메뉴 건너뛰기




Volumn 53, Issue 5, 2004, Pages 1261-1270

Role of Caveolin-1 in the Modulation of Lipolysis and Lipid Droplet Formation

Author keywords

[No Author keywords available]

Indexed keywords

BETA 3 ADRENERGIC RECEPTOR STIMULATING AGENT; CAVEOLIN 1; CELL PROTEIN; CYCLIC AMP DEPENDENT PROTEIN KINASE; FAT DROPLET; PERILIPIN; UNCLASSIFIED DRUG;

EID: 2342510295     PISSN: 00121797     EISSN: None     Source Type: Journal    
DOI: 10.2337/diabetes.53.5.1261     Document Type: Article
Times cited : (270)

References (50)
  • 1
    • 0033543699 scopus 로고    scopus 로고
    • Regulation of cAMP-mediated signal transduction via interaction of caveolins with the catalytic subunit of protein kinase A
    • Razani B, Rubin CS, Lisanti MP: Regulation of cAMP-mediated signal transduction via interaction of caveolins with the catalytic subunit of protein kinase A. J Biol Chem 274:26353-26360, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 26353-26360
    • Razani, B.1    Rubin, C.S.2    Lisanti, M.P.3
  • 2
    • 0033306884 scopus 로고    scopus 로고
    • Caveolin-1 interacts with the insulin receptor and can differentially modulate insulin signaling in transfected Cos-7 cells and rat adipose cells
    • Nystrom FH, Chen H, Cong LN, Li Y, Quon MJ: Caveolin-1 interacts with the insulin receptor and can differentially modulate insulin signaling in transfected Cos-7 cells and rat adipose cells. Mol Endocrinol 13:2013-2024, 1999
    • (1999) Mol Endocrinol , vol.13 , pp. 2013-2024
    • Nystrom, F.H.1    Chen, H.2    Cong, L.N.3    Li, Y.4    Quon, M.J.5
  • 3
    • 0035809931 scopus 로고    scopus 로고
    • Caveolin-2 is targeted to lipid droplets, a new "membrane domain" in the cell
    • Fujimoto T, Kogo H, Ishiguro K, Tauchi K, Nomura R: Caveolin-2 is targeted to lipid droplets, a new "membrane domain" in the cell. J Cell Biol 152:1079-1085, 2001
    • (2001) J Cell Biol , vol.152 , pp. 1079-1085
    • Fujimoto, T.1    Kogo, H.2    Ishiguro, K.3    Tauchi, K.4    Nomura, R.5
  • 4
    • 0035809923 scopus 로고    scopus 로고
    • Accumulation of caveolin in the endoplasmic reticulum redirects the protein to lipid storage droplets
    • Ostermeyer AG, Paci JM, Zeng Y, Lublin DM, Munro S, Brown DA: Accumulation of caveolin in the endoplasmic reticulum redirects the protein to lipid storage droplets. J Cell Biol 152:1071-1078, 2001
    • (2001) J Cell Biol , vol.152 , pp. 1071-1078
    • Ostermeyer, A.G.1    Paci, J.M.2    Zeng, Y.3    Lublin, D.M.4    Munro, S.5    Brown, D.A.6
  • 5
    • 0035809933 scopus 로고    scopus 로고
    • A caveolin dominant negative mutant associates with lipid bodies and induces intracellular cholesterol imbalance
    • Pol A, Luetterforst R, Lindsay M, Heino S, Ikonen E, Parton RG: A caveolin dominant negative mutant associates with lipid bodies and induces intracellular cholesterol imbalance. J Cell Biol 152:1057-1070, 2001
    • (2001) J Cell Biol , vol.152 , pp. 1057-1070
    • Pol, A.1    Luetterforst, R.2    Lindsay, M.3    Heino, S.4    Ikonen, E.5    Parton, R.G.6
  • 6
    • 0035923507 scopus 로고    scopus 로고
    • The many dimensions of cAMP signaling
    • Schwartz JH: The many dimensions of cAMP signaling. Proc Natl Acad Sci USA 98:13482-13484, 2001
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 13482-13484
    • Schwartz, J.H.1
  • 7
    • 0036345413 scopus 로고    scopus 로고
    • Regulation of lipolysis: Natriuretic peptides and the development of cachexia
    • Kalra P, Tigas S: Regulation of lipolysis: natriuretic peptides and the development of cachexia. Int J Cardiol 85:125-132, 2002
    • (2002) Int J Cardiol , vol.85 , pp. 125-132
    • Kalra, P.1    Tigas, S.2
  • 10
    • 2642614548 scopus 로고    scopus 로고
    • Identification of novel phosphorylation sites in hormone-sensitive lipase that are phosphorylated in response to isoproterenol and govern activation properties in vitro
    • Anthonsen MW, Ronnstrand L, Wernstedt C, Degerman E, Holm C: Identification of novel phosphorylation sites in hormone-sensitive lipase that are phosphorylated in response to isoproterenol and govern activation properties in vitro. J Biol Chem 273:215-221, 1998
    • (1998) J Biol Chem , vol.273 , pp. 215-221
    • Anthonsen, M.W.1    Ronnstrand, L.2    Wernstedt, C.3    Degerman, E.4    Holm, C.5
  • 12
    • 0033165872 scopus 로고    scopus 로고
    • Lipotransin: A novel docking protein for hormone-sensitive lipase
    • Syu LJ, Saltiel AR: Lipotransin: a novel docking protein for hormone-sensitive lipase. Mol Cell 4:109-115, 1999
    • (1999) Mol Cell , vol.4 , pp. 109-115
    • Syu, L.J.1    Saltiel, A.R.2
  • 13
    • 0026783771 scopus 로고
    • Mechanism of hormone-stimulated lipolysis in adipocytes: Translocation of hormone-sensitive lipase to the lipid storage droplet
    • Egan JJ, Greenberg AS, Chang MK, Wek SA, Moos MC Jr, Londos C: Mechanism of hormone-stimulated lipolysis in adipocytes: translocation of hormone-sensitive lipase to the lipid storage droplet. Proc Natl Acad Sci USA 89:8537-8541, 1992
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 8537-8541
    • Egan, J.J.1    Greenberg, A.S.2    Chang, M.K.3    Wek, S.A.4    Moos Jr., M.C.5    Londos, C.6
  • 14
    • 0033961989 scopus 로고    scopus 로고
    • The lipolytic stimulation of 3T3-L1 adipocytes promotes the translocation of hormone-sensitive lipase to the surfaces of lipid storage droplets
    • Brasaemle DL, Levin DM, Adler-Wailes DC, Londos C: The lipolytic stimulation of 3T3-L1 adipocytes promotes the translocation of hormone-sensitive lipase to the surfaces of lipid storage droplets. Biochim Biophys Acta 1483:251-262, 2000
    • (2000) Biochim Biophys Acta , vol.1483 , pp. 251-262
    • Brasaemle, D.L.1    Levin, D.M.2    Adler-Wailes, D.C.3    Londos, C.4
  • 15
    • 0034681341 scopus 로고    scopus 로고
    • Translocation of hormone-sensitive lipase and perilipin upon lipolytic stimulation of rat adipocytes
    • Clifford GM, Londos C, Kraemer FB, Vernon RG, Yeaman SJ: Translocation of hormone-sensitive lipase and perilipin upon lipolytic stimulation of rat adipocytes. J Biol Chem 275:5011-5015, 2000
    • (2000) J Biol Chem , vol.275 , pp. 5011-5015
    • Clifford, G.M.1    Londos, C.2    Kraemer, F.B.3    Vernon, R.G.4    Yeaman, S.J.5
  • 16
    • 0242290249 scopus 로고    scopus 로고
    • Mutational analysis of the hormone-sensitive lipase translocation reaction in adipocytes
    • Su CL, Sztalryd C, Contreras JA, Holm C, Kimmel AR, Londos C: Mutational analysis of the hormone-sensitive lipase translocation reaction in adipocytes. J Biol Chem 278:43615-43619, 2003
    • (2003) J Biol Chem , vol.278 , pp. 43615-43619
    • Su, C.L.1    Sztalryd, C.2    Contreras, J.A.3    Holm, C.4    Kimmel, A.R.5    Londos, C.6
  • 17
    • 0037477829 scopus 로고    scopus 로고
    • Perilipin A is essential for the translocation of hormone-sensitive lipase during lipolytic activation
    • Sztalryd C, Xu G, Dorward H, Tansey JT, Contreras JA, Kimmel AR, Londos C: Perilipin A is essential for the translocation of hormone-sensitive lipase during lipolytic activation. J Cell Biol 161:1093-1103, 2003
    • (2003) J Cell Biol , vol.161 , pp. 1093-1103
    • Sztalryd, C.1    Xu, G.2    Dorward, H.3    Tansey, J.T.4    Contreras, J.A.5    Kimmel, A.R.6    Londos, C.7
  • 18
    • 0024516569 scopus 로고
    • Phosphorylation of bovine hormone-sensitive lipase by the AMP-activated protein kinase: A possible antilipolytic mechanism
    • Garton AJ, Campbell DG, Carling D, Hardie DG, Colbran RJ, Yeaman SJ: Phosphorylation of bovine hormone-sensitive lipase by the AMP-activated protein kinase: a possible antilipolytic mechanism. Eur J Biochem 179: 249-254, 1989
    • (1989) Eur J Biochem , vol.179 , pp. 249-254
    • Garton, A.J.1    Campbell, D.G.2    Carling, D.3    Hardie, D.G.4    Colbran, R.J.5    Yeaman, S.J.6
  • 19
    • 0034623950 scopus 로고    scopus 로고
    • Perilipin A increases triacylglycerol storage by decreasing the rate of triacylglycerol hydrolysis
    • Brasaemle DL, Rubin B, Harten IA, Gruia-Gray J, Kimmel AR, Londos C: Perilipin A increases triacylglycerol storage by decreasing the rate of triacylglycerol hydrolysis. J Biol Chem 275:38486-38493, 2000
    • (2000) J Biol Chem , vol.275 , pp. 38486-38493
    • Brasaemle, D.L.1    Rubin, B.2    Harten, I.A.3    Gruia-Gray, J.4    Kimmel, A.R.5    Londos, C.6
  • 20
    • 0030697399 scopus 로고    scopus 로고
    • Translocation of perilipin and hormone-sensitive lipase in response to lipolytic hormones
    • Clifford GM, McCormick DK, Vernon RG, Yeaman SJ: Translocation of perilipin and hormone-sensitive lipase in response to lipolytic hormones (Abstract). Biochem Soc Trans 25:S672, 1997
    • (1997) Biochem Soc Trans , vol.25
    • Clifford, G.M.1    McCormick, D.K.2    Vernon, R.G.3    Yeaman, S.J.4
  • 22
    • 0347065339 scopus 로고    scopus 로고
    • Lipase-selective functional domains of perilipin A differentially regulate constitutive and protein kinase A-stimulated lipolysis
    • Zhang HH, Souza SC, Muliro KV, Kraemer FB, Obin MS, Greenberg AS:. Lipase-selective functional domains of perilipin A differentially regulate constitutive and protein kinase A-stimulated lipolysis. J Biol Chem, 2003
    • (2003) J Biol Chem
    • Zhang, H.H.1    Souza, S.C.2    Muliro, K.V.3    Kraemer, F.B.4    Obin, M.S.5    Greenberg, A.S.6
  • 25
    • 0028998905 scopus 로고
    • Perilipins are associated with cholesteryl ester droplets in steroidogenic adrenal cortical and Leydig cells
    • Servetnick DA, Brasaemle DL, Gruia-Gray J, Kimmel AR, Wolff J, Londos C: Perilipins are associated with cholesteryl ester droplets in steroidogenic adrenal cortical and Leydig cells. J Biol Chem 270:16970-16973, 1995
    • (1995) J Biol Chem , vol.270 , pp. 16970-16973
    • Servetnick, D.A.1    Brasaemle, D.L.2    Gruia-Gray, J.3    Kimmel, A.R.4    Wolff, J.5    Londos, C.6
  • 29
    • 26744463978 scopus 로고    scopus 로고
    • Adipose tissue protocols
    • Ailhaud G, Ed. Totowa, NJ, Humana Press
    • Carpéné C: Adipose tissue protocols. In Methods in Molecular Biology. Ailhaud G, Ed. Totowa, NJ, Humana Press, 2001, p. 129-140
    • (2001) Methods in Molecular Biology , pp. 129-140
    • Carpéné, C.1
  • 31
    • 0035477058 scopus 로고    scopus 로고
    • Ligand-independent activation of oestrogen receptor alpha by caveolin-1
    • Schlegel A, Wang C, Pestell RG, Lisanti MP: Ligand-independent activation of oestrogen receptor alpha by caveolin-1. Biochem J 359:203-210, 2001
    • (2001) Biochem J , vol.359 , pp. 203-210
    • Schlegel, A.1    Wang, C.2    Pestell, R.G.3    Lisanti, M.P.4
  • 33
    • 0032852479 scopus 로고    scopus 로고
    • CREB: A stimulus-induced transcription factor activated by a diverse array of extracellular signals
    • Shaywitz AJ, Greenberg ME: CREB: a stimulus-induced transcription factor activated by a diverse array of extracellular signals. Annu Rev Biochem 68:821-861, 1999
    • (1999) Annu Rev Biochem , vol.68 , pp. 821-861
    • Shaywitz, A.J.1    Greenberg, M.E.2
  • 34
    • 0025772167 scopus 로고
    • Perilipin, a major hormonally regulated adipocyte-specific phosphoprotein associated with the periphery of lipid storage droplets
    • Greenberg AS, Egan JJ, Wek SA, Garty NB, Blanchette-Mackie EJ, Londos C: Perilipin, a major hormonally regulated adipocyte-specific phosphoprotein associated with the periphery of lipid storage droplets. J Biol Chem 266:11341-11346, 1991
    • (1991) J Biol Chem , vol.266 , pp. 11341-11346
    • Greenberg, A.S.1    Egan, J.J.2    Wek, S.A.3    Garty, N.B.4    Blanchette-Mackie, E.J.5    Londos, C.6
  • 35
    • 0035810964 scopus 로고    scopus 로고
    • Lipid droplets: Proteins floating on a pool of fat
    • Brown DA: Lipid droplets: proteins floating on a pool of fat. Curr Biol 11:R446-449, 2001
    • (2001) Curr Biol , vol.11
    • Brown, D.A.1
  • 37
    • 0037113954 scopus 로고    scopus 로고
    • The surface of lipid droplets is a phospholipid monolayer with a unique fatty acid composition
    • Tauchi-Sato K, Ozeki S, Houjou T, Taguchi R, Fujimoto T: The surface of lipid droplets is a phospholipid monolayer with a unique fatty acid composition. J Biol Chem 277:44507-44512, 2002
    • (2002) J Biol Chem , vol.277 , pp. 44507-44512
    • Tauchi-Sato, K.1    Ozeki, S.2    Houjou, T.3    Taguchi, R.4    Fujimoto, T.5
  • 39
    • 0037200026 scopus 로고    scopus 로고
    • Functional conservation for lipid storage droplet association among Perilipin, ADRP, and TIP47 (PAT)-related proteins in mammals, Drosophila, and Dictyostelium
    • Miura S, Gan JW, Brzostowski J, Parisi MJ, Schultz CJ, Londos C, Oliver B, Kimmel AR: Functional conservation for lipid storage droplet association among Perilipin, ADRP, and TIP47 (PAT)-related proteins in mammals, Drosophila, and Dictyostelium. J Biol Chem 277:32253-32257, 2002
    • (2002) J Biol Chem , vol.277 , pp. 32253-32257
    • Miura, S.1    Gan, J.W.2    Brzostowski, J.3    Parisi, M.J.4    Schultz, C.J.5    Londos, C.6    Oliver, B.7    Kimmel, A.R.8
  • 41
    • 0030724392 scopus 로고    scopus 로고
    • Adipose differentiation-related protein is an ubiquitously expressed lipid storage droplet-associated protein
    • Brasaemle DL, Barber T, Wolins NE, Serrero G, Blanchette-Mackie FJ, Londos C: Adipose differentiation-related protein is an ubiquitously expressed lipid storage droplet-associated protein. J Lipid Res 38:2249-2263, 1997
    • (1997) J Lipid Res , vol.38 , pp. 2249-2263
    • Brasaemle, D.L.1    Barber, T.2    Wolins, N.E.3    Serrero, G.4    Blanchette-Mackie, F.J.5    Londos, C.6
  • 43
    • 0141814912 scopus 로고    scopus 로고
    • Localization of mammalian NAD(P)H steroid dehydrogenase-like protein on lipid droplets
    • Ohashi M, Mizushima N, Kabeya Y, Yoshimori T: Localization of mammalian NAD(P)H steroid dehydrogenase-like protein on lipid droplets. J Biol Chem 278:30319-36829, 2003
    • (2003) J Biol Chem , vol.278 , pp. 30319-36829
    • Ohashi, M.1    Mizushima, N.2    Kabeya, Y.3    Yoshimori, T.4
  • 44
    • 0023649685 scopus 로고
    • Rearrangement of the vimentin cytoskeleton during adipose conversion: Formation of an intermediate filament cage around lipid globules
    • Franke WW, Hergt M, Grund C: Rearrangement of the vimentin cytoskeleton during adipose conversion: formation of an intermediate filament cage around lipid globules. Cell 49:131-141, 1987
    • (1987) Cell , vol.49 , pp. 131-141
    • Franke, W.W.1    Hergt, M.2    Grund, C.3
  • 45
    • 0027145164 scopus 로고
    • Isolation of cDNAs for perilipins A and B: Sequence and expression of lipid droplet-associated proteins of adipocytes
    • Greenberg AS, Egan JJ, Wek SA, Moos MC Jr, Londos C, Kimmel AR: Isolation of cDNAs for perilipins A and B: sequence and expression of lipid droplet-associated proteins of adipocytes. Proc Natl Acad Sci USA 90:12035-12039, 1993
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 12035-12039
    • Greenberg, A.S.1    Egan, J.J.2    Wek, S.A.3    Moos Jr., M.C.4    Londos, C.5    Kimmel, A.R.6
  • 46
    • 0035192750 scopus 로고    scopus 로고
    • Post-translational control of endothelial nitric oxide synthase: Why isn't calcium/calmodulin enough?
    • Fulton D, Gratton JP, Sessa WC: Post-translational control of endothelial nitric oxide synthase: why isn't calcium/calmodulin enough? J Pharmacol Exp Ther 299:818-824, 2001
    • (2001) J Pharmacol Exp Ther , vol.299 , pp. 818-824
    • Fulton, D.1    Gratton, J.P.2    Sessa, W.C.3
  • 47
    • 0039397709 scopus 로고    scopus 로고
    • Dissecting the interaction between nitric oxide synthase (NOS) and caveolin: Functional significance of the NOS caveolin binding domain in vivo
    • Garcia-Cardena G, Martasek P, Masters BS, Skidd PM, Couet J, Li S, Lisanti MP, Sessa WC: Dissecting the interaction between nitric oxide synthase (NOS) and caveolin: functional significance of the NOS caveolin binding domain in vivo. J Biol Chem 272:25437-25440, 1997
    • (1997) J Biol Chem , vol.272 , pp. 25437-25440
    • Garcia-Cardena, G.1    Martasek, P.2    Masters, B.S.3    Skidd, P.M.4    Couet, J.5    Li, S.6    Lisanti, M.P.7    Sessa, W.C.8
  • 48
    • 0038269336 scopus 로고    scopus 로고
    • The caveolar nitric oxide synthase/arginine regeneration system for NO production in endothelial cells
    • Solomonson LP, Flam BR, Pendleton LC, Goodwin BL, Eichler DC: The caveolar nitric oxide synthase/arginine regeneration system for NO production in endothelial cells. J Exp Biol 206:2083-2087, 2003
    • (2003) J Exp Biol , vol.206 , pp. 2083-2087
    • Solomonson, L.P.1    Flam, B.R.2    Pendleton, L.C.3    Goodwin, B.L.4    Eichler, D.C.5
  • 49
    • 0036199988 scopus 로고    scopus 로고
    • Regulation of endothelial nitric oxide synthase: Location, location, location
    • Shaul PW: Regulation of endothelial nitric oxide synthase: location, location, location. Annu Rev Physiol 64:749-774, 2002
    • (2002) Annu Rev Physiol , vol.64 , pp. 749-774
    • Shaul, P.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.