메뉴 건너뛰기




Volumn 1781, Issue 5, 2008, Pages 277-281

Protein kinase CβI interacts with the β1-adrenergic signaling pathway to attenuate lipolysis in rat adipocytes

Author keywords

Adrenergic receptor; Adipocyte; Lipolysis; PKC; PKC I

Indexed keywords

4,5 BIS(4 FLUOROANILINO)PHTHALIMIDE; BETA 1 ADRENERGIC RECEPTOR; DOBUTAMINE; PHORBOL 13 ACETATE 12 MYRISTATE; PROTEIN KINASE C ALPHA; PROTEIN KINASE C BETA; PROTEIN KINASE C BETA INHIBITOR; PROTEIN KINASE C BETAI; PROTEIN KINASE C BETAII; PROTEIN KINASE C DELTA; PROTEIN KINASE C EPSILON; PROTEIN KINASE C ZETA; ROTTLERIN; RUBOXISTAURIN; BETA ADRENERGIC RECEPTOR STIMULATING AGENT; ISOENZYME; PROTEIN KINASE C;

EID: 43149096898     PISSN: 13881981     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbalip.2008.03.007     Document Type: Article
Times cited : (8)

References (42)
  • 1
    • 29044440372 scopus 로고    scopus 로고
    • Signalling mechanisms regulating lipolysis
    • Carmen G.-Y., and Víctor S.-M. Signalling mechanisms regulating lipolysis. Cell. Signal. 18 (2006) 401-408
    • (2006) Cell. Signal. , vol.18 , pp. 401-408
    • Carmen, G.-Y.1    Víctor, S.-M.2
  • 2
    • 0034032303 scopus 로고    scopus 로고
    • Obesity - a genetic disease of adipose tissue?
    • Arner P. Obesity - a genetic disease of adipose tissue?. Br. J. Nutr. 83 (2000) S9-S16
    • (2000) Br. J. Nutr. , vol.83
    • Arner, P.1
  • 3
    • 34247383057 scopus 로고    scopus 로고
    • Molecular mechanism of insulin resistance
    • Bhattacharya S., Dey D., and Roy S.S. Molecular mechanism of insulin resistance. J. Biosci. 32 (2007) 405-413
    • (2007) J. Biosci. , vol.32 , pp. 405-413
    • Bhattacharya, S.1    Dey, D.2    Roy, S.S.3
  • 5
    • 33847714769 scopus 로고    scopus 로고
    • Control of adipose triglyceride lipase action by serine 517 of perilipin A globally regulates protein kinase A-stimulated lipolysis in adipocytes
    • Miyoshi H., Perfield J.W., Souza S.C., Shen W.J., Zhang H.H., Stancheva Z.S., Kraemer F.B., Obin M.S., and Greenberg A.S. Control of adipose triglyceride lipase action by serine 517 of perilipin A globally regulates protein kinase A-stimulated lipolysis in adipocytes. J. Biol. Chem. 282 (2007) 996-1002
    • (2007) J. Biol. Chem. , vol.282 , pp. 996-1002
    • Miyoshi, H.1    Perfield, J.W.2    Souza, S.C.3    Shen, W.J.4    Zhang, H.H.5    Stancheva, Z.S.6    Kraemer, F.B.7    Obin, M.S.8    Greenberg, A.S.9
  • 6
    • 0032143284 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase: the key switch mechanism in insulin signalling
    • Shepherd P.R., Withers D.J., and Siddle K. Phosphoinositide 3-kinase: the key switch mechanism in insulin signalling. Biochem. J. 333 (1998) 471-490
    • (1998) Biochem. J. , vol.333 , pp. 471-490
    • Shepherd, P.R.1    Withers, D.J.2    Siddle, K.3
  • 8
    • 0034984029 scopus 로고    scopus 로고
    • Insulin-sensitive phospholipid signaling systems and glucose transport. Update II
    • Farese R.V. Insulin-sensitive phospholipid signaling systems and glucose transport. Update II. Exp. Biol. Med. 226 (2001) 283-295
    • (2001) Exp. Biol. Med. , vol.226 , pp. 283-295
    • Farese, R.V.1
  • 9
    • 33746983981 scopus 로고    scopus 로고
    • Specific protein kinase C isoforms as transducers and modulators of insulin signaling
    • Sampson S.R., and Cooper D.R. Specific protein kinase C isoforms as transducers and modulators of insulin signaling. Mol. Genet. Metab. 89 (2006) 32-47
    • (2006) Mol. Genet. Metab. , vol.89 , pp. 32-47
    • Sampson, S.R.1    Cooper, D.R.2
  • 10
    • 34548629361 scopus 로고    scopus 로고
    • Protein kinase C-dependent antilipolysis by insulin in rat adipocytes
    • Nakamura J. Protein kinase C-dependent antilipolysis by insulin in rat adipocytes. Biochim. Biophys. Acta 1771 (2007) 1195-1201
    • (2007) Biochim. Biophys. Acta , vol.1771 , pp. 1195-1201
    • Nakamura, J.1
  • 11
    • 33644615824 scopus 로고    scopus 로고
    • Protein kinase C attenuates β-adrenergic receptor-mediated lipolysis, probably through inhibition of the β1-adrenergic receptor system
    • Nakamura J. Protein kinase C attenuates β-adrenergic receptor-mediated lipolysis, probably through inhibition of the β1-adrenergic receptor system. Arch. Biochem. Biophys. 447 (2006) 1-10
    • (2006) Arch. Biochem. Biophys. , vol.447 , pp. 1-10
    • Nakamura, J.1
  • 12
    • 1842635735 scopus 로고    scopus 로고
    • Augmentation of lipolysis in adipocytes from fed rats, but not from starved rats, by inhibition of rolipram-sensitive phosphodiesterase 4
    • Nakamura J., Okamura N., and Kawakami Y. Augmentation of lipolysis in adipocytes from fed rats, but not from starved rats, by inhibition of rolipram-sensitive phosphodiesterase 4. Arch. Biochem. Biophys. 425 (2004) 106-114
    • (2004) Arch. Biochem. Biophys. , vol.425 , pp. 106-114
    • Nakamura, J.1    Okamura, N.2    Kawakami, Y.3
  • 13
    • 0031907117 scopus 로고    scopus 로고
    • Activation of protein kinase C triggers its ubiquitination and degradation
    • Lu Z., Liu D., Hornia A., Devonish W., Pagano M., and Foster D.A. Activation of protein kinase C triggers its ubiquitination and degradation. Mol. Cell. Biol. 18 (1998) 839-845
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 839-845
    • Lu, Z.1    Liu, D.2    Hornia, A.3    Devonish, W.4    Pagano, M.5    Foster, D.A.6
  • 15
    • 0033605582 scopus 로고    scopus 로고
    • Role of protein kinase C in the translational regulation of lipoprotein lipase in adipocytes
    • Ranganathan G., Kaakaji R., and Kern P.A. Role of protein kinase C in the translational regulation of lipoprotein lipase in adipocytes. J. Biol. Chem. 274 (1999) 9122-9127
    • (1999) J. Biol. Chem. , vol.274 , pp. 9122-9127
    • Ranganathan, G.1    Kaakaji, R.2    Kern, P.A.3
  • 18
    • 0036300538 scopus 로고    scopus 로고
    • Lipid-induced insulin resistance in human muscle is associated with changes in diacylglycerol, protein kinase C and IkB-α
    • Itani S.I., Ruderman N.B., Schmieder F., and Boden G. Lipid-induced insulin resistance in human muscle is associated with changes in diacylglycerol, protein kinase C and IkB-α. Diabetes 51 (2002) 2005-2011
    • (2002) Diabetes , vol.51 , pp. 2005-2011
    • Itani, S.I.1    Ruderman, N.B.2    Schmieder, F.3    Boden, G.4
  • 20
    • 0032813243 scopus 로고    scopus 로고
    • Tissue and isoform-selective activation of protein kinase C in insulin-resistant obese Zucker rats - effects of feeding
    • Qu X., Seale J.P., and Donnelly R. Tissue and isoform-selective activation of protein kinase C in insulin-resistant obese Zucker rats - effects of feeding. J. Endocrinol. 162 (1999) 207-214
    • (1999) J. Endocrinol. , vol.162 , pp. 207-214
    • Qu, X.1    Seale, J.P.2    Donnelly, R.3
  • 21
    • 0032915470 scopus 로고    scopus 로고
    • Translocation of protein kinase C isoforms in rat muscle in response to fasting and refeeding
    • Palmer R.M., Nieto R.M., Lobley G.E., Silva P.D., Thom A., and Thompson M.G. Translocation of protein kinase C isoforms in rat muscle in response to fasting and refeeding. Br. J. Nutr. 81 (1999) 153-157
    • (1999) Br. J. Nutr. , vol.81 , pp. 153-157
    • Palmer, R.M.1    Nieto, R.M.2    Lobley, G.E.3    Silva, P.D.4    Thom, A.5    Thompson, M.G.6
  • 22
    • 3042736838 scopus 로고    scopus 로고
    • Selective inhibition of protein kinase Cβ2 prevents acute effects of high glucose on vascular cell adhesion molecule-1 expression in human endothelial cells
    • Kouroedov A., Eto M., Joch H., Volpe M., Lüscher T.F., and Cosentino F. Selective inhibition of protein kinase Cβ2 prevents acute effects of high glucose on vascular cell adhesion molecule-1 expression in human endothelial cells. Circulation 110 (2004) 91-96
    • (2004) Circulation , vol.110 , pp. 91-96
    • Kouroedov, A.1    Eto, M.2    Joch, H.3    Volpe, M.4    Lüscher, T.F.5    Cosentino, F.6
  • 23
    • 0032933179 scopus 로고    scopus 로고
    • Effect of serum starvation on expression and phosphorylation of PKC-α and p53 in V79 cells: implications for cell death
    • Hasan N.M., Adams G.E., and Joiner M.C. Effect of serum starvation on expression and phosphorylation of PKC-α and p53 in V79 cells: implications for cell death. Int. J. Cancer 80 (1999) 400-405
    • (1999) Int. J. Cancer , vol.80 , pp. 400-405
    • Hasan, N.M.1    Adams, G.E.2    Joiner, M.C.3
  • 26
    • 33646384146 scopus 로고    scopus 로고
    • Selective role of PKCβ enzymatic function in regulating cell survival mediated by B cell antigen receptor cross-linking
    • Venkataraman C., Chen X.C., Na S., Lee L., Neote K., and Tan S.-L. Selective role of PKCβ enzymatic function in regulating cell survival mediated by B cell antigen receptor cross-linking. Immunol. Lett. 105 (2006) 83-89
    • (2006) Immunol. Lett. , vol.105 , pp. 83-89
    • Venkataraman, C.1    Chen, X.C.2    Na, S.3    Lee, L.4    Neote, K.5    Tan, S.-L.6
  • 27
    • 12144273607 scopus 로고    scopus 로고
    • PKC-δ-dependent activation of oxidative stress in adipocytes of obese and insulin-resistant mice: role for NADPH oxidase
    • Talior I., Tennenbaum T., Kuroki T., and Eldar-Finkelman H. PKC-δ-dependent activation of oxidative stress in adipocytes of obese and insulin-resistant mice: role for NADPH oxidase. Am. J. Physiol. 288 (2005) E405-E411
    • (2005) Am. J. Physiol. , vol.288
    • Talior, I.1    Tennenbaum, T.2    Kuroki, T.3    Eldar-Finkelman, H.4
  • 28
    • 0034306450 scopus 로고    scopus 로고
    • Specificity and mechanism of action of some commonly used protein kinase inhibitors
    • Davies S.P., Reddy H., Caivano M., and Cohen P. Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochem. J. 351 (2000) 95-105
    • (2000) Biochem. J. , vol.351 , pp. 95-105
    • Davies, S.P.1    Reddy, H.2    Caivano, M.3    Cohen, P.4
  • 29
    • 4644285230 scopus 로고    scopus 로고
    • Role of specific protein kinase C isoforms in modulation of β1- and β2-adrenergic receptors
    • Guimond J., Mamarbachi A.M., Allen B.G., Rindt H., and Hébert T.E. Role of specific protein kinase C isoforms in modulation of β1- and β2-adrenergic receptors. Cell. Signal. 17 (2005) 49-58
    • (2005) Cell. Signal. , vol.17 , pp. 49-58
    • Guimond, J.1    Mamarbachi, A.M.2    Allen, B.G.3    Rindt, H.4    Hébert, T.E.5
  • 30
    • 0028050218 scopus 로고
    • Modulation of adenylylcyclase by protein kinase C in human neurotumor SK-N-MC cells: evidence that the α isozyme mediates both potentiation and desensitization
    • Zhou X.-M., Curran P., Baumgold J., and Fishman P.H. Modulation of adenylylcyclase by protein kinase C in human neurotumor SK-N-MC cells: evidence that the α isozyme mediates both potentiation and desensitization. J. Neurochem. 63 (1994) 1361-1370
    • (1994) J. Neurochem. , vol.63 , pp. 1361-1370
    • Zhou, X.-M.1    Curran, P.2    Baumgold, J.3    Fishman, P.H.4
  • 31
    • 1442265683 scopus 로고    scopus 로고
    • Protein kinase C regulates functional coupling of β1-adrenergic receptors to Gi/o-mediated responses in cardiac myocytes
    • Belevych A.E., Juranek I., and Harvey R.D. Protein kinase C regulates functional coupling of β1-adrenergic receptors to Gi/o-mediated responses in cardiac myocytes. FASEB J. 18 (2004) 367-369
    • (2004) FASEB J. , vol.18 , pp. 367-369
    • Belevych, A.E.1    Juranek, I.2    Harvey, R.D.3
  • 32
    • 0034253195 scopus 로고    scopus 로고
    • β-Adrenergic mechanisms in cardiac diseases. A perspective
    • Chakraborti S., Chakraborti T., and Shaw G. β-Adrenergic mechanisms in cardiac diseases. A perspective. Cell. Signal. 12 (2000) 499-513
    • (2000) Cell. Signal. , vol.12 , pp. 499-513
    • Chakraborti, S.1    Chakraborti, T.2    Shaw, G.3
  • 33
    • 0036230306 scopus 로고    scopus 로고
    • Inhibition of cAMP accumulation by k-receptor activation in isolated iris-ciliary bodies: role of phosphodiesterase and protein kinase C
    • Dortch-Carnes J., and Potter D.E. Inhibition of cAMP accumulation by k-receptor activation in isolated iris-ciliary bodies: role of phosphodiesterase and protein kinase C. J. Pharmacol. Exp. Ther. 301 (2002) 599-604
    • (2002) J. Pharmacol. Exp. Ther. , vol.301 , pp. 599-604
    • Dortch-Carnes, J.1    Potter, D.E.2
  • 34
    • 0037337159 scopus 로고    scopus 로고
    • Regulation of the ABC kinases by phosphorylation: protein kinase C as a paradigm
    • Newton A.C. Regulation of the ABC kinases by phosphorylation: protein kinase C as a paradigm. Biochem. J. 370 (2003) 361-371
    • (2003) Biochem. J. , vol.370 , pp. 361-371
    • Newton, A.C.1
  • 35
    • 0034810991 scopus 로고    scopus 로고
    • Insulin activates phospholipase C-g1 via a PI-3 kinase dependent mechanism in 3T3-L1 adipocytes
    • Eichhorn J., Kayali A.G., Austin D.A., and Webster N.J.G. Insulin activates phospholipase C-g1 via a PI-3 kinase dependent mechanism in 3T3-L1 adipocytes. Biochem. Biophys. Res. Commun. 282 (2001) 615-620
    • (2001) Biochem. Biophys. Res. Commun. , vol.282 , pp. 615-620
    • Eichhorn, J.1    Kayali, A.G.2    Austin, D.A.3    Webster, N.J.G.4
  • 36
    • 0032883639 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of specific protein kinase C isoenzymes participates in insulin stimulation of glucose transport in primary cultures of rat skeletal muscle
    • Braiman L., Sheffi-Friedman L., Bak A., Tennenbaum T., and Sampson S.R. Tyrosine phosphorylation of specific protein kinase C isoenzymes participates in insulin stimulation of glucose transport in primary cultures of rat skeletal muscle. Diabetes 48 (1999) 1922-1929
    • (1999) Diabetes , vol.48 , pp. 1922-1929
    • Braiman, L.1    Sheffi-Friedman, L.2    Bak, A.3    Tennenbaum, T.4    Sampson, S.R.5
  • 37
    • 0028279297 scopus 로고
    • Transcriptional modulation by n-butyric acid of β1-, β2-, and β3-adrenergic receptor balance in 3T3-F442A adipocytes
    • Krief S., Fève B., Baude B., Zilberfarb V., Strosberg A.D., Pairault J., and Emorine L.J. Transcriptional modulation by n-butyric acid of β1-, β2-, and β3-adrenergic receptor balance in 3T3-F442A adipocytes. J. Biol. Chem. 269 (1994) 6664-6670
    • (1994) J. Biol. Chem. , vol.269 , pp. 6664-6670
    • Krief, S.1    Fève, B.2    Baude, B.3    Zilberfarb, V.4    Strosberg, A.D.5    Pairault, J.6    Emorine, L.J.7
  • 38
    • 0034880780 scopus 로고    scopus 로고
    • The sympathetic nervous system in white adipose tissue regulation
    • Rayner D.V. The sympathetic nervous system in white adipose tissue regulation. Proc. Nutr. Soc. 60 (2001) 357-364
    • (2001) Proc. Nutr. Soc. , vol.60 , pp. 357-364
    • Rayner, D.V.1
  • 39
    • 0031252806 scopus 로고    scopus 로고
    • Role of β1- and β3-adrenoceptors in the regulation of lipolysis and thermogenesis in rat brown adipocytes
    • Atgié C., D'Allaire F., and Bukowiecki L.J. Role of β1- and β3-adrenoceptors in the regulation of lipolysis and thermogenesis in rat brown adipocytes. Am. J. Physiol. 273 (1997) C1136-C1142
    • (1997) Am. J. Physiol. , vol.273
    • Atgié, C.1    D'Allaire, F.2    Bukowiecki, L.J.3
  • 41
    • 32544443287 scopus 로고    scopus 로고
    • Human skeletal muscle lipolysis is more responsive to epinephrine than to norepinephrine stimulation in vivo
    • Qvisth V., Hagström-Toft E., Enoksson S., Moberg E., Arner P., and Bolinder J. Human skeletal muscle lipolysis is more responsive to epinephrine than to norepinephrine stimulation in vivo. J. Clin. Endocrinol. Metab. 91 (2006) 6286-6296
    • (2006) J. Clin. Endocrinol. Metab. , vol.91 , pp. 6286-6296
    • Qvisth, V.1    Hagström-Toft, E.2    Enoksson, S.3    Moberg, E.4    Arner, P.5    Bolinder, J.6
  • 42
    • 0031016659 scopus 로고    scopus 로고
    • Transgenic mice overexpressing the β1-adrenergic receptor in adipose tissue are resistant to obesity
    • Soloveva V., Graves R.A., Rasenick M.M., Spiegelman B.M., and Ross S.R. Transgenic mice overexpressing the β1-adrenergic receptor in adipose tissue are resistant to obesity. Mol. Endocrinol. 11 (1997) 27-38
    • (1997) Mol. Endocrinol. , vol.11 , pp. 27-38
    • Soloveva, V.1    Graves, R.A.2    Rasenick, M.M.3    Spiegelman, B.M.4    Ross, S.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.