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Volumn 1452, Issue 1, 1999, Pages 60-67

N-terminal glycation of cholecystokinin-8 abolishes its insulinotropic action on clonal pancreatic B-cells

Author keywords

BRIN BD11 cell; Cholecystokinin 8; Glycation; Insulin secretion

Indexed keywords

CHOLECYSTOKININ OCTAPEPTIDE; INSULIN;

EID: 0032881940     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4889(99)00108-1     Document Type: Article
Times cited : (13)

References (43)
  • 1
    • 0002572979 scopus 로고
    • Cholecystokinin
    • in: J.H. Walsh, G.J. Dockray (Eds.), Raven Press, New York
    • R.A. Liddle, Cholecystokinin, in: J.H. Walsh, G.J. Dockray (Eds.), Gut Peptides Biochemistry and Physiology, Raven Press, New York, 1994, pp. 175-216.
    • (1994) Gut Peptides Biochemistry and Physiology , pp. 175-216
    • Liddle, R.A.1
  • 2
    • 0028300692 scopus 로고
    • Biological actions of cholecystokinin
    • Crawley J.N., Corwin R.L. Biological actions of cholecystokinin. Peptides. 15:1995;731-755.
    • (1995) Peptides , vol.15 , pp. 731-755
    • Crawley, J.N.1    Corwin, R.L.2
  • 3
    • 0024323683 scopus 로고
    • Cholecystokinin in plasma
    • Cantor P. Cholecystokinin in plasma. Digestion. 42:1989;181-201.
    • (1989) Digestion , vol.42 , pp. 181-201
    • Cantor, P.1
  • 5
    • 0021905218 scopus 로고
    • Cholecystokinin bioactivity in human plasma: Molecular forms, responses to feeding and relationship to gall bladder contraction
    • Liddle R.A., Goldfine I.D., Rosen M.S., Taplitz R.A., Williams J.A. Cholecystokinin bioactivity in human plasma: molecular forms, responses to feeding and relationship to gall bladder contraction. J. Clin. Invest. 75:1985;1144-1152.
    • (1985) J. Clin. Invest. , vol.75 , pp. 1144-1152
    • Liddle, R.A.1    Goldfine, I.D.2    Rosen, M.S.3    Taplitz, R.A.4    Williams, J.A.5
  • 6
    • 0022596392 scopus 로고
    • Evidence that cholecystokinin interacts with specific receptors and regulates insulin release in isolated rat islets of Langerhans
    • Verspohl E.J., Ammon H.P.T., Williams J.A., Goldfine I.D. Evidence that cholecystokinin interacts with specific receptors and regulates insulin release in isolated rat islets of Langerhans. Diabetes. 35:1986;38-43.
    • (1986) Diabetes , vol.35 , pp. 38-43
    • Verspohl, E.J.1    Ammon, H.P.T.2    Williams, J.A.3    Goldfine, I.D.4
  • 7
    • 0022465619 scopus 로고
    • Influence of cholecystokinin on insulin output from isolated perifused pancreatic islets
    • Zawalich W.S., Cote S.B., Diaz V.A. Influence of cholecystokinin on insulin output from isolated perifused pancreatic islets. Endocrinology. 119:1986;616-621.
    • (1986) Endocrinology , vol.119 , pp. 616-621
    • Zawalich, W.S.1    Cote, S.B.2    Diaz, V.A.3
  • 9
    • 0031596422 scopus 로고    scopus 로고
    • 2 contributes to the insulinotropic action of cholecystokinin-8 in rat islets: Dissociation from the mechanism of carbachol
    • 2 contributes to the insulinotropic action of cholecystokinin-8 in rat islets: Dissociation from the mechanism of carbachol. Diabetes. 47:1998;1436-1443.
    • (1998) Diabetes , vol.47 , pp. 1436-1443
    • Simonsson, E.1    Karlsson, S.2    Ahren, B.3
  • 10
    • 0002255197 scopus 로고
    • Enteroinsular axis
    • in: J.H. Walsh, G.J. Dockray (Eds.), Raven Press, New York
    • J.C. Brown, Enteroinsular axis, in: J.H. Walsh, G.J. Dockray (Eds.), Gut Peptides Biochemistry and Physiology, Raven Press, New York, 1994, pp. 765-784.
    • (1994) Gut Peptides Biochemistry and Physiology , pp. 765-784
    • Brown, J.C.1
  • 11
    • 0141562800 scopus 로고    scopus 로고
    • Hormonal and neural control of endocrine pancreatic function
    • in: J. Pickup, G. Williams (Eds.), Blackwell Scientific Publications, Oxford
    • P.R. Flatt, Hormonal and neural control of endocrine pancreatic function, in: J. Pickup, G. Williams (Eds.), Textbook of Diabetes, 2 edn., Blackwell Scientific Publications, Oxford, 1997, pp. 9.1-9.17.
    • (1997) Textbook of Diabetes, 2 Edn. , pp. 91-917
    • Flatt, P.R.1
  • 13
    • 0030691128 scopus 로고    scopus 로고
    • Effects of non-glycated and glycated glucagon-like peptide-1 amide on glucose metabolism in isolated mouse abdominal muscle
    • O'Harte F.P.M., Gray A.M., Abdel-Wahab Y.H.A., Flatt P.R. Effects of non-glycated and glycated glucagon-like peptide-1 amide on glucose metabolism in isolated mouse abdominal muscle. Peptides. 18:1997;1327-1333.
    • (1997) Peptides , vol.18 , pp. 1327-1333
    • O'Harte, F.P.M.1    Gray, A.M.2    Abdel-Wahab, Y.H.A.3    Flatt, P.R.4
  • 14
    • 0031721266 scopus 로고    scopus 로고
    • Glycation of glucagon-like peptide-1 (7-36) amide: Characterisation and impaired action on rat insulin secreting cells
    • O'Harte F.P.M., Abdel-Wahab Y.H.A., Conlon J.M., Flatt P.R. Glycation of glucagon-like peptide-1 (7-36) amide: Characterisation and impaired action on rat insulin secreting cells. Diabetologia. 41:1998;1187-1193.
    • (1998) Diabetologia , vol.41 , pp. 1187-1193
    • O'Harte, F.P.M.1    Abdel-Wahab, Y.H.A.2    Conlon, J.M.3    Flatt, P.R.4
  • 15
    • 0031690197 scopus 로고    scopus 로고
    • Glycated cholecystokinin-8 has an enhanced satiating activity and is protected against enzymatic degradation
    • O'Harte F.P.M., Mooney M.H., Kelly C.M.N., Flatt P.R. Glycated cholecystokinin-8 has an enhanced satiating activity and is protected against enzymatic degradation. Diabetes. 47:1998;1619-1624.
    • (1998) Diabetes , vol.47 , pp. 1619-1624
    • O'Harte, F.P.M.1    Mooney, M.H.2    Kelly, C.M.N.3    Flatt, P.R.4
  • 16
    • 0031757194 scopus 로고    scopus 로고
    • Amino terminal glycation of gastric inhibitory polypeptide enhances its insulinotropic action on clonal pancreatic B-cells
    • O'Harte F.P.M., Abdel-Wahab Y.H.A., Conlon J.M., Flatt P.R. Amino terminal glycation of gastric inhibitory polypeptide enhances its insulinotropic action on clonal pancreatic B-cells. Biochim. Biophys. Acta. 1425:1998;319-327.
    • (1998) Biochim. Biophys. Acta , vol.1425 , pp. 319-327
    • O'Harte, F.P.M.1    Abdel-Wahab, Y.H.A.2    Conlon, J.M.3    Flatt, P.R.4
  • 17
    • 0032587206 scopus 로고    scopus 로고
    • N-terminally glycated gastric inhibitory polypeptide exhibits amino-peptidase resistance and enhanced antihyperglycemic activity
    • O'Harte F.P.M., Mooney M., Flatt P.R. N-terminally glycated gastric inhibitory polypeptide exhibits amino-peptidase resistance and enhanced antihyperglycemic activity. Diabetes. 48:1999;758-765.
    • (1999) Diabetes , vol.48 , pp. 758-765
    • O'Harte, F.P.M.1    Mooney, M.2    Flatt, P.R.3
  • 18
    • 0023391387 scopus 로고
    • Neuropeptide regulation of appetite and weight
    • Morley J.E. Neuropeptide regulation of appetite and weight. Endocrinol. Rev. 8:1987;256-287.
    • (1987) Endocrinol. Rev. , vol.8 , pp. 256-287
    • Morley, J.E.1
  • 19
    • 0025917573 scopus 로고
    • Role of CCK in the regulation of food intake
    • Silver A.J., Morley J.E. Role of CCK in the regulation of food intake. Prog. Neurobiol. 36:1991;23-34.
    • (1991) Prog. Neurobiol. , vol.36 , pp. 23-34
    • Silver, A.J.1    Morley, J.E.2
  • 20
    • 0027414248 scopus 로고
    • Reduced postprandial cholecystokinin (CCK) secretion in patients with non-insulin-dependent diabetes mellitus: Evidence for a role of CCK in regulating postprandial hyperglycemia
    • Rushakoff R.A., Goldfine I.D., Beccaria L.J., Mathur A., Brand R.J., Liddle R.A. Reduced postprandial cholecystokinin (CCK) secretion in patients with non-insulin-dependent diabetes mellitus: Evidence for a role of CCK in regulating postprandial hyperglycemia. J. Clin. Endocrinol. Metab. 76:1993;489-493.
    • (1993) J. Clin. Endocrinol. Metab. , vol.76 , pp. 489-493
    • Rushakoff, R.A.1    Goldfine, I.D.2    Beccaria, L.J.3    Mathur, A.4    Brand, R.J.5    Liddle, R.A.6
  • 22
    • 0019471997 scopus 로고
    • Abnormal plasma glucose and insulin responses in heterozygous lean (ob/+) mice
    • Flatt P.R., Bailey C.J. Abnormal plasma glucose and insulin responses in heterozygous lean (ob/+) mice. Diabetologia. 20:1981;573-577.
    • (1981) Diabetologia , vol.20 , pp. 573-577
    • Flatt, P.R.1    Bailey, C.J.2
  • 23
    • 0030473543 scopus 로고    scopus 로고
    • Identification of the site of glycation of human insulin
    • O'Harte F.P.M., Højrup P., Barnett C.R., Flatt P.R. Identification of the site of glycation of human insulin. Peptides. 17:1996;1323-1330.
    • (1996) Peptides , vol.17 , pp. 1323-1330
    • O'Harte, F.P.M.1    Højrup, P.2    Barnett, C.R.3    Flatt, P.R.4
  • 25
    • 0031030963 scopus 로고    scopus 로고
    • Characterisation of insulin glycation in insulin-secreting cells maintained in tissue culture
    • Abdel-Wahab Y.H.A., O'Harte F.P.M., Barnett C.R., Flatt P.R. Characterisation of insulin glycation in insulin-secreting cells maintained in tissue culture. J. Endocrinol. 152:1997;59-67.
    • (1997) J. Endocrinol. , vol.152 , pp. 59-67
    • Abdel-Wahab, Y.H.A.1    O'Harte, F.P.M.2    Barnett, C.R.3    Flatt, P.R.4
  • 26
    • 0029828189 scopus 로고    scopus 로고
    • Mechanisms of amino acid induced insulin secretion from the glucose-responsive BRIN-BD11 pancreatic B-cell line
    • McClenaghan N.H., Barnett C.R., O'Harte F.P.M., Flatt P.R. Mechanisms of amino acid induced insulin secretion from the glucose-responsive BRIN-BD11 pancreatic B-cell line. J. Endocrinol. 151:1996;349-357.
    • (1996) J. Endocrinol. , vol.151 , pp. 349-357
    • McClenaghan, N.H.1    Barnett, C.R.2    O'Harte, F.P.M.3    Flatt, P.R.4
  • 27
    • 0031974943 scopus 로고    scopus 로고
    • Insulin-releasing action of the novel antidiabetic agent BTS 67582
    • McClenaghan N.H., Flatt P.R., Bailey C.J. Insulin-releasing action of the novel antidiabetic agent BTS 67582. Br. J. Pharmacol. 123:1998;400-404.
    • (1998) Br. J. Pharmacol. , vol.123 , pp. 400-404
    • McClenaghan, N.H.1    Flatt, P.R.2    Bailey, C.J.3
  • 28
    • 0027974139 scopus 로고
    • Evidence for cholecystokinin receptor subtype in endocrine pancreas
    • Verspohl E.J., Hafner B., He X., Knittle J.J. Evidence for cholecystokinin receptor subtype in endocrine pancreas. Peptides. 15:1994;1353-1360.
    • (1994) Peptides , vol.15 , pp. 1353-1360
    • Verspohl, E.J.1    Hafner, B.2    He, X.3    Knittle, J.J.4
  • 29
    • 0021956275 scopus 로고
    • Localisation of saturable CCK binding sites in rat pancreatic islets by light and electron microscope autoradiography
    • Sakamoto C., Goldfine I.D., Roach E., Williams J.A. Localisation of saturable CCK binding sites in rat pancreatic islets by light and electron microscope autoradiography. Diabetes. 34:1985;390-394.
    • (1985) Diabetes , vol.34 , pp. 390-394
    • Sakamoto, C.1    Goldfine, I.D.2    Roach, E.3    Williams, J.A.4
  • 30
    • 0023573056 scopus 로고
    • Interactions of cholecystokinin and glucose in rat pancreatic islets
    • Zawalich W.S., Takuwa N., Takuwa Y., Diaz V.A., Rasmussen H. Interactions of cholecystokinin and glucose in rat pancreatic islets. Diabetes. 36:1987;426-433.
    • (1987) Diabetes , vol.36 , pp. 426-433
    • Zawalich, W.S.1    Takuwa, N.2    Takuwa, Y.3    Diaz, V.A.4    Rasmussen, H.5
  • 31
    • 0025773375 scopus 로고
    • Cholecystokinin-stimulated insulin secretion and protein kinase C in rat pancreatic islets
    • Karlsson S., Ahren B. Cholecystokinin-stimulated insulin secretion and protein kinase C in rat pancreatic islets. Acta Physiol. Scand. 142:1991;397-403.
    • (1991) Acta Physiol. Scand. , vol.142 , pp. 397-403
    • Karlsson, S.1    Ahren, B.2
  • 32
    • 0026625634 scopus 로고
    • Effects of CCK-8 on the cytoplasmic free calcium concentration in isolated rat islet cells
    • Fridolf T., Karlsson S., Ahren B. Effects of CCK-8 on the cytoplasmic free calcium concentration in isolated rat islet cells. Biochem. Biophys. Res. Commun. 184:1992;878-882.
    • (1992) Biochem. Biophys. Res. Commun. , vol.184 , pp. 878-882
    • Fridolf, T.1    Karlsson, S.2    Ahren, B.3
  • 34
    • 0024836493 scopus 로고
    • Glucagonostatic and insulinotropic action of glucagon-like peptide-1-(7-36)-amide
    • Komatsu R., Matsuyama T., Namba M. Glucagonostatic and insulinotropic action of glucagon-like peptide-1-(7-36)-amide. Diabetes. 38:1989;902-905.
    • (1989) Diabetes , vol.38 , pp. 902-905
    • Komatsu, R.1    Matsuyama, T.2    Namba, M.3
  • 35
    • 0024515406 scopus 로고
    • Glucagon-like peptide-1(7-37) actions on endocrine pancreas
    • Weir G.C., Mojsov S., Hendrick G.K., Habener J.F. Glucagon-like peptide-1(7-37) actions on endocrine pancreas. Diabetes. 38:1989;338-342.
    • (1989) Diabetes , vol.38 , pp. 338-342
    • Weir, G.C.1    Mojsov, S.2    Hendrick, G.K.3    Habener, J.F.4
  • 36
    • 0028305599 scopus 로고
    • Cholecystokinin receptor family: Molecular cloning, structure and functional expression in rat, guinea pig and human
    • Wank S.A., Pisegna J.R., Weerth A. Cholecystokinin receptor family: Molecular cloning, structure and functional expression in rat, guinea pig and human. Ann. NY Acad. Sci. 713:1994;49-66.
    • (1994) Ann. NY Acad. Sci. , vol.713 , pp. 49-66
    • Wank, S.A.1    Pisegna, J.R.2    Weerth, A.3
  • 37
    • 0028845124 scopus 로고
    • Cholecystokinin receptors
    • Wank S.A. Cholecystokinin receptors. Am. J. Physiol. 269:1995;G628-G646.
    • (1995) Am. J. Physiol. , vol.269
    • Wank, S.A.1
  • 38
    • 0023890519 scopus 로고
    • Cholecystokinin CCK-33 stimulates insulin secretion from the perfused rat pancreas: Studies on the structure-activity relationship
    • Sandberg E., Ahren B., Tendler D., Efendic S. Cholecystokinin CCK-33 stimulates insulin secretion from the perfused rat pancreas: Studies on the structure-activity relationship. Pharmacol. Toxicol. 63:1988;42-45.
    • (1988) Pharmacol. Toxicol. , vol.63 , pp. 42-45
    • Sandberg, E.1    Ahren, B.2    Tendler, D.3    Efendic, S.4
  • 39
    • 0025266913 scopus 로고
    • Glucagon-like peptide-1 analogs: Effects on insulin secretion and 3′,5′-monophosphate formation
    • Gefel D., Hendrick G.K., Mojsov S., Habener J., Weir G.C. Glucagon-like peptide-1 analogs: effects on insulin secretion and 3′,5′-monophosphate formation. Endocrinology. 126:1990;2164-2168.
    • (1990) Endocrinology , vol.126 , pp. 2164-2168
    • Gefel, D.1    Hendrick, G.K.2    Mojsov, S.3    Habener, J.4    Weir, G.C.5
  • 40
    • 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 B-cells
    • Göke R., Fehmann H.-C., Linn T., Schmidt H., Karuse M., Eng J., Goke B. 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 B-cells. J. Biol. Chem. 268:1993;19650-19655.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19650-19655
    • Göke, R.1    Fehmann, H.-C.2    Linn, T.3    Schmidt, H.4    Karuse, M.5    Eng, J.6    Goke, B.7
  • 41
    • 0028953577 scopus 로고
    • Degradation of glucagon-like peptide-1 by human plasma in vitro yields an N-terminally truncated peptide that is a major endogenous peptide in vivo
    • Deacon C.F., Johnsen A.H., Holst J.J. Degradation of glucagon-like peptide-1 by human plasma in vitro yields an N-terminally truncated peptide that is a major endogenous peptide in vivo. J. Clin. Endocrinol. Metab. 80:1995;952-957.
    • (1995) J. Clin. Endocrinol. Metab. , vol.80 , pp. 952-957
    • Deacon, C.F.1    Johnsen, A.H.2    Holst, J.J.3
  • 42
    • 0031782440 scopus 로고    scopus 로고
    • Dipepidyl peptidase IV resistant analogues of glucagon-like peptide-1 which have extended metabolic stability and improved biological activity
    • Deacon C.F., Knudsen L.B., Madsen K., Wiberg F.C., Jacobsen O., Holst J.J. Dipepidyl peptidase IV resistant analogues of glucagon-like peptide-1 which have extended metabolic stability and improved biological activity. Diabetologia. 41:1998;271-278.
    • (1998) Diabetologia , vol.41 , pp. 271-278
    • Deacon, C.F.1    Knudsen, L.B.2    Madsen, K.3    Wiberg, F.C.4    Jacobsen, O.5    Holst, J.J.6


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