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Volumn 202, Issue 1-2, 1999, Pages 101-108

Dexamethasone-induced decrease in HMG-CoA reductase and protein-farnesyl transferase activities does not impair ras processing in AR 4-2 J cells

Author keywords

HMG CoA reductase; Protein farnesyl transferase; ras processing

Indexed keywords

DEXAMETHASONE; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE; PROTEIN FARNESYLTRANSFERASE; RAS PROTEIN;

EID: 0033379416     PISSN: 03008177     EISSN: None     Source Type: Journal    
DOI: 10.1023/a:1007016403736     Document Type: Article
Times cited : (4)

References (41)
  • 1
    • 0027210447 scopus 로고
    • Posttranslational processing of the ras superfamily of small GTP-binding proteins
    • Newman CMH, Magee AI: Posttranslational processing of the ras superfamily of small GTP-binding proteins. Biochim Biophys Acta 1155: 79-96, 1993
    • (1993) Biochim Biophys Acta , vol.1155 , pp. 79-96
    • Newman, C.M.H.1    Magee, A.I.2
  • 2
    • 0026735063 scopus 로고
    • Protein isoprenylation and methylation at carboxyl-terminal cysteine residues
    • Clarke S: Protein isoprenylation and methylation at carboxyl-terminal cysteine residues. Ann Rev Biochem 61: 355-386, 1992
    • (1992) Ann Rev Biochem , vol.61 , pp. 355-386
    • Clarke, S.1
  • 3
    • 0026037624 scopus 로고
    • A CAAX or a CAAL motif and a second signal are sufficient for plasma membrane targeting of ras proteins
    • Hancock JF, Cadwallader K, Paterson H, Marshall CJ: A CAAX or a CAAL motif and a second signal are sufficient for plasma membrane targeting of ras proteins. EMBO J 10: 4033-4039, 1991
    • (1991) EMBO J , vol.10 , pp. 4033-4039
    • Hancock, J.F.1    Cadwallader, K.2    Paterson, H.3    Marshall, C.J.4
  • 4
    • 0026747866 scopus 로고
    • Isoprenoid addition to Ras protein is the critical modification for its membrane association and transforming activity
    • Kato K, Cox AD, Hisaka MM, Graham SM, Buss JE, Der CJ: Isoprenoid addition to Ras protein is the critical modification for its membrane association and transforming activity. Proc Natl Acad Sci (USA) 89: 6403-6407, 1992
    • (1992) Proc Natl Acad Sci (USA) , vol.89 , pp. 6403-6407
    • Kato, K.1    Cox, A.D.2    Hisaka, M.M.3    Graham, S.M.4    Buss, J.E.5    Der, C.J.6
  • 8
    • 0027933505 scopus 로고
    • Properties and kinetic mechanism of recombinant mammalian protein geranylgeranyltransferase type I
    • Zhang FL, Moomaw JF, Casey PJ: Properties and kinetic mechanism of recombinant mammalian protein geranylgeranyltransferase type I. J Biol Chem 269: 23465-23470, 1994
    • (1994) J Biol Chem , vol.269 , pp. 23465-23470
    • Zhang, F.L.1    Moomaw, J.F.2    Casey, P.J.3
  • 9
    • 0028988427 scopus 로고
    • Mammalian geranylgeranyl-transferase-I: Substrate specificity, kinetic mechanism, metal requirements, and affinity labeling
    • Yokoyama K, McGeady P, Gelb MH: Mammalian geranylgeranyl-transferase-I: Substrate specificity, kinetic mechanism, metal requirements, and affinity labeling. Biochem 34: 1344-1354, 1995
    • (1995) Biochem , vol.34 , pp. 1344-1354
    • Yokoyama, K.1    McGeady, P.2    Gelb, M.H.3
  • 10
    • 0029966304 scopus 로고    scopus 로고
    • Protein prenyltransferases
    • Casey PJ, Seabra MC: Protein prenyltransferases. J Biol Chem 271: 5289-5292, 1996
    • (1996) J Biol Chem , vol.271 , pp. 5289-5292
    • Casey, P.J.1    Seabra, M.C.2
  • 11
    • 0029985151 scopus 로고    scopus 로고
    • Effect of insulin on farnesyltransferase activity in 3T3-L1 adipocytes
    • Goalstone ML, Draznin B: Effect of insulin on farnesyltransferase activity in 3T3-L1 adipocytes. J Biol Chem 271: 27585-27589, 1996
    • (1996) J Biol Chem , vol.271 , pp. 27585-27589
    • Goalstone, M.L.1    Draznin, B.2
  • 12
    • 0030690195 scopus 로고    scopus 로고
    • Insulin stimulates the phosphorylation and activity of farnesyltransferase via the ras-mitogen-activated proteinkinase pathway
    • Goalstone M, Carel K, Leitner JW, Draznin B: Insulin stimulates the phosphorylation and activity of farnesyltransferase via the ras-mitogen-activated proteinkinase pathway. Endocrinology 138: 5119-5124, 1997
    • (1997) Endocrinology , vol.138 , pp. 5119-5124
    • Goalstone, M.1    Carel, K.2    Leitner, J.W.3    Draznin, B.4
  • 13
    • 0025120211 scopus 로고
    • Regulation of the mevalonate pathway
    • Goldstein JL, Brown MS: Regulation of the mevalonate pathway. Nature 343: 425-430, 1990
    • (1990) Nature , vol.343 , pp. 425-430
    • Goldstein, J.L.1    Brown, M.S.2
  • 14
    • 0027311304 scopus 로고
    • Transcriptional regulation by lovastatin and 25-hydroxycholesterol in HepG2 cells and molecular cloning and expression of the cDNA for the human hepatic squalene synthase
    • Jiang G, McKenzie TL, Conrad DG, Shechter I: Transcriptional regulation by lovastatin and 25-hydroxycholesterol in HepG2 cells and molecular cloning and expression of the cDNA for the human hepatic squalene synthase. J Biol Chem 268: 12818-12824, 1993
    • (1993) J Biol Chem , vol.268 , pp. 12818-12824
    • Jiang, G.1    McKenzie, T.L.2    Conrad, D.G.3    Shechter, I.4
  • 15
    • 0028216631 scopus 로고
    • Branch-point reactions in the biosynthesis of cholesterol, dolichol, ubiquinone and prenylated proteins
    • Grünler J, Ericsson J, Dallner G: Branch-point reactions in the biosynthesis of cholesterol, dolichol, ubiquinone and prenylated proteins. Biochim Biophys Acta 1212: 259-277, 1994
    • (1994) Biochim Biophys Acta , vol.1212 , pp. 259-277
    • Grünler, J.1    Ericsson, J.2    Dallner, G.3
  • 16
    • 0030723114 scopus 로고    scopus 로고
    • Post-translational regulation of mevalonate kinase by intermediates of the cholesterol and nonsterol isoprene biosynthetic pathways
    • Hinson DD, Chambliss KL, Toth MJ, Tanaka RD, Gibson KM: Post-translational regulation of mevalonate kinase by intermediates of the cholesterol and nonsterol isoprene biosynthetic pathways. J Lipid Res 38: 2216-2223, 1997
    • (1997) J Lipid Res , vol.38 , pp. 2216-2223
    • Hinson, D.D.1    Chambliss, K.L.2    Toth, M.J.3    Tanaka, R.D.4    Gibson, K.M.5
  • 17
    • 0021961927 scopus 로고
    • Glucocorticoids increase amylase mRNA levels, secretory organelles, and secretion in pancreatic acinar AR4-2J cells
    • Logsdon CD, Moessner J, Williams JA, Goldfine ID: Glucocorticoids increase amylase mRNA levels, secretory organelles, and secretion in pancreatic acinar AR4-2J cells. J Cell Biol 100: 1200-1208, 1985
    • (1985) J Cell Biol , vol.100 , pp. 1200-1208
    • Logsdon, C.D.1    Moessner, J.2    Williams, J.A.3    Goldfine, I.D.4
  • 18
    • 0026013192 scopus 로고
    • Functional and molecular characterization of CCK receptors in the rat pancreatic acinar cell line AR 4-2J
    • Lambert M, Bui ND, Christophe J: Functional and molecular characterization of CCK receptors in the rat pancreatic acinar cell line AR 4-2J. Reg Pep 32: 151-167, 1991
    • (1991) Reg Pep , vol.32 , pp. 151-167
    • Lambert, M.1    Bui, N.D.2    Christophe, J.3
  • 19
    • 0025814971 scopus 로고
    • Regulation of amylase and chymotrypsinogen expression by dexamethasone and caerulein in serum-free cultured pancreatic acinar AR4-2J cells
    • Estival A, Pradel P, Wicker-Planquart C, Vaysse N, Puigserver A, Clemente F: Regulation of amylase and chymotrypsinogen expression by dexamethasone and caerulein in serum-free cultured pancreatic acinar AR4-2J cells. Biochem J 279: 197-201, 1991
    • (1991) Biochem J , vol.279 , pp. 197-201
    • Estival, A.1    Pradel, P.2    Wicker-Planquart, C.3    Vaysse, N.4    Puigserver, A.5    Clemente, F.6
  • 21
    • 0028050404 scopus 로고
    • Growth-promoting effects of glycine-extended progastrin
    • Seva C, Dickinson CJ, Yamada T: Growth-promoting effects of glycine-extended progastrin. Science 265: 410-412, 1994
    • (1994) Science , vol.265 , pp. 410-412
    • Seva, C.1    Dickinson, C.J.2    Yamada, T.3
  • 22
    • 0025630619 scopus 로고
    • Internalization-sequestration and degradation of cholecystokinin (CCK) in tumoral rat pancreatic AR 4-2J cells
    • Svoboda M, Dupuche MH, Lambert M, Bui D, Christophe J: Internalization-sequestration and degradation of cholecystokinin (CCK) in tumoral rat pancreatic AR 4-2J cells. Biochim Biophys Acta 1055: 207-216, 1990
    • (1990) Biochim Biophys Acta , vol.1055 , pp. 207-216
    • Svoboda, M.1    Dupuche, M.H.2    Lambert, M.3    Bui, D.4    Christophe, J.5
  • 23
    • 33748037939 scopus 로고
    • Amylases, α and β
    • Bernfeld P: Amylases, α and β. Meth Enzymol 1: 149-158, 1955
    • (1955) Meth Enzymol , vol.1 , pp. 149-158
    • Bernfeld, P.1
  • 25
    • 0028959503 scopus 로고
    • Suppression of the proliferation of ras-transformed cells by fluoromevalonate, an inhibitor of mevalonate metabolism
    • Cuthbert JA, Lipsky PE: Suppression of the proliferation of ras-transformed cells by fluoromevalonate, an inhibitor of mevalonate metabolism. Cancer Res 55: 1732-1740, 1995
    • (1995) Cancer Res , vol.55 , pp. 1732-1740
    • Cuthbert, J.A.1    Lipsky, P.E.2
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685, 1970
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 0025053605 scopus 로고
    • The sensitivity of dot immunoassay for the peptides helodermin, histidine-isoleucinamide (PHI) and histidine-methioninamide (PHM) increases after peptide cross-linking to proteins prefixed on nitrocellulose
    • Gourlet P, Svoboda M, Cauvin A, Christophe J: The sensitivity of dot immunoassay for the peptides helodermin, histidine-isoleucinamide (PHI) and histidine-methioninamide (PHM) increases after peptide cross-linking to proteins prefixed on nitrocellulose. J Immunol Meth 133: 151-157, 1990
    • (1990) J Immunol Meth , vol.133 , pp. 151-157
    • Gourlet, P.1    Svoboda, M.2    Cauvin, A.3    Christophe, J.4
  • 28
    • 0027971885 scopus 로고
    • Relative quantitative analysis of glucagon receptor mRNA in rat tissues
    • Svoboda M, Tastenoy M, Vertongen P, Robberecht P: Relative quantitative analysis of glucagon receptor mRNA in rat tissues. Mol Cell Endocrinol 105: 131-137, 1994
    • (1994) Mol Cell Endocrinol , vol.105 , pp. 131-137
    • Svoboda, M.1    Tastenoy, M.2    Vertongen, P.3    Robberecht, P.4
  • 29
    • 0023604660 scopus 로고
    • Isoprenylated proteins in cultured cells: Subcellular distribution and changes related to altered morphology and growth arrest induced by mevalonate deprivation
    • Maltese WA, Sheridan KM: Isoprenylated proteins in cultured cells: Subcellular distribution and changes related to altered morphology and growth arrest induced by mevalonate deprivation. J Cell Physiol 133: 471-481, 1987
    • (1987) J Cell Physiol , vol.133 , pp. 471-481
    • Maltese, W.A.1    Sheridan, K.M.2
  • 30
    • 0021204120 scopus 로고
    • Evidence for post-translational incorporation of a product of mevalonic acid into Swiss 3T3 cell
    • Schmidt RA, Schneider CJ, Glomset JA: Evidence for post-translational incorporation of a product of mevalonic acid into Swiss 3T3 cell. J Biol Chem 259: 10175-10180, 1984
    • (1984) J Biol Chem , vol.259 , pp. 10175-10180
    • Schmidt, R.A.1    Schneider, C.J.2    Glomset, J.A.3
  • 31
    • 0026095237 scopus 로고
    • Glucocorticoids stimulate ornithine decarboxylase gene expression in pancreatic AR42J cells
    • Rosewics S, Logsdon CD: Glucocorticoids stimulate ornithine decarboxylase gene expression in pancreatic AR42J cells. Gastroenterology 101: 1102-1108, 1991
    • (1991) Gastroenterology , vol.101 , pp. 1102-1108
    • Rosewics, S.1    Logsdon, C.D.2
  • 32
    • 0028007527 scopus 로고
    • Transient stabilization of cholecystokinin a receptor mRNA by glucocorticoids in pancreatic AR42J cells
    • Rosewicz S, Riecken EO, Kaiser A: Transient stabilization of cholecystokinin A receptor mRNA by glucocorticoids in pancreatic AR42J cells. Am J Physiol 267: G772-G777, 1994
    • (1994) Am J Physiol , vol.267
    • Rosewicz, S.1    Riecken, E.O.2    Kaiser, A.3
  • 33
    • 0028200515 scopus 로고
    • Bombesin receptor gene expression in rat pancreatic acinar AR42J cells: Transcriptional regulation by glucocorticoids
    • Rosewicz S, Detjen K, Kaiser A, Prosenc N, Cervos-Navarro J, Riecken EO, Haller H: Bombesin receptor gene expression in rat pancreatic acinar AR42J cells: Transcriptional regulation by glucocorticoids. Gastroenterology 107:208-218, 1994
    • (1994) Gastroenterology , vol.107 , pp. 208-218
    • Rosewicz, S.1    Detjen, K.2    Kaiser, A.3    Prosenc, N.4    Cervos-Navarro, J.5    Riecken, E.O.6    Haller, H.7
  • 34
    • 0025853527 scopus 로고
    • Glandular kallikrein gene expression is selectively down-regulated by glucocorticoids in pancreatic AR42J cells
    • Rosewicz S, Detjen K, Logsdon CD, Chen LM, Chao J, Riecken EO: Glandular kallikrein gene expression is selectively down-regulated by glucocorticoids in pancreatic AR42J cells. Endocrinology 128:2216-2222, 1991
    • (1991) Endocrinology , vol.128 , pp. 2216-2222
    • Rosewicz, S.1    Detjen, K.2    Logsdon, C.D.3    Chen, L.M.4    Chao, J.5    Riecken, E.O.6
  • 36
    • 0031591692 scopus 로고    scopus 로고
    • Differential expression of Rab3 isoforms during differentiation of pancreatic acinar cell line AR42J
    • Klengel R, Piiper A, Pittelkow S, Zeuzem S: Differential expression of Rab3 isoforms during differentiation of pancreatic acinar cell line AR42J. Biochem Biophys Res Commun 236: 719-722, 1997
    • (1997) Biochem Biophys Res Commun , vol.236 , pp. 719-722
    • Klengel, R.1    Piiper, A.2    Pittelkow, S.3    Zeuzem, S.4
  • 37
    • 0030962347 scopus 로고    scopus 로고
    • The potential of farnesyltransferase inhibitors as cancer chemotherapeutics
    • Gibbs JB, Oliff A: The potential of farnesyltransferase inhibitors as cancer chemotherapeutics. Ann Rev Pharmacol Toxicol 37: 143-166, 1997
    • (1997) Ann Rev Pharmacol Toxicol , vol.37 , pp. 143-166
    • Gibbs, J.B.1    Oliff, A.2
  • 38
    • 0030749458 scopus 로고    scopus 로고
    • Farnesyltransferase inhibitors and cancer treatment: Targeting simply Ras?
    • Cox AD, Der CJ: Farnesyltransferase inhibitors and cancer treatment: Targeting simply Ras? Biochim Biophys Acta 1333: F51-F71, 1997
    • (1997) Biochim Biophys Acta , vol.1333
    • Cox, A.D.1    Der, C.J.2
  • 39
    • 0025202968 scopus 로고
    • Differential inhibitory effects of lovastatin on protein isoprenylation and sterol synthesis
    • Sinensky M, Beck LA, Leonard S, Evans R: Differential inhibitory effects of lovastatin on protein isoprenylation and sterol synthesis. J Biol Chem 265: 19937-19941, 1990
    • (1990) J Biol Chem , vol.265 , pp. 19937-19941
    • Sinensky, M.1    Beck, L.A.2    Leonard, S.3    Evans, R.4
  • 40
    • 0031434108 scopus 로고    scopus 로고
    • Induction of the cholesterol metabolic pathway regulates the farnesylation of RAS in embryonic chick heart cells: A new role for Ras in regulating the expression of muscarinic receptors and G proteins
    • Gadbut AP, Wu L, Tang D, Papageorge A, Watson JA, Galper JB: Induction of the cholesterol metabolic pathway regulates the farnesylation of RAS in embryonic chick heart cells: A new role for Ras in regulating the expression of muscarinic receptors and G proteins. Embo J 16: 7250-7260, 1997
    • (1997) Embo J , vol.16 , pp. 7250-7260
    • Gadbut, A.P.1    Wu, L.2    Tang, D.3    Papageorge, A.4    Watson, J.A.5    Galper, J.B.6
  • 41
    • 0027788125 scopus 로고
    • Ras Protein p21 processing enzyme farnesyltransferase in chemical carcinogen-induced murine skin tumors
    • Agarwal R, Khan SG, Athar M, Zaidi SIA, Bickers DR, Mukhtar H: ras Protein p21 processing enzyme farnesyltransferase in chemical carcinogen-induced murine skin tumors. Mol Carcinogen 8: 290-298, 1993
    • (1993) Mol Carcinogen , vol.8 , pp. 290-298
    • Agarwal, R.1    Khan, S.G.2    Athar, M.3    Sia, Z.4    Bickers, D.R.5    Mukhtar, H.6


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