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Volumn 49, Issue 2, 2011, Pages 89-99

CAMP increases the sensitivity of exocytosis to Ca2+ primarily through protein kinase A in mouse pancreatic beta cells

Author keywords

Pancreatic beta cells

Indexed keywords

ADENOSINE DERIVATIVE; CALCIUM ION; CYCLIC AMP; CYCLIC AMP DEPENDENT PROTEIN KINASE; GUANINE NUCLEOTIDE EXCHANGE FACTOR; INSULIN; N6 PHENYLADENOSINE 3',5' CYCLIC MONOPHOSPHATE; UNCLASSIFIED DRUG;

EID: 79952040814     PISSN: 01434160     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceca.2010.12.005     Document Type: Article
Times cited : (49)

References (50)
  • 1
    • 34047149839 scopus 로고    scopus 로고
    • Cx36-mediated coupling reduces beta-cell heterogeneity, confines the stimulating glucose concentration range, and affects insulin release kinetics
    • Speier S., Gjinovci A., Charollais A., Meda P., Rupnik M. Cx36-mediated coupling reduces beta-cell heterogeneity, confines the stimulating glucose concentration range, and affects insulin release kinetics. Diabetes 2007, 56:1078-1086.
    • (2007) Diabetes , vol.56 , pp. 1078-1086
    • Speier, S.1    Gjinovci, A.2    Charollais, A.3    Meda, P.4    Rupnik, M.5
  • 2
    • 0033556082 scopus 로고    scopus 로고
    • Molecular mechanisms and regulation of insulin exocytosis as a paradigm of endocrine secretion
    • Lang J. Molecular mechanisms and regulation of insulin exocytosis as a paradigm of endocrine secretion. Eur. J. Biochem. 1999, 259:3-17.
    • (1999) Eur. J. Biochem. , vol.259 , pp. 3-17
    • Lang, J.1
  • 3
    • 0034511895 scopus 로고    scopus 로고
    • Beta-granule transport and exocytosis
    • Easom R.A. Beta-granule transport and exocytosis. Semin. Cell Dev. Biol. 2000, 11:253-266.
    • (2000) Semin. Cell Dev. Biol. , vol.11 , pp. 253-266
    • Easom, R.A.1
  • 4
    • 0027235323 scopus 로고
    • Calcium-independent potentiation of insulin release by cyclic AMP in single beta-cells
    • Ammala C., Ashcroft F.M., Rorsman P. Calcium-independent potentiation of insulin release by cyclic AMP in single beta-cells. Nature 1993, 363:356-358.
    • (1993) Nature , vol.363 , pp. 356-358
    • Ammala, C.1    Ashcroft, F.M.2    Rorsman, P.3
  • 5
    • 0029797647 scopus 로고    scopus 로고
    • Regulation of insulin secretion by phospholipase C
    • Zawalich W.S., Zawalich K.C. Regulation of insulin secretion by phospholipase C. Am. J. Physiol. 1996, 271:409-416.
    • (1996) Am. J. Physiol. , vol.271 , pp. 409-416
    • Zawalich, W.S.1    Zawalich, K.C.2
  • 6
    • 0030792753 scopus 로고    scopus 로고
    • Protein kinase A-dependent and -independent stimulation of exocytosis by cAMP in mouse pancreatic B-cells
    • Renström E., Eliasson L., Rorsman P. Protein kinase A-dependent and -independent stimulation of exocytosis by cAMP in mouse pancreatic B-cells. J. Physiol. 1997, 502:105-118.
    • (1997) J. Physiol. , vol.502 , pp. 105-118
    • Renström, E.1    Eliasson, L.2    Rorsman, P.3
  • 7
    • 0037378045 scopus 로고    scopus 로고
    • Secretory granule exocytosis
    • Burgoyne R.D., Morgan A. Secretory granule exocytosis. Physiol. Rev. 2003, 83:581-632.
    • (2003) Physiol. Rev. , vol.83 , pp. 581-632
    • Burgoyne, R.D.1    Morgan, A.2
  • 8
    • 3242730474 scopus 로고    scopus 로고
    • Role of incretin hormones in the regulation of insulin secretion in diabetic and nondiabetic humans
    • Holst J.J., Gromada J. Role of incretin hormones in the regulation of insulin secretion in diabetic and nondiabetic humans. Am. J. Physiol. Endocrinol. Metab. 2004, 287:E199-206.
    • (2004) Am. J. Physiol. Endocrinol. Metab. , vol.287
    • Holst, J.J.1    Gromada, J.2
  • 9
    • 25444520038 scopus 로고    scopus 로고
    • PKA-dependent and PKA-independent pathways for cAMP-regulated exocytosis
    • Seino S., Shibasaki T. PKA-dependent and PKA-independent pathways for cAMP-regulated exocytosis. Physiol. Rev. 2005, 85:1303-1342.
    • (2005) Physiol. Rev. , vol.85 , pp. 1303-1342
    • Seino, S.1    Shibasaki, T.2
  • 10
    • 0028054814 scopus 로고
    • Increased transmitter release at excitatory synapses produced by direct activation of adenylate cyclase in rat hippocampal slices
    • Chavez-Noriega L.E., Stevens C.F. Increased transmitter release at excitatory synapses produced by direct activation of adenylate cyclase in rat hippocampal slices. J. Neurosci. 1994, 14:310-317.
    • (1994) J. Neurosci. , vol.14 , pp. 310-317
    • Chavez-Noriega, L.E.1    Stevens, C.F.2
  • 12
    • 0041843655 scopus 로고    scopus 로고
    • Distinct potentiation of L-type currents and secretion by cAMP in rat chromaffin cells
    • Carabelli V., Giancippoli A., Baldelli P., Carbone E., Artalejo A.R. Distinct potentiation of L-type currents and secretion by cAMP in rat chromaffin cells. Biophys. J. 2003, 85:1326-1337.
    • (2003) Biophys. J. , vol.85 , pp. 1326-1337
    • Carabelli, V.1    Giancippoli, A.2    Baldelli, P.3    Carbone, E.4    Artalejo, A.R.5
  • 13
    • 0029774271 scopus 로고    scopus 로고
    • Dopamine (D2) receptor regulation of intracellular calcium and membrane capacitance changes in rat melanotrophs
    • Lee A.K., Dopamine (D2) receptor regulation of intracellular calcium and membrane capacitance changes in rat melanotrophs. J. Physiol. 1996, 495(Pt 3):627-640.
    • (1996) J. Physiol. , vol.495 , Issue.PART 3 , pp. 627-640
    • Lee, A.K.1
  • 14
    • 0032530616 scopus 로고    scopus 로고
    • Modulation of the unitary exocytic event amplitude by cAMP in rat melanotrophs
    • Sikdar S.K., Kreft M., Zorec R. Modulation of the unitary exocytic event amplitude by cAMP in rat melanotrophs. J. Physiol. 1998, 511(Pt 3):851-859.
    • (1998) J. Physiol. , vol.511 , Issue.PART 3 , pp. 851-859
    • Sikdar, S.K.1    Kreft, M.2    Zorec, R.3
  • 15
    • 0037337832 scopus 로고    scopus 로고
    • SUR1 regulates PKA-independent cAMP-induced granule priming in mouse pancreatic B-cells
    • Eliasson L., Ma X., Renstrom E., et al. SUR1 regulates PKA-independent cAMP-induced granule priming in mouse pancreatic B-cells. J. Gen. Physiol. 2003, 121:181-197.
    • (2003) J. Gen. Physiol. , vol.121 , pp. 181-197
    • Eliasson, L.1    Ma, X.2    Renstrom, E.3
  • 16
    • 10344258585 scopus 로고    scopus 로고
    • Protein kinase activation increases insulin secretion by sensitizing the secretory machinery to Ca2+
    • Wan Q.F., Dong Y., Yang H., Lou X., Ding J., Xu T. Protein kinase activation increases insulin secretion by sensitizing the secretory machinery to Ca2+. J. Gen. Physiol. 2004, 124:653-662.
    • (2004) J. Gen. Physiol. , vol.124 , pp. 653-662
    • Wan, Q.F.1    Dong, Y.2    Yang, H.3    Lou, X.4    Ding, J.5    Xu, T.6
  • 17
    • 25844507819 scopus 로고    scopus 로고
    • CAMP increases Ca2+-dependent exocytosis through both PKA and Epac2 in mouse melanotrophs from pituitary tissue slices
    • Sedej S., Rose T., Rupnik M. cAMP increases Ca2+-dependent exocytosis through both PKA and Epac2 in mouse melanotrophs from pituitary tissue slices. J. Physiol. 2005, 567:799-813.
    • (2005) J. Physiol. , vol.567 , pp. 799-813
    • Sedej, S.1    Rose, T.2    Rupnik, M.3
  • 18
    • 34547114234 scopus 로고    scopus 로고
    • Two cAMP-dependent pathways differentially regulate exocytosis of large dense-core and small vesicles in mouse beta-cells
    • Hatakeyama H., Takahashi N., Kishimoto T., Nemoto T., Kasai H. Two cAMP-dependent pathways differentially regulate exocytosis of large dense-core and small vesicles in mouse beta-cells. J. Physiol. 2007, 582:1087-1098.
    • (2007) J. Physiol. , vol.582 , pp. 1087-1098
    • Hatakeyama, H.1    Takahashi, N.2    Kishimoto, T.3    Nemoto, T.4    Kasai, H.5
  • 19
    • 40049101849 scopus 로고    scopus 로고
    • Role of the cAMP sensor Epac as a determinant of KATP channel ATP sensitivity in human pancreatic beta-cells and rat INS-1 cells
    • Kang G., Leech C.A., Chepurny O.G., Coetzee W.A., Holz G.G. Role of the cAMP sensor Epac as a determinant of KATP channel ATP sensitivity in human pancreatic beta-cells and rat INS-1 cells. J. Physiol. 2008, 586:1307-1319.
    • (2008) J. Physiol. , vol.586 , pp. 1307-1319
    • Kang, G.1    Leech, C.A.2    Chepurny, O.G.3    Coetzee, W.A.4    Holz, G.G.5
  • 21
    • 68149136367 scopus 로고    scopus 로고
    • The cAMP sensor Epac2 is a direct target of antidiabetic sulfonylurea drugs
    • Zhang C.-L., Katoh M., Shibasaki T., et al. The cAMP sensor Epac2 is a direct target of antidiabetic sulfonylurea drugs. Science 2009, 325:607-610.
    • (2009) Science , vol.325 , pp. 607-610
    • Zhang, C.-L.1    Katoh, M.2    Shibasaki, T.3
  • 22
    • 0347990624 scopus 로고    scopus 로고
    • Epac: a new cAMP-binding protein in support of glucagon-like peptide-1 receptor-mediated signal transduction in the pancreatic B-cell
    • Holz G.G. Epac: a new cAMP-binding protein in support of glucagon-like peptide-1 receptor-mediated signal transduction in the pancreatic B-cell. Diabetes 2004, 53:5-13.
    • (2004) Diabetes , vol.53 , pp. 5-13
    • Holz, G.G.1
  • 23
    • 12244305595 scopus 로고    scopus 로고
    • New insights concerning the glucose-dependent insulin secretagogue action of glucagon-like peptide-1 in pancreatic beta-cells
    • Holz G.G. New insights concerning the glucose-dependent insulin secretagogue action of glucagon-like peptide-1 in pancreatic beta-cells. Horm. Metab. Res. 2004, 36:787-794.
    • (2004) Horm. Metab. Res. , vol.36 , pp. 787-794
    • Holz, G.G.1
  • 24
    • 85047680153 scopus 로고    scopus 로고
    • Ca2+/calmodulin and cyclic 3,5′ adenosine monophosphate control movement of secretory granules through protein phosphorylation/dephosphorylation in the pancreatic beta-cell
    • Hisatomi M., Hidaka H., Niki I. Ca2+/calmodulin and cyclic 3,5′ adenosine monophosphate control movement of secretory granules through protein phosphorylation/dephosphorylation in the pancreatic beta-cell. Endocrinology 1996, 137:4644-4649.
    • (1996) Endocrinology , vol.137 , pp. 4644-4649
    • Hisatomi, M.1    Hidaka, H.2    Niki, I.3
  • 25
    • 0036606587 scopus 로고    scopus 로고
    • Phosphorylation-dependent interaction of the synaptic vesicle proteins cysteine string protein and synaptotagmin I
    • Evans G.J., Morgan A. Phosphorylation-dependent interaction of the synaptic vesicle proteins cysteine string protein and synaptotagmin I. Biochem. J. 2002, 364:343-347.
    • (2002) Biochem. J. , vol.364 , pp. 343-347
    • Evans, G.J.1    Morgan, A.2
  • 26
    • 0035071322 scopus 로고    scopus 로고
    • Phosphorylation of Snapin by PKA modulates its interaction with the SNARE complex
    • Chheda M.G., Ashery U., Thakur P., Rettig J., Sheng Z.H. Phosphorylation of Snapin by PKA modulates its interaction with the SNARE complex. Nat. Cell Biol. 2001, 3:331-338.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 331-338
    • Chheda, M.G.1    Ashery, U.2    Thakur, P.3    Rettig, J.4    Sheng, Z.H.5
  • 27
    • 37649002935 scopus 로고    scopus 로고
    • Essential role of Epac2/Rap1 signaling in regulation of insulin granule dynamics by cAMP
    • Shibasaki T., Takahashi H., Miki T., et al. Essential role of Epac2/Rap1 signaling in regulation of insulin granule dynamics by cAMP. Proc. Natl. Acad. Sci. 2007, 104:19333-19338.
    • (2007) Proc. Natl. Acad. Sci. , vol.104 , pp. 19333-19338
    • Shibasaki, T.1    Takahashi, H.2    Miki, T.3
  • 28
    • 0035824548 scopus 로고    scopus 로고
    • Critical role of cAMP-GEFII·Rim2 complex in incretin-potentiated insulin secretion
    • Kashima Y., Miki T., Shibasaki T., et al. Critical role of cAMP-GEFII·Rim2 complex in incretin-potentiated insulin secretion. J. Biol. Chem. 2001, 276:46046-46053.
    • (2001) J. Biol. Chem. , vol.276 , pp. 46046-46053
    • Kashima, Y.1    Miki, T.2    Shibasaki, T.3
  • 29
    • 0037184610 scopus 로고    scopus 로고
    • Piccolo, a Ca2+ sensor in pancreatic β-cells
    • Fujimoto K., Shibasaki T., Yokoi N., et al. Piccolo, a Ca2+ sensor in pancreatic β-cells. J. Biol. Chem. 2002, 277:50497-50502.
    • (2002) J. Biol. Chem. , vol.277 , pp. 50497-50502
    • Fujimoto, K.1    Shibasaki, T.2    Yokoi, N.3
  • 30
    • 0042329356 scopus 로고    scopus 로고
    • A novel approach to in situ characterization of pancreatic β-cells
    • Speier S., Rupnik M. A novel approach to in situ characterization of pancreatic β-cells. Pflüg. Arch. Eur. J. Physiol. 2003, 446:553-558.
    • (2003) Pflüg. Arch. Eur. J. Physiol. , vol.446 , pp. 553-558
    • Speier, S.1    Rupnik, M.2
  • 31
    • 0013657423 scopus 로고
    • Discrete changes of cell membrane capacitance observed under conditions of enhanced secretion in bovine adrenal chromaffin cells
    • Neher E., Marty A. Discrete changes of cell membrane capacitance observed under conditions of enhanced secretion in bovine adrenal chromaffin cells. Proc. Natl. Acad. Sci. U.S.A. 1982, 79:6712-6716.
    • (1982) Proc. Natl. Acad. Sci. U.S.A. , vol.79 , pp. 6712-6716
    • Neher, E.1    Marty, A.2
  • 32
    • 0027937697 scopus 로고
    • Releasable pools and the kinetics of exocytosis in adrenal chromaffin cells
    • Horrigan F.T., Bookman R.J. Releasable pools and the kinetics of exocytosis in adrenal chromaffin cells. Neuron 1994, 13:1119-1129.
    • (1994) Neuron , vol.13 , pp. 1119-1129
    • Horrigan, F.T.1    Bookman, R.J.2
  • 33
    • 0027338262 scopus 로고
    • A low affinity Ca2+ receptor controls the final steps in peptide secretion from pituitary melanotrophs
    • Thomas P., Wong J.G., Lee A.K., Almers W. A low affinity Ca2+ receptor controls the final steps in peptide secretion from pituitary melanotrophs. Neuron 1993, 11:93-104.
    • (1993) Neuron , vol.11 , pp. 93-104
    • Thomas, P.1    Wong, J.G.2    Lee, A.K.3    Almers, W.4
  • 34
    • 0042879951 scopus 로고    scopus 로고
    • Insulin granule dynamics in pancreatic beta cells
    • Rorsman P., Renstrom E. Insulin granule dynamics in pancreatic beta cells. Diabetologia 2003, 46:1029-1045.
    • (2003) Diabetologia , vol.46 , pp. 1029-1045
    • Rorsman, P.1    Renstrom, E.2
  • 35
    • 1642443172 scopus 로고    scopus 로고
    • Voltage-activated Ca(2+) channels and their role in the endocrine function of the pituitary gland in newborn and adult mice
    • Sedej S., Tsujimoto T., Zorec R., Rupnik M. Voltage-activated Ca(2+) channels and their role in the endocrine function of the pituitary gland in newborn and adult mice. J. Physiol. 2004, 555:769-782.
    • (2004) J. Physiol. , vol.555 , pp. 769-782
    • Sedej, S.1    Tsujimoto, T.2    Zorec, R.3    Rupnik, M.4
  • 36
    • 34249781153 scopus 로고    scopus 로고
    • Ca2+-secretion coupling is impaired in diabetic Goto Kakizaki rats
    • Rose T., Efendic S., Rupnik M. Ca2+-secretion coupling is impaired in diabetic Goto Kakizaki rats. J. Gen. Physiol. 2007, 129:493-508.
    • (2007) J. Gen. Physiol. , vol.129 , pp. 493-508
    • Rose, T.1    Efendic, S.2    Rupnik, M.3
  • 37
    • 0030874610 scopus 로고    scopus 로고
    • Rapid ATP-dependent priming of secretory granules precedes Ca(2+)-induced exocytosis in mouse pancreatic B-cells
    • Eliasson L., Renstrom E., Ding W.G., Proks P., Rorsman P. Rapid ATP-dependent priming of secretory granules precedes Ca(2+)-induced exocytosis in mouse pancreatic B-cells. J. Physiol. 1997, 503:399-412.
    • (1997) J. Physiol. , vol.503 , pp. 399-412
    • Eliasson, L.1    Renstrom, E.2    Ding, W.G.3    Proks, P.4    Rorsman, P.5
  • 38
    • 0024564947 scopus 로고
    • Comparison of the two classes of binding sites (A and B) of type I and type II cyclic-AMP-dependent protein kinases by using cyclic nucleotide analogs
    • Dagfinn R.G., Roald E., Robert H.S., Jon P.M., Stein Ove D.Ř.S. Comparison of the two classes of binding sites (A and B) of type I and type II cyclic-AMP-dependent protein kinases by using cyclic nucleotide analogs. Eur. J. Biochem. 1989, 181:19-31.
    • (1989) Eur. J. Biochem. , vol.181 , pp. 19-31
    • Dagfinn, R.G.1    Roald, E.2    Robert, H.S.3    Jon, P.M.4    Stein Ove, D.Ř.S.5
  • 39
    • 0037022308 scopus 로고    scopus 로고
    • The SNARE protein SNAP-25 is linked to fast calcium triggering of exocytosis
    • Sørensen J.B., Matti U., Wei S.-H., et al. The SNARE protein SNAP-25 is linked to fast calcium triggering of exocytosis. Proc. Natl. Acad. Sci. U.S.A. 2002, 99:1627-1632.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 1627-1632
    • Sørensen, J.B.1    Matti, U.2    Wei, S.-H.3
  • 40
    • 45849136363 scopus 로고    scopus 로고
    • CAPS facilitates filling of the rapidly releasable pool of large dense-core vesicles
    • Liu Y., Schirra C., Stevens D.R., et al. CAPS facilitates filling of the rapidly releasable pool of large dense-core vesicles. J. Neurosci. 2008, 28:5594-5601.
    • (2008) J. Neurosci. , vol.28 , pp. 5594-5601
    • Liu, Y.1    Schirra, C.2    Stevens, D.R.3
  • 41
    • 33751090050 scopus 로고    scopus 로고
    • A comparison between exocytic control mechanisms in adrenal chromaffin cells and a glutamatergic synapse
    • Neher E. A comparison between exocytic control mechanisms in adrenal chromaffin cells and a glutamatergic synapse. Pflüg. Arch. Eur. J. Physiol. 2006, 453:261-268.
    • (2006) Pflüg. Arch. Eur. J. Physiol. , vol.453 , pp. 261-268
    • Neher, E.1
  • 42
    • 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 F.M., 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
  • 43
    • 2442650287 scopus 로고    scopus 로고
    • Capacitance measurements of exocytosis in mouse pancreatic alpha-, beta- and delta-cells within intact islets of Langerhans
    • Gopel S., Zhang Q., Eliasson L., Ma X.S., Galvanovskis J., Kanno T., Salehi A., Rorsman P. Capacitance measurements of exocytosis in mouse pancreatic alpha-, beta- and delta-cells within intact islets of Langerhans. J. Physiol. 2004, 556:711-726.
    • (2004) J. Physiol. , vol.556 , pp. 711-726
    • Gopel, S.1    Zhang, Q.2    Eliasson, L.3    Ma, X.S.4    Galvanovskis, J.5    Kanno, T.6    Salehi, A.7    Rorsman, P.8
  • 45
    • 0035201145 scopus 로고    scopus 로고
    • Fast exocytosis with few Ca(2+) channels in insulin-secreting mouse pancreatic B cells
    • Barg S., Ma X., Eliasson L., et al. Fast exocytosis with few Ca(2+) channels in insulin-secreting mouse pancreatic B cells. Biophys. J. 2001, 81:3308-3323.
    • (2001) Biophys. J. , vol.81 , pp. 3308-3323
    • Barg, S.1    Ma, X.2    Eliasson, L.3
  • 46
    • 52049106127 scopus 로고    scopus 로고
    • Multiple roles of calcium ions in the regulation of neurotransmitter release
    • Neher E., Sakaba T. Multiple roles of calcium ions in the regulation of neurotransmitter release. Neuron 2008, 59:861-872.
    • (2008) Neuron , vol.59 , pp. 861-872
    • Neher, E.1    Sakaba, T.2
  • 47
    • 0036868797 scopus 로고    scopus 로고
    • Glucose-stimulated signaling pathways in biphasic insulin secretion
    • Straub S.G., Sharp G.W. Glucose-stimulated signaling pathways in biphasic insulin secretion. Diabetes Metab. Res. Rev. 2002, 18:451-463.
    • (2002) Diabetes Metab. Res. Rev. , vol.18 , pp. 451-463
    • Straub, S.G.1    Sharp, G.W.2
  • 48
    • 0029782660 scopus 로고    scopus 로고
    • Simultaneous capacitance and amperometric measurements of exocytosis: a comparison
    • Oberhauser A.F., Robinson I.M., Fernandez J.M. Simultaneous capacitance and amperometric measurements of exocytosis: a comparison. Biophys. J. 1996, 71:1131-1139.
    • (1996) Biophys. J. , vol.71 , pp. 1131-1139
    • Oberhauser, A.F.1    Robinson, I.M.2    Fernandez, J.M.3
  • 49
    • 0030857288 scopus 로고    scopus 로고
    • Stages of regulated exocytosis
    • Martin T.F. Stages of regulated exocytosis. Trends Cell Biol. 1997, 7:271-276.
    • (1997) Trends Cell Biol. , vol.7 , pp. 271-276
    • Martin, T.F.1
  • 50
    • 34948822833 scopus 로고    scopus 로고
    • Interaction between Munc13-1 and RIM is critical for glucagon-like peptide-1 mediated rescue of exocytotic defects in Munc13-1 deficient pancreatic beta-cells
    • Kwan E.P., Xie L., Sheu L., Ohtsuka T., Gaisano H.Y. Interaction between Munc13-1 and RIM is critical for glucagon-like peptide-1 mediated rescue of exocytotic defects in Munc13-1 deficient pancreatic beta-cells. Diabetes 2007, 56:2579-2588.
    • (2007) Diabetes , vol.56 , pp. 2579-2588
    • Kwan, E.P.1    Xie, L.2    Sheu, L.3    Ohtsuka, T.4    Gaisano, H.Y.5


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