenient model for analysis of insulin action. However, to date very little is known regarding the effect of insulin on glucose uptake and metabolism in Drosophila. Here we show that, in contrast to effects seen in mammals, insulin did not alter [(3)H]2-deoxyglucose uptake and in fact decreased glycogen synthesis ( approximately 30%) in embryonic Drosophila Kc cells. Insulin significantly increased ( approximately 1.5-fold) the production of (14)CO(2) from D-[1-(14)C]glucose while the production of (14)CO(2) from D-[6-(14)C]glucose was not altered. Thus, insulin-stimulated glucose oxidation did not occur via increasing Krebs cycle activity but rather by stimulating the pentose phosphate pathway. Indeed, inhibition of the oxidative pentose phosphate pathway by 6-aminonicotinamide abolished the effect of insulin on (14)CO(2) from D-[U-(14)C]glucose. A corresponding increase in lactate production but no change in incorporation of D-[U-(14)C]glucose into total lipids was observed in response to insulin. Glucose metabolism via the pentose phosphate pathway may provide an important source of 5'-phosphate for DNA synthesis and cell replication. This novel observation correlates well with the fact that control of growth and development is the major role of insulin-like peptides in Drosophila. Thus, although intracellular signaling is well conserved, the metabolic effects of insulin are dramatically different between Drosophila and mammals.

Published
2003
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19. Cold acclimation reduces hepatic protein Kinase B and AMP-activated protein kinase phosphorylation and increases gluconeogenesis in Rats

Author

Diane M Sepa-Kishi, George Bikopoulos, Glen Katsnelson, Rolando B. Ceddia, and Ayesha Iqbal

Subjects
Male, AMPK, 0301 basic medicine, medicine.medical_specialty, Physiology, Acclimatization, Thermoregulation, Signalling Pathways, Glycogen Synthase Kinase 3, 03 medical and health sciences, chemistry.chemical_compound, AMP-Activated Protein Kinase Kinases, AMP-activated protein kinase, GSK-3, Physiology (medical), Internal medicine, Metabolism and Regulation, PGC‐1α, medicine, Cold acclimation, Animals, Phosphorylation, Rats, Wistar, Glycogen synthase, Protein kinase A, HNF4α, Protein kinase B, fatty acid oxidation, Original Research, biology, Glycogen, Gluconeogenesis, Receptor, Insulin, Rats, Cold Temperature, Insulin receptor, Glycogen Synthase, 030104 developmental biology, Endocrinology, Liver, chemistry, glycogen, biology.protein, Fatty Acid Synthases, Protein Kinases, Protein Processing, Post-Translational, Proto-Oncogene Proteins c-akt, Acetyl-CoA Carboxylase
Abstract

This study investigated the molecular and metabolic responses of the liver to cold‐induced thermogenesis. To accomplish that, male Wistar rats were exposed to cold (4°C) for 7 days. Livers were then extracted and used for the determination of glucose and fatty acid oxidation, glycogen content, the expression and content of proteins involved in insulin signaling, as well as in the regulation of gluconeogenesis and de novo lipid synthesis. Despite being hyperphagic, cold‐acclimated rats displayed normoglycemia with reduced insulinemia, which suggests improved whole‐body insulin sensitivity. However, liver protein kinase B (AKT) and glycogen synthase kinase 3 (GSK3) phosphorylations were markedly reduced along with the expressions of the insulin receptor (IR) and its substrates IRS1 and IRS2, whereas glycogen synthase (GS) phosphorylation increased. Thus, major signaling steps of the glycogen synthesis pathway in the liver were inhibited. Furthermore, glucagonemia and hepatic glucose and fatty acid oxidation were increased, whereas liver glycogen content was reduced by cold acclimation. This was accompanied by significantly elevated expressions of the gluconeogenic transcription regulators CRTC2, PGC‐1α, and FoxO1, as well as of major gluconeogenic enzymes (G6Pase, FBP1, and PEPCK). Conversely, phosphorylation and contents of AMP‐activated protein kinase (AMPK) and acetyl‐CoA carboxylase (ACC) and fatty acid synthase (FAS) content were markedly downregulated in livers of cold‐acclimated rats. In conclusion, cold acclimation suppressed hepatic glycogen synthesis and promoted profound metabolic changes in the liver so the organ could sustain its ability to regulate whole‐body glucose and lipid metabolism under conditions of high‐energy demand in thermogenic tissues.

Published
2018
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20. Rice ENOD40: isolation and expression analysis in rice and transgenic soybean root nodules

Author

Pallavolu M. Reddy, Kenichi Takane, Rolando B. So, Hiroshi Kouchi, and Jagdish K. Ladha

Subjects
DNA, Complementary, RNA, Untranslated, Root nodule, Molecular Sequence Data, Organogenesis, Plant Science, Oryza, Plant Roots, Botany, Genetics, Amino Acid Sequence, RNA, Messenger, Promoter Regions, Genetic, Plant Proteins, Oryza brachyantha, Oryza sativa, Base Sequence, Sequence Homology, Amino Acid, biology, ENOD40, food and beverages, Cell Biology, Plants, Genetically Modified, biology.organism_classification, Vascular bundle, Plant protein, RNA, Long Noncoding, Soybeans
Abstract

The early nodulin ENOD40 has been proposed as playing a pivotal role in the organogenesis of legume root nodules. We have isolated the ENOD40 gene homologues ObENOD40 and OsENOD40 from the wild and cultivated rice genotypes Oryza brachyantha and Oryza sativa, respectively. Rice ENOD40s contain a sequence at the 5' end (region I) for encoding an oligopeptide that is highly conserved in all legume ENOD40s. Furthermore, at the 3' end (region II), the nucleotide sequence of rice ENOD40s exhibited a considerable homology to the corresponding region in legume ENOD40s. Among various organs of the rice plant, expression of OsENOD40 was detected only in stems. In situ hybridization studies revealed that, within the stem, transcription of OsENOD40 is confined to parenchyma cells surrounding the protoxylem during the early stages of development of lateral vascular bundles that conjoin an emerging leaf. Expression pattern of OsENOD40 promoter-GUS fusion in nodules developed on transgenic hairy roots of soybean was also found to be restricted to peripheral cells of nodule vascular bundles, thus evidencing that rice ENOD40 promoter activity is essentially the same as that of soybean ENOD40. Taken together, these results strongly suggest that OsENOD40 and legume ENOD40s share common, if not identical, functions in differentiation and/or function of vascular bundles.

Published
1999
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21. Maintenance of contractile properties despite impaired skeletal muscle oxidative metabolism in diet‐induced obesity

Author

Thomas J. Hawke, Matthew P. Krause, Dili Dhanani, Karin E Shortreed, Rolando B. Ceddia, and Julianna H Huang

Subjects
medicine.medical_specialty, Oxidative metabolism, business.industry, Skeletal muscle, medicine.disease, Biochemistry, Obesity, Endocrinology, medicine.anatomical_structure, Internal medicine, Genetics, Medicine, business, Molecular Biology, Biotechnology
Published
2009
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24. The Anti‐Lipolytic Effects of Acute AICAR‐Induced AMPK Activation in Visceral and Subcutaneous Rat Adipose Tissue is Independent of HSL Phosphorylation on Serine 563 and 660 Residues

Author

Mandeep Pinky Gaidhu, Nicole M. Anthony, and Rolando B. Ceddia

Subjects
Serine, medicine.medical_specialty, Endocrinology, Chemistry, Internal medicine, Genetics, medicine, Adipose tissue, AMPK, Phosphorylation, Molecular Biology, Biochemistry, Biotechnology
Published
2008
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35. Thermochemical Equilibrium Model of Synthetic Natural Gas Production from Coal Gasification Using Aspen Plus

Author

Rolando Barrera, Carlos Salazar, and Juan F. Pérez

Subjects
Chemical engineering, TP155-156
Abstract

The production of synthetic or substitute natural gas (SNG) from coal is a process of interest in Colombia where the reserves-to-production ratio (R/P) for natural gas is expected to be between 7 and 10 years, while the R/P for coal is forecasted to be around 90 years. In this work, the process to produce SNG by means of coal-entrained flow gasifiers is modeled under thermochemical equilibrium with the Gibbs free energy approach. The model was developed using a complete and comprehensive Aspen Plus model. Two typical technologies used in entrained flow gasifiers such as coal dry and coal slurry are modeled and simulated. Emphasis is put on interactions between the fuel feeding technology and selected energy output parameters of coal-SNG process, that is, energy efficiencies, power, and SNG quality. It was found that coal rank does not significantly affect energy indicators such as cold gas, process, and global efficiencies. However, feeding technology clearly has an effect on the process due to the gasifying agent. Simulations results are compared against available technical data with good accuracy. Thus, the proposed model is considered as a versatile and useful computational tool to study and optimize the coal to SNG process.

Published
2014
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36. NO-donor melatonin derivatives: synthesis and in vitro pharmacological characterization.

Author

Chegaev K, Lazzarato L, Rolando B, Marini E, Tosco P, Cena C, Fruttero R, Bertolini F, Reist M, Carrupt PA, Lucini V, Fraschini F, and Gasco A

Subjects
Alkaline Phosphatase metabolism, Animals, Antioxidants chemical synthesis, Antioxidants chemistry, Antioxidants pharmacology, Humans, In Vitro Techniques, Lipid Peroxidation drug effects, Male, Melatonin chemical synthesis, Melatonin pharmacology, Microsomes, Liver drug effects, Microsomes, Liver metabolism, Molecular Structure, Nitric Oxide Donors chemistry, Rats, Rats, Wistar, Receptor, Melatonin, MT1 metabolism, Receptor, Melatonin, MT2 metabolism, Recombinant Proteins metabolism, Thiobarbituric Acid Reactive Substances metabolism, Vasodilation drug effects, Melatonin analogs & derivatives, Nitric Oxide Donors chemical synthesis, Nitric Oxide Donors pharmacology
Abstract

Numerous studies document that melatonin possesses a broad-spectrum antioxidant activity. It traps a number of reactive oxygen species (ROS) such as hydroxyl and peroxyl radicals, singlet oxygen and hypochlorous acid. It also inhibits peroxynitrite-induced reactions. It is known that atherosclerosis progression involves ROS-induced oxidation of low-density lipoproteins in sub-endothelial space and the depletion of nitric oxide (NO) in blood vessels, as well as a decreased sensitivity of the vessels to the actions of NO. Considering this, a series of new NO-donor antioxidants were designed and synthesized by joining melatonin with NO-donor nitrooxy and furoxan moieties as polyvalent agents potentially useful for the treatment of cardiovascular diseases involving atherosclerotic vascular changes. The in vitro antioxidant properties of the resulting products were assessed in the thiobarbituric acid reactive substances assay (TBARS), the ABTS(+.) as well as in the alkaline phosphatase (ALP) assay. The antioxidant capacities of NO-donor melatonins to inhibit lipoperoxidation (TBARS-IC(50)) was predominantly dependent on their lipophilicity, and therefore on their partitioning process into membranes. On the other hand, their comparable capacity to inhibit protein oxidation (ALP-IC(50)) was independent of their lipophilicity and was consistent with their similar ability to participate in electron transfer reactions. All the NO-donor melatonins were also evaluated for their ability to relax rat aorta strips precontracted with 1 microM phenylephrine. Finally, binding affinities and intrinsic activity studies, carried out at MT(1) and MT(2) receptor subtypes, showed a rather complex picture in need of further investigation.

Published
2007
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