Regulated expression and function of the GABA
Baclofen
/ pharmacology
Cell Line
GABA-B Receptor Agonists
/ pharmacology
Humans
Insulin
/ metabolism
Insulin Secretion
Insulin-Secreting Cells
/ metabolism
Islets of Langerhans
/ metabolism
Pancreas
/ metabolism
Receptors, G-Protein-Coupled
/ metabolism
Receptors, GABA-B
/ genetics
Signal Transduction
gamma-Aminobutyric Acid
/ metabolism
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
10 08 2020
10 08 2020
Historique:
received:
06
11
2019
accepted:
26
06
2020
entrez:
12
8
2020
pubmed:
12
8
2020
medline:
18
12
2020
Statut:
epublish
Résumé
G protein-coupled receptors are seven transmembrane signaling molecules that are involved in a wide variety of physiological processes. They constitute a large protein family of receptors with almost 300 members detected in human pancreatic islet preparations. However, the functional role of these receptors in pancreatic islets is unknown in most cases. We generated a new stable human beta cell line from neonatal pancreas. This cell line, named ECN90 expresses both subunits (GABBR1 and GABBR2) of the metabotropic GABA
Identifiants
pubmed: 32778664
doi: 10.1038/s41598-020-69758-6
pii: 10.1038/s41598-020-69758-6
pmc: PMC7417582
doi:
Substances chimiques
GABA-B Receptor Agonists
0
Insulin
0
Receptors, G-Protein-Coupled
0
Receptors, GABA-B
0
gamma-Aminobutyric Acid
56-12-2
Baclofen
H789N3FKE8
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
13469Références
Leahy, J. L. Pathogenesis of type 2 diabetes mellitus. Arch. Med. Res.36, 197–209 (2005).
pubmed: 15925010
Ahrén, B. Islet G protein-coupled receptors as potential targets for treatment of type 2 diabetes. Nat. Rev. Drug Discov.8, 369–385 (2009).
pubmed: 19365392
Wootten, D., Christopoulos, A., Marti-Solano, M., Babu, M. M. & Sexton, P. M. Mechanisms of signalling and biased agonism in G protein-coupled receptors. Nat. Rev. Mol. Cell Biol.19, 638–653 (2018).
pubmed: 30104700
Pavlos, N. J. & Friedman, P. A. GPCR signaling and trafficking: the long and short of it. Trends Endocrinol. Metab.28, 213–226 (2017).
pubmed: 27889227
Bowery, N. G. et al. International Union of Pharmacology. XXXIII. Mammalian gamma-aminobutyric acid(B) receptors: structure and function. Pharmacol. Rev.54, 247–264 (2002).
pubmed: 12037141
Olsen, R. W. & Sieghart, W. International union of lassification on the basis of subunit composition, pharmacology, and function. Pharmacol. Rev.60, 243–260 (2008).
pubmed: 18790874
pmcid: 2847512
Chessler, S. D. & Lernmark, A. Alternative splicing of GAD67 results in the synthesis of a third form of glutamic-acid decarboxylase in human islets and other non-neural tissues. J. Biol. Chem.275, 5188–5192 (2000).
pubmed: 10671565
Braun, M. et al. Gamma-aminobutyric acid (GABA) is an autocrine excitatory transmitter in human pancreatic beta-cells. Diabetes59, 1694–1701 (2010).
pubmed: 20413510
pmcid: 2889769
Korol, S. V. et al. Functional characterization of native, high-affinity GABAA receptors in human pancreatic β cells. EBioMedicine30, 273–282 (2018).
pubmed: 29606630
pmcid: 5952339
Amisten, S., Salehi, A., Rorsman, P., Jones, P. M. & Persaud, S. J. An atlas and functional analysis of G-protein coupled receptors in human islets of Langerhans. Pharmacol. Ther.139, 359–391 (2013).
pubmed: 23694765
Braun, M. et al. GABAB receptor activation inhibits exocytosis in rat pancreatic beta-cells by G-protein-dependent activation of calcineurin. J. Physiol. (Lond.)559, 397–409 (2004).
Wang, Q., Ren, L., Wan, Y. & Prud’homme, G. J. GABAergic regulation of pancreatic islet cells: physiology and antidiabetic effects. J. Cell. Physiol. https://doi.org/10.1002/jcp.28214 (2019).
doi: 10.1002/jcp.28214
pubmed: 32048739
pmcid: 7028135
Tian, J. et al. γ-Aminobutyric acid regulates both the survival and replication of human β-cells. Diabetes62, 3760–3765 (2013).
pubmed: 23995958
pmcid: 3806626
Hill, D. R. & Bowery, N. G. 3H-baclofen and 3H-GABA bind to bicuculline-insensitive GABA B sites in rat brain. Nature290, 149–152 (1981).
pubmed: 6259535
Scharfmann, R. et al. Development of a conditionally immortalized human pancreatic β cell line. J. Clin. Invest.124, 2087–2098 (2014).
pubmed: 24667639
pmcid: 4001549
Ravassard, P. et al. A genetically engineered human pancreatic β cell line exhibiting glucose-inducible insulin secretion. J. Clin. Invest.121, 3589–3597 (2011).
pubmed: 21865645
pmcid: 3163974
Hill, D. R. GABAB receptor modulation of adenylate cyclase activity in rat brain slices. Br. J. Pharmacol.84, 249–257 (1985).
pubmed: 2579700
pmcid: 1987231
Kaupmann, K. et al. Human gamma-aminobutyric acid type B receptors are differentially expressed and regulate inwardly rectifying K+ channels. Proc. Natl. Acad. Sci. USA.95, 14991–14996 (1998).
pubmed: 9844003
Odagaki, Y. & Koyama, T. Identification of galpha subtype(s) involved in gamma-aminobutyric acid(B) receptor-mediated high-affinity guanosine triphosphatase activity in rat cerebral cortical membranes. Neurosci. Lett.297, 137–141 (2001).
pubmed: 11121889
Richards, P. et al. MondoA is an essential glucose-responsive transcription factor in human pancreatic β-cells. Diabetes67, 461–472 (2018).
pubmed: 29282201
Siegel, E. G. & Creutzfeldt, W. Stimulation of insulin release in isolated rat islets by GIP in physiological concentrations and its relation to islet cyclic AMP content. Diabetologia28, 857–861 (1985).
pubmed: 2417905
Furman, B., Ong, W. K. & Pyne, N. J. Cyclic AMP signaling in pancreatic islets. Adv. Exp. Med. Biol.654, 281–304 (2010).
pubmed: 20217503
Arda, H. E. et al. Age-dependent pancreatic gene regulation reveals mechanisms governing human β cell function. Cell Metab.23, 909–920 (2016).
pubmed: 27133132
pmcid: 4864151
Culina, S. et al. Islet-reactive CD8+ T cell frequencies in the pancreas, but not in blood, distinguish type 1 diabetic patients from healthy donors. Sci Immunol3, (2018).
Jones, K. A. et al. GABA(B) receptors function as a heteromeric assembly of the subunits GABA(B)R1 and GABA(B)R2. Nature396, 674–679 (1998).
pubmed: 9872315
Kaupmann, K. et al. GABA(B)-receptor subtypes assemble into functional heteromeric complexes. Nature396, 683–687 (1998).
pubmed: 9872317
Kuner, R. et al. Role of heteromer formation in GABAB receptor function. Science283, 74–77 (1999).
pubmed: 9872744
White, J. H. et al. Heterodimerization is required for the formation of a functional GABA(B) receptor. Nature396, 679–682 (1998).
pubmed: 9872316
Ong, J. & Kerr, D. I. GABA-receptors in peripheral tissues. Life Sci.46, 1489–1501 (1990).
pubmed: 2162457
Bowery, N. G., Hudson, A. L. & Price, G. W. GABAA and GABAB receptor site distribution in the rat central nervous system. Neuroscience20, 365–383 (1987).
pubmed: 3035421
Bowery, N. G. GABAB receptor pharmacology. Annu. Rev. Pharmacol. Toxicol.33, 109–147 (1993).
pubmed: 8388192
Regard, J. B., Sato, I. T. & Coughlin, S. R. Anatomical profiling of G protein-coupled receptor expression. Cell135, 561–571 (2008).
pubmed: 18984166
pmcid: 2590943
Arntfield, M. E. & van der Kooy, D. β-Cell evolution: How the pancreas borrowed from the brain: the shared toolbox of genes expressed by neural and pancreatic endocrine cells may reflect their evolutionary relationship. BioEssays33, 582–587 (2011).
pubmed: 21681773
Doly, S. et al. GABAB receptor cell-surface export is controlled by an endoplasmic reticulum gatekeeper. Mol. Psychiatry21, 480–490 (2016).
pubmed: 26033241
Couve, A. et al. Cyclic AMP-dependent protein kinase phosphorylation facilitates GABA(B) receptor-effector coupling. Nat. Neurosci.5, 415–424 (2002).
pubmed: 11976702
Seino, S., Takahashi, H., Fujimoto, W. & Shibasaki, T. Roles of cAMP signalling in insulin granule exocytosis. Diabetes Obes Metab11(Suppl 4), 180–188 (2009).
pubmed: 19817800
Svendsen, B. et al. Insulin Secretion depends on intra-islet glucagon signaling. Cell Rep25, 1127-1134.e2 (2018).
pubmed: 30380405
Zhu, L. et al. Intra-islet glucagon signaling is critical for maintaining glucose homeostasis. JCI Insight5, (2019).
Tsonkova, V. G. et al. The EndoC-βH1 cell line is a valid model of human beta cells and applicable for screenings to identify novel drug target candidates. Mol. Metab.8, 144–157 (2018).
pubmed: 29307512
Suckale, J. & Solimena, M. The insulin secretory granule as a signaling hub. Trends Endocrinol. Metab.21, 599–609 (2010).
pubmed: 20609596
Rorsman, P. et al. Activation by adrenaline of a low-conductance G protein-dependent K+ channel in mouse pancreatic B cells. Nature349, 77–79 (1991).
pubmed: 1898674
Blanchet, E. et al. Feedback inhibition of CREB signaling promotes beta cell dysfunction in insulin resistance. Cell. Rep.10, 1149–1157 (2015).
pubmed: 25704817
pmcid: 4872509
Hang, Y. & Stein, R. MafA and MafB activity in pancreatic β cells. Trends Endocrinol. Metab.22, 364–373 (2011).
pubmed: 21719305
pmcid: 3189696
Steiner, D. F. & James, D. E. Cellular and molecular biology of the beta cell. Diabetologia35(Suppl 2), S41-48 (1992).
pubmed: 1478377
Sosa-Pineda, B., Chowdhury, K., Torres, M., Oliver, G. & Gruss, P. The Pax4 gene is essential for differentiation of insulin-producing beta cells in the mammalian pancreas. Nature386, 399–402 (1997).
pubmed: 9121556
Lorenzo, P. I., Cobo-Vuilleumier, N. & Gauthier, B. R. Therapeutic potential of pancreatic PAX4-regulated pathways in treating diabetes mellitus. Curr. Opin. Pharmacol.43, 1–10 (2018).
pubmed: 30048825
Chen, Z. et al. cAMP/CREB-regulated LINC00473 marks LKB1-inactivated lung cancer and mediates tumor growth. J. Clin. Invest.126, 2267–2279 (2016).
pubmed: 27140397
pmcid: 4887185
Herzberg-Schäfer, S., Heni, M., Stefan, N., Häring, H.-U. & Fritsche, A. Impairment of GLP1-induced insulin secretion: role of genetic background, insulin resistance and hyperglycaemia. Diabetes Obes. Metab.14(Suppl 3), 85–90 (2012).
pubmed: 22928568
Castaing, M. et al. Blood glucose normalization upon transplantation of human embryonic pancreas into beta-cell-deficient SCID mice. Diabetologia44, 2066–2076 (2001).
pubmed: 11719839
Oshima, M. et al. Virus-like infection induces human β cell dedifferentiation. JCI Insight3, (2018).
Ihler, F. et al. Expression of a neuroendocrine gene signature in gastric tumor cells from CEA 424-SV40 large T antigen-transgenic mice depends on SV40 large T antigen. PLoS ONE7, e29846 (2012).
pubmed: 22253802
pmcid: 3258231
Duvillié, B. et al. The mesenchyme controls the timing of pancreatic beta-cell differentiation. Diabetes55, 582–589 (2006).
pubmed: 16505219