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Volumn 36, Issue 8, 2004, Pages 584-595

The Caveolin genes: From cell biology to medicine

Author keywords

Atherosclerosis; Cancer; Cardiomyopathy; Genetic disease; Mouse animal models; Muscular dystrophy; Vascular disease

Indexed keywords

CAVEOLIN 1; CAVEOLIN 2; CAVEOLIN 3; CHOLESTEROL; ENDOTHELIAL NITRIC OXIDE SYNTHASE; MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN P44; PROTEIN TYROSINE KINASE; STRUCTURAL PROTEIN;

EID: 11144226727     PISSN: 07853890     EISSN: None     Source Type: Journal    
DOI: 10.1080/07853890410018899     Document Type: Short Survey
Times cited : (333)

References (111)
  • 1
    • 0000855817 scopus 로고
    • Fine Structure of Blood Capillaries
    • Palade GE. Fine Structure of Blood Capillaries. J Appl Physiol 1953;24:1424-36.
    • (1953) J Appl Physiol , vol.24 , pp. 1424-1436
    • Palade, G.E.1
  • 2
    • 0026454933 scopus 로고
    • Sequence and expression of caveolin, a protein component of caveolae plasma membrane domains phosphorylated on tyrosine in Rous sarcoma virus-transformed fibroblasts
    • Glenney JR, Jr, Soppet D. Sequence and expression of caveolin, a protein component of caveolae plasma membrane domains phosphorylated on tyrosine in Rous sarcoma virus-transformed fibroblasts. Proc Natl Acad Sci USA 1992; 89: 10517-21.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10517-10521
    • Glenney Jr., J.R.1    Soppet, D.2
  • 3
    • 0026640940 scopus 로고
    • VIP 21, A 21-kD membrane protein is an integral component of trans-Golgi-network-derived transport vesicles
    • Kurzchalia T, Dupree P, Parton RG, Kellner R, Virta H, Lehnert M, et al. VIP 21, A 21-kD membrane protein is an integral component of trans-Golgi-network-derived transport vesicles. J Cell Biol 1992;118:1003-14.
    • (1992) J Cell Biol , vol.118 , pp. 1003-1014
    • Kurzchalia, T.1    Dupree, P.2    Parton, R.G.3    Kellner, R.4    Virta, H.5    Lehnert, M.6
  • 4
  • 5
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • Brown DA, London E. Functions of lipid rafts in biological membranes. Annu Rev Cell Dev Biol 1998;14:111-36.
    • (1998) Annu Rev Cell Dev Biol , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 6
    • 0035943423 scopus 로고    scopus 로고
    • Emerging themes in lipid rafts and caveolae
    • Galbiati F, Razani B, Lisanti MP. Emerging themes in lipid rafts and caveolae. Cell 2001;106:403-11.
    • (2001) Cell , vol.106 , pp. 403-411
    • Galbiati, F.1    Razani, B.2    Lisanti, M.P.3
  • 7
    • 0027275642 scopus 로고
    • Signal transducing molecules and GPI-linked proteins form a caveolin- rich insoluble complex in MDCK cells
    • Sargiacomo M, Sudol M, Tang Z-L, Lisanti MP. Signal transducing molecules and GPI-linked proteins form a caveolin- rich insoluble complex in MDCK cells. J Cell Biol 1993;122:789-807.
    • (1993) J Cell Biol , vol.122 , pp. 789-807
    • Sargiacomo, M.1    Sudol, M.2    Tang, Z.-L.3    Lisanti, M.P.4
  • 8
    • 0028319060 scopus 로고
    • Characterization of caveolin-rich membrane domains isolated from an endothelial-rich source: Implications for human disease
    • Lisanti MP, Scherer PE, Vidugiriene J, Tang Z-L, Hermanoski-Vosatka A, Tu Y-H, et al. Characterization of caveolin-rich membrane domains isolated from an endothelial-rich source: Implications for human disease. J Cell Biol 1994;126:111-26.
    • (1994) J Cell Biol , vol.126 , pp. 111-126
    • Lisanti, M.P.1    Scherer, P.E.2    Vidugiriene, J.3    Tang, Z.-L.4    Hermanoski-Vosatka, A.5    Tu, Y.-H.6
  • 9
  • 10
    • 0028997529 scopus 로고
    • Caveolae purification and GPI-linked protein sorting in polarized epithelia
    • Lisanti MP, Tang Z-T, Scherer P, Sargiacomo M. Caveolae purification and GPI-linked protein sorting in polarized epithelia. Meth Enzymol 1995;250:655-68.
    • (1995) Meth Enzymol , vol.250 , pp. 655-668
    • Lisanti, M.P.1    Tang, Z.-T.2    Scherer, P.3    Sargiacomo, M.4
  • 11
    • 0032619824 scopus 로고    scopus 로고
    • Purification of caveolae-derived membrane microdomains containing lipid-anchored signaling molecules, such as GPI-anchored proteins, H-Ras, Src- family tyrosine kinases, eNOS, and G-protein alpha-, beta-, and gamma- subunits
    • Lisanti MP, Sargiacomo M, Scherer PE. Purification of caveolae-derived membrane microdomains containing lipid-anchored signaling molecules, such as GPI-anchored proteins, H-Ras, Src- family tyrosine kinases, eNOS, and G-protein alpha-, beta-, and gamma- subunits. Methods Mol Biol 1999;116:51-60.
    • (1999) Methods Mol Biol , vol.116 , pp. 51-60
    • Lisanti, M.P.1    Sargiacomo, M.2    Scherer, P.E.3
  • 13
    • 0035851197 scopus 로고    scopus 로고
    • Caveolin-1 null mice are viable but show evidence of hyperproliferative and vascular abnormalities
    • Razani B, Engelman JA, Wang XB, Schubert W, Zhang XL, Marks CB, et al. Caveolin-1 null mice are viable but show evidence of hyperproliferative and vascular abnormalities. J Biol Chem 2001;276:38121-38.
    • (2001) J Biol Chem , vol.276 , pp. 38121-38138
    • Razani, B.1    Engelman, J.A.2    Wang, X.B.3    Schubert, W.4    Zhang, X.L.5    Marks, C.B.6
  • 14
    • 0037040994 scopus 로고    scopus 로고
    • Caveolin-1-deficient mice are lean, resistant to diet-induced obesity, and show hypertriglyceridemia with adipocyte abnormalities
    • Razani B, Combs TP, Wang XB, Frank PG, Park DS, Russell RG, et al. Caveolin-1-deficient mice are lean, resistant to diet-induced obesity, and show hypertriglyceridemia with adipocyte abnormalities. J Biol Chem 2002;277:8635-47.
    • (2002) J Biol Chem , vol.277 , pp. 8635-8647
    • Razani, B.1    Combs, T.P.2    Wang, X.B.3    Frank, P.G.4    Park, D.S.5    Russell, R.G.6
  • 15
    • 0036123019 scopus 로고    scopus 로고
    • Caveolin-2-deficient mice show evidence of severe pulmonary dysfunction without disruption of caveolae
    • Razani B, Wang XB, Engelman JA, Battista M, Lagaud G, Zhang XL, et al. Caveolin-2-deficient mice show evidence of severe pulmonary dysfunction without disruption of caveolae. Mol Cell Biol 2002;22:2329-44.
    • (2002) Mol Cell Biol , vol.22 , pp. 2329-2344
    • Razani, B.1    Wang, X.B.2    Engelman, J.A.3    Battista, M.4    Lagaud, G.5    Zhang, X.L.6
  • 16
    • 0035964954 scopus 로고    scopus 로고
    • Loss of Caveolae, Vascular Dysfunction, and Pulmonary Defects in Caveolin-1 Gene-Disrupted Mice
    • Drab M, Verkade P, Elger M, Kasper M, Lohn M, Lauterbach B, et al. Loss of Caveolae, Vascular Dysfunction, and Pulmonary Defects in Caveolin-1 Gene-Disrupted Mice. Science 2001;293:2449-52.
    • (2001) Science , vol.293 , pp. 2449-2452
    • Drab, M.1    Verkade, P.2    Elger, M.3    Kasper, M.4    Lohn, M.5    Lauterbach, B.6
  • 17
  • 18
    • 2142677810 scopus 로고    scopus 로고
    • Caveolin-3 null mice show a loss of caveolae, changes in the microdomain distribution of the dystrophin-glycoprotein complex, and T- tubule abnormalities
    • Galbiati F, Engelman JA, Volonte D, Zhang XL, Minetti C, Li M, et al. Caveolin-3 null mice show a loss of caveolae, changes in the microdomain distribution of the dystrophin-glycoprotein complex, and T- tubule abnormalities. J Biol Chem 2001;19:19.
    • (2001) J Biol Chem , vol.19 , pp. 19
    • Galbiati, F.1    Engelman, J.A.2    Volonte, D.3    Zhang, X.L.4    Minetti, C.5    Li, M.6
  • 19
    • 0037064033 scopus 로고    scopus 로고
    • Caveolin-3 knock-out mice develop a progressive cardiomyopathy and show hyperactivation of the p42/44 MAPK cascade
    • Woodman SE, Park DS, Cohen AW, Cheung MW, Chandra M, Shirani J, et al. Caveolin-3 knock-out mice develop a progressive cardiomyopathy and show hyperactivation of the p42/44 MAPK cascade. J Biol Chem 2002;277:38988-97.
    • (2002) J Biol Chem , vol.277 , pp. 38988-38997
    • Woodman, S.E.1    Park, D.S.2    Cohen, A.W.3    Cheung, M.W.4    Chandra, M.5    Shirani, J.6
  • 21
    • 14444285478 scopus 로고    scopus 로고
    • Cell-type and tissue-specific expression of caveolin-2. Caveolins 1 and 2 co-localize and form a stable hetero-oligomeric complex in vivo
    • Scherer PE, Lewis RY, Volonte D, Engelman JA, Galbiati F, Couet J, et al. Cell-type and tissue-specific expression of caveolin-2. Caveolins 1 and 2 co-localize and form a stable hetero-oligomeric complex in vivo. J Biol Chem 1997;272: 29337-46.
    • (1997) J Biol Chem , vol.272 , pp. 29337-29346
    • Scherer, P.E.1    Lewis, R.Y.2    Volonte, D.3    Engelman, J.A.4    Galbiati, F.5    Couet, J.6
  • 22
    • 0033520374 scopus 로고    scopus 로고
    • Expression of caveolin-1 is required for the transport of caveolin-2 to the plasma membrane. Retention of caveolin-2 at the level of the Golgi complex
    • Parolini I, Sargiacomo M, Galbiati F, Rizzo G, Grignani F, Engelman JA, et al. Expression of caveolin-1 is required for the transport of caveolin-2 to the plasma membrane. Retention of caveolin-2 at the level of the Golgi complex. J Biol Chem 1999;274:25718-25.
    • (1999) J Biol Chem , vol.274 , pp. 25718-25725
    • Parolini, I.1    Sargiacomo, M.2    Galbiati, F.3    Rizzo, G.4    Grignani, F.5    Engelman, J.A.6
  • 23
    • 0030060941 scopus 로고    scopus 로고
    • Molecular cloning of caveolin-3, a novel member of the caveolin gene family expressed predominantly in muscle
    • Tang Z-L, Scherer PE, Okamoto T, Song K, Chu C, Kohtz DS, et al. Molecular cloning of caveolin-3, a novel member of the caveolin gene family expressed predominantly in muscle. J Biol Chem 1996;271:2255-61.
    • (1996) J Biol Chem , vol.271 , pp. 2255-2261
    • Tang, Z.-L.1    Scherer, P.E.2    Okamoto, T.3    Song, K.4    Chu, C.5    Kohtz, D.S.6
  • 24
    • 0030561979 scopus 로고
    • M-caveolin, a muscle-specific caveolin-related protein
    • Way M, Parton R. M-caveolin, a muscle-specific caveolin-related protein. FEBS Lett 1995;376:108-12.
    • (1995) FEBS Lett , vol.376 , pp. 108-112
    • Way, M.1    Parton, R.2
  • 25
    • 15844401780 scopus 로고    scopus 로고
    • Expression of caveolin-3 in skeletal, cardiac, and smooth muscle cells. Caveolin-3 is a component of the sarcolemma and co-fractionates with dystrophin and dystrophin-associated glycoproteins
    • Song KS, Scherer PE, Tang Z-L, Okamoto T, Li S, Chafel M, et al. Expression of caveolin-3 in skeletal, cardiac, and smooth muscle cells. Caveolin-3 is a component of the sarcolemma and co-fractionates with dystrophin and dystrophin-associated glycoproteins. J Biol Chem 1996; 271: 15160-5.
    • (1996) J Biol Chem , vol.271 , pp. 15160-15165
    • Song, K.S.1    Scherer, P.E.2    Tang, Z.-L.3    Okamoto, T.4    Li, S.5    Chafel, M.6
  • 26
    • 0026499749 scopus 로고
    • The sequence of human caveolin reveals identity with VIP 21, a component of transport vesicles
    • Glenney JR. The sequence of human caveolin reveals identity with VIP 21, a component of transport vesicles. FEBS Lett 1992;314:45-8.
    • (1992) FEBS Lett , vol.314 , pp. 45-48
    • Glenney, J.R.1
  • 27
    • 0036830114 scopus 로고    scopus 로고
    • Multiple functions of caveolin-1
    • Liu P, Rudick M, Anderson RG. Multiple functions of caveolin-1. J Biol Chem 2002;277:41295-8.
    • (2002) J Biol Chem , vol.277 , pp. 41295-41298
    • Liu, P.1    Rudick, M.2    Anderson, R.G.3
  • 28
    • 0029003932 scopus 로고
    • Caveolin isoforms differ in their N-terminal protein sequence and subcellular distribution: Identification and epitope mapping of an isoform-specific monoclonal antibody probe
    • Scherer PE, Tang Z-L, Chun MC, Sargiacomo M, Lodish HF, Lisanti MP. Caveolin isoforms differ in their N-terminal protein sequence and subcellular distribution: Identification and epitope mapping of an isoform-specific monoclonal antibody probe. J Biol Chem 1995;270:16395-401.
    • (1995) J Biol Chem , vol.270 , pp. 16395-16401
    • Scherer, P.E.1    Tang, Z.-L.2    Chun, M.C.3    Sargiacomo, M.4    Lodish, H.F.5    Lisanti, M.P.6
  • 30
    • 0029803093 scopus 로고    scopus 로고
    • Src tyrosine kinases, G alpha subunits and H-Ras share a common membrane-anchored scaffolding protein, Caveolin. Caveolin binding negatively regulates the auto-activation of Src tyrosine kinases
    • Li S, Couet J, Lisanti MP. Src tyrosine kinases, G alpha subunits and H-Ras share a common membrane-anchored scaffolding protein, Caveolin. Caveolin binding negatively regulates the auto-activation of Src tyrosine kinases. J Biol Chem 1996;271:29182-90.
    • (1996) J Biol Chem , vol.271 , pp. 29182-29190
    • Li, S.1    Couet, J.2    Lisanti, M.P.3
  • 31
    • 0030941001 scopus 로고    scopus 로고
    • Identification of peptide and protein ligands for the caveolin-scaffolding domain. Implications for the interaction of caveolin with caveolae-associated proteins
    • Couet J, Li S, Okamoto T, Ikezu T, Lisanti MP. Identification of peptide and protein ligands for the caveolin-scaffolding domain. Implications for the interaction of caveolin with caveolae-associated proteins. J Biol Chem 1997;272:6525-33.
    • (1997) J Biol Chem , vol.272 , pp. 6525-6533
    • Couet, J.1    Li, S.2    Okamoto, T.3    Ikezu, T.4    Lisanti, M.P.5
  • 32
    • 0036733284 scopus 로고    scopus 로고
    • Caveolae: From cell biology to animal physiology
    • Razani B, Woodman SE, Lisanti MP. Caveolae: from cell biology to animal physiology. Pharmacol Rev 2002;54:431-67.
    • (2002) Pharmacol Rev , vol.54 , pp. 431-467
    • Razani, B.1    Woodman, S.E.2    Lisanti, M.P.3
  • 33
    • 0029014820 scopus 로고
    • Endothelial caveolae have the molecular transport machinery for vesicle budding, docking, and fusion including VAMP, NSF, SNAP, annexins, and GTPases
    • Schnitzer JE, Liu J, Oh P. Endothelial caveolae have the molecular transport machinery for vesicle budding, docking, and fusion including VAMP, NSF, SNAP, annexins, and GTPases. J Biol Chem 1995;270:14399-404.
    • (1995) J Biol Chem , vol.270 , pp. 14399-14404
    • Schnitzer, J.E.1    Liu, J.2    Oh, P.3
  • 34
    • 0032489880 scopus 로고    scopus 로고
    • Dynamin at the neck of caveolae mediates their budding to form transport vesicles by GTP-driven fission from the plasma membrane of endothelium
    • Oh P, McIntosh DP, Schnitzer JE. Dynamin at the neck of caveolae mediates their budding to form transport vesicles by GTP-driven fission from the plasma membrane of endothelium. J Cell Biol 1998;141:101-14.
    • (1998) J Cell Biol , vol.141 , pp. 101-114
    • Oh, P.1    McIntosh, D.P.2    Schnitzer, J.E.3
  • 37
    • 0030027901 scopus 로고    scopus 로고
    • Expression and characterization of recombinant caveolin: Purification by poly-histidine tagging and cholesterol-dependent incorporation into defined lipid membranes
    • Li S, Song KS, Lisanti MP. Expression and characterization of recombinant caveolin: Purification by poly-histidine tagging and cholesterol-dependent incorporation into defined lipid membranes. J Biol Chem 1996;271:568-73.
    • (1996) J Biol Chem , vol.271 , pp. 568-573
    • Li, S.1    Song, K.S.2    Lisanti, M.P.3
  • 38
    • 0036279556 scopus 로고    scopus 로고
    • Alterations in membrane cholesterol that affect structure and function of caveolae
    • Smart EJ, Anderson RG. Alterations in membrane cholesterol that affect structure and function of caveolae. Methods Enzymol 2002;353:131-9.
    • (2002) Methods Enzymol , vol.353 , pp. 131-139
    • Smart, E.J.1    Anderson, R.G.2
  • 39
    • 0039252798 scopus 로고    scopus 로고
    • p42/44 MAP kinase-dependent and -independent signaling pathways regulate caveolin-1 gene expression. Activation of Ras-MAP kinase and protein kinase A signaling cascades transcriptionally down-regulates caveolin-1 promoter activity
    • Engelman JA, Zhang XL, Razani B, Pestell RG, Lisanti MP. p42/44 MAP kinase-dependent and -independent signaling pathways regulate caveolin-1 gene expression. Activation of Ras-MAP kinase and protein kinase A signaling cascades transcriptionally down-regulates caveolin-1 promoter activity. J Biol Chem 1999;274:32333-41.
    • (1999) J Biol Chem , vol.274 , pp. 32333-32341
    • Engelman, J.A.1    Zhang, X.L.2    Razani, B.3    Pestell, R.G.4    Lisanti, M.P.5
  • 40
    • 0030982565 scopus 로고    scopus 로고
    • Two sterol regulatory element-like sequences mediate up-regulation of caveolin gene transcription in response to low density lipoprotein free cholesterol
    • Bist A, Fielding PE, Fielding CJ. Two sterol regulatory element-like sequences mediate up-regulation of caveolin gene transcription in response to low density lipoprotein free cholesterol. Proc Natl Acad Sci USA 1997;94:10693-8.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10693-10698
    • Bist, A.1    Fielding, P.E.2    Fielding, C.J.3
  • 41
    • 0029799891 scopus 로고    scopus 로고
    • A role for caveolin in transport of cholesterol from endoplasmic reticulum to plasma membrane
    • Smart EJ, Ying Y-s, Donzell WC, Anderson RGW. A role for caveolin in transport of cholesterol from endoplasmic reticulum to plasma membrane. J Biol Chem 1996;271:29427-35.
    • (1996) J Biol Chem , vol.271 , pp. 29427-29435
    • Smart, E.J.1    Ying, Y.-S.2    Donzell, W.C.3    Anderson, R.G.W.4
  • 42
    • 0030997431 scopus 로고    scopus 로고
    • Murine SR-BI, a high density lipoprotein receptor that mediates selective lipid uptake, is N-glycosylated and fatty acylated and colocalizes with plasma membrane caveolae
    • Babitt J, Trigatti B, Rigotti A, Smart EJ, Anderson RGW, Xu S, et al. Murine SR-BI, a high density lipoprotein receptor that mediates selective lipid uptake, is N-glycosylated and fatty acylated and colocalizes with plasma membrane caveolae. J Biol Chem 1997;272:13242-9.
    • (1997) J Biol Chem , vol.272 , pp. 13242-13249
    • Babitt, J.1    Trigatti, B.2    Rigotti, A.3    Smart, E.J.4    Anderson, R.G.W.5    Xu, S.6
  • 43
    • 0035963902 scopus 로고    scopus 로고
    • Caveolae and intracellular trafficking of cholesterol
    • Fielding CJ, Fielding PE. Caveolae and intracellular trafficking of cholesterol. Adv Drug Deliv Rev 2001;49:251-64.
    • (2001) Adv Drug Deliv Rev , vol.49 , pp. 251-264
    • Fielding, C.J.1    Fielding, P.E.2
  • 44
    • 0032577647 scopus 로고    scopus 로고
    • Caveolin-mediated regulation of signaling along the p42/ 44 MAP kinase cascade in vivo. A role for the caveolin-scaffolding domain
    • Engelman JA, Chu C, Lin A, Jo H, Ikezu T, Okamoto T, et al. Caveolin-mediated regulation of signaling along the p42/ 44 MAP kinase cascade in vivo. A role for the caveolin-scaffolding domain. FEBS Lett 1998;428:205-11.
    • (1998) FEBS Lett , vol.428 , pp. 205-211
    • Engelman, J.A.1    Chu, C.2    Lin, A.3    Jo, H.4    Ikezu, T.5    Okamoto, T.6
  • 45
    • 0032538790 scopus 로고    scopus 로고
    • Targeted downregulation of caveolin-1 is sufficient to drive cell transformation and hyperactivate the p42/44 MAP kinase cascade
    • Galbiati F, Volonte D, Engelman JA, Watanabe G, Burk R, Pestell RG, et al. Targeted downregulation of caveolin-1 is sufficient to drive cell transformation and hyperactivate the p42/44 MAP kinase cascade. EMBO J 1998;17:6633-48.
    • (1998) EMBO J , vol.17 , pp. 6633-6648
    • Galbiati, F.1    Volonte, D.2    Engelman, J.A.3    Watanabe, G.4    Burk, R.5    Pestell, R.G.6
  • 46
    • 0034647728 scopus 로고    scopus 로고
    • The cyclin D1 gene is transcriptionally repressed by caveolin-1
    • Hulit J, Bash T, Fu M, Galbiati F, Albanese C, Sage DR, et al. The cyclin D1 gene is transcriptionally repressed by caveolin-1. J Biol Chem 2000;275:21203-9.
    • (2000) J Biol Chem , vol.275 , pp. 21203-21209
    • Hulit, J.1    Bash, T.2    Fu, M.3    Galbiati, F.4    Albanese, C.5    Sage, D.R.6
  • 47
    • 0024317054 scopus 로고
    • Tyrosine phosphorylation of a 22-kDa protein is correlated with transformation by Rous sarcoma virus
    • Glenney JR, Jr. Tyrosine phosphorylation of a 22-kDa protein is correlated with transformation by Rous sarcoma virus. J Biol Chem 1989;264:20163-6.
    • (1989) J Biol Chem , vol.264 , pp. 20163-20166
    • Glenney Jr., J.R.1
  • 48
    • 0028953271 scopus 로고
    • Reduction of caveolin and caveolae in oncogenically transformed cells
    • Koleske AJ, Baltimore D, Lisanti MP. Reduction of caveolin and caveolae in oncogenically transformed cells. Proc Natl Acad Sci USA 1995;92:1381-5.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 1381-1385
    • Koleske, A.J.1    Baltimore, D.2    Lisanti, M.P.3
  • 49
    • 0032546319 scopus 로고    scopus 로고
    • Tumor cell growth inhibition by caveolin re-expression in human breast cancer cells
    • Lee SW, Reimer CL, Oh P, Campbell DB, Schnitzer JE. Tumor cell growth inhibition by caveolin re-expression in human breast cancer cells. Oncogene 1998;16:1391-7.
    • (1998) Oncogene , vol.16 , pp. 1391-1397
    • Lee, S.W.1    Reimer, C.L.2    Oh, P.3    Campbell, D.B.4    Schnitzer, J.E.5
  • 50
    • 0030960332 scopus 로고    scopus 로고
    • Recombinant expression of caveolin-1 in oncogenically transformed cells abrogates anchorage-independent growth
    • Engelman JA, Wykoff CC, Yasuhara S, Song KS, Okamoto T, Lisanti MP. Recombinant expression of caveolin-1 in oncogenically transformed cells abrogates anchorage-independent growth. J Biol Chem 1997;272:16374-81.
    • (1997) J Biol Chem , vol.272 , pp. 16374-16381
    • Engelman, J.A.1    Wykoff, C.C.2    Yasuhara, S.3    Song, K.S.4    Okamoto, T.5    Lisanti, M.P.6
  • 51
    • 0037018405 scopus 로고    scopus 로고
    • Caveolin-1 inhibits anchorage-independent growth, anoikis and invasiveness in MCF-7 human breast cancer cells
    • Fiucci G, Ravid D, Reich R, Liscovitch M. Caveolin-1 inhibits anchorage-independent growth, anoikis and invasiveness in MCF-7 human breast cancer cells. Oncogene 2002;21:2365-75.
    • (2002) Oncogene , vol.21 , pp. 2365-2375
    • Fiucci, G.1    Ravid, D.2    Reich, R.3    Liscovitch, M.4
  • 52
    • 0033147405 scopus 로고    scopus 로고
    • Involvement of caveolin-1 in meiotic cell-cycle progression in Caenorhabditis elegans
    • Scheel J, Srinivasan J, Honnert U, Henske A, Kurzchalia TV. Involvement of caveolin-1 in meiotic cell-cycle progression in Caenorhabditis elegans. Nat Cell Biol 1999;1:127-9.
    • (1999) Nat Cell Biol , vol.1 , pp. 127-129
    • Scheel, J.1    Srinivasan, J.2    Honnert, U.3    Henske, A.4    Kurzchalia, T.V.5
  • 53
    • 0035158471 scopus 로고    scopus 로고
    • Caveolin-1 expression negatively regulates cell cycle progression by inducing G(0)/G(1) arrest via a p53/ p21(WAF1/Cip1)-dependent mechanism
    • Galbiati F, Volonte D, Liu J, Capozza F, Frank PG, Zhu L, et al. Caveolin-1 expression negatively regulates cell cycle progression by inducing G(0)/G(1) arrest via a p53/ p21(WAF1/Cip1)-dependent mechanism. Mol Biol Cell 2001;12:2229-44.
    • (2001) Mol Biol Cell , vol.12 , pp. 2229-2244
    • Galbiati, F.1    Volonte, D.2    Liu, J.3    Capozza, F.4    Frank, P.G.5    Zhu, L.6
  • 54
    • 2642549186 scopus 로고    scopus 로고
    • Combined loss of INK4a and caveolin-1 synergistically enhances cell proliferation and oncogene-induced tumorigenesis
    • Williams TM, Lee H, Cheung MW, Cohen AW, Razani B, Iyengar P, et al. Combined loss of INK4a and caveolin-1 synergistically enhances cell proliferation and oncogene-induced tumorigenesis. J Biol Chem 2004;279:24745-56.
    • (2004) J Biol Chem , vol.279 , pp. 24745-24756
    • Williams, T.M.1    Lee, H.2    Cheung, M.W.3    Cohen, A.W.4    Razani, B.5    Iyengar, P.6
  • 55
    • 0034617210 scopus 로고    scopus 로고
    • Up-regulation of caveolin attenuates epidermal growth factor signaling in senescent cells
    • Park WY, Park JS, Cho KA, Kim DI, Ko YG, Seo JS, et al. Up-regulation of caveolin attenuates epidermal growth factor signaling in senescent cells. J Biol Chem 2000; 275: 20847-52.
    • (2000) J Biol Chem , vol.275 , pp. 20847-20852
    • Park, W.Y.1    Park, J.S.2    Cho, K.A.3    Kim, D.I.4    Ko, Y.G.5    Seo, J.S.6
  • 56
    • 0345736990 scopus 로고    scopus 로고
    • Downregulation of caveolin-1 function by EGF leads to the loss of E-cadherin, increased transcriptional activity of beta-catenin, and enhanced tumor cell invasion
    • Lu Z, Ghosh S, Wang Z, Hunter T. Downregulation of caveolin-1 function by EGF leads to the loss of E-cadherin, increased transcriptional activity of beta-catenin, and enhanced tumor cell invasion. Cancer Cell 2003;4:499-515.
    • (2003) Cancer Cell , vol.4 , pp. 499-515
    • Lu, Z.1    Ghosh, S.2    Wang, Z.3    Hunter, T.4
  • 57
  • 58
    • 4043107128 scopus 로고    scopus 로고
    • Mutation and aberrant expression of Caveolin-1 in human oral squamous cell carcinomas and oral cancer cell lines
    • Han SE, Park KH, Lee G, Huh YJ, Min BM. Mutation and aberrant expression of Caveolin-1 in human oral squamous cell carcinomas and oral cancer cell lines. Int J Oncol 2004; 24:435-40.
    • (2004) Int J Oncol , vol.24 , pp. 435-440
    • Han, S.E.1    Park, K.H.2    Lee, G.3    Huh, Y.J.4    Min, B.M.5
  • 59
    • 0037905722 scopus 로고    scopus 로고
    • Caveolin-1 and caveolin-2,together with three bone morphogenetic protein-related genes, may encode novel tumor suppressors down-regulated in sporadic follicular thyroid carcinogenesis
    • Aldred MA, Ginn-Pease ME, Morrison CD, Popkie AP, Gimm O, Hoang-Vu C, et al. Caveolin-1 and caveolin-2,together with three bone morphogenetic protein-related genes, may encode novel tumor suppressors down-regulated in sporadic follicular thyroid carcinogenesis. Cancer Res 2003;63:2864-71.
    • (2003) Cancer Res , vol.63 , pp. 2864-2871
    • Aldred, M.A.1    Ginn-Pease, M.E.2    Morrison, C.D.3    Popkie, A.P.4    Gimm, O.5    Hoang-Vu, C.6
  • 60
    • 0031758918 scopus 로고    scopus 로고
    • Genes encoding human caveolin-1 and -2 are co-localized to the D7S522 locus (7q31.1), a known fragile site (FRA7G) that is frequently deleted in human cancers
    • Engelman JA, Zhang XL, Lisanti MP. Genes encoding human caveolin-1 and -2 are co-localized to the D7S522 locus (7q31.1), a known fragile site (FRA7G) that is frequently deleted in human cancers. FEBS Lett 1998; 436: 403-10.
    • (1998) FEBS Lett , vol.436 , pp. 403-410
    • Engelman, J.A.1    Zhang, X.L.2    Lisanti, M.P.3
  • 62
    • 0038751964 scopus 로고    scopus 로고
    • Absence of caveolin-1 sensitizes mouse skin to carcinogen-induced epidermal hyperplasia and tumor formation
    • Capozza F, Williams TM, Schubert W, McClain S, Bouzahzah B, Sotgia F, et al. Absence of caveolin-1 sensitizes mouse skin to carcinogen-induced epidermal hyperplasia and tumor formation. Am J Pathol 2003;162:2029-39.
    • (2003) Am J Pathol , vol.162 , pp. 2029-2039
    • Capozza, F.1    Williams, T.M.2    Schubert, W.3    McClain, S.4    Bouzahzah, B.5    Sotgia, F.6
  • 63
    • 0037342807 scopus 로고    scopus 로고
    • Loss of caveolin-1 gene expression accelerates the development of dysplastic mammary lesions in tumor-prone transgenic mice
    • Williams TM, Cheung MW, Park DS, Razani B, Cohen AW, Muller WJ, et al. Loss of caveolin-1 gene expression accelerates the development of dysplastic mammary lesions in tumor-prone transgenic mice. Mol Biol Cell 2003;14:1027-42.
    • (2003) Mol Biol Cell , vol.14 , pp. 1027-1042
    • Williams, T.M.1    Cheung, M.W.2    Park, D.S.3    Razani, B.4    Cohen, A.W.5    Muller, W.J.6
  • 64
    • 0035965995 scopus 로고    scopus 로고
    • Caveolae-deficient endothelial cells show defects in the uptake and transport of albumin in vivo
    • Schubert W, Frank PG, Razani B, Park DS, Chow CW, Lisanti MP. Caveolae-deficient endothelial cells show defects in the uptake and transport of albumin in vivo. J Biol Chem 2001;276:48619-22.
    • (2001) J Biol Chem , vol.276 , pp. 48619-48622
    • Schubert, W.1    Frank, P.G.2    Razani, B.3    Park, D.S.4    Chow, C.W.5    Lisanti, M.P.6
  • 65
    • 0037131313 scopus 로고    scopus 로고
    • Microvascular hyperpermeability in caveolin-1 (-/-) knock-out mice. Treatment with a specific nitric-oxide synthase inhibitor, L-NAME restores normal microvascular permeability in Cav-1 null mice
    • Schubert W, Frank PG, Woodman SE, Hyogo H, Cohen DE, Chow CW, et al. Microvascular hyperpermeability in caveolin-1 (-/-) knock-out mice. Treatment with a specific nitric-oxide synthase inhibitor, L-NAME restores normal microvascular permeability in Cav-1 null mice. J Biol Chem 2002;277:40091-8.
    • (2002) J Biol Chem , vol.277 , pp. 40091-40098
    • Schubert, W.1    Frank, P.G.2    Woodman, S.E.3    Hyogo, H.4    Cohen, D.E.5    Chow, C.W.6
  • 66
    • 0034529950 scopus 로고    scopus 로고
    • In vivo delivery of the caveolin-1 scaffolding domain inhibits nitric oxide synthesis and reduces inflammation
    • Bucci M, Gratton JP, Rudic RD, Acevedo L, Roviezzo F, Cirino G, et al. In vivo delivery of the caveolin-1 scaffolding domain inhibits nitric oxide synthesis and reduces inflammation. Nat Med 2000;6:1362-7.
    • (2000) Nat Med , vol.6 , pp. 1362-1367
    • Bucci, M.1    Gratton, J.P.2    Rudic, R.D.3    Acevedo, L.4    Roviezzo, F.5    Cirino, G.6
  • 68
    • 0037155864 scopus 로고    scopus 로고
    • Caveolin-1 expression enhances endothelial capillary tubule formation
    • Liu J, Wang XB, Park DS, Lisanti MP. Caveolin-1 expression enhances endothelial capillary tubule formation. J Biol Chem 2002;277:10661-8.
    • (2002) J Biol Chem , vol.277 , pp. 10661-10668
    • Liu, J.1    Wang, X.B.2    Park, D.S.3    Lisanti, M.P.4
  • 70
  • 71
    • 0032921302 scopus 로고    scopus 로고
    • Caveolin and its cellular and subcellular immunolocalisation in lung alveolar epithelium: Implications for alveolar epithelial type I cell function
    • Newman GR, Campbell L, von Ruhland C, Jasani B, Gumbleton M. Caveolin and its cellular and subcellular immunolocalisation in lung alveolar epithelium: implications for alveolar epithelial type I cell function. Cell Tissue Res 1999;295:111-20.
    • (1999) Cell Tissue Res , vol.295 , pp. 111-120
    • Newman, G.R.1    Campbell, L.2    Von Ruhland, C.3    Jasani, B.4    Gumbleton, M.5
  • 73
    • 0037143769 scopus 로고    scopus 로고
    • Defects in caveolin-1 cause dilated cardiomyopathy and pulmonary hypertension in knockout mice
    • Zhao YY, Liu Y, Stan RV, Fan L, Gu Y, Dalton N, et al. Defects in caveolin-1 cause dilated cardiomyopathy and pulmonary hypertension in knockout mice. Proc Natl Acad Sci USA 2002;99:11375-80.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 11375-11380
    • Zhao, Y.Y.1    Liu, Y.2    Stan, R.V.3    Fan, L.4    Gu, Y.5    Dalton, N.6
  • 74
    • 0037303007 scopus 로고    scopus 로고
    • Caveolin-1 null mice develop cardiac hypertrophy with hyperactivation of p42/44 MAP kinase in cardiac fibroblasts
    • Cohen AW, Park DS, Woodman SE, Williams TM, Chandra M, Shirani J, et al. Caveolin-1 null mice develop cardiac hypertrophy with hyperactivation of p42/44 MAP kinase in cardiac fibroblasts. Am J Physiol Cell Physiol 2003;284: C457-74.
    • (2003) Am J Physiol Cell Physiol , vol.284
    • Cohen, A.W.1    Park, D.S.2    Woodman, S.E.3    Williams, T.M.4    Chandra, M.5    Shirani, J.6
  • 75
    • 0036080902 scopus 로고    scopus 로고
    • Caveolin-1/3 double-knockout mice are viable, but lack both muscle and non-muscle caveolae, and develop a severe cardiomyopathic phenotype
    • Park DS, Woodman SE, Schubert W, Cohen AW, Frank PG, Chandra M, et al. Caveolin-1/3 double-knockout mice are viable, but lack both muscle and non-muscle caveolae, and develop a severe cardiomyopathic phenotype. Am J Pathol 2002;160:2207-17.
    • (2002) Am J Pathol , vol.160 , pp. 2207-2217
    • Park, D.S.1    Woodman, S.E.2    Schubert, W.3    Cohen, A.W.4    Frank, P.G.5    Chandra, M.6
  • 77
    • 0030853953 scopus 로고    scopus 로고
    • Direct Interaction of Endothelial Nitric-oxide Synthase and Caveolin-1 Inhibits Synthase Activity
    • Ju H, Zou R, Venema VJ, Venema RC. Direct Interaction of Endothelial Nitric-oxide Synthase and Caveolin-1 Inhibits Synthase Activity. J Biol Chem 1997;272:18522-5.
    • (1997) J Biol Chem , vol.272 , pp. 18522-18525
    • Ju, H.1    Zou, R.2    Venema, V.J.3    Venema, R.C.4
  • 78
    • 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, Siler-Masters BS, Skidd PM, Couet JC, Li S, et al. Dissecting the interaction between nitric oxide synthase (NOS) and caveolin: Functional significance of the NOS caveolin binding domain in vivo. J Biol Chem (Communication) 1997;272:25437-40.
    • (1997) J Biol Chem (Communication) , vol.272 , pp. 25437-25440
    • Garcia-Cardena, G.1    Martasek, P.2    Siler-Masters, B.S.3    Skidd, P.M.4    Couet, J.C.5    Li, S.6
  • 79
    • 0242693224 scopus 로고    scopus 로고
    • Transgenic overexpression of caveolin-3 in the heart induces a cardiomyopathic phenotype
    • Aravamudan B, Volonte D, Ramani R, Gursoy E, Lisanti MP, London B, et al. Transgenic overexpression of caveolin-3 in the heart induces a cardiomyopathic phenotype. Hum Mol Genet 2003;12:2777-88.
    • (2003) Hum Mol Genet , vol.12 , pp. 2777-2788
    • Aravamudan, B.1    Volonte, D.2    Ramani, R.3    Gursoy, E.4    Lisanti, M.P.5    London, B.6
  • 80
    • 10744220034 scopus 로고    scopus 로고
    • Identification and functional analysis of a caveolin-3 mutation associated with familial hypertrophic cardiomyopathy
    • Hayashi T, Arimura T, Ueda K, Shibata H, Hohda S, Takahashi M, et al. Identification and functional analysis of a caveolin-3 mutation associated with familial hypertrophic cardiomyopathy. Biochem Biophys Res Commun 2004;313: 178-84.
    • (2004) Biochem Biophys Res Commun , vol.313 , pp. 178-184
    • Hayashi, T.1    Arimura, T.2    Ueda, K.3    Shibata, H.4    Hohda, S.5    Takahashi, M.6
  • 81
    • 0031920515 scopus 로고    scopus 로고
    • Mutations in the caveolin-3 gene cause autosomal dominant limb-girdle muscular dystrophy
    • Minetti C, Sotogia F, Bruno C, Scartezzini P, Broda P, Bado M, et al. Mutations in the caveolin-3 gene cause autosomal dominant limb-girdle muscular dystrophy. Nat Genet 1998; 18:365-8.
    • (1998) Nat Genet , vol.18 , pp. 365-368
    • Minetti, C.1    Sotogia, F.2    Bruno, C.3    Scartezzini, P.4    Broda, P.5    Bado, M.6
  • 82
    • 0033520482 scopus 로고    scopus 로고
    • Phenotypic behavior of caveolin-3 mutations that cause autosomal dominant limb girdle muscular dystrophy (LGMD-1C). Retention of LGMD-1C caveolin-3 mutants within the Golgi complex
    • Galbiati F, Volonte D, Minetti C, Chu JB, Lisanti MP. Phenotypic behavior of caveolin-3 mutations that cause autosomal dominant limb girdle muscular dystrophy (LGMD-1C). Retention of LGMD-1C caveolin-3 mutants within the Golgi complex. J Biol Chem 1999;274:25632-41.
    • (1999) J Biol Chem , vol.274 , pp. 25632-25641
    • Galbiati, F.1    Volonte, D.2    Minetti, C.3    Chu, J.B.4    Lisanti, M.P.5
  • 83
    • 0034531315 scopus 로고    scopus 로고
    • Limb-girdle muscular dystrophy (LGMD-1C) mutants of caveolin-3 undergo ubiquitination and proteasomal degradation. Treatment with proteasomal inhibitors blocks the dominant negative effect of LGMD-1C mutants and rescues wild-type caveolin-3
    • Galbiati F, Volonte D, Minetti C, Bregman DB, Lisanti MP. Limb-girdle muscular dystrophy (LGMD-1C) mutants of caveolin-3 undergo ubiquitination and proteasomal degradation. Treatment with proteasomal inhibitors blocks the dominant negative effect of LGMD-1C mutants and rescues wild-type caveolin-3. J Biol Chem 2000;275:37702-11.
    • (2000) J Biol Chem , vol.275 , pp. 37702-37711
    • Galbiati, F.1    Volonte, D.2    Minetti, C.3    Bregman, D.B.4    Lisanti, M.P.5
  • 84
    • 0036791604 scopus 로고    scopus 로고
    • Caveolin-1 mutations (P132L and null) and the pathogenesis of breast cancer: Caveolin-1 (P132L) behaves in a dominant-negative manner and caveolin-1 (-/-) null mice show mammary epithelial cell hyperplasia
    • Lee H, Park DS, Razani B, Russell RG, Pestell RG, Lisanti MP. Caveolin-1 mutations (P132L and null) and the pathogenesis of breast cancer: caveolin-1 (P132L) behaves in a dominant-negative manner and caveolin-1 (-/-) null mice show mammary epithelial cell hyperplasia. Am J Pathol 2002;161:1357-69.
    • (2002) Am J Pathol , vol.161 , pp. 1357-1369
    • Lee, H.1    Park, D.S.2    Razani, B.3    Russell, R.G.4    Pestell, R.G.5    Lisanti, M.P.6
  • 85
    • 0035253580 scopus 로고    scopus 로고
    • Transgenic mice expressing mutant caveolin-3 show severe myopathy associated with increased nNOS activity
    • Sunada Y, Ohi H, Hase A, Hosono T, Arata S, Higuchi S, et al. Transgenic mice expressing mutant caveolin-3 show severe myopathy associated with increased nNOS activity. Hum Mol Genet 2001;10:173-8.
    • (2001) Hum Mol Genet , vol.10 , pp. 173-178
    • Sunada, Y.1    Ohi, H.2    Hase, A.3    Hosono, T.4    Arata, S.5    Higuchi, S.6
  • 87
    • 0032504045 scopus 로고    scopus 로고
    • Increased caveolin-3 levels in mdx mouse muscles
    • Vaghy PL, Fang J, Wu W, Vaghy LP. Increased caveolin-3 levels in mdx mouse muscles. FEBS Lett 1998;431:125-7.
    • (1998) FEBS Lett , vol.431 , pp. 125-127
    • Vaghy, P.L.1    Fang, J.2    Wu, W.3    Vaghy, L.P.4
  • 89
    • 12944317278 scopus 로고    scopus 로고
    • Transgenic overexpression of caveolin-3 in skeletal muscle fibers induces a Duchenne-like muscular dystrophy phenotype
    • Galbiati F, Volonte D, Chu JB, Li M, Fine SW, Fu M, et al. Transgenic overexpression of caveolin-3 in skeletal muscle fibers induces a Duchenne-like muscular dystrophy phenotype. Proc Natl Acad Sci USA 2000;97:9689-94.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 9689-9694
    • Galbiati, F.1    Volonte, D.2    Chu, J.B.3    Li, M.4    Fine, S.W.5    Fu, M.6
  • 91
    • 0034532164 scopus 로고    scopus 로고
    • Caveolin-3 directly interacts with the C-terminal tail of beta-dystroglycan. Identification of a central WW-like domain within caveolin family members
    • Sotgia F, Lee JK, Das K, Bedford M, Petrucci TC, Macioce P, et al. Caveolin-3 directly interacts with the C-terminal tail of beta-dystroglycan. Identification of a central WW-like domain within caveolin family members. J Biol Chem 2000;275:38048-58.
    • (2000) J Biol Chem , vol.275 , pp. 38048-38058
    • Sotgia, F.1    Lee, J.K.2    Das, K.3    Bedford, M.4    Petrucci, T.C.5    Macioce, P.6
  • 92
    • 0344412990 scopus 로고    scopus 로고
    • Phosphofructokinase muscle-specific isoform requires caveolin-3 expression for plasma membrane recruitment and caveolar targeting: Implications for the pathogenesis of caveolin-related muscle diseases
    • Sotgia F, Bonuccelli G, Minetti C, Woodman SE, Capozza F, Kemp RG, et al. Phosphofructokinase muscle-specific isoform requires caveolin-3 expression for plasma membrane recruitment and caveolar targeting: implications for the pathogenesis of caveolin-related muscle diseases. Am J Pathol 2003;163:2619-34.
    • (2003) Am J Pathol , vol.163 , pp. 2619-2634
    • Sotgia, F.1    Bonuccelli, G.2    Minetti, C.3    Woodman, S.E.4    Capozza, F.5    Kemp, R.G.6
  • 93
    • 0346121432 scopus 로고    scopus 로고
    • A caveolin-3 mutant that causes limb girdle muscular dystrophy type 1 C disrupts Src localization and activity and induces apoptosis in skeletal myotubes
    • Smythe GM, Eby JC, Disatnik MH, Rando TA. A caveolin-3 mutant that causes limb girdle muscular dystrophy type 1 C disrupts Src localization and activity and induces apoptosis in skeletal myotubes. J Cell Sci 2003;116:4739-49.
    • (2003) J Cell Sci , vol.116 , pp. 4739-4749
    • Smythe, G.M.1    Eby, J.C.2    Disatnik, M.H.3    Rando, T.A.4
  • 94
    • 0034944010 scopus 로고    scopus 로고
    • Mutations in CAV3 cause mechanical hyperirritability of skeletal muscle in rippling muscle disease
    • Betz RC, Schoser BG, Kasper D, Ricker K, Ramirez A, Stein V, et al. Mutations in CAV3 cause mechanical hyperirritability of skeletal muscle in rippling muscle disease. Nat Genet 2001;28:218-9.
    • (2001) Nat Genet , vol.28 , pp. 218-219
    • Betz, R.C.1    Schoser, B.G.2    Kasper, D.3    Ricker, K.4    Ramirez, A.5    Stein, V.6
  • 95
  • 96
    • 17044449846 scopus 로고    scopus 로고
    • Mutation in the CAV3 gene causes partial caveolin-3 deficiency and hyperCKemia
    • Carbone I, Bruno C, Sotgia F, Bado M, Broda P, Masetti E, et al. Mutation in the CAV3 gene causes partial caveolin-3 deficiency and hyperCKemia. Neurology 2000;54:1373-6.
    • (2000) Neurology , vol.54 , pp. 1373-1376
    • Carbone, I.1    Bruno, C.2    Sotgia, F.3    Bado, M.4    Broda, P.5    Masetti, E.6
  • 97
    • 1342267006 scopus 로고    scopus 로고
    • Caveolinopathies: Mutations in caveolin-3 cause four distinct autosomal dominant muscle diseases
    • Woodman SE, Sotgia F, Galbiati F, Minetti C, Lisanti MP. Caveolinopathies: mutations in caveolin-3 cause four distinct autosomal dominant muscle diseases. Neurology 2004; 62: 538-43.
    • (2004) Neurology , vol.62 , pp. 538-543
    • Woodman, S.E.1    Sotgia, F.2    Galbiati, F.3    Minetti, C.4    Lisanti, M.P.5
  • 98
    • 0037378555 scopus 로고    scopus 로고
    • Disruption of the caveolin-1 gene impairs renal calcium reabsorption and leads to hypercalciuria and urolithiasis
    • Cao G, Yang G, Timme TL, Saika T, Truong LD, Satoh T, et al. Disruption of the caveolin-1 gene impairs renal calcium reabsorption and leads to hypercalciuria and urolithiasis. Am J Pathol 2003;162:1241-8.
    • (2003) Am J Pathol , vol.162 , pp. 1241-1248
    • Cao, G.1    Yang, G.2    Timme, T.L.3    Saika, T.4    Truong, L.D.5    Satoh, T.6
  • 100
  • 101
    • 0029836236 scopus 로고    scopus 로고
    • Insulin-stimulated glucose uptake involves the transition of glucose transporters to a caveolae-rich fraction within the plasma membrane: Implications for type II diabetes
    • Gustavsson J, Parpal S, Stralfors P. Insulin-stimulated glucose uptake involves the transition of glucose transporters to a caveolae-rich fraction within the plasma membrane: implications for type II diabetes. Mol Med 1996;2:367-72.
    • (1996) Mol Med , vol.2 , pp. 367-372
    • Gustavsson, J.1    Parpal, S.2    Stralfors, P.3
  • 102
    • 0036484936 scopus 로고    scopus 로고
    • Insulin induces translocation of glucose transporter GLUT4 to plasma membrane caveolae in adipocytes
    • Karlsson M, Thorn H, Parpal S, Stralfors P, Gustavsson J. Insulin induces translocation of glucose transporter GLUT4 to plasma membrane caveolae in adipocytes, FASEB J 2002; 16:249-51.
    • (2002) FASEB J , vol.16 , pp. 249-251
    • Karlsson, M.1    Thorn, H.2    Parpal, S.3    Stralfors, P.4    Gustavsson, J.5
  • 104
    • 0038363367 scopus 로고    scopus 로고
    • The adipocyte plasma membrane caveolin functional/structural organization is necessary for the efficient endocytosis of GLUT4
    • Shigematsu S, Watson RT, Khan AH, Pessin JE. The adipocyte plasma membrane caveolin functional/structural organization is necessary for the efficient endocytosis of GLUT4. J Biol Chem 2003;278:10683-90.
    • (2003) J Biol Chem , vol.278 , pp. 10683-10690
    • Shigematsu, S.1    Watson, R.T.2    Khan, A.H.3    Pessin, J.E.4
  • 105
    • 0032077150 scopus 로고    scopus 로고
    • Insulin-induced protein tyrosine phosphorylation cascade and signalling molecules are localized in a caveolin-enriched cell membrane domain
    • Smith RM, Harada S, Smith JA, Zhang S, Jarett L. Insulin-induced protein tyrosine phosphorylation cascade and signalling molecules are localized in a caveolin-enriched cell membrane domain. Cell Signal 1998;10:355-62.
    • (1998) Cell Signal , vol.10 , pp. 355-362
    • Smith, R.M.1    Harada, S.2    Smith, J.A.3    Zhang, S.4    Jarett, L.5
  • 107
    • 0032745869 scopus 로고    scopus 로고
    • Localization of the insulin receptor in caveolae of adipocyte plasma membrane
    • Gustavsson J, Parpal S, Karlsson M, Ramsing C, Thorn H, Borg M, et al. Localization of the insulin receptor in caveolae of adipocyte plasma membrane. FASEB J 1999;13:1961-71.
    • (1999) FASEB J , vol.13 , pp. 1961-1971
    • Gustavsson, J.1    Parpal, S.2    Karlsson, M.3    Ramsing, C.4    Thorn, H.5    Borg, M.6
  • 108
    • 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 1999;13:2013-24.
    • (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
  • 109
    • 0037119387 scopus 로고    scopus 로고
    • The insulin receptor catalyzes the tyrosine phosphorylation of caveolin-1
    • Kimura A, Mora S, Shigematsu S, Pessin JE, Saltiel AR. The insulin receptor catalyzes the tyrosine phosphorylation of caveolin-1. J Biol Chem 2002;277:30153-8.
    • (2002) J Biol Chem , vol.277 , pp. 30153-30158
    • Kimura, A.1    Mora, S.2    Shigematsu, S.3    Pessin, J.E.4    Saltiel, A.R.5
  • 110
    • 0035971086 scopus 로고    scopus 로고
    • Cholesterol depletion disrupts caveolae and insulin receptor signaling for metabolic control via insulin receptor substrate-1, but not for mitogen-activated protein kinase control
    • Parpal S, Karlsson M, Thorn H, Stralfors P. Cholesterol depletion disrupts caveolae and insulin receptor signaling for metabolic control via insulin receptor substrate-1, but not for mitogen-activated protein kinase control. J Biol Chem 2001; 276:9670-8.
    • (2001) J Biol Chem , vol.276 , pp. 9670-9678
    • Parpal, S.1    Karlsson, M.2    Thorn, H.3    Stralfors, P.4
  • 111
    • 0037663884 scopus 로고    scopus 로고
    • Caveolin-1-deficient mice show insulin resistance and defective insulin receptor protein expression in adipose tissue
    • Cohen AW, Razani B, Wang XB, Combs TP, Williams TM, Scherer PE, et al. Caveolin-1-deficient mice show insulin resistance and defective insulin receptor protein expression in adipose tissue. Am J Physiol Cell Physiol 2003;285:C222-35.
    • (2003) Am J Physiol Cell Physiol , vol.285
    • Cohen, A.W.1    Razani, B.2    Wang, X.B.3    Combs, T.P.4    Williams, T.M.5    Scherer, P.E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.