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Volumn 147, Issue 11, 2006, Pages 5294-5302

Decreased glucagon responsiveness by bile acids: a role for protein kinase Cα and glucagon receptor phosphorylation

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; ADENYLATE CYCLASE; BILE ACID; CHENODEOXYCHOLIC ACID; CYCLIC AMP; FORSKOLIN; GLUCAGON RECEPTOR; GUANINE NUCLEOTIDE BINDING PROTEIN; OKADAIC ACID; PHORBOL 13 ACETATE 12 MYRISTATE; PHOSPHORUS 32; PROTEIN KINASE C ALPHA; PROTEIN KINASE INHIBITOR;

EID: 33751258265     PISSN: 00137227     EISSN: 00137227     Source Type: Journal    
DOI: 10.1210/en.2006-0516     Document Type: Article
Times cited : (9)

References (47)
  • 1
    • 0035716295 scopus 로고    scopus 로고
    • Family-B G-protein-coupled receptors
    • REVIEWS3013
    • Harmar AJ 2001 Family-B G-protein-coupled receptors. Genome Biol 2:REVIEWS3013
    • (2001) Genome Biol , vol.2
    • Harmar, A.J.1
  • 3
    • 0032800486 scopus 로고    scopus 로고
    • Signal transduction and hepatocellular bile acid transport: Cross talk between bile acids and second messengers
    • Bouscarel B, Kroll S, Fromm H 1999 Signal transduction and hepatocellular bile acid transport: cross talk between bile acids and second messengers. Gastroenterology 117:433-452
    • (1999) Gastroenterology , vol.117 , pp. 433-452
    • Bouscarel, B.1    Kroll, S.2    Fromm, H.3
  • 4
    • 0037223063 scopus 로고    scopus 로고
    • Regulation of G protein-coupled receptor kinases and arrestins during receptor desensitization
    • Kohout TA, Lefkowitz RJ 2003 Regulation of G protein-coupled receptor kinases and arrestins during receptor desensitization. Mol Pharmacol 63:9-18
    • (2003) Mol Pharmacol , vol.63 , pp. 9-18
    • Kohout, T.A.1    Lefkowitz, R.J.2
  • 5
    • 0035805528 scopus 로고    scopus 로고
    • Regulation of membrane targeting of the G protein-coupled receptor kinase 2 by protein kinase A and its anchoring protein AKAP79
    • Cong M, Perry SJ, Lin FT, Fraser ID, Hu LA, Chen W, Pitcher JA, Scott JD, Lefkowitz RJ 2001 Regulation of membrane targeting of the G protein-coupled receptor kinase 2 by protein kinase A and its anchoring protein AKAP79. J Biol Chem 276:15192-15199
    • (2001) J Biol Chem , vol.276 , pp. 15192-15199
    • Cong, M.1    Perry, S.J.2    Lin, F.T.3    Fraser, I.D.4    Hu, L.A.5    Chen, W.6    Pitcher, J.A.7    Scott, J.D.8    Lefkowitz, R.J.9
  • 6
    • 0030841172 scopus 로고    scopus 로고
    • Effect of cholestasis on regulation of cAMP synthesis by glucagon and bile acids in isolated hepatocytes
    • Matsuzaki Y, Bouscarel B, Le M, Ceryak S, Gettys TW, Shoda J, Fromm H 1997 Effect of cholestasis on regulation of cAMP synthesis by glucagon and bile acids in isolated hepatocytes. Am J Physiol 273:G164-G173
    • (1997) Am J Physiol , vol.273
    • Matsuzaki, Y.1    Bouscarel, B.2    Le, M.3    Ceryak, S.4    Gettys, T.W.5    Shoda, J.6    Fromm, H.7
  • 7
    • 0028954737 scopus 로고
    • Ursodeoxycholic acid inhibits glucagon-induced cAMP formation in hamster hepatocytes: A role for PKC
    • Bouscarel B, Gettys TW, Fromm H, Dubner H 1995 Ursodeoxycholic acid inhibits glucagon-induced cAMP formation in hamster hepatocytes: a role for PKC. Am J Physiol 268:G300-G310
    • (1995) Am J Physiol , vol.268
    • Bouscarel, B.1    Gettys, T.W.2    Fromm, H.3    Dubner, H.4
  • 8
    • 0031798966 scopus 로고    scopus 로고
    • Changes in G protein expression account for impaired modulation of hepatic cAMP formation after bile duct-ligation
    • Bouscarel B, Matsuzaki Y, Le M, Gettys TW, Fromm H 1998 Changes in G protein expression account for impaired modulation of hepatic cAMP formation after bile duct-ligation. Am J Physiol 274:G1151-G1159
    • (1998) Am J Physiol , vol.274
    • Bouscarel, B.1    Matsuzaki, Y.2    Le, M.3    Gettys, T.W.4    Fromm, H.5
  • 9
    • 0028888589 scopus 로고
    • Alteration of cAMP-mediated hormonal responsiveness by bile acids in cells of nonhepatic origin
    • Bouscarel B, Ceryak S, Gettys TW, Fromm H, Noonan F 1995 Alteration of cAMP-mediated hormonal responsiveness by bile acids in cells of nonhepatic origin. Am J Physiol 268:G908-G916
    • (1995) Am J Physiol , vol.268
    • Bouscarel, B.1    Ceryak, S.2    Gettys, T.W.3    Fromm, H.4    Noonan, F.5
  • 12
    • 15844395343 scopus 로고    scopus 로고
    • Phosphorylation of PKC activation loop plays an important role in receptor-mediated translocation of PKC
    • Seki T, Matsubayashi H, Amano T, Shirai Y, Saito N, Sakai N 2005 Phosphorylation of PKC activation loop plays an important role in receptor-mediated translocation of PKC. Genes Cells 10:225-239
    • (2005) Genes Cells , vol.10 , pp. 225-239
    • Seki, T.1    Matsubayashi, H.2    Amano, T.3    Shirai, Y.4    Saito, N.5    Sakai, N.6
  • 13
    • 0023655187 scopus 로고
    • Down-regulation of protein kinase C is due to an increased rate of degradation
    • Young S, Parker PJ, Ullrich A, Stabel S 1987 Down-regulation of protein kinase C is due to an increased rate of degradation. Biochem J 244:775-779
    • (1987) Biochem J , vol.244 , pp. 775-779
    • Young, S.1    Parker, P.J.2    Ullrich, A.3    Stabel, S.4
  • 14
    • 0023764824 scopus 로고
    • The molecular heterogeneity of protein kinase C and its implications for cellular regulation
    • Nishizuka Y 1988 The molecular heterogeneity of protein kinase C and its implications for cellular regulation. Nature 334:661-665
    • (1988) Nature , vol.334 , pp. 661-665
    • Nishizuka, Y.1
  • 15
    • 0021237780 scopus 로고
    • Phorbol diesters promote β-adrenergic receptor phosphorylation and adenylate cyclase desensitization in duck erythrocytes
    • Sibley DR, Nambi P, Peters JR, Lefkowitz RJ 1984 Phorbol diesters promote β-adrenergic receptor phosphorylation and adenylate cyclase desensitization in duck erythrocytes. Biochem Biophys Res Commun 121:973-979
    • (1984) Biochem Biophys Res Commun , vol.121 , pp. 973-979
    • Sibley, D.R.1    Nambi, P.2    Peters, J.R.3    Lefkowitz, R.J.4
  • 16
    • 0030052418 scopus 로고    scopus 로고
    • Protein kinase C-dependent modulation of stimulatory guanine nucleotide binding protein of fetal rat skin keratinocytes
    • Tamura T, Takahashi H, Iizuka H 1996 Protein kinase C-dependent modulation of stimulatory guanine nucleotide binding protein of fetal rat skin keratinocytes. Arch Dermatol Res 288:24-30
    • (1996) Arch Dermatol Res , vol.288 , pp. 24-30
    • Tamura, T.1    Takahashi, H.2    Iizuka, H.3
  • 17
    • 0023127427 scopus 로고
    • The rapid desensitization of glucagon-stimulated adenylate cyclase is a cyclic AMP-independent process that can be mimicked by hormones which stimulate inositol phospholipid metabolism
    • Murphy GJ, Hruby VJ, Trivedi D, Wakelam MJO, Houslay MD 1987 The rapid desensitization of glucagon-stimulated adenylate cyclase is a cyclic AMP-independent process that can be mimicked by hormones which stimulate inositol phospholipid metabolism. Biochem J 243:39-46
    • (1987) Biochem J , vol.243 , pp. 39-46
    • Murphy, G.J.1    Hruby, V.J.2    Trivedi, D.3    Wakelam, M.J.O.4    Houslay, M.D.5
  • 18
    • 0033516651 scopus 로고    scopus 로고
    • Two cytoplasmic loops of the glucagon receptor are required to elevate cAMP or intracellular calcium
    • Cypess AM, Unson CG, Wu CR, Sakmar TP 1999 Two cytoplasmic loops of the glucagon receptor are required to elevate cAMP or intracellular calcium. J Biol Chem 274:19455-19464
    • (1999) J Biol Chem , vol.274 , pp. 19455-19464
    • Cypess, A.M.1    Unson, C.G.2    Wu, C.R.3    Sakmar, T.P.4
  • 19
    • 0034795255 scopus 로고    scopus 로고
    • Modulation of glucagon receptor expression and response in transfected human embryonic kidney cells
    • Ikegami T, Cypess AM, Bouscarel B 2001 Modulation of glucagon receptor expression and response in transfected human embryonic kidney cells. Am J Physiol Cell Physiol 281:C1396-C1402
    • (2001) Am J Physiol Cell Physiol , vol.281
    • Ikegami, T.1    Cypess, A.M.2    Bouscarel, B.3
  • 20
    • 0016374975 scopus 로고
    • A highly sensitive adenylate cyclase assay
    • Salomon Y, Londos C, Rodbell M 1974 A highly sensitive adenylate cyclase assay. Anal Biochem 58:541-548
    • (1974) Anal Biochem , vol.58 , pp. 541-548
    • Salomon, Y.1    Londos, C.2    Rodbell, M.3
  • 21
    • 33745781887 scopus 로고    scopus 로고
    • Bile acids stimulate PKCα autophosphorylation and activation: Role in the attenuation of prostaglandin E1-induced cAMP production in human dermal fibroblasts
    • Le M, Krilov L, Meng J, Chapin-Kennedy K, Ceryak S, Bouscarel B 2006 Bile acids stimulate PKCα autophosphorylation and activation: role in the attenuation of prostaglandin E1-induced cAMP production in human dermal fibroblasts. Am J Physiol Gastrointest Liver Physiol 291:G275-G287
    • (2006) Am J Physiol Gastrointest Liver Physiol , vol.291
    • Le, M.1    Krilov, L.2    Meng, J.3    Chapin-Kennedy, K.4    Ceryak, S.5    Bouscarel, B.6
  • 22
    • 0344310763 scopus 로고    scopus 로고
    • Mechanisms of β-adrenergic receptor desensitization and resensitization
    • Lefkowitz RJ, Pitcher J, Krueger K, Daaka Y 1998 Mechanisms of β-adrenergic receptor desensitization and resensitization. Adv Pharmacol 42:416-420
    • (1998) Adv Pharmacol , vol.42 , pp. 416-420
    • Lefkowitz, R.J.1    Pitcher, J.2    Krueger, K.3    Daaka, Y.4
  • 23
    • 0030469432 scopus 로고    scopus 로고
    • Glucagon and its receptor in various tissues
    • Christophe J 1996 Glucagon and its receptor in various tissues. Ann NY Acad Sci 805:31-42
    • (1996) Ann NY Acad Sci , vol.805 , pp. 31-42
    • Christophe, J.1
  • 24
    • 0029984153 scopus 로고    scopus 로고
    • Human glucagon receptor monoclonal antibodies: Antagonism of glucagon action and use in receptor characterization
    • Buggy J, Rossomando A, MacDougall M, Mierz D, Wunderlich D, Yoo Warren H 1996 Human glucagon receptor monoclonal antibodies: antagonism of glucagon action and use in receptor characterization. Horm Metab Res 28:215-219
    • (1996) Horm Metab Res , vol.28 , pp. 215-219
    • Buggy, J.1    Rossomando, A.2    MacDougall, M.3    Mierz, D.4    Wunderlich, D.5    Yoo Warren, H.6
  • 26
    • 0029810617 scopus 로고    scopus 로고
    • Heterologous desensitization of the glucagon-like peptide-1 receptor by phorbol esters requires phosphorylation of the cytoplasmic tail at four different sites
    • Widmann C, Dolci W, Thorens B 1996 Heterologous desensitization of the glucagon-like peptide-1 receptor by phorbol esters requires phosphorylation of the cytoplasmic tail at four different sites. J Biol Chem 271:19957-19963
    • (1996) J Biol Chem , vol.271 , pp. 19957-19963
    • Widmann, C.1    Dolci, W.2    Thorens, B.3
  • 27
    • 0023776093 scopus 로고
    • Vasoactive intestinal peptide receptor/adenylate cyclase system: Differences between agonist- And protein kinase C-mediated desensitization and further evidence for receptor internalization
    • Turner JT, Bollinger DW, Toews ML 1988 Vasoactive intestinal peptide receptor/adenylate cyclase system: differences between agonist- and protein kinase C-mediated desensitization and further evidence for receptor internalization. J Pharmacol Exp Ther 247:417-423
    • (1988) J Pharmacol Exp Ther , vol.247 , pp. 417-423
    • Turner, J.T.1    Bollinger, D.W.2    Toews, M.L.3
  • 28
    • 0035132949 scopus 로고    scopus 로고
    • G-protein-coupled receptor kinase 3- And protein kinase C-mediated desensitization of the PACAP receptor type 1 in human Y-79 retinoblastoma cells
    • Dautzenberg FM, Hauger RL 2001 G-protein-coupled receptor kinase 3- and protein kinase C-mediated desensitization of the PACAP receptor type 1 in human Y-79 retinoblastoma cells. Neuropharmacology 40:394-407
    • (2001) Neuropharmacology , vol.40 , pp. 394-407
    • Dautzenberg, F.M.1    Hauger, R.L.2
  • 30
    • 0028941914 scopus 로고
    • A role for protein kinase C-mediated phosphorylation in eliciting glucagon desensitization in rat hepatocytes
    • Savage A, Zeng L, Houslay MD 1995 A role for protein kinase C-mediated phosphorylation in eliciting glucagon desensitization in rat hepatocytes. Biochem J 307:281-285
    • (1995) Biochem J , vol.307 , pp. 281-285
    • Savage, A.1    Zeng, L.2    Houslay, M.D.3
  • 31
    • 0037674329 scopus 로고    scopus 로고
    • Distinct protein kinase C isoforms mediate regulation of vascular endothelial growth factor expression by A2A adenosine receptor activation and phorbol esters in pheochromocytoma PC12 cells
    • Gardner AM, Olah ME 2003 Distinct protein kinase C isoforms mediate regulation of vascular endothelial growth factor expression by A2A adenosine receptor activation and phorbol esters in pheochromocytoma PC12 cells. J Biol Chem 278:15421-15428
    • (2003) J Biol Chem , vol.278 , pp. 15421-15428
    • Gardner, A.M.1    Olah, M.E.2
  • 32
    • 0030220253 scopus 로고    scopus 로고
    • Possible involvement of protein kinase C-ε in phorbol ester-induced growth inhibition of human lymphoblastic cells
    • Mihalik R, Farkas G, Kopper L, Benczur M, Farago A 1996 Possible involvement of protein kinase C-ε in phorbol ester-induced growth inhibition of human lymphoblastic cells. Int J Biochem Cell Biol 28:925-933
    • (1996) Int J Biochem Cell Biol , vol.28 , pp. 925-933
    • Mihalik, R.1    Farkas, G.2    Kopper, L.3    Benczur, M.4    Farago, A.5
  • 35
    • 0014526250 scopus 로고
    • Conjugated and unconjugated serum bile acid level in patients with hepatobiliary diseases
    • Makino I, Nakagawa S, Mashimo K 1969 Conjugated and unconjugated serum bile acid level in patients with hepatobiliary diseases. Gastroenterology 56:1033-1039
    • (1969) Gastroenterology , vol.56 , pp. 1033-1039
    • Makino, I.1    Nakagawa, S.2    Mashimo, K.3
  • 37
    • 0029998598 scopus 로고    scopus 로고
    • Protein kinase C alters the responsiveness of adenylyl cyclases to G protein α and βγ subunits
    • Zimmermann G, Taussig R 1996 Protein kinase C alters the responsiveness of adenylyl cyclases to G protein α and βγ subunits. J Biol Chem 271:27161-27166
    • (1996) J Biol Chem , vol.271 , pp. 27161-27166
    • Zimmermann, G.1    Taussig, R.2
  • 38
    • 0032455112 scopus 로고    scopus 로고
    • Depletion of protein kinase C-α by antisense oligonucleotides alters β-adrenergic function and reverses the phorbol ester-induced reduction of isoproterenol-induced adenosine 3′-5′-cyclic monophosphate accumulation in murine Swiss 3T3 fibroblasts
    • Levesque L, Crooke ST 1998 Depletion of protein kinase C-α by antisense oligonucleotides alters β-adrenergic function and reverses the phorbol ester-induced reduction of isoproterenol-induced adenosine 3′-5′-cyclic monophosphate accumulation in murine Swiss 3T3 fibroblasts. J Pharmacol Exp Ther 287:425-434
    • (1998) J Pharmacol Exp Ther , vol.287 , pp. 425-434
    • Levesque, L.1    Crooke, S.T.2
  • 40
    • 0030906632 scopus 로고    scopus 로고
    • Bile salt-induced apoptosis of hepatocytes involves activation of protein kinase C
    • Jones BA, Rao Y-P, Stravitz RT, Gores GJ, Rao YP 1997 Bile salt-induced apoptosis of hepatocytes involves activation of protein kinase C. Am J Physiol 272:G1109-G1115
    • (1997) Am J Physiol , vol.272
    • Jones, B.A.1    Rao, Y.-P.2    Stravitz, R.T.3    Gores, G.J.4    Rao, Y.P.5
  • 42
    • 17044411372 scopus 로고    scopus 로고
    • Bile acid deoxycholate induces differential subcellular localisation of the PKC isoenzymes β1, ε and δ in colonic epithelial cells in a sodium butyrate insensitive manner
    • Looby E, Long A, Kelleher D, Volkov Y 2005 Bile acid deoxycholate induces differential subcellular localisation of the PKC isoenzymes β1, ε and δ in colonic epithelial cells in a sodium butyrate insensitive manner. Int J Cancer 114:887-895
    • (2005) Int J Cancer , vol.114 , pp. 887-895
    • Looby, E.1    Long, A.2    Kelleher, D.3    Volkov, Y.4
  • 43
    • 0021278290 scopus 로고
    • The phorbol ester, TPA inhibits glucagon-stimulated adenylate cyclase activity
    • Heyworth CM, Whetton AD, Kinsella AR, Houslay MD 1984 The phorbol ester, TPA inhibits glucagon-stimulated adenylate cyclase activity. FEBS Lett 170:38-42
    • (1984) FEBS Lett , vol.170 , pp. 38-42
    • Heyworth, C.M.1    Whetton, A.D.2    Kinsella, A.R.3    Houslay, M.D.4
  • 44
    • 33747787335 scopus 로고    scopus 로고
    • Bacterial expression of functional, biotinylated peripheral cannabinoid receptor CB2
    • in press
    • Krepkiy D, Wong K, Gawrisch K, Yeliseev A, Bacterial expression of functional, biotinylated peripheral cannabinoid receptor CB2. Protein Expr Purif, in press
    • Protein Expr Purif
    • Krepkiy, D.1    Wong, K.2    Gawrisch, K.3    Yeliseev, A.4
  • 45
    • 0029838532 scopus 로고    scopus 로고
    • Purification of a rat neurotensin receptor expressed in Escherichia coli
    • Tucker J, Grisshammer R 1996 Purification of a rat neurotensin receptor expressed in Escherichia coli. Biochem J 317(Pt 3):891-899
    • (1996) Biochem J , vol.317 , Issue.PART 3 , pp. 891-899
    • Tucker, J.1    Grisshammer, R.2
  • 46
    • 20144385917 scopus 로고    scopus 로고
    • Molecular characterization of a purified 5-HT4 receptor: A structural basis for drug efficacy
    • Baneres JL, Mesnier D, Martin A, Joubert L, Dumuis A, Bockaert J 2005 Molecular characterization of a purified 5-HT4 receptor: a structural basis for drug efficacy. J Biol Chem 280:20253-20260
    • (2005) J Biol Chem , vol.280 , pp. 20253-20260
    • Baneres, J.L.1    Mesnier, D.2    Martin, A.3    Joubert, L.4    Dumuis, A.5    Bockaert, J.6
  • 47
    • 0033105104 scopus 로고    scopus 로고
    • Instability of the G-protein β5 subunit in detergent
    • Jones MB, Garrison JC 1999 Instability of the G-protein β5 subunit in detergent. Anal Biochem 268:126-133
    • (1999) Anal Biochem , vol.268 , pp. 126-133
    • Jones, M.B.1    Garrison, J.C.2


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