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Volumn 38, Issue 12, 2006, Pages 2151-2163

Different roles of protein kinase C-βI and -δ in the regulation of adipocyte differentiation

Author keywords

Adipocyte; Adipogenesis; Differentiation; PKC; Signaling

Indexed keywords

12 (2 CYANOETHYL) 6,7,12,13 TETRAHYDRO 13 METHYL 5 OXOINDOLO[2,3 A]PYRROLO[3,4 C]CARBAZOLE; 2 [1 (3 AMIDINOTHIOPROPYL) 1H INDOL 3 YL] 3 (1 METHYL 1H INDOL 3 YL)MALEIMIDE; DEXAMETHASONE; EPIDERMAL GROWTH FACTOR; INSULIN; ISOBUTYLMETHYLXANTHINE; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA AGONIST; PHORBOL 13 ACETATE 12 MYRISTATE; PROTEIN KINASE C; PROTEIN KINASE C ALPHA; PROTEIN KINASE C BETA1; PROTEIN KINASE C DELTA; PROTEIN KINASE C INHIBITOR; PROTEIN KINASE C MU; ROTTLERIN; TRANSFORMING GROWTH FACTOR BETA1; TROGLITAZONE; UNCLASSIFIED DRUG;

EID: 33748692452     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biocel.2006.06.009     Document Type: Article
Times cited : (39)

References (47)
  • 4
    • 0025743893 scopus 로고
    • Differentiation of 3T3-L1 fibroblasts to adipocytes induced by transfection of ras oncogenes
    • Benito M., Porras A., Nebreda A.R., and Santos E. Differentiation of 3T3-L1 fibroblasts to adipocytes induced by transfection of ras oncogenes. Science 253 (1991) 565-568
    • (1991) Science , vol.253 , pp. 565-568
    • Benito, M.1    Porras, A.2    Nebreda, A.R.3    Santos, E.4
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 72 (1976) 248-254
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0023274509 scopus 로고
    • Ia binding ligands and cAMP stimulate nuclear translocation of PKC in B lymphocytes
    • Cambier J.C., Newell M.K., Justement L.B., McGuire J.C., Leach K.L., and Chen Z.Z. Ia binding ligands and cAMP stimulate nuclear translocation of PKC in B lymphocytes. Nature 327 (1987) 629-632
    • (1987) Nature , vol.327 , pp. 629-632
    • Cambier, J.C.1    Newell, M.K.2    Justement, L.B.3    McGuire, J.C.4    Leach, K.L.5    Chen, Z.Z.6
  • 10
    • 0027104825 scopus 로고
    • The role of protein kinase C isoenzymes in the regulation of cell proliferation and differentiation
    • Clemens M.J., Trayner I., and Menaya J. The role of protein kinase C isoenzymes in the regulation of cell proliferation and differentiation. Journal of Cell Science 103 (1992) 881-887
    • (1992) Journal of Cell Science , vol.103 , pp. 881-887
    • Clemens, M.J.1    Trayner, I.2    Menaya, J.3
  • 11
    • 0032585532 scopus 로고    scopus 로고
    • Regulation of conventional protein kinase C isozymes by phosphoinositide-dependent kinase 1 (PDK-1)
    • Dutil E.M., Toker A., and Newton A.C. Regulation of conventional protein kinase C isozymes by phosphoinositide-dependent kinase 1 (PDK-1). Current Biology 8 (1998) 1366-1375
    • (1998) Current Biology , vol.8 , pp. 1366-1375
    • Dutil, E.M.1    Toker, A.2    Newton, A.C.3
  • 12
    • 0033610788 scopus 로고    scopus 로고
    • Specific inhibitors of 38p mitogen-activated protein kinase block 3T3-L1 adipogenesis
    • Engelman J.A., Lisanti M.P., and Scherer P.E. Specific inhibitors of 38p mitogen-activated protein kinase block 3T3-L1 adipogenesis. The Journal of Biological Chemistry 273 (1998) 32111-32120
    • (1998) The Journal of Biological Chemistry , vol.273 , pp. 32111-32120
    • Engelman, J.A.1    Lisanti, M.P.2    Scherer, P.E.3
  • 15
    • 0033838459 scopus 로고    scopus 로고
    • Insulin-activated protein kinase Cβ bypasses Ras and stimulates mitogen-activated protein kinase activity and cell proliferation in muscle cells
    • Formisano P., Oriente F., Fiory F., Caruso M., Miele C., Maitan M.A., et al. Insulin-activated protein kinase Cβ bypasses Ras and stimulates mitogen-activated protein kinase activity and cell proliferation in muscle cells. Molecular and Cellular Biology 21 (2000) 6323-6333
    • (2000) Molecular and Cellular Biology , vol.21 , pp. 6323-6333
    • Formisano, P.1    Oriente, F.2    Fiory, F.3    Caruso, M.4    Miele, C.5    Maitan, M.A.6
  • 16
    • 0024160854 scopus 로고
    • Characterization of a new oral antidiabetic agent CS-045: Studies in KK and ob/ob mice and Zucker fatty rats
    • Fujiwara T., Yoshioka S., Yoshioka T., Ushiyama I., and Horikoshi H. Characterization of a new oral antidiabetic agent CS-045: Studies in KK and ob/ob mice and Zucker fatty rats. Diabetes 37 (1988) 1549-1558
    • (1988) Diabetes , vol.37 , pp. 1549-1558
    • Fujiwara, T.1    Yoshioka, S.2    Yoshioka, T.3    Ushiyama, I.4    Horikoshi, H.5
  • 17
    • 0031026224 scopus 로고    scopus 로고
    • PKC-A pivotal regulator of early development
    • Gallicano G.I., Yousef M.C., and Capco D.G. PKC-A pivotal regulator of early development. Bioessays 19 (1997) 29-36
    • (1997) Bioessays , vol.19 , pp. 29-36
    • Gallicano, G.I.1    Yousef, M.C.2    Capco, D.G.3
  • 19
    • 0027253641 scopus 로고
    • Differential translocation of protein kinase C isozymes by thrombin and platelet-derived growth factor
    • Ha K.S., and Exton J.H. Differential translocation of protein kinase C isozymes by thrombin and platelet-derived growth factor. The Journal of Biological Chemistry 268 (1993) 10534-10539
    • (1993) The Journal of Biological Chemistry , vol.268 , pp. 10534-10539
    • Ha, K.S.1    Exton, J.H.2
  • 20
    • 0038776380 scopus 로고    scopus 로고
    • Inhibition of adipogenesis through MAP kinase-mediated phosphorylation of PPARγ
    • Hu E., Kim J.B., Sarraf P., and Spiegelman B.M. Inhibition of adipogenesis through MAP kinase-mediated phosphorylation of PPARγ. Science 274 (1996) 2100-2103
    • (1996) Science , vol.274 , pp. 2100-2103
    • Hu, E.1    Kim, J.B.2    Sarraf, P.3    Spiegelman, B.M.4
  • 21
    • 0027322679 scopus 로고
    • Protein kinase C isoenzymes: Divergence in signal transduction?
    • Hug H., and Sarre T.F. Protein kinase C isoenzymes: Divergence in signal transduction?. The Biochemical Journal 291 (1993) 329-343
    • (1993) The Biochemical Journal , vol.291 , pp. 329-343
    • Hug, H.1    Sarre, T.F.2
  • 23
    • 0024850568 scopus 로고
    • Insulin stimulates the translocation of protein kinase C in rat adipocytes
    • Ishizuka T., Cooper D.R., and Farese R.V. Insulin stimulates the translocation of protein kinase C in rat adipocytes. FEBS Letters 257 (1989) 337-340
    • (1989) FEBS Letters , vol.257 , pp. 337-340
    • Ishizuka, T.1    Cooper, D.R.2    Farese, R.V.3
  • 24
    • 0034703616 scopus 로고    scopus 로고
    • The role of atypical and conventional PKC in dehydroepiandrosterone-induced glucose uptake and dexamethasone-induced insulin resistance
    • Kajita K., Ishizuka T., Miura A., Ishizawa M., Kanoh Y., and Yasuda K. The role of atypical and conventional PKC in dehydroepiandrosterone-induced glucose uptake and dexamethasone-induced insulin resistance. Biochemistry and Biophysical Research Communications 277 (2000) 361-367
    • (2000) Biochemistry and Biophysical Research Communications , vol.277 , pp. 361-367
    • Kajita, K.1    Ishizuka, T.2    Miura, A.3    Ishizawa, M.4    Kanoh, Y.5    Yasuda, K.6
  • 25
    • 0026517080 scopus 로고
    • Enhancement of adipocyte differentiation by an insulin-sensitizing agent
    • Kletzien R.F., Clarke S.D., and Ulrich R.G. Enhancement of adipocyte differentiation by an insulin-sensitizing agent. Molecular Pharmacology 41 (1992) 393-398
    • (1992) Molecular Pharmacology , vol.41 , pp. 393-398
    • Kletzien, R.F.1    Clarke, S.D.2    Ulrich, R.G.3
  • 26
    • 0029587272 scopus 로고
    • Zeta PKC in rat preadipocytes: Modulation by insulin and serum mitogenic factors and possible role in adipogenesis
    • Lacasa D., Agli B., and Giudicelli Y. Zeta PKC in rat preadipocytes: Modulation by insulin and serum mitogenic factors and possible role in adipogenesis. Biochemical and Biophysical Research Communications 217 (1995) 123-130
    • (1995) Biochemical and Biophysical Research Communications , vol.217 , pp. 123-130
    • Lacasa, D.1    Agli, B.2    Giudicelli, Y.3
  • 27
    • 2442448425 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase activity by valproic acid blocks adipogenesis
    • Lagace D.C., and Nachtigal M.W. Inhibition of histone deacetylase activity by valproic acid blocks adipogenesis. The Journal of Biological Chemistry 279 (2004) 18851-18860
    • (2004) The Journal of Biological Chemistry , vol.279 , pp. 18851-18860
    • Lagace, D.C.1    Nachtigal, M.W.2
  • 28
    • 0029062839 scopus 로고
    • Transcriptional regulation of gene expression during adipocyte differentiation
    • MacDougald O.A., and Lane M.D. Transcriptional regulation of gene expression during adipocyte differentiation. Annual Reviews of Biochemistry 64 (1995) 345-373
    • (1995) Annual Reviews of Biochemistry , vol.64 , pp. 345-373
    • MacDougald, O.A.1    Lane, M.D.2
  • 32
    • 0029988355 scopus 로고    scopus 로고
    • Up-regulation of intracellular signalling pathways may play a central pathogenic role in hypertension, atherogenesis, insulin resistance, and cancer promotion-the 'PKC syndrome'
    • McCarty M.F. Up-regulation of intracellular signalling pathways may play a central pathogenic role in hypertension, atherogenesis, insulin resistance, and cancer promotion-the 'PKC syndrome'. Medical Hypotheses 46 (1996) 191-221
    • (1996) Medical Hypotheses , vol.46 , pp. 191-221
    • McCarty, M.F.1
  • 33
    • 0029913277 scopus 로고    scopus 로고
    • Protein kinase C isoform expression during the differentiation of 3T3-L1 preadipocytes: Loss of protein kinase C-alpha isoform correlates with loss of phorbol 12-myristate 13-acetate activation of nuclear factor kappaB and acquisition of the adipocyte phenotype
    • McGowan K., DeVente J., Carey J.O., Ways D.K., and Pekala P.H. Protein kinase C isoform expression during the differentiation of 3T3-L1 preadipocytes: Loss of protein kinase C-alpha isoform correlates with loss of phorbol 12-myristate 13-acetate activation of nuclear factor kappaB and acquisition of the adipocyte phenotype. Journal of Cellular Physiology 167 (1996) 113-120
    • (1996) Journal of Cellular Physiology , vol.167 , pp. 113-120
    • McGowan, K.1    DeVente, J.2    Carey, J.O.3    Ways, D.K.4    Pekala, P.H.5
  • 35
    • 0028048358 scopus 로고
    • Abrogation of the suppressive effects of dexamethasone by PKC activation or CD28 triggering
    • Nijhuis E.W., Hinloopen B., Odding J., and Nagelkerken L. Abrogation of the suppressive effects of dexamethasone by PKC activation or CD28 triggering. Cellular Immunology 156 (1994) 438-447
    • (1994) Cellular Immunology , vol.156 , pp. 438-447
    • Nijhuis, E.W.1    Hinloopen, B.2    Odding, J.3    Nagelkerken, L.4
  • 36
    • 0021227676 scopus 로고
    • The role of protein kinase C in cell surface signal transduction and tumour promotion
    • Nishizuka Y. The role of protein kinase C in cell surface signal transduction and tumour promotion. Nature 308 (1984) 693-698
    • (1984) Nature , vol.308 , pp. 693-698
    • Nishizuka, Y.1
  • 37
    • 0026451081 scopus 로고
    • Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C
    • Nishizuka Y. Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C. Science 258 (1992) 607-614
    • (1992) Science , vol.258 , pp. 607-614
    • Nishizuka, Y.1
  • 38
    • 0026045711 scopus 로고
    • Structural and functional diversities of a family of signal transducing protein kinases, protein kinase C family; two distinct classes of PKC, conventional cPKC and novel nPKC
    • Ohno S., Akita Y., Hata A., Osada S., Kubo K., Konno Y., et al. Structural and functional diversities of a family of signal transducing protein kinases, protein kinase C family; two distinct classes of PKC, conventional cPKC and novel nPKC. Advances in Enzyme Regulation 31 (1991) 287-303
    • (1991) Advances in Enzyme Regulation , vol.31 , pp. 287-303
    • Ohno, S.1    Akita, Y.2    Hata, A.3    Osada, S.4    Kubo, K.5    Konno, Y.6
  • 40
    • 0028359032 scopus 로고
    • Protein kinase C inhibitors enhance differentiation of rat adipocyte precursor cells in serum-free culture
    • Shinohara O., Murata Y., Kubota C., and Shinagawa T. Protein kinase C inhibitors enhance differentiation of rat adipocyte precursor cells in serum-free culture. Biochemical Medicine and Metabolic Biology 51 (1994) 85-90
    • (1994) Biochemical Medicine and Metabolic Biology , vol.51 , pp. 85-90
    • Shinohara, O.1    Murata, Y.2    Kubota, C.3    Shinagawa, T.4
  • 41
    • 0032435504 scopus 로고    scopus 로고
    • Subspecies-specific targeting mechanism of protein kinase C
    • Shirai Y., Sakai N., and Saito N. Subspecies-specific targeting mechanism of protein kinase C. Japanese Journal of Pharmacology 78 (1998) 411-417
    • (1998) Japanese Journal of Pharmacology , vol.78 , pp. 411-417
    • Shirai, Y.1    Sakai, N.2    Saito, N.3
  • 42
    • 0031898610 scopus 로고    scopus 로고
    • PPAR-gamma: Adipogenic regulator and thiazolidine receptor
    • Spiegelman B.M. PPAR-gamma: Adipogenic regulator and thiazolidine receptor. Diabetes 47 (1998) 507-514
    • (1998) Diabetes , vol.47 , pp. 507-514
    • Spiegelman, B.M.1
  • 43
    • 0037080343 scopus 로고    scopus 로고
    • The protein-tyrosine-phosphatase SHP2 is phosphorylated on serine residues 576 and 591 by protein kinase C isoforms alpha, beta 1, beta 2, and eta
    • Strack V., Krutzfeldt J., Kellerer M., Ullrich A., Lammers R., and Haring H.U. The protein-tyrosine-phosphatase SHP2 is phosphorylated on serine residues 576 and 591 by protein kinase C isoforms alpha, beta 1, beta 2, and eta. Biochemistry 41 (2002) 603-608
    • (2002) Biochemistry , vol.41 , pp. 603-608
    • Strack, V.1    Krutzfeldt, J.2    Kellerer, M.3    Ullrich, A.4    Lammers, R.5    Haring, H.U.6
  • 44
    • 0018869666 scopus 로고
    • Induction of fatty acid synthetase synthesis in differentiating 3T3-L1 preadipocytes
    • Student A.K., Hsu R.Y., and Lane M.D. Induction of fatty acid synthetase synthesis in differentiating 3T3-L1 preadipocytes. The Journal of Biological Chemistry 255 (1980) 4745-4750
    • (1980) The Journal of Biological Chemistry , vol.255 , pp. 4745-4750
    • Student, A.K.1    Hsu, R.Y.2    Lane, M.D.3
  • 45
    • 0028231383 scopus 로고
    • Cyclic AMP inhibits phosphatidylinositol-coupled and -uncoupled mitogenic signals in T lymphocytes. Evidence that camp alters PKC-induced transcription regulation of members of the jun and fos family of genes
    • Tamir A., and Isakov N. Cyclic AMP inhibits phosphatidylinositol-coupled and -uncoupled mitogenic signals in T lymphocytes. Evidence that camp alters PKC-induced transcription regulation of members of the jun and fos family of genes. Journal of Immunology 152 (1994) 3391-3399
    • (1994) Journal of Immunology , vol.152 , pp. 3391-3399
    • Tamir, A.1    Isakov, N.2
  • 46
    • 0025990261 scopus 로고
    • Involvement of alpha- and beta-PKC in the differentiation of 3T3-L1 cells
    • Ueda H., Ishida Y., and Taniguchi H. Involvement of alpha- and beta-PKC in the differentiation of 3T3-L1 cells. FEBS Letters 292 (1991) 57-60
    • (1991) FEBS Letters , vol.292 , pp. 57-60
    • Ueda, H.1    Ishida, Y.2    Taniguchi, H.3
  • 47
    • 0027241120 scopus 로고
    • Possible involvement of beta-PKC rather than that of alpha-PKC in differentiation of 3T3-L1 cells to adipocytes
    • Ueda H., Ishida Y., and Taniguchi H. Possible involvement of beta-PKC rather than that of alpha-PKC in differentiation of 3T3-L1 cells to adipocytes. European Journal of Clinical Investigation 23 (1993) 382-384
    • (1993) European Journal of Clinical Investigation , vol.23 , pp. 382-384
    • Ueda, H.1    Ishida, Y.2    Taniguchi, H.3


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