메뉴 건너뛰기




Volumn 22, Issue 2, 2011, Pages 74-80

Novel insights into the function of β-cell M3 muscarinic acetylcholine receptors: Therapeutic implications

Author keywords

[No Author keywords available]

Indexed keywords

ANKYRIN; ANKYRIN B; BETA ARRESTIN 1; BETA ARRESTIN 2; BETHANECHOL; CALCIUM; CLOZAPINE; CLOZAPINE N OXIDE; DIACYLGLYCEROL; DIPEPTIDYL PEPTIDASE IV INHIBITOR; GLUCAGON LIKE PEPTIDE 1; GLUCOSE; GUANINE NUCLEOTIDE BINDING PROTEIN ALPHA SUBUNIT; INHIBITORY GUANINE NUCLEOTIDE BINDING PROTEIN; INOSITOL 1,4,5 TRISPHOSPHATE; INSULIN; INSULIN RECEPTOR SUBSTRATE 2; MUSCARINIC AGENT; MUSCARINIC M3 RECEPTOR; OLANZAPINE; PHOSPHOLIPASE C BETA; PROTEIN INHIBITOR; PROTEIN KINASE D; PROTEIN KINASE D1; RGS PROTEIN; RGS4 PROTEIN; SODIUM ION; STIMULATORY GUANINE NUCLEOTIDE BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 79251626567     PISSN: 10432760     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tem.2010.10.004     Document Type: Review
Times cited : (43)

References (49)
  • 1
    • 0037283601 scopus 로고    scopus 로고
    • The relative contributions of insulin resistance and beta-cell dysfunction to the pathophysiology of type 2 diabetes
    • Kahn S.E. The relative contributions of insulin resistance and beta-cell dysfunction to the pathophysiology of type 2 diabetes. Diabetologia 2003, 46:3-19.
    • (2003) Diabetologia , vol.46 , pp. 3-19
    • Kahn, S.E.1
  • 2
    • 67349176115 scopus 로고    scopus 로고
    • Islet G protein-coupled receptors as potential targets for treatment of type 2 diabetes
    • Ahrén B. Islet G protein-coupled receptors as potential targets for treatment of type 2 diabetes. Nat. Rev. Drug. Discov. 2009, 8:369-385.
    • (2009) Nat. Rev. Drug. Discov. , vol.8 , pp. 369-385
    • Ahrén, B.1
  • 3
    • 33847617011 scopus 로고    scopus 로고
    • Mechanisms of action of glucagon-like peptide 1 in the pancreas
    • Doyle M.E., Egan J.M. Mechanisms of action of glucagon-like peptide 1 in the pancreas. Pharmacol. Ther. 2007, 113:546-593.
    • (2007) Pharmacol. Ther. , vol.113 , pp. 546-593
    • Doyle, M.E.1    Egan, J.M.2
  • 4
    • 34248223285 scopus 로고    scopus 로고
    • Biology of incretins: GLP-1 and GIP
    • Baggio L.L., Drucker D.J. Biology of incretins: GLP-1 and GIP. Gastroenterology 2007, 132:2131-2157.
    • (2007) Gastroenterology , vol.132 , pp. 2131-2157
    • Baggio, L.L.1    Drucker, D.J.2
  • 5
    • 36849052080 scopus 로고    scopus 로고
    • i in vivo identifies GPCR regulators of insulin secretion
    • i in vivo identifies GPCR regulators of insulin secretion. J. Clin. Invest. 2007, 117:4034-4043.
    • (2007) J. Clin. Invest. , vol.117 , pp. 4034-4043
    • Regard, J.B.1
  • 6
    • 0034001450 scopus 로고    scopus 로고
    • Autonomic regulation of islet hormone secretion-implications for health and disease
    • Ahrén B. Autonomic regulation of islet hormone secretion-implications for health and disease. Diabetologia 2000, 43:393-410.
    • (2000) Diabetologia , vol.43 , pp. 393-410
    • Ahrén, B.1
  • 7
    • 0034786750 scopus 로고    scopus 로고
    • Mechanisms and physiological significance of the cholinergic control of pancreatic β-cell function
    • Gilon P., Henquin J.C. Mechanisms and physiological significance of the cholinergic control of pancreatic β-cell function. Endocr. Rev. 2001, 22:565-604.
    • (2001) Endocr. Rev. , vol.22 , pp. 565-604
    • Gilon, P.1    Henquin, J.C.2
  • 8
    • 3042785985 scopus 로고    scopus 로고
    • 3 muscarinic acetylcholine receptor-deficient mice
    • 3 muscarinic acetylcholine receptor-deficient mice. Diabetes 2004, 53:1714-1720.
    • (2004) Diabetes , vol.53 , pp. 1714-1720
    • Duttaroy, A.1
  • 9
    • 1342302828 scopus 로고    scopus 로고
    • Effects of muscarinic receptor type 3 knockout on mouse islet secretory responses
    • Zawalich W.S., et al. Effects of muscarinic receptor type 3 knockout on mouse islet secretory responses. Biochem. Biophys. Res. Commun. 2004, 315:872-876.
    • (2004) Biochem. Biophys. Res. Commun. , vol.315 , pp. 872-876
    • Zawalich, W.S.1
  • 10
    • 0023676354 scopus 로고
    • The muscarinic receptor subtype in mouse pancreatic B-cells
    • Henquin J.C., Nenquin M. The muscarinic receptor subtype in mouse pancreatic B-cells. FEBS Lett. 1988, 236:89-92.
    • (1988) FEBS Lett. , vol.236 , pp. 89-92
    • Henquin, J.C.1    Nenquin, M.2
  • 11
    • 0029789994 scopus 로고    scopus 로고
    • Molecular biology of muscarinic acetylcholine receptors
    • Wess J. Molecular biology of muscarinic acetylcholine receptors. Crit. Rev. Neurobiol. 1996, 10:69-99.
    • (1996) Crit. Rev. Neurobiol. , vol.10 , pp. 69-99
    • Wess, J.1
  • 12
    • 33744510095 scopus 로고    scopus 로고
    • 3 muscarinic acetylcholine receptors in regulating insulin release and blood glucose homeostasis in vivo
    • 3 muscarinic acetylcholine receptors in regulating insulin release and blood glucose homeostasis in vivo. Cell Metab. 2006, 3:449-461.
    • (2006) Cell Metab. , vol.3 , pp. 449-461
    • Gautam, D.1
  • 13
    • 0037064035 scopus 로고    scopus 로고
    • + current by muscarinic receptors in mouse pancreatic β-cells
    • + current by muscarinic receptors in mouse pancreatic β-cells. J. Biol. Chem. 2002, 277:38373-38380.
    • (2002) J. Biol. Chem. , vol.277 , pp. 38373-38380
    • Rolland, J.F.1
  • 14
    • 68249089016 scopus 로고    scopus 로고
    • The NALCN ion channel is activated by M3 muscarinic receptors in a pancreatic β-cell line
    • Swayne L.A., et al. The NALCN ion channel is activated by M3 muscarinic receptors in a pancreatic β-cell line. EMBO Rep. 2009, 10:873-880.
    • (2009) EMBO Rep. , vol.10 , pp. 873-880
    • Swayne, L.A.1
  • 15
    • 78049521571 scopus 로고    scopus 로고
    • 3 muscarinic acetylcholine receptors in transgenic mice
    • 3 muscarinic acetylcholine receptors in transgenic mice. Endocrinology 2010, 151:5185-5194.
    • (2010) Endocrinology , vol.151 , pp. 5185-5194
    • Gautam, D.1
  • 16
    • 0042530487 scopus 로고    scopus 로고
    • 3 receptor and greatly impair receptor/G protein coupling
    • 3 receptor and greatly impair receptor/G protein coupling. J. Biol. Chem. 2003, 278:30248-30260.
    • (2003) J. Biol. Chem. , vol.278 , pp. 30248-30260
    • Schmidt, C.1
  • 17
    • 0029862867 scopus 로고    scopus 로고
    • Species differences in the induction of time-dependent potentiation of insulin secretion
    • Zawalich W.S., Zawalich K.C. Species differences in the induction of time-dependent potentiation of insulin secretion. Endocrinology 1996, 137:1664-1669.
    • (1996) Endocrinology , vol.137 , pp. 1664-1669
    • Zawalich, W.S.1    Zawalich, K.C.2
  • 18
    • 61349093537 scopus 로고    scopus 로고
    • Subtype-selective allosteric modulators of muscarinic receptors for the treatment of CNS disorders
    • Conn P.J., et al. Subtype-selective allosteric modulators of muscarinic receptors for the treatment of CNS disorders. Trends Pharmacol. Sci. 2009, 30:148-155.
    • (2009) Trends Pharmacol. Sci. , vol.30 , pp. 148-155
    • Conn, P.J.1
  • 19
    • 0031774720 scopus 로고    scopus 로고
    • International Union of Pharmacology. XVII. Classification of muscarinic acetylcholine receptors
    • Caulfield M.P., Birdsall N.J.M. International Union of Pharmacology. XVII. Classification of muscarinic acetylcholine receptors. Pharmacol. Rev 1998, 50:279-290.
    • (1998) Pharmacol. Rev , vol.50 , pp. 279-290
    • Caulfield, M.P.1    Birdsall, N.J.M.2
  • 20
    • 34548362105 scopus 로고    scopus 로고
    • Muscarinic acetylcholine receptors: mutant mice provide new insights for drug development
    • Wess J., et al. Muscarinic acetylcholine receptors: mutant mice provide new insights for drug development. Nat. Rev. Drug Discov. 2007, 6:721-733.
    • (2007) Nat. Rev. Drug Discov. , vol.6 , pp. 721-733
    • Wess, J.1
  • 21
    • 77952340101 scopus 로고    scopus 로고
    • RGS4 is a negative regulator of insulin release from pancreatic β-cells in vitro and in vivo
    • Ruiz de Azua I., et al. RGS4 is a negative regulator of insulin release from pancreatic β-cells in vitro and in vivo. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:7999-8004.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 7999-8004
    • Ruiz de Azua, I.1
  • 22
    • 0037406701 scopus 로고    scopus 로고
    • Regulation of muscarinic acetylcholine receptor signaling
    • van Koppen C.J., Kaiser B. Regulation of muscarinic acetylcholine receptor signaling. Pharmacol. Ther. 2003, 98:197-220.
    • (2003) Pharmacol. Ther. , vol.98 , pp. 197-220
    • van Koppen, C.J.1    Kaiser, B.2
  • 23
    • 0033783132 scopus 로고    scopus 로고
    • GTPase-activating proteins for heterotrimeric G proteins: regulators of G protein signaling (RGS) and RGS-like proteins
    • Ross E.M., Wilkie T.M. GTPase-activating proteins for heterotrimeric G proteins: regulators of G protein signaling (RGS) and RGS-like proteins. Annu. Rev. Biochem. 2000, 69:795-827.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 795-827
    • Ross, E.M.1    Wilkie, T.M.2
  • 24
    • 30944451158 scopus 로고    scopus 로고
    • RGS proteins have a signalling complex: interactions between RGS proteins and GPCRs, effectors, and auxiliary proteins
    • Abramow-Newerly M., et al. RGS proteins have a signalling complex: interactions between RGS proteins and GPCRs, effectors, and auxiliary proteins. Cell Signal. 2006, 18:579-591.
    • (2006) Cell Signal. , vol.18 , pp. 579-591
    • Abramow-Newerly, M.1
  • 25
    • 33746013755 scopus 로고    scopus 로고
    • Cellular mechanisms that determine selective RGS protein regulation of G protein-coupled receptor signaling
    • Neitzel K.L., Hepler J.R. Cellular mechanisms that determine selective RGS protein regulation of G protein-coupled receptor signaling. Semin. Cell Dev. Biol. 2006, 17:383-389.
    • (2006) Semin. Cell Dev. Biol. , vol.17 , pp. 383-389
    • Neitzel, K.L.1    Hepler, J.R.2
  • 26
    • 36148945617 scopus 로고    scopus 로고
    • R4 RGS proteins: regulation of G-protein signaling and beyond
    • Bansal G., et al. R4 RGS proteins: regulation of G-protein signaling and beyond. Pharmacol. Ther. 2007, 116:473-495.
    • (2007) Pharmacol. Ther. , vol.116 , pp. 473-495
    • Bansal, G.1
  • 27
    • 54049083934 scopus 로고    scopus 로고
    • RGS4 regulates parasympathetic signaling and heart rate control in the sinoatrial node
    • Cifelli C., et al. RGS4 regulates parasympathetic signaling and heart rate control in the sinoatrial node. Circ. Res. 2008, 103:527-535.
    • (2008) Circ. Res. , vol.103 , pp. 527-535
    • Cifelli, C.1
  • 28
    • 75149188804 scopus 로고    scopus 로고
    • RGS4 controls renal blood flow and inhibits cyclosporine-mediated nephrotoxicity
    • Siedlecki A., et al. RGS4 controls renal blood flow and inhibits cyclosporine-mediated nephrotoxicity. Am. J. Transplant. 2010, 10:231-241.
    • (2010) Am. J. Transplant. , vol.10 , pp. 231-241
    • Siedlecki, A.1
  • 29
    • 54349128871 scopus 로고    scopus 로고
    • Regulator of G protein signaling-4 controls fatty acid and glucose homeostasis
    • Iankova I., et al. Regulator of G protein signaling-4 controls fatty acid and glucose homeostasis. Endocrinology 2008, 149:5706-5712.
    • (2008) Endocrinology , vol.149 , pp. 5706-5712
    • Iankova, I.1
  • 30
    • 67651006540 scopus 로고    scopus 로고
    • Breast cancer migration and invasion depend on proteasome degradation of regulator of G-protein signaling 4
    • Xie Y., et al. Breast cancer migration and invasion depend on proteasome degradation of regulator of G-protein signaling 4. Cancer Res. 2009, 69:5743-5751.
    • (2009) Cancer Res. , vol.69 , pp. 5743-5751
    • Xie, Y.1
  • 31
    • 3042604602 scopus 로고    scopus 로고
    • Regional expression of RGS4 mRNA in human brain
    • Erdely H.A., et al. Regional expression of RGS4 mRNA in human brain. Eur. J. Neurosci. 2004, 19:3125-3128.
    • (2004) Eur. J. Neurosci. , vol.19 , pp. 3125-3128
    • Erdely, H.A.1
  • 32
    • 33745712929 scopus 로고    scopus 로고
    • RGS4-dependent attenuation of M4 autoreceptor function in striatal cholinergic interneurons following dopamine depletion
    • Ding J., et al. RGS4-dependent attenuation of M4 autoreceptor function in striatal cholinergic interneurons following dopamine depletion. Nat. Neurosci. 2006, 9:832-842.
    • (2006) Nat. Neurosci. , vol.9 , pp. 832-842
    • Ding, J.1
  • 33
    • 33748746323 scopus 로고    scopus 로고
    • Making the case for a candidate vulnerability gene in schizophrenia: Convergent evidence for regulator of G-protein signaling 4 (RGS4)
    • Levitt P., et al. Making the case for a candidate vulnerability gene in schizophrenia: Convergent evidence for regulator of G-protein signaling 4 (RGS4). Biol. Psychiat. 2006, 60:534-537.
    • (2006) Biol. Psychiat. , vol.60 , pp. 534-537
    • Levitt, P.1
  • 34
    • 36849040472 scopus 로고    scopus 로고
    • A role of RGS proteins in drug addiction
    • Hooks S.B., et al. A role of RGS proteins in drug addiction. Biochem. Pharmacol. 2008, 75:76-84.
    • (2008) Biochem. Pharmacol. , vol.75 , pp. 76-84
    • Hooks, S.B.1
  • 35
    • 34247640671 scopus 로고    scopus 로고
    • Evolving the lock to fit the key to create a family of G protein-coupled receptors potently activated by an inert ligand
    • Armbruster B.N., et al. Evolving the lock to fit the key to create a family of G protein-coupled receptors potently activated by an inert ligand. Proc. Natl. Acad. Sci. U. S. A. 2007, 104:5163-5168.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 5163-5168
    • Armbruster, B.N.1
  • 36
    • 72649084796 scopus 로고    scopus 로고
    • A chemical-genetic approach to study G protein regulation of β cell function in vivo
    • Guettier J.M., et al. A chemical-genetic approach to study G protein regulation of β cell function in vivo. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:19197-19202.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 19197-19202
    • Guettier, J.M.1
  • 37
    • 0036314216 scopus 로고    scopus 로고
    • Phasic insulin release and metabolic regulation in type 2 diabetes
    • Del Prato S., et al. Phasic insulin release and metabolic regulation in type 2 diabetes. Diabetes 2002, 51(Suppl. 1):S109-S116.
    • (2002) Diabetes , vol.51 , Issue.SUPPL. 1
    • Del Prato, S.1
  • 38
    • 0036314212 scopus 로고    scopus 로고
    • Modeling phasic insulin release: immediate and time-dependent effects of glucose
    • Nesher R., Cerasi E. Modeling phasic insulin release: immediate and time-dependent effects of glucose. Diabetes 2002, 51(Suppl. 1):S53-S59.
    • (2002) Diabetes , vol.51 , Issue.SUPPL. 1
    • Nesher, R.1    Cerasi, E.2
  • 39
    • 41349117978 scopus 로고    scopus 로고
    • Preservation of β-cell function by targeting β-cell mass
    • De Koning E.J., et al. Preservation of β-cell function by targeting β-cell mass. Trends Pharmacol. Sci. 2008, 29:218-227.
    • (2008) Trends Pharmacol. Sci. , vol.29 , pp. 218-227
    • De Koning, E.J.1
  • 40
    • 33744932973 scopus 로고    scopus 로고
    • Specific regulation of IRS-2 expression by glucose in rat primary pancreatic islet β-cells
    • Lingohr M.K., et al. Specific regulation of IRS-2 expression by glucose in rat primary pancreatic islet β-cells. J. Biol. Chem. 2006, 281:15884-15892.
    • (2006) J. Biol. Chem. , vol.281 , pp. 15884-15892
    • Lingohr, M.K.1
  • 41
    • 33748675684 scopus 로고    scopus 로고
    • On the role of IRS2 in the regulation of functional β-cell mass
    • Niessen M. On the role of IRS2 in the regulation of functional β-cell mass. Arch. Physiol. Biochem. 2006, 112:65-73.
    • (2006) Arch. Physiol. Biochem. , vol.112 , pp. 65-73
    • Niessen, M.1
  • 42
    • 33845432866 scopus 로고    scopus 로고
    • Regulating insulin signaling and β-cell function through IRS proteins
    • White M.F. Regulating insulin signaling and β-cell function through IRS proteins. Can. J. Physiol. Pharmacol. 2006, 84:725-737.
    • (2006) Can. J. Physiol. Pharmacol. , vol.84 , pp. 725-737
    • White, M.F.1
  • 43
    • 77953203933 scopus 로고    scopus 로고
    • 11-mediated signaling pathway is critical for autocrine potentiation of insulin secretion in mice
    • 11-mediated signaling pathway is critical for autocrine potentiation of insulin secretion in mice. J. Clin. Invest. 2010, 120:2184-2193.
    • (2010) J. Clin. Invest. , vol.120 , pp. 2184-2193
    • Sassmann, A.1
  • 44
    • 77953844541 scopus 로고    scopus 로고
    • Cholinergic augmentation of insulin release requires ankyrin-B
    • Healy J.A., et al. Cholinergic augmentation of insulin release requires ankyrin-B. Sci. Signal. 2010, 3:ra19.
    • (2010) Sci. Signal. , vol.3
    • Healy, J.A.1
  • 45
    • 58249087541 scopus 로고    scopus 로고
    • Regulation of PKD by the MAPK p38δ in insulin secretion and glucose homeostasis
    • Sumara G., et al. Regulation of PKD by the MAPK p38δ in insulin secretion and glucose homeostasis. Cell 2009, 136:235-248.
    • (2009) Cell , vol.136 , pp. 235-248
    • Sumara, G.1
  • 46
    • 0037389225 scopus 로고    scopus 로고
    • Mechanism of persistent protein kinase D1 translocation and activation
    • Oancea E., et al. Mechanism of persistent protein kinase D1 translocation and activation. Dev. Cell 2003, 4:561-574.
    • (2003) Dev. Cell , vol.4 , pp. 561-574
    • Oancea, E.1
  • 47
    • 17844398552 scopus 로고    scopus 로고
    • Inhibitory effects of antipsychotics on carbachol-enhanced insulin secretion from perifused rat islets: role of muscarinic antagonism in antipsychotic-induced diabetes and hyperglycemia
    • Johnson D.E., et al. Inhibitory effects of antipsychotics on carbachol-enhanced insulin secretion from perifused rat islets: role of muscarinic antagonism in antipsychotic-induced diabetes and hyperglycemia. Diabetes 2005, 54:1552-1558.
    • (2005) Diabetes , vol.54 , pp. 1552-1558
    • Johnson, D.E.1
  • 48
    • 77951844975 scopus 로고    scopus 로고
    • Teaching old receptors new tricks: biasing seven-transmembrane receptors
    • Rajagopal S., et al. Teaching old receptors new tricks: biasing seven-transmembrane receptors. Nat. Rev. Drug Discov. 2010, 9:373-386.
    • (2010) Nat. Rev. Drug Discov. , vol.9 , pp. 373-386
    • Rajagopal, S.1
  • 49
    • 77952712188 scopus 로고    scopus 로고
    • 3-muscarinic receptor regulates learning and memory in a receptor phosphorylation/arrestin-dependent manner
    • 3-muscarinic receptor regulates learning and memory in a receptor phosphorylation/arrestin-dependent manner. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:9440-9445.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 9440-9445
    • Poulin, B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.