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1. Stoffwechselerkrankungen mit Nierenbeteiligung

Author

Erger, Florian, Beck, Bodo B., Kömhoff, Martin, Reinhardt, Dietrich, Series Editor, Zimmer, Klaus-Peter, Series Editor, Felderhoff-Müser, Ursula, Series Editor, Krägeloh-Mann, Ingeborg, Series Editor, Weiß, Michael, Series Editor, de Laffolie, Jan, editor, Weber, Stefanie, editor, and Reinshagen, Konrad, editor

Published
2024
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2. Hyporeninemic hypoaldosteronism in RMND1-related mitochondrial disease

Author

Kömhoff, Martin, Gracchi, Valentina, Dijkman, Henry, Beck, Bodo B., and Monnens, Leo

Subjects
Diagnosis, Genetic aspects, Measurement, Risk factors, Health aspects, Aldosterone -- Measurement -- Health aspects, Mitochondrial diseases -- Diagnosis -- Risk factors -- Genetic aspects
Abstract

Author(s): Martin Kömhoff [sup.1] , Valentina Gracchi [sup.2] , Henry Dijkman [sup.3] , Bodo B. Beck [sup.4] , Leo Monnens [sup.5] Author Affiliations: (1) grid.10253.35, 0000 0004 1936 9756, University [...], Background RMND1 is a nuclear gene needed for proper function of mitochondria. A pathogenic gene will cause multiple oxidative phosphorylation defects. A renal phenotype consisting of hyponatremia, hyperkalemia, and acidosis is frequently reported, previously considered to be due to aldosterone insensitivity. Methods Clinical features and pathophysiology of three patients will be reported. DNA of these patients was subjected to exome screening. Results In the first family, one pathogenic heterozygous and one highly probable heterozygous mutation were detected. In the second family, a homozygous pathogenic mutation was present. The electrolyte disbalance was not due to aldosterone insensitivity but to low plasma aldosterone concentration, a consequence of low plasma renin activity. This disbalance can be treated. In all three patients, the kidney function declined. In the first family, both children suffered from an unexplained arterial thrombosis with dire consequences. Conclusions Hyporeninemic hypoaldosteronism is the mechanism causing the electrolyte disbalance reported in patients with RMND1 mutations, and can be treated.

Published
2024
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3. Long-read sequencing identifies a common transposition haplotype predisposing for CLCNKB deletions

Author

Tschernoster, Nikolai, Erger, Florian, Kohl, Stefan, Reusch, Björn, Wenzel, Andrea, Walsh, Stephen, Thiele, Holger, Becker, Christian, Franitza, Marek, Bartram, Malte P., Kömhoff, Martin, Schumacher, Lena, Kukat, Christian, Borodina, Tatiana, Quedenau, Claudia, Nürnberg, Peter, Rinschen, Markus M, Driller, Jan H., Pedersen, Bjørn P., Schlingmann, Karl P., Hüttel, Bruno, Bockenhauer, Detlef, Beck, Bodo, and Altmüller, Janine

Published
2023
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5. MAGED2 Enhances Expression and Function of NCC at the Cell Surface via cAMP Signaling Under Hypoxia.

Author

Radi, Aline, Nasrah, Sadiq, Auer, Michelle, Renigunta, Aparna, Weber, Stefanie, Seaayfan, Elie, and Kömhoff, Martin

Subjects
ADENYLATE cyclase, AMNIOTIC liquid, PROTEOLYSIS, WASTE recycling, CELL physiology
Abstract

Mutations in MAGED2 cause transient antenatal Bartter syndrome (tBS) characterized by excessive amounts of amniotic fluid due to impaired renal salt transport via NKCC2 and NCC, high perinatal mortality, and pre-term birth. Surprisingly, renal salt handling completely normalizes after birth. Previously, we demonstrated that, under hypoxic conditions, MAGED2 depletion enhances endocytosis of GalphaS (Gαs), reducing adenylate cyclase (AC) activation and cAMP production. This impaired cAMP signaling likely contributes to the dysfunction of salt transporters NKCC2 and NCC, explaining salt wasting and the subsequent recovery with renal oxygenation after birth. In this study, we show that MAGED2 depletion significantly decreases both total cellular and plasma membrane NCC expression and activity. We further demonstrate that MAGED2 depletion disrupts NCC trafficking by reducing exocytosis, increasing endocytosis, and promoting lysosomal degradation via enhanced ubiquitination. Additionally, forskolin (FSK), which increases cAMP production by activating AC, rescues NCC expression and localization in MAGED2-depleted cells. Conversely, MAGED2 overexpression increases NCC expression and membrane localization, although this effect is diminished in Gαs-depleted cells, indicating that Gαs acts downstream of MAGED2. In summary, our findings reveal the essential role of MAGED2 in regulating NCC function and trafficking under hypoxic conditions, providing new insights into the mechanisms behind salt loss in tBS and identifying potential therapeutic targets. [ABSTRACT FROM AUTHOR]

Published
2025
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7. Loss of ADAM17 is associated with severe multiorgan dysfunction

Author

Bandsma, Robert HJ, van Goor, Harry, Yourshaw, Michael, Horlings, Rudolf K, Jonkman, Marcel F, Schölvinck, Elisabeth H, Karrenbeld, Arend, Scheenstra, Rene, Kömhoff, Martin, Rump, Patrick, Koopman-Keemink, Yvonne, Nelson, Stanley F, Escher, Johanna C, Cutz, Ernest, and Martín, Martín G

Subjects
Rare Diseases, Hematology, Clinical Research, Genetics, 2.1 Biological and endogenous factors, Aetiology, Good Health and Well Being, ADAM Proteins, ADAM17 Protein, Fatal Outcome, Female, Frameshift Mutation, Genetic Predisposition to Disease, Homozygote, Humans, Infant, Multiple Organ Failure, Tumor Necrosis Factor-alpha, ADAM17, Exome sequencing, Congenital enteropathy, Immunodeficiency, Inflammation, Clinical Sciences, Pathology
Abstract

ADAM metallopeptidase domain 17 (ADAM17) is responsible for processing large numbers of proteins. Recently, 1 family involving 2 patients with a homozygous mutation in ADAM17 were described, presenting with skin lesions and diarrhea. In this report, we describe a second family confirming the existence of this syndrome. The proband presented with severe diarrhea, skin rash, and recurrent sepsis, eventually leading to her death at the age of 10 months. We performed exome sequencing and detailed pathological and immunological investigations. We identified a novel homozygous frameshift mutation in ADAM17 (NM_003183.4:c.308dupA) leading to a premature stop codon. CD4(+) and CD8(+) T-cell stimulation assays showed severely diminished tumor necrosis factor-α and interleukin-2 production. Skin biopsies indicated a focal neutrophilic infiltrate and spongiotic dermatitis. Interestingly, the patient developed unexplained systolic hypertension and nonspecific hepatitis with apoptosis. This report provides evidence for an important role of ADAM17 in human immunological response and underscores its multiorgan involvement.

Published
2015

9. Adressen

Author

Michalk, Dietrich, primary, Schönau, Eckhard, additional, Ahrens, Wiebke, additional, Andres, Oliver, additional, Böhles, Hansjosef, additional, Brämswig, Jürgen H., additional, Brandl, Ulrich, additional, Braun, Max, additional, Brenner, Rolf, additional, Broekaert, Ilse Julia, additional, Büscher, Rainer, additional, Cirak, Sebahattin, additional, Crazzolara, Roman, additional, Diestelhorst, Michael, additional, Dittrich, Sven, additional, Döpfner, Manfred, additional, Dübbers, Martin, additional, Duran, Ibrahim, additional, Eber, Stefan, additional, Eifinger, Frank, additional, Emmel, Mathias, additional, Engelmann, Udo H., additional, Engelmann, Simon U., additional, Fricke, Oliver, additional, Ganser, Gerd, additional, Gontard, Alexander von, additional, Graf, Isabelle, additional, Grüters-Kieslich, Annette, additional, Haak, Rainer, additional, Hartmann, Kathi, additional, Hauffa, Berthold P., additional, Heininger, Ulrich, additional, Herkenrath, Peter, additional, Hesse, Gerhard, additional, Hofbeck, Michael, additional, Holl, Reinhard, additional, Holtmann, Martin, additional, Hoppe, Bernd, additional, Hoyer-Kuhn, Heike, additional, Hünseler, Christoph, additional, Huppertz, Hans-Iko, additional, Hüttenbrink, Karl-Bernd, additional, Keller, Klaus-Michael, additional, Kerzel, Sebastian, additional, Kirschner, Jan, additional, Kirschstein, Martin, additional, Klaus, Günter, additional, Koletzko, Berthold, additional, Koletzko, Sibylle, additional, Kömhoff, Martin, additional, Konrad, Martin, additional, Körner, Robert W., additional, Kuwertz-Bröking, Eberhard, additional, Land, Christof, additional, Landgraf, Pablo, additional, Laws, Hans-Jürgen, additional, Lentze, Michael J., additional, Licht, Christoph, additional, Lowden, Esther, additional, Luckhaus, Johannes, additional, Martakis, Kyriakos, additional, Mohnike, Klaus, additional, Niehues, Tim, additional, Nüsken, Eva, additional, Nüsken, Kai-Dietrich, additional, Nützenadel, Walter, additional, Paditz, Ekkehart, additional, Paul-Buck, Karl, additional, Querfeld, Uwe, additional, Ranke, Michael B., additional, Rascher, Wolfgang, additional, Rehberg, Mirko, additional, Riedel, Frank, additional, Scheyerer, Max J., additional, Schmalz, Gerhard, additional, Schorling, David, additional, Schwahn, Bernd C., additional, Schwarz, Tobias, additional, Schweigerer, Lothar, additional, Seyberth, Hannsjörg, additional, Simon, Thorsten, additional, Sinnecker, Gernot H.G., additional, Sollberg, Stephan, additional, Sperl, Wolfgang, additional, Sprinzl, Georg Mathias, additional, Sreeram, Narayanswami, additional, Striegel, Anne Kathrin, additional, Strunz, Verena, additional, Wabitsch, Martin, additional, Waldegger, Siegfried, additional, Walger, Martin, additional, von Wedel, Hasso, additional, Weiß, Michael, additional, Wiesner, Thomas, additional, Wirth, Stefan, additional, Yagdiran, Ayla, additional, Zöller, Joachim E., additional, and Zuberbier, T., additional

Published
2021
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14. Renal thrombotic microangiopathy in patients with cblC defect: review of an under-recognized entity

Author

Beck, Bodo B., van Spronsen, FrancJan, Diepstra, Arjan, Berger, Rolf M. F., and Kömhoff, Martin

Abstract

Author(s): Bodo B. Beck [sup.1] , FrancJan van Spronsen [sup.2] , Arjan Diepstra [sup.3] , Rolf M. F. Berger [sup.4] , Martin Kömhoff [sup.5] [sup.6] Author Affiliations: (1) 0000 0000 [...], Methylmalonic aciduria and homocystinuria, cobalamin C (cblC) type, is the most common genetic type of functional cobalamin (vitamin B.sub.12) deficiency. This metabolic disease is characterized by marked heterogeneity of neurocognitive disease (microcephaly, seizures, developmental delay, ataxia, hypotonia) and variable extracentral nervous system involvement (failure to thrive, cardiovascular, renal, ocular) manifesting predominantly early in life, sometimes during gestation. To enhance awareness and understanding of renal disease associated with cblC defect, we studied biochemical, genetic, clinical, and histopathological data from 36 patients. Consistent clinical chemistry features of renal disease were intravascular hemolysis, hematuria, and proteinuria in all patients, with nephrotic-range proteinuria observed in three. Renal function ranged from normal to renal failure, with eight patients requiring (intermittent) dialysis. Two thirds were diagnosed with atypical (diarrhea-negative) hemolytic uremic syndrome (HUS). Renal histopathology analyses of biopsy samples from 16 patients revealed glomerular lesions typical of thrombotic microangiopathy (TMA). Treatment with hydroxycobalamin improved renal function in the majority, including three in whom dialysis could be withdrawn. Neurological sequelae were observed in 44 % and cardiopulmonary involvement in 39 % of patients, with half of the latter group demonstrating pulmonary hypertension. Mortality reached 100 % in untreated patients and 79 and 56 % in those with cardiopulmonary or neurological involvement, respectively. In all patients presenting with unclear intravascular hemolysis, hematuria, and proteinuria, cblC defect should be ruled out by determination of blood/plasma homocysteine levels and/or genetic testing, irrespective of actual renal function and neurological status, to ensure timely diagnosis and treatment.

Published
2017
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16. Adressen

Author

Michalk, Dietrich, primary, Schönau, Eckhard, additional, Ahrens, Wiebke, additional, Baumann, Michael A., additional, Böhles, Hansjosef, additional, Brämswig, Jürgen H., additional, Brandl, Ulrich, additional, Brenner, Rolf, additional, Broekaert, Ilse Julia, additional, Büscher, Rainer, additional, Cirak, Sebahattin, additional, Crazzolara, Roman, additional, Diestelhorst, Michael, additional, Dittrich, Sven, additional, Döpfner, Manfred, additional, Dörr, Helmuth-Günther, additional, Dübbers, Martin, additional, Duran, Ibrahim, additional, Eber, Stefan, additional, Eckel, Hans Edmund, additional, Edelmann, Peter, additional, Emmel, Mathias, additional, Engelmann, Udo H., additional, Fartasch, Manige, additional, Fricke, Oliver, additional, Gahr, Manfred, additional, Ganser, Gerd, additional, von Gontard, Alexander, additional, Graf, Isabelle, additional, Grosse, Klaus-Peter, additional, Grüters-Kieslich, Annette, additional, Haak, Rainer, additional, Hauffa, Berthold P., additional, Heininger, Ulrich, additional, Herkenrath, Peter, additional, Hesse, Gerhard, additional, Hofbeck, Michael, additional, Holl, Reinhard, additional, Hoppe, Bernd, additional, Hoyer-Kuhn, Heike, additional, Hünseler, Christoph, additional, Huppertz, Hans-Iko, additional, Hüttenbrink, Karl-Bernd, additional, Keller, Klaus-Michael, additional, Kerzel, Sebastian, additional, Kirschner, Jan, additional, Kirschstein, Martin, additional, Klaus, Günter, additional, Koletzko, Berthold, additional, Koletzko, Sibylle, additional, Kömhoff, Martin, additional, Konrad, Martin, additional, Korge, Bernhard, additional, Kuwertz-Bröking, Eberhard, additional, Land, Christof, additional, Landgraf, Pablo, additional, Lauffer, Heinz, additional, Laws, Hans-Jürgen, additional, Lehmkuhl, Gerd, additional, Lentze, Michael J., additional, Licht, Christoph, additional, von Lilien-Schmidt, Anna-Laura, additional, Lowden, Esther, additional, Luckhaus, Johannes, additional, Mohnike, Klaus, additional, Müller-Wiefel, Dirk E., additional, Niehues, Tim, additional, Nützenadel, Walter, additional, Paditz, Ekkehart, additional, Partsch, Carl-Joachim, additional, Paul-Buck, Karl, additional, Querfeld, Uwe, additional, Ranke, Michael B., additional, Rascher, Wolfgang, additional, Riedel, Frank, additional, Rietschel, Ernst, additional, Roth, Bernhard, additional, Rüssmann, Walter, additional, Rütt, Jürgen, additional, Schmalz, Gerhard, additional, Schorling, David, additional, Schubert, Elke, additional, Schwahn, Bernd, additional, Schwarz, Tobias, additional, Schweigerer, Lothar, additional, Seyberth, Hannsjörg W., additional, Simon, Thorsten, additional, Sinnecker, Gernot H.G., additional, Sollberg, Stephan, additional, Sperl, Wolfgang, additional, Sprinzl, Georg Mathias, additional, Striegel, Anne Kathrin, additional, Stürmer, Konrad, additional, Überall, Michael, additional, Wabitsch, Martin, additional, Waldegger, Siegfried, additional, Walger, Martin, additional, von Wedel, Hasso, additional, Weiß, Michael, additional, Wiesner, Thomas, additional, Wirth, Stefan, additional, Zöller, Joachim E., additional, and Zuberbier, Torsten, additional

Published
2018
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23. Gitelman-Like Syndrome Caused by Pathogenic Variants in mtDNA

Author

Genetica Klinische Genetica, Child Health, Cancer, Viering, Daan, Schlingmann, Karl-Peter, Hureaux, Marguerite, Nijenhuis, Tom, Mallett, Andrew, Chan, Melanie, van Beek, Andre, van Eerde, Albertien, Coulibaly, Jean-Marie, Vallet, Marion, Decramer, Stéphane, Pelletier, Solenne, Klaus, Günter, Kömhoff, Martin, Beetz, Rolf, Patel, Chirag, Shenoy, Mohan, Steenbergen, Eric, Anderson, Glenn, Bongers, Ernie, Bergmann, Carsten, Panneman, Daan, Rodenburg, Richard, Kleta, Robert, Houillier, Pascal, Konrad, Martin, Vargas-Poussou, Rosa, Bockenhauer, Detlef, de Baaij, Jeroen, Genetica Klinische Genetica, Child Health, Cancer, Viering, Daan, Schlingmann, Karl-Peter, Hureaux, Marguerite, Nijenhuis, Tom, Mallett, Andrew, Chan, Melanie, van Beek, Andre, van Eerde, Albertien, Coulibaly, Jean-Marie, Vallet, Marion, Decramer, Stéphane, Pelletier, Solenne, Klaus, Günter, Kömhoff, Martin, Beetz, Rolf, Patel, Chirag, Shenoy, Mohan, Steenbergen, Eric, Anderson, Glenn, Bongers, Ernie, Bergmann, Carsten, Panneman, Daan, Rodenburg, Richard, Kleta, Robert, Houillier, Pascal, Konrad, Martin, Vargas-Poussou, Rosa, Bockenhauer, Detlef, and de Baaij, Jeroen

Published
2022

24. Polyhydramnios, Transient Antenatal Bartterʼs Syndrome, and MAGED2 Mutations

Author

Laghmani, Kamel, Beck, Bodo B., Yang, Sung-Sen, Seaayfan, Elie, Wenzel, Andrea, Reusch, Björn, Vitzthum, Helga, Priem, Dario, Demaretz, Sylvie, Bergmann, Klasien, Duin, Leonie K., Göbel, Heike, Mache, Christoph, Thiele, Holger, Bartram, Malte P., Dombret, Carlos, Altmüller, Janine, Nürnberg, Peter, Benzing, Thomas, Levtchenko, Elena, Seyberth, Hannsjörg W., Klaus, Günter, Yigit, Gökhan, Lin, Shih-Hua, Timmer, Albert, de Koning, Tom J., Scherjon, Sicco A., Schlingmann, Karl P., Bertrand, Mathieu J.M., Rinschen, Markus M., de Backer, Olivier, Konrad, Martin, and Kömhoff, Martin

Published
2016
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28. Der Einfluss von MAGED2 auf NHE3 in humanen embryonalen Nierenzellen (HEK293)

Author

Ruttkowski, Lars Lennart and Kömhoff, Martin (Prof. Dr. med.)

Subjects
Medizin, Bartter, NHE3, Gitleman-Syndorm, Medical sciences Medicine, antenatal, transient, Nephrologie, Kindernephrologie, Bartter-Syndrom, MAGED2, Gitleman, ddc:610
Abstract

Das transiente antenatale Bartter-Syndrom (taBS, OMIM # 300971) ist eine seltene X-chromosomal vererbte Erkrankung, die durch fetale Polyurie, Polyhydramnion, Frühgeburtlichkeit und transienten postnatalen renalen Salzverlust charakterisiert ist. Verantwortlich sind Mutationen des Maged2-Gens, welches einen Einfluss auf die posttranslationale Modifikation von Kanalproteinen im distalen Tubulus hat. Laghmani et al. konnten zeigen, dass NKCC2 und NCC in ihrer Expression durch mutiertes MAGED2 verringert werden. Grund hierfür scheint könnte eine gestörte Interaktion zwischen MAGED2 und dem Chaperon Hsp40, welches für die effiziente Faltung von NKCC2 und NCC notwendig ist, sein (Laghmani et al. 2016). Der extreme Phenotyp lässt vermuten, dass auch weitere Kanalproteine betroffen sind. NHE3 ist ein Na+/H+-Antiporter, der maßgeblich für die Na+-Rückresorption im proximalen Tubulus verantwortlich ist. MAGED2 wird im proximalen Tubulus jedoch nur im Fetus expremiert. Die Regulation von NHE3 ist noch nicht gut verstanden. Eine verminderte Aktivität würde infolge verminderter Salzrückresorption mit verminderter Harnkonzentrierung einhergehen. Ziel dieser Arbeit ist, einen etwaigen Einfluss von MAGED2 auf NHE3 zu überprüfen. Hierzu wurden HEK293-Zellen mit NHE3 und MAGED2 (Wildtyp und Mutante) transfiziert. Mittels SDS-PAGE und Western Blot-Analysen wurden die Proteine über ihre Tags, ihrer Größe entsprechend, identifiziert. Zur Ermittlung einer MAGED2-vermittelten Expression von NHE3 wurden Zellen mit steigenden Dosen MAGED2 (WT und MT) transfiziert. Analysiert wurde die Proteinhalbwertszeit durch Hemmung der Proteinsynthese mittels Cycloheximid (CC) in MAGED2 überexpremierten und knock-down Zellen zu unterschiedlichen Zeitpunkten. Mittels Koimmunpräzipitation (CoIP) wurde nach Protein-Proteininteraktionen gesucht. Eine räumliche Nähe wurde mittels Proximity Ligation Assay (PLA) untersucht. Um die Zelloberflächenintegration zu beurteilen wurden die Zellen mit Biotin behandelt, über welches die Membranproteinfraktion isoliert werden konnte (CSB). Die Ergebnisse der CoIP und PLA entsprachen sich und deuten darauf hin, dass NHE3 und MAGED2 (WT und MT) einen Komplex bilden. In den CC-Versuchen konnten keine MAGED2 vermittelten Unterschiede in der Halbwertszeit von NHE3 gezeigt werden. Die Dose Response-Versuche zeigten keine Veränderung der intrazellulären NHE3-Mengen abhängig von MAGED2. Auch in der CSB zeigte sich keine verringerte Integration von NHE3 in den mit der MAGED2-Mutante transfizierten Zellen im Vergleich zum Wildtyp. Wir konnten mit diesen Versuchen zeigen, dass NHE3 mit MAGED2 einen Komplex bildet und eventuell über andere Proteine miteinander interagiert. Anders als bei NCC und NKCC2, hat MAGED2 jedoch scheinbar keinen Einfluss auf die Proteinstabilität, Zelloberflächenintegration von NHE3 oder auf die Gesamt-NHE3-Proteinmenge. NHE3 könnte jedoch in seiner Funktion eingeschränkt sein. Weitere Untersuchungen sollten dies in Betracht ziehen. NHE3 kann bei MAGED2 Versuchen als negative Kontrolle dienen., The transient antenatal Bartters-Syndrome (taBS) is a rare, x-chromosomal genetic disease, which presents with polyuria, polyhydramnios, prematurity and transient postnatal salt wasting. Mutations of Maged2 were found to be responsible for the phenotype, most likely, by influencing the posttranslational modification of ion channel proteins in the distal kidney tubule. Laghmani et al. were able to show, that NKCC2- and NCC-expression was lowered in the presence of mutant MAGED2. This might be due to an altered interaction of MAGED2, Hsp40 and Gs-α. The severe pehontype suggests, that other ion channel proteins might be affected as well. NHE3 is a Na+/H+-antiporter, which is responsible for most of the Na+-reabsorption in the proximal tubule. However, MAGED2 is expressed in the proximal tuble only during the fetal period. NHE3 regulation is not well known. A lowered activity would present in lower urine concentration. The aim of this study is to find an influence of MAGED2 on NHE3. HEK293-cells were transfected with NHE3 and MAGED2 (wildtype and mutant). For analyzing the effect of MAGED2 on NHE3 protein stability cycloheximide chase (CC) experiments were performed, where protein synthesis was inhibited with cycloheximide in MAGED2 overexpressing cells, as well as MAGED2-knock-down cells, at different timepoints. The influence of MAGED2 on the expression of NHE3 was investigated by co-transfecting NHE3 with increasing doses of MAGED2 (WT and MT). The effect of MAGED2 on the cell surface integration of NHE3 was examined using cell surface biotinylation (CSB) studies. The results of the CoIP and PLA corresponded with one another and showed, that NHE3 and MAGED2 (WT and MT) may co-exist in a protein complex. In the CC, MAGED2 related changes in the halftime of NHE3 could not be observed. The dose response experiments showed no influence of MAGED2 on the levels of intracellular NHE3. Also the CSB could not show any changes in the cell surface integration of NHE3, when transfected with MAGED2 (WT or MT). We were able to show, that MAGED2 and NHE3 form a complex at some point in the cell and might be interacting through other proteins. Other than NCC and NKCC2, MAGED2 does not seem to have an influence on protein expression, protein stability and cell surface integration of NHE3. These studies however do not rule out the possibility that MAGED2 may influence NHE3 function. Further functional studies are required to study the effects of MAGED2 on NHE3 channel function. So far NHE3 can be used as a negative control in MAGED2-based experiments.

Published
2021
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36. MAGE-D2 and HSP40 Protect NKCC2 Against Hypoxia-Induced Endoplasmic Reticulum-Associated Degradation

Author

Nait Meddour, Kahina, Shaukat, Irfan, Demaretz, Sylvie, Bronji, Zaineb, Seaayfan, Elie, Kömhoff, Martin, Laghmani, Kamel, Ingénierie Moléculaire et Physiopathologie Articulaire (IMoPA), Centre National de la Recherche Scientifique (CNRS)-Université de Lorraine (UL), Centre de Recherche des Cordeliers (CRC), Université Pierre et Marie Curie - Paris 6 (UPMC)-École pratique des hautes études (EPHE), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Université Paris Diderot - Paris 7 (UPD7)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM), Centre de Recherche des Cordeliers (CRC (UMR_S 872)), Université Pierre et Marie Curie - Paris 6 (UPMC)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), ANR-17-CE14-0040,Pheno2Geno,Régulation de NKCC2 et NCC par les interactions Protéine-Protéine: Des tubulopathies avec perte de sel à l'hypertension sensible au sel(2017), Laghmani, Kamel, Régulation de NKCC2 et NCC par les interactions Protéine-Protéine: Des tubulopathies avec perte de sel à l'hypertension sensible au sel - - Pheno2Geno2017 - ANR-17-CE14-0040 - AAPG2017 - VALID, Université Paris Diderot - Paris 7 (UPD7)-École pratique des hautes études (EPHE)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM), ANR-17-CE14-0040,Pheno2Geno,Régulation de NKCC2 et NCC par les interactions Protéine-Protéine: Des tubulopathies avec perte de sel à l’hypertension sensible au sel(2017), Université Paris Diderot - Paris 7 (UPD7)-École pratique des hautes études (EPHE), and Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)

Subjects
[SDV] Life Sciences [q-bio], [SDV]Life Sciences [q-bio], [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, ComputingMilieux_MISCELLANEOUS
Abstract

International audience

Published
2019

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