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Volumn 137, Issue 1-2, 2006, Pages 95-104

Signaling mechanisms of secretin receptor

Author keywords

cAMP; IP3; Pathway; Secretin receptor; Signal transduction; Structure

Indexed keywords

4 AMINOBUTYRIC ACID RECEPTOR; G PROTEIN COUPLED RECEPTOR; GLUCAGON LIKE PEPTIDE 1; GLUCAGON LIKE PEPTIDE 2; GUANINE NUCLEOTIDE BINDING PROTEIN; HYPOPHYSIS ADENYLATE CYCLASE ACTIVATING POLYPEPTIDE; NEUROPEPTIDE; SECRETIN;

EID: 33750976173     PISSN: 01670115     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.regpep.2006.02.011     Document Type: Review
Times cited : (21)

References (136)
  • 1
    • 0014866968 scopus 로고
    • Pancreatic response to acidification of various lengths of proximal intestine in the dog
    • Meyer J.H., Way L.W., and Grossman M.I. Pancreatic response to acidification of various lengths of proximal intestine in the dog. Am J Physiol 219 (1970) 971-977
    • (1970) Am J Physiol , vol.219 , pp. 971-977
    • Meyer, J.H.1    Way, L.W.2    Grossman, M.I.3
  • 3
    • 0022626277 scopus 로고
    • Secretin is released by digestive products of fat in dogs
    • Watanabe S., Chey W.Y., Lee K.Y., and Chang T.M. Secretin is released by digestive products of fat in dogs. Gastroenterology 90 (1986) 1008-1017
    • (1986) Gastroenterology , vol.90 , pp. 1008-1017
    • Watanabe, S.1    Chey, W.Y.2    Lee, K.Y.3    Chang, T.M.4
  • 4
    • 0023214684 scopus 로고
    • Secretin is an enterogastrone in humans
    • You C.H., and Chey W.Y. Secretin is an enterogastrone in humans. Dig Dis Sci 32 (1987) 466-471
    • (1987) Dig Dis Sci , vol.32 , pp. 466-471
    • You, C.H.1    Chey, W.Y.2
  • 6
    • 0035716295 scopus 로고    scopus 로고
    • Family-B G-protein-coupled receptors
    • [REVIEWS 3013.1-3013.10]
    • Harmar A.J. Family-B G-protein-coupled receptors. Genome Biol 2 (2001) [REVIEWS 3013.1-3013.10]
    • (2001) Genome Biol , vol.2
    • Harmar, A.J.1
  • 7
  • 8
    • 0028979609 scopus 로고
    • Molecular cloning and functional characterization of a human secretin receptor
    • Chow B.K.C. Molecular cloning and functional characterization of a human secretin receptor. Biochem Biophys Res Commun 212 (1995) 204-211
    • (1995) Biochem Biophys Res Commun , vol.212 , pp. 204-211
    • Chow, B.K.C.1
  • 9
    • 0028910510 scopus 로고
    • Molecular cloning and functional expression of a human pancreatic secretin receptor
    • Jiang S., and Ulrich C. Molecular cloning and functional expression of a human pancreatic secretin receptor. Biochem Biophys Res Commun 207 (1995) 883-890
    • (1995) Biochem Biophys Res Commun , vol.207 , pp. 883-890
    • Jiang, S.1    Ulrich, C.2
  • 10
    • 0028921268 scopus 로고
    • Molecular cloning and expression of a human secretin receptor
    • Patel D.R., Kong Y., and Sreedharan S.P. Molecular cloning and expression of a human secretin receptor. Mol Pharmacol 47 (1995) 467-473
    • (1995) Mol Pharmacol , vol.47 , pp. 467-473
    • Patel, D.R.1    Kong, Y.2    Sreedharan, S.P.3
  • 11
    • 0029043789 scopus 로고
    • Critical contributions of amino-terminal extracellular domains in agonist binding and activation of secretin and vasoactive intestinal polypeptide receptors. Studies of chimeric receptors
    • Holtmann M.H., Hadac E.M., and Miller L.J. Critical contributions of amino-terminal extracellular domains in agonist binding and activation of secretin and vasoactive intestinal polypeptide receptors. Studies of chimeric receptors. J Biol Chem 270 (1995) 14394-14398
    • (1995) J Biol Chem , vol.270 , pp. 14394-14398
    • Holtmann, M.H.1    Hadac, E.M.2    Miller, L.J.3
  • 12
    • 0029016549 scopus 로고
    • Properties of chimeric secretin and VIP receptor proteins indicate the importance of the N-terminal domain for ligand discrimination
    • Vilardaga J.P., De Neef P., Di Paolo E., Bollen A., Waelbroeck M., and Robberecht P. Properties of chimeric secretin and VIP receptor proteins indicate the importance of the N-terminal domain for ligand discrimination. Biochem Biophys Res Commun 211 (1995) 885-891
    • (1995) Biochem Biophys Res Commun , vol.211 , pp. 885-891
    • Vilardaga, J.P.1    De Neef, P.2    Di Paolo, E.3    Bollen, A.4    Waelbroeck, M.5    Robberecht, P.6
  • 13
    • 0030034167 scopus 로고    scopus 로고
    • Lysine 173 residue within the first exoloop of rat secretin receptor is involved in carboxylate moiety recognition of Asp 3 in secretin
    • Vilardaga J.P., Di Paolo E., De Neef P., Waelbroeck M., Bollen A., and Robberecht P. Lysine 173 residue within the first exoloop of rat secretin receptor is involved in carboxylate moiety recognition of Asp 3 in secretin. Biochem Biophys Res Commun 218 (1996) 842-846
    • (1996) Biochem Biophys Res Commun , vol.218 , pp. 842-846
    • Vilardaga, J.P.1    Di Paolo, E.2    De Neef, P.3    Waelbroeck, M.4    Bollen, A.5    Robberecht, P.6
  • 14
    • 0001486718 scopus 로고    scopus 로고
    • The arrangement of the transmembrane helices in the secretin receptor family of G-protein-coupled receptors
    • Donnelly D. The arrangement of the transmembrane helices in the secretin receptor family of G-protein-coupled receptors. FEBS Lett 409 (1997) 431-436
    • (1997) FEBS Lett , vol.409 , pp. 431-436
    • Donnelly, D.1
  • 15
    • 0033152909 scopus 로고    scopus 로고
    • Structure of the integral membrane domain of the GLP1 receptor
    • Frimurer T.M., and Bywater R.P. Structure of the integral membrane domain of the GLP1 receptor. Proteins 35 (1999) 375-386
    • (1999) Proteins , vol.35 , pp. 375-386
    • Frimurer, T.M.1    Bywater, R.P.2
  • 16
    • 0034864511 scopus 로고    scopus 로고
    • Functional segregation of the highly conserved basic motifs within the third endoloop of the human secretin receptor
    • Chan K.Y.Y., Pang R.T.K., and Chow B.K.C. Functional segregation of the highly conserved basic motifs within the third endoloop of the human secretin receptor. Endocrinology 142 (2001) 3926-3934
    • (2001) Endocrinology , vol.142 , pp. 3926-3934
    • Chan, K.Y.Y.1    Pang, R.T.K.2    Chow, B.K.C.3
  • 18
    • 0027950288 scopus 로고
    • Upregulation of secretin receptor gene expression in rat cholangiocytes after bile duct ligation
    • Alpini G., Ulrich C.D., Phillips J.O., Pham L.D., Miller L.J., and LaRusso N.F. Upregulation of secretin receptor gene expression in rat cholangiocytes after bile duct ligation. Am J Physiol 266 (1994) G922-G928
    • (1994) Am J Physiol , vol.266
    • Alpini, G.1    Ulrich, C.D.2    Phillips, J.O.3    Pham, L.D.4    Miller, L.J.5    LaRusso, N.F.6
  • 20
    • 0019804080 scopus 로고
    • Secretin binding sites coupled with adenylate cyclase in rat fundic membranes
    • Gespach C., Bataille D., Vauclin N., Rosselin G., Moroder L., and Wunsch E. Secretin binding sites coupled with adenylate cyclase in rat fundic membranes. Peptides 2 Suppl 2 (1981) 247-251
    • (1981) Peptides , vol.2 , Issue.SUPPL. 2 , pp. 247-251
    • Gespach, C.1    Bataille, D.2    Vauclin, N.3    Rosselin, G.4    Moroder, L.5    Wunsch, E.6
  • 21
    • 0023860184 scopus 로고
    • Pharmacology and molecular identification of secretin receptors in rat gastric glands
    • Bawab W., Gespach C., Marie J.C., Chastre E., and Rosselin G. Pharmacology and molecular identification of secretin receptors in rat gastric glands. Life Sci 42 (1988) 791-798
    • (1988) Life Sci , vol.42 , pp. 791-798
    • Bawab, W.1    Gespach, C.2    Marie, J.C.3    Chastre, E.4    Rosselin, G.5
  • 22
    • 0031859332 scopus 로고    scopus 로고
    • Secretin inhibits gastric acid secretion via a vagal afferent pathway in rats
    • Li P., Chang T.M., and Chey W.Y. Secretin inhibits gastric acid secretion via a vagal afferent pathway in rats. Am J Physiol 275 (1998) G22-G28
    • (1998) Am J Physiol , vol.275
    • Li, P.1    Chang, T.M.2    Chey, W.Y.3
  • 24
    • 0037111283 scopus 로고    scopus 로고
    • What may be the anatomical basis that secretin can improve the mental functions in autism?
    • Koves K., Kausz M., and Horvath K. What may be the anatomical basis that secretin can improve the mental functions in autism?. Regul Pept 109 (2002) 167-172
    • (2002) Regul Pept , vol.109 , pp. 167-172
    • Koves, K.1    Kausz, M.2    Horvath, K.3
  • 26
    • 2642561171 scopus 로고    scopus 로고
    • Secretin controls anion secretion in the rat epididymis in an autocrine/paracrine fashion
    • Chow B.K., Cheung K.H., Tsang E.M., Leung M.C., Lee S.M., and Wong P.Y. Secretin controls anion secretion in the rat epididymis in an autocrine/paracrine fashion. Biol Reprod 70 (2004) 1594-1599
    • (2004) Biol Reprod , vol.70 , pp. 1594-1599
    • Chow, B.K.1    Cheung, K.H.2    Tsang, E.M.3    Leung, M.C.4    Lee, S.M.5    Wong, P.Y.6
  • 27
    • 0033724994 scopus 로고    scopus 로고
    • Expression and motor effects of secretin in small and large intestine of the rat
    • Andersson A., Sundler F., and Ekblad E. Expression and motor effects of secretin in small and large intestine of the rat. Peptides 21 (2000) 1687-1694
    • (2000) Peptides , vol.21 , pp. 1687-1694
    • Andersson, A.1    Sundler, F.2    Ekblad, E.3
  • 30
    • 0348143339 scopus 로고    scopus 로고
    • Secretin, 100 years later
    • Chey W.Y., and Chang T.M. Secretin, 100 years later. J Gastroenterol 38 (2003) 1025-1035
    • (2003) J Gastroenterol , vol.38 , pp. 1025-1035
    • Chey, W.Y.1    Chang, T.M.2
  • 31
    • 0037105663 scopus 로고    scopus 로고
    • Silencing of secretin receptor function by dimerization with a misspliced variant secretin receptor in ductal pancreatic adenocarcinoma
    • Ding W.Q., Cheng Z.J., McElhiney J., Kuntz S.M., and Miller L.J. Silencing of secretin receptor function by dimerization with a misspliced variant secretin receptor in ductal pancreatic adenocarcinoma. Cancer Res 62 (2002) 5223-5229
    • (2002) Cancer Res , vol.62 , pp. 5223-5229
    • Ding, W.Q.1    Cheng, Z.J.2    McElhiney, J.3    Kuntz, S.M.4    Miller, L.J.5
  • 32
    • 15844385219 scopus 로고    scopus 로고
    • Multiple extracellular loop domains contribute critical determinants for agonist binding and activation of the secretin receptor
    • Holtmann M.H., Ganguli S., Hadac E.M., Dolu V., and Miller L.J. Multiple extracellular loop domains contribute critical determinants for agonist binding and activation of the secretin receptor. J Biol Chem 271 (1996) 14944-14949
    • (1996) J Biol Chem , vol.271 , pp. 14944-14949
    • Holtmann, M.H.1    Ganguli, S.2    Hadac, E.M.3    Dolu, V.4    Miller, L.J.5
  • 33
    • 0032513222 scopus 로고    scopus 로고
    • Contribution of the second transmembrane helix of the secretin receptor to the positioning of secretin
    • Di Paolo E., De Neef P., Moguilevsky N., Petry H., Bollen A., Waelbroeck M., and Robberecht P. Contribution of the second transmembrane helix of the secretin receptor to the positioning of secretin. FEBS Lett 424 (1998) 207-210
    • (1998) FEBS Lett , vol.424 , pp. 207-210
    • Di Paolo, E.1    De Neef, P.2    Moguilevsky, N.3    Petry, H.4    Bollen, A.5    Waelbroeck, M.6    Robberecht, P.7
  • 34
    • 0030941907 scopus 로고    scopus 로고
    • Mutational analysis of extracellular cysteine residues of rat secretin receptor shows that disulfide bridges are essential for receptor function
    • Vilardaga J.P., Di Paolo E., Bialek C., De Neef P., Waelbroeck M., Bollen A., and Robberecht P. Mutational analysis of extracellular cysteine residues of rat secretin receptor shows that disulfide bridges are essential for receptor function. Eur J Biochem 246 (1997) 173-180
    • (1997) Eur J Biochem , vol.246 , pp. 173-180
    • Vilardaga, J.P.1    Di Paolo, E.2    Bialek, C.3    De Neef, P.4    Waelbroeck, M.5    Bollen, A.6    Robberecht, P.7
  • 35
    • 0033303551 scopus 로고    scopus 로고
    • Role of N-linked glycosylation on the function and expression of the human secretin receptor
    • Pang R.T.K., Ng S.S.M., Cheng C.H.K., Holtmann M.H., Miller L.J., and Chow B.K.C. Role of N-linked glycosylation on the function and expression of the human secretin receptor. Endocrinology 140 (1999) 5102-5111
    • (1999) Endocrinology , vol.140 , pp. 5102-5111
    • Pang, R.T.K.1    Ng, S.S.M.2    Cheng, C.H.K.3    Holtmann, M.H.4    Miller, L.J.5    Chow, B.K.C.6
  • 36
    • 0034464742 scopus 로고    scopus 로고
    • Uncovering molecular mechanisms involved in activation of G protein-coupled receptors
    • Gether U. Uncovering molecular mechanisms involved in activation of G protein-coupled receptors. Endocr Rev 21 (2000) 90-113
    • (2000) Endocr Rev , vol.21 , pp. 90-113
    • Gether, U.1
  • 37
    • 0021288935 scopus 로고
    • Regulatory mechanisms in pancreas and salivary acini
    • Williams J.A. Regulatory mechanisms in pancreas and salivary acini. Annu Rev Physiol 46 (1984) 361-375
    • (1984) Annu Rev Physiol , vol.46 , pp. 361-375
    • Williams, J.A.1
  • 38
    • 0022541498 scopus 로고
    • Secretin induces rapid increases in inositol trisphosphate, cytosolic Ca2+ and diacylglycerol as well as cyclic AMP in rat pancreatic acini
    • Trimble E.R., Bruzzone R., Biden T.J., and Farese R.V. Secretin induces rapid increases in inositol trisphosphate, cytosolic Ca2+ and diacylglycerol as well as cyclic AMP in rat pancreatic acini. Biochem J 239 (1986) 257-261
    • (1986) Biochem J , vol.239 , pp. 257-261
    • Trimble, E.R.1    Bruzzone, R.2    Biden, T.J.3    Farese, R.V.4
  • 39
    • 0023193492 scopus 로고
    • Secretin stimulates cyclic AMP and inositol trisphosphate production in rat pancreatic acinar tissue by two fully independent mechanisms
    • Trimble E.R., Bruzzone R., Biden T.J., Meehan C.J., Andreu D., and Merrifield R.B. Secretin stimulates cyclic AMP and inositol trisphosphate production in rat pancreatic acinar tissue by two fully independent mechanisms. Proc Natl Acad Sci U S A 84 (1987) 3146-3150
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 3146-3150
    • Trimble, E.R.1    Bruzzone, R.2    Biden, T.J.3    Meehan, C.J.4    Andreu, D.5    Merrifield, R.B.6
  • 41
    • 0018746197 scopus 로고
    • The influence of secretin, glucagon and other peptides, of amino acids, prostaglandin endoperoxide analogues and diazepam on the level of adenosine 3′,5′-cyclic monophosphate in neuroblastoma × glioma hybrid cells
    • Propst F., Moroder L., Wunsch E., and Hamprecht B. The influence of secretin, glucagon and other peptides, of amino acids, prostaglandin endoperoxide analogues and diazepam on the level of adenosine 3′,5′-cyclic monophosphate in neuroblastoma × glioma hybrid cells. J Neurochem 32 (1979) 1495-1500
    • (1979) J Neurochem , vol.32 , pp. 1495-1500
    • Propst, F.1    Moroder, L.2    Wunsch, E.3    Hamprecht, B.4
  • 42
    • 0025016011 scopus 로고
    • Secretin receptors in the neuroglioma hybrid cell line NG108-15. Characterization and regulation of their expression
    • Gossen D., Tastenoy M., Robberecht P., and Christophe J. Secretin receptors in the neuroglioma hybrid cell line NG108-15. Characterization and regulation of their expression. Eur J Biochem 193 (1990) 149-154
    • (1990) Eur J Biochem , vol.193 , pp. 149-154
    • Gossen, D.1    Tastenoy, M.2    Robberecht, P.3    Christophe, J.4
  • 43
    • 0028304466 scopus 로고
    • Properties and regulation of the coupling to adenylate cyclase of secretin receptors stably transfected in Chinese hamster ovary cells
    • Vilardaga J.P., Ciccarelli E., Dubeaux C., De Neef P., Bollen A., and Robberecht P. Properties and regulation of the coupling to adenylate cyclase of secretin receptors stably transfected in Chinese hamster ovary cells. Mol Pharmacol 45 (1994) 1022-1028
    • (1994) Mol Pharmacol , vol.45 , pp. 1022-1028
    • Vilardaga, J.P.1    Ciccarelli, E.2    Dubeaux, C.3    De Neef, P.4    Bollen, A.5    Robberecht, P.6
  • 44
    • 0019160292 scopus 로고
    • Regulation by secretin, vasoactive intestinal peptide, and somatostatin of cyclic AMP accumulation in cultured brain cells
    • van Calker D., Muller M., and Hamprecht B. Regulation by secretin, vasoactive intestinal peptide, and somatostatin of cyclic AMP accumulation in cultured brain cells. Proc Natl Acad Sci U S A 77 (1980) 6907-6911
    • (1980) Proc Natl Acad Sci U S A , vol.77 , pp. 6907-6911
    • van Calker, D.1    Muller, M.2    Hamprecht, B.3
  • 45
    • 0021344152 scopus 로고
    • Secretin receptors on neuroblastoma cell membranes: characterization of 125I-labeled secretin binding and association with adenylate cyclase
    • Roth B.L., Beinfeld M.C., and Howlett A.C. Secretin receptors on neuroblastoma cell membranes: characterization of 125I-labeled secretin binding and association with adenylate cyclase. J Neurochem 42 (1984) 1145-1152
    • (1984) J Neurochem , vol.42 , pp. 1145-1152
    • Roth, B.L.1    Beinfeld, M.C.2    Howlett, A.C.3
  • 46
    • 0022647402 scopus 로고
    • Secretin stimulates cyclic AMP formation in the rat brain
    • Fremeau Jr. R.T., Korman L.Y., and Moody T.W. Secretin stimulates cyclic AMP formation in the rat brain. J Neurochem 46 (1986) 1947-1955
    • (1986) J Neurochem , vol.46 , pp. 1947-1955
    • Fremeau Jr., R.T.1    Korman, L.Y.2    Moody, T.W.3
  • 47
    • 0022514850 scopus 로고
    • Do secretin and vasoactive intestinal peptide have independent receptors on striatal neurons and glial cells in primary cultures?
    • Chneiweiss H., Glowinski J., and Premont J. Do secretin and vasoactive intestinal peptide have independent receptors on striatal neurons and glial cells in primary cultures?. J Neurochem 47 (1986) 608-613
    • (1986) J Neurochem , vol.47 , pp. 608-613
    • Chneiweiss, H.1    Glowinski, J.2    Premont, J.3
  • 48
    • 0027436426 scopus 로고
    • Regulation of neurosecretory habituation by cAMP. Role of adaptation of cAMP signals
    • Martin P.T., Chung B.T., and Koshland Jr. D.E. Regulation of neurosecretory habituation by cAMP. Role of adaptation of cAMP signals. Eur J Biochem 217 (1993) 259-265
    • (1993) Eur J Biochem , vol.217 , pp. 259-265
    • Martin, P.T.1    Chung, B.T.2    Koshland Jr., D.E.3
  • 49
    • 0028894387 scopus 로고
    • Regulation of adenylate cyclase by galanin, neuropeptide Y, secretin and vasoactive intestinal polypeptide in rat frontal cortex, hippocampus and hypothalamus
    • Karelson E., Laasik J., and Sillard R. Regulation of adenylate cyclase by galanin, neuropeptide Y, secretin and vasoactive intestinal polypeptide in rat frontal cortex, hippocampus and hypothalamus. Neuropeptides 28 (1995) 21-28
    • (1995) Neuropeptides , vol.28 , pp. 21-28
    • Karelson, E.1    Laasik, J.2    Sillard, R.3
  • 51
    • 0018611655 scopus 로고
    • Localization and possible function of peptidergic neurons and their interactions with central catecholamine neurons, and the central actions of gut hormones
    • Fuxe K., Andersson K., Hokfelt T., Mutt V., Ferland L., Agnati L.F., Ganten D., Said S., Eneroth P., and Gustafsson J.A. Localization and possible function of peptidergic neurons and their interactions with central catecholamine neurons, and the central actions of gut hormones. Fed Proc 38 (1979) 2333-2340
    • (1979) Fed Proc , vol.38 , pp. 2333-2340
    • Fuxe, K.1    Andersson, K.2    Hokfelt, T.3    Mutt, V.4    Ferland, L.5    Agnati, L.F.6    Ganten, D.7    Said, S.8    Eneroth, P.9    Gustafsson, J.A.10
  • 52
    • 0020524673 scopus 로고
    • Plasma gonadotropin, prolactin levels and hypothalamic tyrosine hydroxylase activity following intraventricular bombesin and secretin in ovariectomized conscious rats
    • Babu G.N., and Vijayan E. Plasma gonadotropin, prolactin levels and hypothalamic tyrosine hydroxylase activity following intraventricular bombesin and secretin in ovariectomized conscious rats. Brain Res Bull 11 (1983) 25-29
    • (1983) Brain Res Bull , vol.11 , pp. 25-29
    • Babu, G.N.1    Vijayan, E.2
  • 53
    • 0020364480 scopus 로고
    • Secretin and vasoactive intestinal peptide acutely increase tyrosine 3-monooxygenase in the rat superior cervical ganglion
    • Ip N.Y., Ho C.K., and Zigmond R.E. Secretin and vasoactive intestinal peptide acutely increase tyrosine 3-monooxygenase in the rat superior cervical ganglion. Proc Natl Acad Sci U S A 79 (1982) 7566-7569
    • (1982) Proc Natl Acad Sci U S A , vol.79 , pp. 7566-7569
    • Ip, N.Y.1    Ho, C.K.2    Zigmond, R.E.3
  • 54
    • 0024545729 scopus 로고
    • Secretin and vasoactive intestinal peptide activate tyrosine hydroxylase in sympathetic nerve endings
    • Schwarzschild M.A., and Zigmond R.E. Secretin and vasoactive intestinal peptide activate tyrosine hydroxylase in sympathetic nerve endings. J Neurosci 9 (1989) 160-166
    • (1989) J Neurosci , vol.9 , pp. 160-166
    • Schwarzschild, M.A.1    Zigmond, R.E.2
  • 55
    • 0026068920 scopus 로고
    • Effects of peptides of the secretin-glucagon family and cyclic nucleotides on tyrosine hydroxylase activity in sympathetic nerve endings
    • Schwarzschild M.A., and Zigmond R.E. Effects of peptides of the secretin-glucagon family and cyclic nucleotides on tyrosine hydroxylase activity in sympathetic nerve endings. J Neurochem 56 (1991) 400-406
    • (1991) J Neurochem , vol.56 , pp. 400-406
    • Schwarzschild, M.A.1    Zigmond, R.E.2
  • 56
    • 1942423278 scopus 로고    scopus 로고
    • Secretin depolarizes nucleus tractus solitarius neurons through activation of a nonselective cationic conductance
    • Yang B., Goulet M., Boismenu R., and Ferguson A.V. Secretin depolarizes nucleus tractus solitarius neurons through activation of a nonselective cationic conductance. Am J Physiol Regul Integr Comp Physiol 286 (2004) R927-R934
    • (2004) Am J Physiol Regul Integr Comp Physiol , vol.286
    • Yang, B.1    Goulet, M.2    Boismenu, R.3    Ferguson, A.V.4
  • 59
    • 23444461769 scopus 로고    scopus 로고
    • Endogenous release and multiple actions of secretin in the rat cerebellum
    • Lee S.M., Chen L., Chow B.K., and Yung W.H. Endogenous release and multiple actions of secretin in the rat cerebellum. Neuroscience 134 (2005) 377-386
    • (2005) Neuroscience , vol.134 , pp. 377-386
    • Lee, S.M.1    Chen, L.2    Chow, B.K.3    Yung, W.H.4
  • 60
    • 0018697616 scopus 로고
    • Low responsiveness of cardiac adenylate cyclase activity to peptide hormones in spontaneously hypertensive rats
    • Chatelain P., Robberecht P., De Neef P., Claeys M., and Christophe J. Low responsiveness of cardiac adenylate cyclase activity to peptide hormones in spontaneously hypertensive rats. FEBS Lett 107 (1979) 86-90
    • (1979) FEBS Lett , vol.107 , pp. 86-90
    • Chatelain, P.1    Robberecht, P.2    De Neef, P.3    Claeys, M.4    Christophe, J.5
  • 61
    • 0019215377 scopus 로고
    • Secretin and VIP-stimulated adenylate cyclase from rat heart. II. Impairment in spontaneous hypertension
    • Chatelain P., Robberecht P., De Neef P., Camus J.C., Heuse D., and Christophe J. Secretin and VIP-stimulated adenylate cyclase from rat heart. II. Impairment in spontaneous hypertension. Pflugers Arch 389 (1980) 29-35
    • (1980) Pflugers Arch , vol.389 , pp. 29-35
    • Chatelain, P.1    Robberecht, P.2    De Neef, P.3    Camus, J.C.4    Heuse, D.5    Christophe, J.6
  • 62
    • 0020561919 scopus 로고
    • The adenylate cyclase activity in heart membranes from normotensive and spontaneously hypertensive rats, after chemical sympathectomy, suggests the presence of presynaptic secretin receptors
    • Chatelain P., Robberecht P., Camus J.C., De Neef P., Waelbroeck M., Roba J., and Christophe J. The adenylate cyclase activity in heart membranes from normotensive and spontaneously hypertensive rats, after chemical sympathectomy, suggests the presence of presynaptic secretin receptors. Eur J Pharmacol 93 (1983) 271-276
    • (1983) Eur J Pharmacol , vol.93 , pp. 271-276
    • Chatelain, P.1    Robberecht, P.2    Camus, J.C.3    De Neef, P.4    Waelbroeck, M.5    Roba, J.6    Christophe, J.7
  • 63
    • 0019486257 scopus 로고
    • Impairment of hormone-stimulated cardiac adenylate cyclase activity in the genetically obese (fa/fa) Zucker rat
    • Chatelain P., Robberecht P., De Neef P., Camus J.C., Poloczek P., and Christophe J. Impairment of hormone-stimulated cardiac adenylate cyclase activity in the genetically obese (fa/fa) Zucker rat. Pflugers Arch 390 (1981) 10-16
    • (1981) Pflugers Arch , vol.390 , pp. 10-16
    • Chatelain, P.1    Robberecht, P.2    De Neef, P.3    Camus, J.C.4    Poloczek, P.5    Christophe, J.6
  • 64
    • 0020573399 scopus 로고
    • The cardiac inotropic response to secretin is lower in genetically obese (fa/fa) than in lean (fa/?) Zucker rats
    • Robberecht P., De Neef P., Camus J.C., Waelbroeck M., Fontaine J., and Christophe J. The cardiac inotropic response to secretin is lower in genetically obese (fa/fa) than in lean (fa/?) Zucker rats. Pflugers Arch 398 (1983) 217-220
    • (1983) Pflugers Arch , vol.398 , pp. 217-220
    • Robberecht, P.1    De Neef, P.2    Camus, J.C.3    Waelbroeck, M.4    Fontaine, J.5    Christophe, J.6
  • 65
    • 0019835484 scopus 로고
    • Decreased secretin and glucagon responsiveness of adenylate cyclase in cardiac membranes from hypothyroid rats
    • Robberecht P., Pochet R., Chatelain P., Verloes A., Camus J.C., De Neef P., and Christophe J. Decreased secretin and glucagon responsiveness of adenylate cyclase in cardiac membranes from hypothyroid rats. FEBS Lett 132 (1981) 33-36
    • (1981) FEBS Lett , vol.132 , pp. 33-36
    • Robberecht, P.1    Pochet, R.2    Chatelain, P.3    Verloes, A.4    Camus, J.C.5    De Neef, P.6    Christophe, J.7
  • 66
    • 0020061567 scopus 로고
    • Early decrease in secretin-, glucagon-, and isoproterenol-stimulated cardiac adenylate cyclase activity in rats treated with isoproterenol
    • Chatelain P., Robberecht P., De Neef P., Camus J.C., and Christophe J. Early decrease in secretin-, glucagon-, and isoproterenol-stimulated cardiac adenylate cyclase activity in rats treated with isoproterenol. Biochem Pharmacol 31 (1982) 347-352
    • (1982) Biochem Pharmacol , vol.31 , pp. 347-352
    • Chatelain, P.1    Robberecht, P.2    De Neef, P.3    Camus, J.C.4    Christophe, J.5
  • 67
    • 0022461469 scopus 로고
    • Alteration of secretin-stimulated cardiac adenylate cyclase activity in rats with portacaval shunt
    • De Fontaine S., Robberecht P., De Neef P., and Christophe J. Alteration of secretin-stimulated cardiac adenylate cyclase activity in rats with portacaval shunt. Peptides 7 (1986) 645-649
    • (1986) Peptides , vol.7 , pp. 645-649
    • De Fontaine, S.1    Robberecht, P.2    De Neef, P.3    Christophe, J.4
  • 69
  • 70
    • 0021170097 scopus 로고
    • Heart receptors for VIP, PHI and secretin are able to activate adenylate cyclase and to mediate inotropic and chronotropic effects. Species variations and physiopathology
    • Christophe J., Waelbroeck M., Chatelain P., and Robberecht P. Heart receptors for VIP, PHI and secretin are able to activate adenylate cyclase and to mediate inotropic and chronotropic effects. Species variations and physiopathology. Peptides 5 (1984) 341-353
    • (1984) Peptides , vol.5 , pp. 341-353
    • Christophe, J.1    Waelbroeck, M.2    Chatelain, P.3    Robberecht, P.4
  • 71
    • 0022398580 scopus 로고
    • Effects of secretin infusion on myocardial performance and metabolism in the dog
    • Gunnes P., Smiseth O.A., Lygren I., and Jorde R. Effects of secretin infusion on myocardial performance and metabolism in the dog. J Cardiovasc Pharmacol 7 (1985) 1183-1187
    • (1985) J Cardiovasc Pharmacol , vol.7 , pp. 1183-1187
    • Gunnes, P.1    Smiseth, O.A.2    Lygren, I.3    Jorde, R.4
  • 73
    • 0019793642 scopus 로고
    • Peptide receptors in human lung tumor cells in culture: vasoactive intestinal peptide (VIP) and secretin interaction with the Calu-1 and SW-900 cell lines
    • Laburthe M., Boissard C., Chevalier G., Zweibaum A., and Rosselin G. Peptide receptors in human lung tumor cells in culture: vasoactive intestinal peptide (VIP) and secretin interaction with the Calu-1 and SW-900 cell lines. Regul Pept 2 (1981) 219-230
    • (1981) Regul Pept , vol.2 , pp. 219-230
    • Laburthe, M.1    Boissard, C.2    Chevalier, G.3    Zweibaum, A.4    Rosselin, G.5
  • 74
    • 0022551233 scopus 로고
    • Secretin/vasoactive intestinal peptide-stimulated secretion of bombesin/gastrin releasing peptide from human small cell carcinoma of the lung
    • Korman L.Y., Carney D.N., Citron M.L., and Moody T.W. Secretin/vasoactive intestinal peptide-stimulated secretion of bombesin/gastrin releasing peptide from human small cell carcinoma of the lung. Cancer Res 46 (1986) 1214-1218
    • (1986) Cancer Res , vol.46 , pp. 1214-1218
    • Korman, L.Y.1    Carney, D.N.2    Citron, M.L.3    Moody, T.W.4
  • 75
    • 0024338352 scopus 로고
    • The release of bombesin-like peptides from small cell lung cancer cells
    • Moody T.W., and Korman L.Y. The release of bombesin-like peptides from small cell lung cancer cells. Ann N Y Acad Sci 547 (1988) 351-359
    • (1988) Ann N Y Acad Sci , vol.547 , pp. 351-359
    • Moody, T.W.1    Korman, L.Y.2
  • 77
    • 0031005275 scopus 로고    scopus 로고
    • Gastric mucin secretion from cultured rat epithelial cells
    • Tani S., Okuda M., Morishige R., and Tanaka T. Gastric mucin secretion from cultured rat epithelial cells. Biol Pharm Bull 20 (1997) 482-485
    • (1997) Biol Pharm Bull , vol.20 , pp. 482-485
    • Tani, S.1    Okuda, M.2    Morishige, R.3    Tanaka, T.4
  • 78
    • 0036364712 scopus 로고    scopus 로고
    • Mechanisms of gastric mucus secretion from cultured rat gastric epithelial cells induced by carbachol, cholecystokinin octapeptide, secretin, and prostaglandin E2
    • Tani S., Suzuki T., Kano S., Tanaka T., Sunaga K., Morishige R., and Tsuda T. Mechanisms of gastric mucus secretion from cultured rat gastric epithelial cells induced by carbachol, cholecystokinin octapeptide, secretin, and prostaglandin E2. Biol Pharm Bull 25 (2002) 14-18
    • (2002) Biol Pharm Bull , vol.25 , pp. 14-18
    • Tani, S.1    Suzuki, T.2    Kano, S.3    Tanaka, T.4    Sunaga, K.5    Morishige, R.6    Tsuda, T.7
  • 79
    • 0019310303 scopus 로고
    • Evidence for a cyclic AMP system highly sensitive to secretin in gastric glands isolated from the rat fundus and antrum
    • Gespach C., Bataille D., Dupont C., Rosselin G., Wunsch E., and Jaeger E. Evidence for a cyclic AMP system highly sensitive to secretin in gastric glands isolated from the rat fundus and antrum. Biochim Biophys Acta 630 (1980) 433-441
    • (1980) Biochim Biophys Acta , vol.630 , pp. 433-441
    • Gespach, C.1    Bataille, D.2    Dupont, C.3    Rosselin, G.4    Wunsch, E.5    Jaeger, E.6
  • 80
    • 0022467030 scopus 로고
    • Actions of vasoactive intestinal peptide and secretin on chief cells prepared from guinea pig stomach
    • Sutliff V.E., Raufman J.P., Jensen R.T., and Gardner J.D. Actions of vasoactive intestinal peptide and secretin on chief cells prepared from guinea pig stomach. Am J Physiol 251 (1986) G96-G102
    • (1986) Am J Physiol , vol.251
    • Sutliff, V.E.1    Raufman, J.P.2    Jensen, R.T.3    Gardner, J.D.4
  • 81
    • 0028290135 scopus 로고
    • Inhibitory action of somatostatin on cAMP dependent pepsinogen secretion from rat gastric chief cells: involvement of pertussis toxin-sensitive G-protein
    • Tanaka T., and Tani S. Inhibitory action of somatostatin on cAMP dependent pepsinogen secretion from rat gastric chief cells: involvement of pertussis toxin-sensitive G-protein. Biol Pharm Bull 17 (1994) 415-418
    • (1994) Biol Pharm Bull , vol.17 , pp. 415-418
    • Tanaka, T.1    Tani, S.2
  • 82
    • 0023863239 scopus 로고
    • Biliary physiology in rats with bile ductular cell hyperplasia. Evidence for a secretory function of proliferated bile ductules
    • Alpini G., Lenzi R., Sarkozi L., and Tavoloni N. Biliary physiology in rats with bile ductular cell hyperplasia. Evidence for a secretory function of proliferated bile ductules. J Clin Invest 81 (1988) 569-578
    • (1988) J Clin Invest , vol.81 , pp. 569-578
    • Alpini, G.1    Lenzi, R.2    Sarkozi, L.3    Tavoloni, N.4
  • 83
    • 0036697798 scopus 로고    scopus 로고
    • Regulation of cholangiocyte secretion
    • Fitz J.G. Regulation of cholangiocyte secretion. Semin Liver Dis 22 (2002) 241-249
    • (2002) Semin Liver Dis , vol.22 , pp. 241-249
    • Fitz, J.G.1
  • 84
    • 0026508822 scopus 로고
    • Localization and characterization of secretin binding sites expressed by rat bile duct epithelium
    • Farouk M., Vigna S.R., McVey D.C., and Meyers W.C. Localization and characterization of secretin binding sites expressed by rat bile duct epithelium. Gastroenterology 102 (1992) 963-968
    • (1992) Gastroenterology , vol.102 , pp. 963-968
    • Farouk, M.1    Vigna, S.R.2    McVey, D.C.3    Meyers, W.C.4
  • 88
    • 0026710665 scopus 로고
    • Secretin stimulates exocytosis in isolated bile duct epithelial cells by a cyclic AMP-mediated mechanism
    • Kato A., Gores G.J., and LaRusso N.F. Secretin stimulates exocytosis in isolated bile duct epithelial cells by a cyclic AMP-mediated mechanism. J Biol Chem 267 (1992) 15523-15529
    • (1992) J Biol Chem , vol.267 , pp. 15523-15529
    • Kato, A.1    Gores, G.J.2    LaRusso, N.F.3
  • 89
    • 0026787649 scopus 로고
    • Secretin stimulates bile ductular secretory activity through the cAMP system
    • Lenzen R., Alpini G., and Tavoloni N. Secretin stimulates bile ductular secretory activity through the cAMP system. Am J Physiol 263 (1992) G527-G532
    • (1992) Am J Physiol , vol.263
    • Lenzen, R.1    Alpini, G.2    Tavoloni, N.3
  • 90
    • 0029844370 scopus 로고    scopus 로고
    • Regrowth of the rat biliary tree after 70% partial hepatectomy is coupled to increased secretin-induced ductal secretion
    • LeSage G., Glaser S.S., Gubba S., Robertson W.E., Phinizy J.L., Lasater J., Rodgers R.E., and Alpini G. Regrowth of the rat biliary tree after 70% partial hepatectomy is coupled to increased secretin-induced ductal secretion. Gastroenterology 111 (1996) 1633-1644
    • (1996) Gastroenterology , vol.111 , pp. 1633-1644
    • LeSage, G.1    Glaser, S.S.2    Gubba, S.3    Robertson, W.E.4    Phinizy, J.L.5    Lasater, J.6    Rodgers, R.E.7    Alpini, G.8
  • 93
    • 0031011414 scopus 로고    scopus 로고
    • Secretin promotes osmotic water transport in rat cholangiocytes by increasing aquaporin-1 water channels in plasma membrane. Evidence for a secretin-induced vesicular translocation of aquaporin-1
    • Marinelli R.A., Pham L., Agre P., and LaRusso N.F. Secretin promotes osmotic water transport in rat cholangiocytes by increasing aquaporin-1 water channels in plasma membrane. Evidence for a secretin-induced vesicular translocation of aquaporin-1. J Biol Chem 272 (1997) 12984-12988
    • (1997) J Biol Chem , vol.272 , pp. 12984-12988
    • Marinelli, R.A.1    Pham, L.2    Agre, P.3    LaRusso, N.F.4
  • 94
    • 0032953874 scopus 로고    scopus 로고
    • Secretin induces the apical insertion of aquaporin-1 water channels in rat cholangiocytes
    • Marinelli R.A., Tietz P.S., Pham L.D., Rueckert L., Agre P., and LaRusso N.F. Secretin induces the apical insertion of aquaporin-1 water channels in rat cholangiocytes. Am J Physiol 276 (1999) G280-G286
    • (1999) Am J Physiol , vol.276
    • Marinelli, R.A.1    Tietz, P.S.2    Pham, L.D.3    Rueckert, L.4    Agre, P.5    LaRusso, N.F.6
  • 95
    • 0015236721 scopus 로고
    • Intestinal secretion: stimulation by peptides
    • Barbezat G.O., and Grossman M.I. Intestinal secretion: stimulation by peptides. Science 174 (1971) 422-424
    • (1971) Science , vol.174 , pp. 422-424
    • Barbezat, G.O.1    Grossman, M.I.2
  • 96
    • 0015290382 scopus 로고
    • Effects of secretin and glucagon on intestinal transport of ions and water in the rat
    • Hubel K.A. Effects of secretin and glucagon on intestinal transport of ions and water in the rat. Proc Soc Exp Biol Med 139 (1972) 656-658
    • (1972) Proc Soc Exp Biol Med , vol.139 , pp. 656-658
    • Hubel, K.A.1
  • 97
    • 0018908489 scopus 로고
    • Effect of pentagastrin, secretin and cholecystokinin on intestinal water and sodium absorption in the rat
    • Pansu D., Bosshard A., Dechelette M.A., and Vagne M. Effect of pentagastrin, secretin and cholecystokinin on intestinal water and sodium absorption in the rat. Digestion 20 (1980) 201-206
    • (1980) Digestion , vol.20 , pp. 201-206
    • Pansu, D.1    Bosshard, A.2    Dechelette, M.A.3    Vagne, M.4
  • 98
    • 0021241623 scopus 로고
    • Secretin, VIP, and PHI stimulate rat proximal duodenal surface epithelial bicarbonate secretion in vivo
    • Isenberg J.I., Wallin B., Johansson C., Smedfors B., Mutt V., Tatemoto K., and Emas S. Secretin, VIP, and PHI stimulate rat proximal duodenal surface epithelial bicarbonate secretion in vivo. Regul Pept 8 (1984) 315-320
    • (1984) Regul Pept , vol.8 , pp. 315-320
    • Isenberg, J.I.1    Wallin, B.2    Johansson, C.3    Smedfors, B.4    Mutt, V.5    Tatemoto, K.6    Emas, S.7
  • 99
    • 0029835287 scopus 로고    scopus 로고
    • Bicarbonate secretion in the guinea pig duodenum: functional characterization of peptide hormone receptors in duodenal enterocytes
    • Reimer R., Odes H.S., Beil W., Schwenk M., Muallem R., and Sewing K.F. Bicarbonate secretion in the guinea pig duodenum: functional characterization of peptide hormone receptors in duodenal enterocytes. Pharmacology 52 (1996) 339-346
    • (1996) Pharmacology , vol.52 , pp. 339-346
    • Reimer, R.1    Odes, H.S.2    Beil, W.3    Schwenk, M.4    Muallem, R.5    Sewing, K.F.6
  • 100
    • 0023025009 scopus 로고
    • Effect of secretin and caerulein on the absorption of water, electrolytes and glucose from the jejunum of dogs
    • Hirose S., Shimazaki K., and Hattori N. Effect of secretin and caerulein on the absorption of water, electrolytes and glucose from the jejunum of dogs. Digestion 35 (1986) 205-210
    • (1986) Digestion , vol.35 , pp. 205-210
    • Hirose, S.1    Shimazaki, K.2    Hattori, N.3
  • 101
    • 0014805475 scopus 로고
    • Effect of secretin on small bowel myoelectric activity of conscious healthy dogs
    • Hermon-Taylor J., and Code C.F. Effect of secretin on small bowel myoelectric activity of conscious healthy dogs. Am J Dig Dis 15 (1970) 545-550
    • (1970) Am J Dig Dis , vol.15 , pp. 545-550
    • Hermon-Taylor, J.1    Code, C.F.2
  • 102
    • 0014800181 scopus 로고
    • The effect of secretin and cholecystokinin-pancreozymin on the intraluminal pressure of the jejunum in the unanesthetized dog
    • Ramirez M., and Farrar J.T. The effect of secretin and cholecystokinin-pancreozymin on the intraluminal pressure of the jejunum in the unanesthetized dog. Am J Dig Dis 15 (1970) 539-544
    • (1970) Am J Dig Dis , vol.15 , pp. 539-544
    • Ramirez, M.1    Farrar, J.T.2
  • 103
  • 104
    • 0014421410 scopus 로고
    • Effect of pure natural and synthetic secretion on Brunner's gland secretion in dogs
    • Love J.W., Walder A.I., and Bingham C. Effect of pure natural and synthetic secretion on Brunner's gland secretion in dogs. Nature 219 (1968) 731-732
    • (1968) Nature , vol.219 , pp. 731-732
    • Love, J.W.1    Walder, A.I.2    Bingham, C.3
  • 105
    • 0014533236 scopus 로고
    • Hormonal control of Brunner's glands
    • Stening G.F., and Grossman M.I. Hormonal control of Brunner's glands. Gastroenterology 56 (1969) 1047-1052
    • (1969) Gastroenterology , vol.56 , pp. 1047-1052
    • Stening, G.F.1    Grossman, M.I.2
  • 106
    • 0023748711 scopus 로고
    • Interaction of neurotensin with caerulein or secretin on digestive tract growth in rats
    • Hoang H.D., Wood J.G., Bussjaeger L.J., and Solomon T.E. Interaction of neurotensin with caerulein or secretin on digestive tract growth in rats. Regul Pept 22 (1988) 275-284
    • (1988) Regul Pept , vol.22 , pp. 275-284
    • Hoang, H.D.1    Wood, J.G.2    Bussjaeger, L.J.3    Solomon, T.E.4
  • 107
    • 0022837399 scopus 로고
    • Release of secretin by licorice extract in dogs
    • Watanabe S.I., Chey W.Y., Lee K.Y., and Chang T.M. Release of secretin by licorice extract in dogs. Pancreas 1 (1986) 449-454
    • (1986) Pancreas , vol.1 , pp. 449-454
    • Watanabe, S.I.1    Chey, W.Y.2    Lee, K.Y.3    Chang, T.M.4
  • 108
    • 0026706780 scopus 로고
    • The origin of and subcellular mechanisms causing pancreatic bicarbonate secretion
    • Raeder M.G. The origin of and subcellular mechanisms causing pancreatic bicarbonate secretion. Gastroenterology 103 (1992) 1674-1684
    • (1992) Gastroenterology , vol.103 , pp. 1674-1684
    • Raeder, M.G.1
  • 109
    • 0023782863 scopus 로고
    • Secretin-regulated chloride channel on the apical plasma membrane of pancreatic duct cells
    • Gray M.A., Greenwell J.R., and Argent B.E. Secretin-regulated chloride channel on the apical plasma membrane of pancreatic duct cells. J Membr Biol 105 (1988) 131-142
    • (1988) J Membr Biol , vol.105 , pp. 131-142
    • Gray, M.A.1    Greenwell, J.R.2    Argent, B.E.3
  • 113
    • 0020070843 scopus 로고
    • Characterization of secretin and vasoactive intestinal peptide receptors in rat pancreatic plasma membranes using the native peptides, secretin-(7-27) and five secretin analogues
    • Robberecht P., Waelbroeck M., Noyer M., Chatelain P., De Neef P., Konig W., and Christophe J. Characterization of secretin and vasoactive intestinal peptide receptors in rat pancreatic plasma membranes using the native peptides, secretin-(7-27) and five secretin analogues. Digestion 23 (1982) 201-210
    • (1982) Digestion , vol.23 , pp. 201-210
    • Robberecht, P.1    Waelbroeck, M.2    Noyer, M.3    Chatelain, P.4    De Neef, P.5    Konig, W.6    Christophe, J.7
  • 114
    • 0020805434 scopus 로고
    • Use of 125I-secretin to identify and characterize high-affinity secretin receptors on pancreatic acini
    • Jensen R.T., Charlton C.G., Adachi H., Jones S.W., O'Donohue T.L., and Gardner J.D. Use of 125I-secretin to identify and characterize high-affinity secretin receptors on pancreatic acini. Am J Physiol 245 (1983) G186-G195
    • (1983) Am J Physiol , vol.245
    • Jensen, R.T.1    Charlton, C.G.2    Adachi, H.3    Jones, S.W.4    O'Donohue, T.L.5    Gardner, J.D.6
  • 117
    • 0021187329 scopus 로고
    • Importance of disulfide bonds in receptors for vasoactive intestinal peptide and secretin in rat pancreatic plasma membranes
    • Robberecht P., Waelbroeck M., Camus J.C., De Neef P., and Christophe J. Importance of disulfide bonds in receptors for vasoactive intestinal peptide and secretin in rat pancreatic plasma membranes. Biochim Biophys Acta 773 (1984) 271-278
    • (1984) Biochim Biophys Acta , vol.773 , pp. 271-278
    • Robberecht, P.1    Waelbroeck, M.2    Camus, J.C.3    De Neef, P.4    Christophe, J.5
  • 118
    • 0023180794 scopus 로고
    • Receptors for vasoactive intestinal peptide and secretin on guinea pig pancreatic acini
    • Zhou Z.C., Gardner J.D., and Jensen R.T. Receptors for vasoactive intestinal peptide and secretin on guinea pig pancreatic acini. Peptides 8 (1987) 633-637
    • (1987) Peptides , vol.8 , pp. 633-637
    • Zhou, Z.C.1    Gardner, J.D.2    Jensen, R.T.3
  • 119
    • 0028825598 scopus 로고
    • Secretin potentiates cholecystokinin-stimulated amylase release by AR4-2J cells via a stimulation of phospholipase C
    • Bold R.J., Ishizuka J., Townsend Jr. C.M., and Thompson J.C. Secretin potentiates cholecystokinin-stimulated amylase release by AR4-2J cells via a stimulation of phospholipase C. J Cell Physiol 165 (1995) 172-176
    • (1995) J Cell Physiol , vol.165 , pp. 172-176
    • Bold, R.J.1    Ishizuka, J.2    Townsend Jr., C.M.3    Thompson, J.C.4
  • 120
    • 0017413632 scopus 로고
    • Regulation of amylase release from dispersed pancreatic acinar cells
    • Gardner J.D., and Jackson M.J. Regulation of amylase release from dispersed pancreatic acinar cells. J Physiol 270 (1977) 439-454
    • (1977) J Physiol , vol.270 , pp. 439-454
    • Gardner, J.D.1    Jackson, M.J.2
  • 121
    • 0019364097 scopus 로고
    • Effects of vasoactive intestinal polypeptide (VIP), secretin and gastrin on insulin secretion in the mouse
    • Ahren B., and Lundquist I. Effects of vasoactive intestinal polypeptide (VIP), secretin and gastrin on insulin secretion in the mouse. Diabetologia 20 (1981) 54-59
    • (1981) Diabetologia , vol.20 , pp. 54-59
    • Ahren, B.1    Lundquist, I.2
  • 122
    • 0020561824 scopus 로고
    • Secretin inhibits glucagon in the isolated perfused dog pancreas
    • Hisatomi A., and Unger R.H. Secretin inhibits glucagon in the isolated perfused dog pancreas. Diabetes 32 (1983) 970-973
    • (1983) Diabetes , vol.32 , pp. 970-973
    • Hisatomi, A.1    Unger, R.H.2
  • 123
    • 0035448968 scopus 로고    scopus 로고
    • Regulation of slowly activating potassium current (I(Ks)) by secretin in rat pancreatic acinar cells
    • Kim S.J., Kim J.K., Pavenstadt H., Greger R., Hug M.J., and Bleich M. Regulation of slowly activating potassium current (I(Ks)) by secretin in rat pancreatic acinar cells. J Physiol 535 (2001) 349-358
    • (2001) J Physiol , vol.535 , pp. 349-358
    • Kim, S.J.1    Kim, J.K.2    Pavenstadt, H.3    Greger, R.4    Hug, M.J.5    Bleich, M.6
  • 124
    • 0034045206 scopus 로고    scopus 로고
    • Dual effect of secretin on nephron filtration and proximal reabsorption depending on the route of administration
    • Romano G., Giagu P., Favret G., and Bartoli E. Dual effect of secretin on nephron filtration and proximal reabsorption depending on the route of administration. Peptides 21 (2000) 723-728
    • (2000) Peptides , vol.21 , pp. 723-728
    • Romano, G.1    Giagu, P.2    Favret, G.3    Bartoli, E.4
  • 125
    • 0021610719 scopus 로고
    • Plasma secretin, pancreozymin, and somatostatin-like hormone in chronic renal failure patients
    • Grekas D.M., Raptis S., and Tourkantonis A.A. Plasma secretin, pancreozymin, and somatostatin-like hormone in chronic renal failure patients. Uremia Invest 8 (1984) 117-120
    • (1984) Uremia Invest , vol.8 , pp. 117-120
    • Grekas, D.M.1    Raptis, S.2    Tourkantonis, A.A.3
  • 128
    • 0025345541 scopus 로고
    • Secretory agonists stimulate a rise in intracellular cyclic AMP but not Ca2+ and inositol phosphates in cultured rat epididymal epithelium
    • Wong P.Y., and Huang S.J. Secretory agonists stimulate a rise in intracellular cyclic AMP but not Ca2+ and inositol phosphates in cultured rat epididymal epithelium. Exp Physiol 75 (1990) 321-337
    • (1990) Exp Physiol , vol.75 , pp. 321-337
    • Wong, P.Y.1    Huang, S.J.2
  • 129
    • 0022485466 scopus 로고
    • Vasoactive intestinal peptide stimulates androgen biosynthesis by cultured neonatal testicular cells
    • Kasson B.G., Lim P., and Hsueh A.J. Vasoactive intestinal peptide stimulates androgen biosynthesis by cultured neonatal testicular cells. Mol Cell Endocrinol 48 (1986) 21-29
    • (1986) Mol Cell Endocrinol , vol.48 , pp. 21-29
    • Kasson, B.G.1    Lim, P.2    Hsueh, A.J.3
  • 130
    • 0031936197 scopus 로고    scopus 로고
    • Secretin and vasoactive intestinal peptide receptors: members of a unique family of G protein-coupled receptors
    • Ulrich C.D., Holtmann M., and Miller L.J. Secretin and vasoactive intestinal peptide receptors: members of a unique family of G protein-coupled receptors. Gastroenterology 114 (1998) 382-397
    • (1998) Gastroenterology , vol.114 , pp. 382-397
    • Ulrich, C.D.1    Holtmann, M.2    Miller, L.J.3
  • 131
    • 0032571340 scopus 로고    scopus 로고
    • Molecular mechanisms of G protein-coupled receptor desensitization and resensitization
    • Ferguson S.S., Zhang J., Barak L.S., and Caron M.G. Molecular mechanisms of G protein-coupled receptor desensitization and resensitization. Life Sci 62 (1998) 1561-1565
    • (1998) Life Sci , vol.62 , pp. 1561-1565
    • Ferguson, S.S.1    Zhang, J.2    Barak, L.S.3    Caron, M.G.4
  • 132
    • 0029790078 scopus 로고    scopus 로고
    • Role of receptor phosphorylation in desensitization and internalization of the secretin receptor
    • Holtmann M.H., Roettger B.F., Pinon D.I., and Miller L.J. Role of receptor phosphorylation in desensitization and internalization of the secretin receptor. J Biol Chem 271 (1996) 23566-23571
    • (1996) J Biol Chem , vol.271 , pp. 23566-23571
    • Holtmann, M.H.1    Roettger, B.F.2    Pinon, D.I.3    Miller, L.J.4
  • 133
    • 0032549651 scopus 로고    scopus 로고
    • A role for receptor kinases in the regulation of class II G protein-coupled receptors. Phosphorylation and desensitization of the secretin receptor
    • Shetzline M.A., Premont R.T., Walker J.K., Vigna S.R., and Caron M.G. A role for receptor kinases in the regulation of class II G protein-coupled receptors. Phosphorylation and desensitization of the secretin receptor. J Biol Chem 273 (1998) 6756-6762
    • (1998) J Biol Chem , vol.273 , pp. 6756-6762
    • Shetzline, M.A.1    Premont, R.T.2    Walker, J.K.3    Vigna, S.R.4    Caron, M.G.5
  • 134
    • 0033615739 scopus 로고    scopus 로고
    • Properties of secretin receptor internalization differ from those of the beta(2)-adrenergic receptor
    • Walker J.K., Premont R.T., Barak L.S., Caron M.G., and Shetzline M.A. Properties of secretin receptor internalization differ from those of the beta(2)-adrenergic receptor. J Biol Chem 274 (1999) 31515-31523
    • (1999) J Biol Chem , vol.274 , pp. 31515-31523
    • Walker, J.K.1    Premont, R.T.2    Barak, L.S.3    Caron, M.G.4    Shetzline, M.A.5
  • 135
    • 0033559278 scopus 로고    scopus 로고
    • Real-time evaluation of human secretin receptor activity using cytosensor microphysiometry
    • Ng S.S., Pang R.T., Chow B.K., and Cheng C.H. Real-time evaluation of human secretin receptor activity using cytosensor microphysiometry. J Cell Biochem 72 (1999) 517-527
    • (1999) J Cell Biochem , vol.72 , pp. 517-527
    • Ng, S.S.1    Pang, R.T.2    Chow, B.K.3    Cheng, C.H.4


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