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Volumn 125, Issue 12, 2015, Pages 4714-4728

GLP-1 stimulates insulin secretion by PKC-dependent TRPM4 and TRPM5 activation

(23)  Shigeto, Makoto a,b,c   Ramracheya, Reshma a   Tarasov, Andrei I a,d   Cha, Chae Young a,b   Chibalina, Margarita V a   Hastoy, Benoit a   Philippaert, Koenraad e   Reinbothe, Thomas b   Rorsman, Nils a,f   Salehi, Albert b   Sones, William R a   Vergari, Elisa a   Weston, Cathryn g   Gorelik, Julia h   Katsura, Masashi c   Nikolaev, Viacheslav O i   Vennekens, Rudi e   Zaccolo, Manuela f   Galione, Antony f   Johnson, Paul R V a,d   more..


Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM CHANNEL L TYPE; DIACYLGLYCEROL; ENZYME INHIBITOR; GLUCAGON LIKE PEPTIDE 1; INSULIN; ISRADIPINE; PROTEIN KINASE C; SODIUM ION; THAPSIGARGIN; TOLBUTAMIDE; TRANSIENT RECEPTOR POTENTIAL CHANNEL M4; TRANSIENT RECEPTOR POTENTIAL CHANNEL M5; PHORBOL 13 ACETATE 12 MYRISTATE; TRANSIENT RECEPTOR POTENTIAL CHANNEL M; TRPM4 PROTEIN, HUMAN; TRPM4 PROTEIN, MOUSE; TRPM5 PROTEIN, HUMAN; TRPM5 PROTEIN, MOUSE;

EID: 84948843973     PISSN: 00219738     EISSN: 15588238     Source Type: Journal    
DOI: 10.1172/JCI81975     Document Type: Article
Times cited : (143)

References (63)
  • 1
    • 79959936188 scopus 로고    scopus 로고
    • National regional and global trends in fasting plasma glucose and diabetes prevalence since 1980: Systematic analysis of health examination surveys and epidemiological studies with 370 country-years and 2.7 million participants
    • Danaei G, et al. National, regional, and global trends in fasting plasma glucose and diabetes prevalence since 1980: systematic analysis of health examination surveys and epidemiological studies with 370 country-years and 2.7 million participants. Lancet. 2011;378(9785):31-40.
    • (2011) Lancet. , vol.378 , Issue.9785 , pp. 31-40
    • Danaei, G.1
  • 2
    • 84875684003 scopus 로고    scopus 로고
    • Islet β cell mass in diabetes and how it relates to function, birth, and death
    • Weir GC, Bonner-Weir S. Islet β cell mass in diabetes and how it relates to function, birth, and death. Ann N Y Acad Sci. 2013;1281:92-105.
    • (2013) Ann N y Acad Sci. , vol.1281 , pp. 92-105
    • Weir, G.C.1    Bonner-Weir, S.2
  • 3
    • 84884538670 scopus 로고    scopus 로고
    • Dipeptidyl peptidase-4 inhibitors for the treatment of type 2 diabetes: Comparison, efficacy and safety
    • Deacon CF, Holst JJ. Dipeptidyl peptidase-4 inhibitors for the treatment of type 2 diabetes: comparison, efficacy and safety. Expert Opin Pharmacother. 2013;14(15):2047-2058.
    • (2013) Expert Opin Pharmacother. , vol.14 , Issue.15 , pp. 2047-2058
    • Deacon, C.F.1    Holst, J.J.2
  • 4
    • 84901462249 scopus 로고    scopus 로고
    • Cardiovascular actions of incretin-based therapies
    • Ussher JR, Drucker DJ. Cardiovascular actions of incretin-based therapies. Circ Res. 2014;114(11):1788-1803.
    • (2014) Circ Res. , vol.114 , Issue.11 , pp. 1788-1803
    • Ussher, J.R.1    Drucker, D.J.2
  • 5
    • 34147189738 scopus 로고    scopus 로고
    • The dipeptidyl peptidase IV inhibitor vildagliptin suppresses endogenous glucose production and enhances islet function after single-dose administration in type 2 diabetic patients
    • Balas B, et al. The dipeptidyl peptidase IV inhibitor vildagliptin suppresses endogenous glucose production and enhances islet function after single-dose administration in type 2 diabetic patients. J Clin Endocrinol Metab. 2007;92(4):1249-1255.
    • (2007) J Clin Endocrinol Metab. , vol.92 , Issue.4 , pp. 1249-1255
    • Balas, B.1
  • 8
    • 0036305993 scopus 로고    scopus 로고
    • Glucagon-like peptide-1 (GLP-1) and glucose metabolism in human myocytes
    • Luque MA, et al. Glucagon-like peptide-1 (GLP-1) and glucose metabolism in human myocytes. J Endocrinol. 2002;173(3):465-473.
    • (2002) J Endocrinol. , vol.173 , Issue.3 , pp. 465-473
    • Luque, M.A.1
  • 9
    • 0031731228 scopus 로고    scopus 로고
    • Effects of glucagon-like peptide 1 on the kinetics of glycogen synthase a in hepatocytes from normal and diabetic rats
    • Lopez-Delgado MI, Morales M, Villanueva-Penacarrillo ML, Malaisse WJ, Valverde I. Effects of glucagon-like peptide 1 on the kinetics of glycogen synthase a in hepatocytes from normal and diabetic rats. Endocrinology. 1998;139(6):2811-2817.
    • (1998) Endocrinology. , vol.139 , Issue.6 , pp. 2811-2817
    • Lopez-Delgado, M.I.1    Morales, M.2    Villanueva-Penacarrillo, M.L.3    Malaisse, W.J.4    Valverde, I.5
  • 11
    • 0027397282 scopus 로고
    • Presence and characterization of glucagon-like peptide-1(7-36) amide receptors in solubilized membranes of rat adipose tissue
    • Valverde I, Merida E, Delgado E, Trapote MA, Villanueva-Penacarrillo ML. Presence and characterization of glucagon-like peptide-1(7-36) amide receptors in solubilized membranes of rat adipose tissue. Endocrinology. 1993;132(1):75-79.
    • (1993) Endocrinology. , vol.132 , Issue.1 , pp. 75-79
    • Valverde, I.1    Merida, E.2    Delgado, E.3    Trapote, M.A.4    Villanueva-Penacarrillo, M.L.5
  • 12
    • 0026351810 scopus 로고
    • GLP-1(7-36) amide stimulates insulin secretion in rat islets: Studies on the mode of action
    • Fridolf T, Ahren B. GLP-1(7-36) amide stimulates insulin secretion in rat islets: studies on the mode of action. Diabetes Res. 1991;16(4):185-191.
    • (1991) Diabetes Res. , vol.16 , Issue.4 , pp. 185-191
    • Fridolf, T.1    Ahren, B.2
  • 14
    • 10644293820 scopus 로고    scopus 로고
    • Glucagon-like peptide-1: Regulation of insulin secretion and therapeutic potential
    • Gromada J, Brock B, Schmitz O, Rorsman P. Glucagon-like peptide-1: regulation of insulin secretion and therapeutic potential. Basic Clin Pharmacol Toxicol. 2004;95(6):252-262.
    • (2004) Basic Clin Pharmacol Toxicol. , vol.95 , Issue.6 , pp. 252-262
    • Gromada, J.1    Brock, B.2    Schmitz, O.3    Rorsman, P.4
  • 15
    • 33847617011 scopus 로고    scopus 로고
    • Mechanisms of action of glu-cagon-like peptide 1 in the pancreas
    • Doyle ME, Egan JM. Mechanisms of action of glu-cagon-like peptide 1 in the pancreas. Pharmacol Ther. 2007;113(3):546-593.
    • (2007) Pharmacol Ther. , vol.113 , Issue.3 , pp. 546-593
    • Doyle, M.E.1    Egan, J.M.2
  • 16
    • 0033760442 scopus 로고    scopus 로고
    • Triggering and amplifying pathways of regulation of insulin secretion by glucose
    • Henquin JC. Triggering and amplifying pathways of regulation of insulin secretion by glucose. Diabetes. 2000;49(11):1751-1760.
    • (2000) Diabetes. , vol.49 , Issue.11 , pp. 1751-1760
    • Henquin, J.C.1
  • 17
    • 0027184119 scopus 로고
    • Exendin-4 is a high potency agonist and truncated exendin-(9-39)-amide an antagonist at the glucagon-like peptide 1-(7-36)-amide receptor of insulin-secreting beta-cells
    • Goke R, et al. Exendin-4 is a high potency agonist and truncated exendin-(9-39)-amide an antagonist at the glucagon-like peptide 1-(7-36)-amide receptor of insulin-secreting beta-cells. J Biol Chem. 1993;268(26):19650-19655.
    • (1993) J Biol Chem. , vol.268 , Issue.26 , pp. 19650-19655
    • Goke, R.1
  • 18
    • 0034108646 scopus 로고    scopus 로고
    • Potent derivatives of glucagon-like peptide-1 with pharmacokinetic properties suitable for once daily administration
    • Knudsen LB, et al. Potent derivatives of glucagon-like peptide-1 with pharmacokinetic properties suitable for once daily administration. J Med Chem. 2000;43(9):1664-1669.
    • (2000) J Med Chem. , vol.43 , Issue.9 , pp. 1664-1669
    • Knudsen, L.B.1
  • 19
    • 35748957503 scopus 로고    scopus 로고
    • The physiology of glucagon-like peptide 1
    • Holst JJ. The physiology of glucagon-like peptide 1. Physiol Rev. 2007;87(4):1409-1439.
    • (2007) Physiol Rev. , vol.87 , Issue.4 , pp. 1409-1439
    • Holst, J.J.1
  • 20
    • 0037471354 scopus 로고    scopus 로고
    • Different role of intracellular loops of glucagon-like peptide-1 receptor in G-protein coupling
    • Bavec A, Hallbrink M, Langel U, Zorko M. Different role of intracellular loops of glucagon-like peptide-1 receptor in G-protein coupling. Regul Pept. 2003;111(1-3):137-144.
    • (2003) Regul Pept. , vol.111 , Issue.1-3 , pp. 137-144
    • Bavec, A.1    Hallbrink, M.2    Langel, U.3    Zorko, M.4
  • 21
    • 0035831283 scopus 로고    scopus 로고
    • Different domains in the third intracellular loop of the GLP-1 receptor are responsible for Galpha(s) and Galpha(i)/Galpha(o) activation
    • Hallbrink M, Holmqvist T, Olsson M, Ostenson CG, Efendic S, Langel U. Different domains in the third intracellular loop of the GLP-1 receptor are responsible for Galpha(s) and Galpha(i)/Galpha(o) activation. Biochim Biophys Acta. 2001;1546(1):79-86.
    • (2001) Biochim Biophys Acta. , vol.1546 , Issue.1 , pp. 79-86
    • Hallbrink, M.1    Holmqvist, T.2    Olsson, M.3    Ostenson, C.G.4    Efendic, S.5    Langel, U.6
  • 22
    • 0032941026 scopus 로고    scopus 로고
    • Pancreatic gluca-gon-like peptide-1 receptor couples to multiple G proteins and activates mitogen-activated protein kinase pathways in Chinese hamster ovary cells
    • Montrose-Rafizadeh C, et al. Pancreatic gluca-gon-like peptide-1 receptor couples to multiple G proteins and activates mitogen-activated protein kinase pathways in Chinese hamster ovary cells. Endocrinology. 1999;140(3):1132-1140.
    • (1999) Endocrinology. , vol.140 , Issue.3 , pp. 1132-1140
    • Montrose-Rafizadeh, C.1
  • 24
    • 0027473729 scopus 로고
    • Pancreatic beta-cells are rendered glucose-competent by the insulinotropic hormone glucagon-like peptide-1(7-37)
    • Holz GGt, Kuhtreiber WM, Habener JF. Pancreatic beta-cells are rendered glucose-competent by the insulinotropic hormone glucagon-like peptide-1(7-37). Nature. 1993;361(6410):362-365.
    • (1993) Nature. , vol.361 , Issue.6410 , pp. 362-365
    • GGt, H.1    Kuhtreiber, W.M.2    Habener, J.F.3
  • 25
    • 84924815340 scopus 로고    scopus 로고
    • + current properties in islet α-and β-cells reflect cell-specific Scn3a and Scn9a expression
    • + current properties in islet α-and β-cells reflect cell-specific Scn3a and Scn9a expression. J Physiol. 2014;592(pt 21):4677-4696.
    • (2014) J Physiol. , vol.592 , pp. 4677-4696
    • Zhang, Q.1
  • 26
    • 0030846483 scopus 로고    scopus 로고
    • Multisite regulation of insulin secretion by cAMP-increasing agonists: Evidence that glu-cagon-like peptide 1 and glucagon act via distinct receptors
    • Gromada J, Ding WG, Barg S, Renstrom E, Rors-man P. Multisite regulation of insulin secretion by cAMP-increasing agonists: evidence that glu-cagon-like peptide 1 and glucagon act via distinct receptors. Pflugers Arch. 1997;434(5):515-524.
    • (1997) Pflugers Arch. , vol.434 , Issue.5 , pp. 515-524
    • Gromada, J.1    Ding, W.G.2    Barg, S.3    Renstrom, E.4    Rors-Man, P.5
  • 27
    • 4444377903 scopus 로고    scopus 로고
    • Novel single chain cAMP sensors for receptor-induced signal propagation
    • Nikolaev VO, Bunemann M, Hein L, Han-nawacker A, Lohse MJ. Novel single chain cAMP sensors for receptor-induced signal propagation. J Biol Chem. 2004;279(36):37215-37218.
    • (2004) J Biol Chem. , vol.279 , Issue.36 , pp. 37215-37218
    • Nikolaev, V.O.1    Bunemann, M.2    Hein, L.3    Han-Nawacker, A.4    Lohse, M.J.5
  • 28
    • 33746907024 scopus 로고    scopus 로고
    • Subcellular dynamics of protein kinase A activity visualized by FRET-based reporters
    • Allen MD, Zhang J. Subcellular dynamics of protein kinase A activity visualized by FRET-based reporters. Biochem Biophys Res Commun. 2006;348(2):716-721.
    • (2006) Biochem Biophys Res Commun. , vol.348 , Issue.2 , pp. 716-721
    • Allen, M.D.1    Zhang, J.2
  • 30
    • 79955061032 scopus 로고    scopus 로고
    • Protein kinase D signaling: Multiple biological functions in health and disease
    • Rozengurt E. Protein kinase D signaling: multiple biological functions in health and disease. Physiology. 2011;26(1):23-33.
    • (2011) Physiology. , vol.26 , Issue.1 , pp. 23-33
    • Rozengurt, E.1
  • 31
    • 0028232708 scopus 로고
    • The role of protein kinase-C in signal transduction through vasopressin and acetylcholine receptors in pancreatic B-cells from normal mouse
    • Gao ZY, Gilon P, Henquin JC. The role of protein kinase-C in signal transduction through vasopressin and acetylcholine receptors in pancreatic B-cells from normal mouse. Endocrinology. 1994;135(1):191-199.
    • (1994) Endocrinology. , vol.135 , Issue.1 , pp. 191-199
    • Gao, Z.Y.1    Gilon, P.2    Henquin, J.C.3
  • 33
    • 84904546714 scopus 로고    scopus 로고
    • Investigating G protein signalling bias at the glucagon-like peptide-1 receptor in yeast
    • Weston C, Poyner D, Patel V, Dowell S, Ladds G. Investigating G protein signalling bias at the glucagon-like peptide-1 receptor in yeast. Br J Pharmacol. 2014;171(15):3651-3665.
    • (2014) Br J Pharmacol. , vol.171 , Issue.15 , pp. 3651-3665
    • Weston, C.1    Poyner, D.2    Patel, V.3    Dowell, S.4    Ladds, G.5
  • 35
    • 82455205940 scopus 로고    scopus 로고
    • Electrophysiology of pancreatic β-cells in intact mouse islets of Langerhans
    • Rorsman P, Eliasson L, Kanno T, Zhang Q, Gopel S. Electrophysiology of pancreatic β-cells in intact mouse islets of Langerhans. Prog Biophys Mol Biol. 2011;107(2):224-235.
    • (2011) Prog Biophys Mol Biol. , vol.107 , Issue.2 , pp. 224-235
    • Rorsman, P.1    Eliasson, L.2    Kanno, T.3    Zhang, Q.4    Gopel, S.5
  • 36
    • 84888011324 scopus 로고    scopus 로고
    • Glucose principally regulates insulin secretion in mouse islets by controlling the numbers of granule fusion events per cell
    • Low JT, et al. Glucose principally regulates insulin secretion in mouse islets by controlling the numbers of granule fusion events per cell. Diabetologia. 2013;56(12):2629-2637.
    • (2013) Diabetologia. , vol.56 , Issue.12 , pp. 2629-2637
    • Low, J.T.1
  • 37
    • 42449108189 scopus 로고    scopus 로고
    • 2+ signal that is essential for insulin secretion in mouse pancreatic islets
    • 2+ signal that is essential for insulin secretion in mouse pancreatic islets. Diabetes. 2008;57(4):868-878.
    • (2008) Diabetes. , vol.57 , Issue.4 , pp. 868-878
    • Kim, B.J.1
  • 39
    • 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(2):235-248.
    • (2009) Cell. , vol.136 , Issue.2 , pp. 235-248
    • Sumara, G.1
  • 40
    • 0026043449 scopus 로고
    • GLP-1(7-36)amide-stimulated insulin secretion in rat islets is sodium-dependent
    • Fridolf T, Ahren B. GLP-1(7-36)amide-stimulated insulin secretion in rat islets is sodium-dependent. Biochem Biophys Res Commun. 1991;179(1):701-706.
    • (1991) Biochem Biophys Res Commun. , vol.179 , Issue.1 , pp. 701-706
    • Fridolf, T.1    Ahren, B.2
  • 41
    • 0029867644 scopus 로고    scopus 로고
    • GLP-1 depolarizes the rat pancreatic beta cell in a Na(+)-dependent manner
    • Kato M, Ma HT, Tatemoto K. GLP-1 depolarizes the rat pancreatic beta cell in a Na(+)-dependent manner. Regul Pept. 1996;62(1):23-27.
    • (1996) Regul Pept. , vol.62 , Issue.1 , pp. 23-27
    • Kato, M.1    Ma, H.T.2    Tatemoto, K.3
  • 42
    • 0043234534 scopus 로고    scopus 로고
    • 2+-activated cation channel TRPM4
    • 2+-activated cation channel TRPM4. J Biol Chem. 2003;278(33):30813-30820.
    • (2003) J Biol Chem. , vol.278 , Issue.33 , pp. 30813-30820
    • Nilius, B.1
  • 43
    • 33846940717 scopus 로고    scopus 로고
    • Insights into TRPM4 function, regulation and physiological role
    • Vennekens R, Nilius B. Insights into TRPM4 function, regulation and physiological role. Handb Exp Pharmacol. 2007;(179):269-285.
    • (2007) Handb Exp Pharmacol. , Issue.179 , pp. 269-285
    • Vennekens, R.1    Nilius, B.2
  • 44
    • 33846901590 scopus 로고    scopus 로고
    • TRPM5 and taste transduction
    • Liman ER. TRPM5 and taste transduction. Handb Exp Pharmacol. 2007;(179):287-298.
    • (2007) Handb Exp Pharmacol. , Issue.179 , pp. 287-298
    • Liman, E.R.1
  • 45
    • 0034880655 scopus 로고    scopus 로고
    • Determinants of the impaired secretion of glucagon-like peptide-1 in type 2 diabetic patients
    • Toft-Nielsen MB, et al. Determinants of the impaired secretion of glucagon-like peptide-1 in type 2 diabetic patients. J Clin Endocrinol Metab. 2001;86(8):3717-3723.
    • (2001) J Clin Endocrinol Metab. , vol.86 , Issue.8 , pp. 3717-3723
    • Toft-Nielsen, M.B.1
  • 46
    • 0033303516 scopus 로고    scopus 로고
    • Glucagon-like peptide-1-(7-36)amide is transformed to glucagon-like peptide-1-(9-36)amide by dipeptidyl peptidase IV in the capillaries supplying the L cells of the porcine intestine
    • Hansen L, Deacon CF, Orskov C, Holst JJ. Glucagon-like peptide-1-(7-36)amide is transformed to glucagon-like peptide-1-(9-36)amide by dipeptidyl peptidase IV in the capillaries supplying the L cells of the porcine intestine. Endocrinology. 1999;140(11) 5356-5363.
    • (1999) Endocrinology. , vol.140 , Issue.11 , pp. 5356-5363
    • Hansen, L.1    Deacon, C.F.2    Orskov, C.3    Holst, J.J.4
  • 47
    • 0025266913 scopus 로고
    • Glucagon-like peptide-I analogs: Effects on insulin secretion and adenosine 3', 5'-monophosphate formation
    • Gefel D, Hendrick GK, Mojsov S, Habener J, Weir GC. Glucagon-like peptide-I analogs: effects on insulin secretion and adenosine 3', 5'-monophosphate formation. Endocrinology. 1990;126(4):2164-2168.
    • (1990) Endocrinology. , vol.126 , Issue.4 , pp. 2164-2168
    • Gefel, D.1    Hendrick, G.K.2    Mojsov, S.3    Habener, J.4    Weir, G.C.5
  • 48
    • 3042792777 scopus 로고    scopus 로고
    • Comparative effects of GLP-1 and GIP on cAMP production insulin secretion and in vivo antidiabetic actions following substitution of Ala8/Ala2 with 2-aminobutyric acid
    • Green BD, Gault VA, Flatt PR, Harriott P, Greer B, O'Harte FP. Comparative effects of GLP-1 and GIP on cAMP production, insulin secretion, and in vivo antidiabetic actions following substitution of Ala8/Ala2 with 2-aminobutyric acid. Arch Biochem Biophys. 2004;428(2):136-143.
    • (2004) Arch Biochem Biophys. , vol.428 , Issue.2 , pp. 136-143
    • Green, B.D.1    Gault, V.A.2    Flatt, P.R.3    Harriott, P.4    Greer, B.5    O'Harte, F.P.6
  • 49
    • 17844399596 scopus 로고    scopus 로고
    • Glucagon-like peptide-1 mediates the therapeutic actions of DPP-IV inhibitors
    • Holst JJ, Deacon CF. Glucagon-like peptide-1 mediates the therapeutic actions of DPP-IV inhibitors. Diabetologia. 2005;48(4):612-615.
    • (2005) Diabetologia. , vol.48 , Issue.4 , pp. 612-615
    • Holst, J.J.1    Deacon, C.F.2
  • 50
    • 0029149848 scopus 로고
    • Glucagon-like peptide i increases cytoplasmic calcium in insulin-secreting beta TC3-cells by enhancement of intracellular calcium mobilization
    • Gromada J, et al. Glucagon-like peptide I increases cytoplasmic calcium in insulin-secreting beta TC3-cells by enhancement of intracellular calcium mobilization. Diabetes. 1995;44(7):767-774.
    • (1995) Diabetes. , vol.44 , Issue.7 , pp. 767-774
    • Gromada, J.1
  • 51
    • 56649117651 scopus 로고    scopus 로고
    • Low, but physiological, concentration of GLP-1 stimulates insulin secretion independent of the cAMP-dependent protein kinase pathway
    • Shigeto M, Katsura M, Matsuda M, Ohkuma S, Kaku K. Low, but physiological, concentration of GLP-1 stimulates insulin secretion independent of the cAMP-dependent protein kinase pathway J Pharmacol Sci. 2008;108(3):274-279.
    • (2008) J Pharmacol Sci. , vol.108 , Issue.3 , pp. 274-279
    • Shigeto, M.1    Katsura, M.2    Matsuda, M.3    Ohkuma, S.4    Kaku, K.5
  • 52
    • 58149375854 scopus 로고    scopus 로고
    • Effect of glucagon-like peptide-1 on p-and a-cell function in isolated islet and whole pancreas transplant recipients
    • Rickels MR, Mueller R, Markmann JF, Naji A. Effect of glucagon-like peptide-1 on p-and a-cell function in isolated islet and whole pancreas transplant recipients. J Clin Endocrinol Metab. 2009;94(1):181-189.
    • (2009) J Clin Endocrinol Metab. , vol.94 , Issue.1 , pp. 181-189
    • Rickels, M.R.1    Mueller, R.2    Markmann, J.F.3    Naji, A.4
  • 53
    • 34247844682 scopus 로고    scopus 로고
    • Increased IgE-dependent mast cell activation and anaphylactic responses in mice lacking the calcium-activated nonse-lective cation channel TRPM4
    • Vennekens R, et al. Increased IgE-dependent mast cell activation and anaphylactic responses in mice lacking the calcium-activated nonse-lective cation channel TRPM4. Nat Immunol. 2007;8(3):312-320.
    • (2007) Nat Immunol. , vol.8 , Issue.3 , pp. 312-320
    • Vennekens, R.1
  • 54
    • 84907814142 scopus 로고    scopus 로고
    • TPC1 has two variant isoforms, and their removal has different effects on endo-lysosomal functions compared to loss of TPC2
    • Ruas M, et al. TPC1 has two variant isoforms, and their removal has different effects on endo-lysosomal functions compared to loss of TPC2. Mol Cell Biol. 2014;34(21):3981-3992.
    • (2014) Mol Cell Biol. , vol.34 , Issue.21 , pp. 3981-3992
    • Ruas, M.1
  • 55
    • 67349287016 scopus 로고    scopus 로고
    • NAADP mobilizes calcium from acidic organelles through two-pore channels
    • Calcraft PJ, et al. NAADP mobilizes calcium from acidic organelles through two-pore channels. Nature. 2009;459(7246):596-600.
    • (2009) Nature. , vol.459 , Issue.7246 , pp. 596-600
    • Calcraft, P.J.1
  • 56
    • 0024532674 scopus 로고
    • Large-scale purification of human islets utilizing discontinuous albumin gradient on IBM 2991 cell separator
    • Lake SP, et al. Large-scale purification of human islets utilizing discontinuous albumin gradient on IBM 2991 cell separator. Diabetes. 1989;38(suppl 1):143-145.
    • (1989) Diabetes. , vol.38 , pp. 143-145
    • Lake, S.P.1
  • 58
    • 0027235323 scopus 로고
    • Calcium-independent potentiation of insulin release by cyclic AMP in single β-cells
    • Ammala C, Ashcroft FM, Rorsman P. Calcium-independent potentiation of insulin release by cyclic AMP in single β-cells. Nature. 1993;363(6427):356-358.
    • (1993) Nature. , vol.363 , Issue.6427 , pp. 356-358
    • Ammala, C.1    Ashcroft, F.M.2    Rorsman, P.3
  • 59
    • 0027763496 scopus 로고
    • Exocytosis elicited by action potentials and voltage-clamp calcium currents in individual mouse pancreatic B-cells
    • Ammala C, Eliasson L, Bokvist K, Larsson O, Ashcroft FM, Rorsman P. Exocytosis elicited by action potentials and voltage-clamp calcium currents in individual mouse pancreatic B-cells. J Physiol. 1993;472:665-688.
    • (1993) J Physiol. , vol.472 , pp. 665-688
    • Ammala, C.1    Eliasson, L.2    Bokvist, K.3    Larsson, O.4    Ashcroft, F.M.5    Rorsman, P.6
  • 60
    • 48249083049 scopus 로고    scopus 로고
    • Voltage-gated ion channels in human pancreatic β-cells: Electrophysiological characterization and role in insulin secretion
    • Braun M, et al. Voltage-gated ion channels in human pancreatic β-cells: electrophysiological characterization and role in insulin secretion. Diabetes. 2008;57(6):1618-1628.
    • (2008) Diabetes. , vol.57 , Issue.6 , pp. 1618-1628
    • Braun, M.1
  • 61
    • 0344339740 scopus 로고    scopus 로고
    • Activation of Ca(2+)-dependent K(+) channels contributes to rhythmic firing of action potentials in mouse pancreatic β cells
    • Gopel SO, et al. Activation of Ca(2+)-dependent K(+) channels contributes to rhythmic firing of action potentials in mouse pancreatic β cells. J Gen Phys iol. 1999;114(6):759-770.
    • (1999) J Gen Phys Iol. , vol.114 , Issue.6 , pp. 759-770
    • Gopel, S.O.1
  • 62
    • 61749086774 scopus 로고    scopus 로고
    • Expression of an activating mutation in the gene encoding the KATP channel subunit Kir6.2 in mouse pancreatic β cells recapitulates neonatal diabetes
    • Girard CA, et al. Expression of an activating mutation in the gene encoding the KATP channel subunit Kir6.2 in mouse pancreatic β cells recapitulates neonatal diabetes. J Clin Invest. 2009;119(1):80-90.
    • (2009) J Clin Invest. , vol.119 , Issue.1 , pp. 80-90
    • Girard, C.A.1
  • 63
    • 84901913372 scopus 로고    scopus 로고
    • Optogenetic control of insulin secretion in intact pancreatic islets with β-cell-specific expression of Channelrhodopsin-2
    • Reinbothe TM, Safi F, Axelsson AS, Mollet IG, Rosengren AH. Optogenetic control of insulin secretion in intact pancreatic islets with β-cell-specific expression of Channelrhodopsin-2. Islets. 2014;6(1):e28095.
    • (2014) Islets. , vol.6 , Issue.1 , pp. e28095
    • Reinbothe, T.M.1    Safi, F.2    Axelsson, A.S.3    Mollet, I.G.4    Rosengren, A.H.5


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