메뉴 건너뛰기




Volumn 1746, Issue 3, 2005, Pages 322-333

Getting rid of caveolins: Phenotypes of caveolin-deficient animals

Author keywords

Caveolae; Caveolin; Knockout mouse; Metabolic disorder; Signaling

Indexed keywords

CAVEOLIN 1; CAVEOLIN 2; CAVEOLIN 3; CELL MARKER; MEMBRANE PROTEIN;

EID: 29144505268     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2005.06.001     Document Type: Review
Times cited : (130)

References (113)
  • 1
    • 0026640940 scopus 로고
    • VIP21, a 21-kD membrane protein is an integral component of trans-Golgi-network-derived transport vesicles
    • T.V. Kurzchalia, P. Dupree, R.G. Parton, R. Kellner, H. Virta, M. Lehnert, and K. Simons VIP21, a 21-kD membrane protein is an integral component of trans-Golgi-network-derived transport vesicles J. Cell Biol. 118 1992 1003 1014
    • (1992) J. Cell Biol. , vol.118 , pp. 1003-1014
    • Kurzchalia, T.V.1    Dupree, P.2    Parton, R.G.3    Kellner, R.4    Virta, H.5    Lehnert, M.6    Simons, K.7
  • 3
    • 0033147405 scopus 로고    scopus 로고
    • Involvement of caveolin-1 in meiotic cell-cycle progression in Caenorhabditis elegans
    • J. Scheel, J. Srinivasan, U. Honnert, A. Henske, and T.V. Kurzchalia Involvement of caveolin-1 in meiotic cell-cycle progression in Caenorhabditis elegans Nat. Cell Biol. 1 1999 127 129
    • (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
  • 5
    • 0035877753 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
    • F. Galbiati, J.A. Engelman, D. Volonte, X.L. Zhang, C. Minetti, M. Li, H. Hou Jr., B. Kneitz, W. Edelmann, and M.P. Lisanti 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. 276 2001 21425 21433
    • (2001) J. Biol. Chem. , vol.276 , pp. 21425-21433
    • Galbiati, F.1    Engelman, J.A.2    Volonte, D.3    Zhang, X.L.4    Minetti, C.5    Li, M.6    Hou Jr., H.7    Kneitz, B.8    Edelmann, W.9    Lisanti, M.P.10
  • 13
    • 0033520479 scopus 로고    scopus 로고
    • Caveolin-2 localizes to the Golgi complex but redistributes to plasma membrane, caveolae, and rafts when co-expressed with caveolin-1
    • R. Mora, V.L. Bonilha, A. Marmorstein, P.E. Scherer, D. Brown, M.P. Lisanti, and E. Rodriguez-Boulan Caveolin-2 localizes to the Golgi complex but redistributes to plasma membrane, caveolae, and rafts when co-expressed with caveolin-1 J. Biol. Chem. 274 1999 25708 25717
    • (1999) J. Biol. Chem. , vol.274 , pp. 25708-25717
    • Mora, R.1    Bonilha, V.L.2    Marmorstein, A.3    Scherer, P.E.4    Brown, D.5    Lisanti, M.P.6    Rodriguez-Boulan, E.7
  • 15
    • 0000855817 scopus 로고
    • Fine structure of blood capillaries
    • G.E. Palade Fine structure of blood capillaries J. Appl. Physiol. 24 1953 1424 1436
    • (1953) J. Appl. Physiol. , vol.24 , pp. 1424-1436
    • Palade, G.E.1
  • 16
    • 0029809310 scopus 로고    scopus 로고
    • Role of GTP hydrolysis in fission of caveolae directly from plasma membranes
    • J.E. Schnitzer, P. Oh, and D.P. McIntosh Role of GTP hydrolysis in fission of caveolae directly from plasma membranes Science 274 1996 239 242
    • (1996) Science , vol.274 , pp. 239-242
    • Schnitzer, J.E.1    Oh, P.2    McIntosh, D.P.3
  • 17
    • 0242268532 scopus 로고    scopus 로고
    • Lipid rafts and caveolae as portals for endocytosis: New insights and common mechanisms
    • R.G. Parton, and A.A. Richards Lipid rafts and caveolae as portals for endocytosis: new insights and common mechanisms Traffic 4 2003 724 738
    • (2003) Traffic , vol.4 , pp. 724-738
    • Parton, R.G.1    Richards, A.A.2
  • 18
    • 0035965995 scopus 로고    scopus 로고
    • Caveolae-deficient endothelial cells show defects in the uptake and transport of albumin in vivo
    • W. Schubert, P.G. Frank, B. Razani, D.S. Park, C.W. Chow, and M.P. Lisanti Caveolae-deficient endothelial cells show defects in the uptake and transport of albumin in vivo J. Biol. Chem. 276 2001 48619 48622
    • (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
  • 19
    • 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
    • W. Schubert, P.G. Frank, S.E. Woodman, H. Hyogo, D.E. Cohen, C.W. Chow, and M.P. Lisanti 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. 277 2002 40091 40098
    • (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    Lisanti, M.P.7
  • 20
    • 0031558768 scopus 로고    scopus 로고
    • Structure of detergent-resistant membrane domains: Does phase separation occur in biological membranes?
    • D.A. Brown, and E. London Structure of detergent-resistant membrane domains: does phase separation occur in biological membranes? Biochem. Biophys. Res. Commun. 240 1997 1 7
    • (1997) Biochem. Biophys. Res. Commun. , vol.240 , pp. 1-7
    • Brown, D.A.1    London, E.2
  • 21
    • 0028000605 scopus 로고
    • Sequestration of GPI-anchored proteins in caveolae triggered by cross-linking
    • S. Mayor, K.G. Rothberg, and F.R. Maxfield Sequestration of GPI-anchored proteins in caveolae triggered by cross-linking Science 264 1994 1948 1951
    • (1994) Science , vol.264 , pp. 1948-1951
    • Mayor, S.1    Rothberg, K.G.2    Maxfield, F.R.3
  • 22
    • 0028138521 scopus 로고
    • Regulated internalization of caveolae
    • R.G. Parton, B. Joggerst, and K. Simons Regulated internalization of caveolae J. Cell Biol. 127 1994 1199 1215
    • (1994) J. Cell Biol. , vol.127 , pp. 1199-1215
    • Parton, R.G.1    Joggerst, B.2    Simons, K.3
  • 23
    • 0025133358 scopus 로고
    • Vectorial apical delivery and slow endocytosis of a glycolipid-anchored fusion protein in transfected MDCK cells
    • M.P. Lisanti, I.W. Caras, T. Gilbert, D. Hanzel, and E. Rodriguez-Boulan Vectorial apical delivery and slow endocytosis of a glycolipid-anchored fusion protein in transfected MDCK cells Proc. Natl. Acad. Sci. U. S. A. 87 1990 7419 7423
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 7419-7423
    • Lisanti, M.P.1    Caras, I.W.2    Gilbert, T.3    Hanzel, D.4    Rodriguez-Boulan, E.5
  • 24
    • 0027363575 scopus 로고
    • Caveolin forms a hetero-oligomeric protein complex that interacts with an apical GPI-linked protein: Implications for the biogenesis of caveolae
    • M.P. Lisanti, Z.L. Tang, and M. Sargiacomo Caveolin forms a hetero-oligomeric protein complex that interacts with an apical GPI-linked protein: implications for the biogenesis of caveolae J. Cell Biol. 123 1993 595 604
    • (1993) J. Cell Biol. , vol.123 , pp. 595-604
    • Lisanti, M.P.1    Tang, Z.L.2    Sargiacomo, M.3
  • 26
    • 0036239115 scopus 로고    scopus 로고
    • Endocytosis via caveolae
    • L. Pelkmans, and A. Helenius Endocytosis via caveolae Traffic 3 2002 311 320
    • (2002) Traffic , vol.3 , pp. 311-320
    • Pelkmans, L.1    Helenius, A.2
  • 27
    • 0035017308 scopus 로고    scopus 로고
    • Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the ER
    • L. Pelkmans, J. Kartenbeck, and A. Helenius Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the ER Nat. Cell Biol. 3 2001 473 483
    • (2001) Nat. Cell Biol. , vol.3 , pp. 473-483
    • Pelkmans, L.1    Kartenbeck, J.2    Helenius, A.3
  • 28
    • 0037134014 scopus 로고    scopus 로고
    • Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae
    • L. Pelkmans, D. Puntener, and A. Helenius Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae Science 296 2002 535 539
    • (2002) Science , vol.296 , pp. 535-539
    • Pelkmans, L.1    Puntener, D.2    Helenius, A.3
  • 29
    • 0037470170 scopus 로고    scopus 로고
    • Glycosphingolipids internalized via caveolar-related endocytosis rapidly merge with the clathrin pathway in early endosomes and form microdomains for recycling
    • D.K. Sharma, A. Choudhury, R.D. Singh, C.L. Wheatley, D.L. Marks, and R.E. Pagano Glycosphingolipids internalized via caveolar-related endocytosis rapidly merge with the clathrin pathway in early endosomes and form microdomains for recycling J. Biol. Chem. 278 2003 7564 7572
    • (2003) J. Biol. Chem. , vol.278 , pp. 7564-7572
    • Sharma, D.K.1    Choudhury, A.2    Singh, R.D.3    Wheatley, C.L.4    Marks, D.L.5    Pagano, R.E.6
  • 30
    • 13444273098 scopus 로고    scopus 로고
    • Clathrin- and caveolin-1-independent endocytosis: Entry of simian virus 40 into cells devoid of caveolae
    • E.M. Damm, L. Pelkmans, J. Kartenbeck, A. Mezzacasa, T. Kurzchalia, and A. Helenius Clathrin- and caveolin-1-independent endocytosis: entry of simian virus 40 into cells devoid of caveolae J. Cell Biol. 168 2005 477 488
    • (2005) J. Cell Biol. , vol.168 , pp. 477-488
    • Damm, E.M.1    Pelkmans, L.2    Kartenbeck, J.3    Mezzacasa, A.4    Kurzchalia, T.5    Helenius, A.6
  • 33
    • 0037429690 scopus 로고    scopus 로고
    • Relationship between cholesterol trafficking and signaling in rafts and caveolae
    • C.J. Fielding, and P.E. Fielding Relationship between cholesterol trafficking and signaling in rafts and caveolae Biochim. Biophys. Acta 1610 2003 219 228
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 219-228
    • Fielding, C.J.1    Fielding, P.E.2
  • 34
    • 0034158315 scopus 로고    scopus 로고
    • Caveolins and cellular cholesterol balance
    • E. Ikonen, and R.G. Parton Caveolins and cellular cholesterol balance Traffic 1 2000 212 217
    • (2000) Traffic , vol.1 , pp. 212-217
    • Ikonen, E.1    Parton, R.G.2
  • 35
    • 0031888035 scopus 로고    scopus 로고
    • Regulation of caveolin and caveolae by cholesterol in MDCK cells
    • D. Hailstones, L.S. Sleer, R.G. Parton, and K.K. Stanley Regulation of caveolin and caveolae by cholesterol in MDCK cells J. Lipid Res. 39 1998 369 379
    • (1998) J. Lipid Res. , vol.39 , pp. 369-379
    • Hailstones, D.1    Sleer, L.S.2    Parton, R.G.3    Stanley, K.K.4
  • 36
    • 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
    • A. Bist, P.E. Fielding, and C.J. Fielding 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. U. S. A. 94 1997 10693 10698
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 10693-10698
    • Bist, A.1    Fielding, P.E.2    Fielding, C.J.3
  • 37
    • 0030970279 scopus 로고    scopus 로고
    • Caveolin mRNA levels are up-regulated by free cholesterol and down-regulated by oxysterols in fibroblast monolayers
    • C.J. Fielding, A. Bist, and P.E. Fielding Caveolin mRNA levels are up-regulated by free cholesterol and down-regulated by oxysterols in fibroblast monolayers Proc. Natl. Acad. Sci. U. S. A. 94 1997 3753 3758
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 3753-3758
    • Fielding, C.J.1    Bist, A.2    Fielding, P.E.3
  • 39
    • 14744270462 scopus 로고    scopus 로고
    • Caveolin-1 expression is essential for proper nonshivering thermogenesis in brown adipose tissue
    • A.W. Cohen, W. Schubert, D.L. Brasaemle, P.E. Scherer, and M.P. Lisanti Caveolin-1 expression is essential for proper nonshivering thermogenesis in brown adipose tissue Diabetes 54 2005 679 686
    • (2005) Diabetes , vol.54 , pp. 679-686
    • Cohen, A.W.1    Schubert, W.2    Brasaemle, D.L.3    Scherer, P.E.4    Lisanti, M.P.5
  • 44
    • 0027986804 scopus 로고
    • Two naturally occurring mutations in the kinase domain of insulin receptor accelerate degradation of the insulin receptor and impair the kinase activity
    • T. Imamura, Y. Takata, T. Sasaoka, Y. Takada, H. Morioka, T. Haruta, T. Sawa, M. Iwanishi, Y.G. Hu, and Y. Suzuki Two naturally occurring mutations in the kinase domain of insulin receptor accelerate degradation of the insulin receptor and impair the kinase activity J. Biol. Chem. 269 1994 31019 31027
    • (1994) J. Biol. Chem. , vol.269 , pp. 31019-31027
    • Imamura, T.1    Takata, Y.2    Sasaoka, T.3    Takada, Y.4    Morioka, H.5    Haruta, T.6    Sawa, T.7    Iwanishi, M.8    Hu, Y.G.9    Suzuki, Y.10
  • 46
    • 0025155555 scopus 로고
    • Functional properties of a naturally occurring Trp1200-Ser1200 mutation of the insulin receptor
    • D.E. Moller, A. Yokota, F. Ginsberg-Fellner, and J.S. Flier Functional properties of a naturally occurring Trp1200-Ser1200 mutation of the insulin receptor Mol. Endocrinol. 4 1990 1183 1191
    • (1990) Mol. Endocrinol. , vol.4 , pp. 1183-1191
    • Moller, D.E.1    Yokota, A.2    Ginsberg-Fellner, F.3    Flier, J.S.4
  • 47
    • 0024995838 scopus 로고
    • A naturally occurring mutation of insulin receptor alanine 1134 impairs tyrosine kinase function and is associated with dominantly inherited insulin resistance
    • D.E. Moller, A. Yokota, M.F. White, A.G. Pazianos, and J.S. Flier A naturally occurring mutation of insulin receptor alanine 1134 impairs tyrosine kinase function and is associated with dominantly inherited insulin resistance J. Biol. Chem. 265 1990 14979 14985
    • (1990) J. Biol. Chem. , vol.265 , pp. 14979-14985
    • Moller, D.E.1    Yokota, A.2    White, M.F.3    Pazianos, A.G.4    Flier, J.S.5
  • 48
    • 0035809931 scopus 로고    scopus 로고
    • Caveolin-2 is targeted to lipid droplets, a new "membrane domain" in the cell
    • T. Fujimoto, H. Kogo, K. Ishiguro, K. Tauchi, and R. Nomura Caveolin-2 is targeted to lipid droplets, a new "membrane domain" in the cell J. Cell Biol. 152 2001 1079 1085
    • (2001) J. Cell Biol. , vol.152 , pp. 1079-1085
    • Fujimoto, T.1    Kogo, H.2    Ishiguro, K.3    Tauchi, K.4    Nomura, R.5
  • 49
    • 0035809923 scopus 로고    scopus 로고
    • Accumulation of caveolin in the endoplasmic reticulum redirects the protein to lipid storage droplets
    • A.G. Ostermeyer, J.M. Paci, Y. Zeng, D.M. Lublin, S. Munro, and D.A. Brown Accumulation of caveolin in the endoplasmic reticulum redirects the protein to lipid storage droplets J. Cell Biol. 152 2001 1071 1078
    • (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
  • 50
    • 0035809933 scopus 로고    scopus 로고
    • A caveolin dominant negative mutant associates with lipid bodies and induces intracellular cholesterol imbalance
    • A. Pol, R. Luetterforst, M. Lindsay, S. Heino, E. Ikonen, and R.G. Parton A caveolin dominant negative mutant associates with lipid bodies and induces intracellular cholesterol imbalance J. Cell Biol. 152 2001 1057 1070
    • (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
  • 51
    • 0942287191 scopus 로고    scopus 로고
    • Chinese hamster ovary K2 cell lipid droplets appear to be metabolic organelles involved in membrane traffic
    • P. Liu, Y. Ying, Y. Zhao, D.I. Mundy, M. Zhu, and R.G. Anderson Chinese hamster ovary K2 cell lipid droplets appear to be metabolic organelles involved in membrane traffic J. Biol. Chem. 279 2004 3787 3792
    • (2004) J. Biol. Chem. , vol.279 , pp. 3787-3792
    • Liu, P.1    Ying, Y.2    Zhao, Y.3    Mundy, D.I.4    Zhu, M.5    Anderson, R.G.6
  • 52
    • 8744267532 scopus 로고    scopus 로고
    • Proteomic analysis of proteins associated with lipid droplets of basal and lipolytically stimulated 3T3-L1 adipocytes
    • D.L. Brasaemle, G. Dolios, L. Shapiro, and R. Wang Proteomic analysis of proteins associated with lipid droplets of basal and lipolytically stimulated 3T3-L1 adipocytes J. Biol. Chem. 279 2004 46835 46842
    • (2004) J. Biol. Chem. , vol.279 , pp. 46835-46842
    • Brasaemle, D.L.1    Dolios, G.2    Shapiro, L.3    Wang, R.4
  • 53
    • 16344368798 scopus 로고    scopus 로고
    • Cholesterol and fatty acids regulate dynamic caveolin trafficking through the Golgi complex and between the cell surface and lipid bodies
    • A. Pol, S. Martin, M.A. Fernandez, M. Ingelmo-Torres, C. Ferguson, C. Enrich, and R.G. Parton Cholesterol and fatty acids regulate dynamic caveolin trafficking through the Golgi complex and between the cell surface and lipid bodies Mol. Biol. Cell 16 2005 2091 2105
    • (2005) Mol. Biol. Cell , vol.16 , pp. 2091-2105
    • Pol, A.1    Martin, S.2    Fernandez, M.A.3    Ingelmo-Torres, M.4    Ferguson, C.5    Enrich, C.6    Parton, R.G.7
  • 55
    • 15944365201 scopus 로고    scopus 로고
    • Caveolin, cholesterol, and lipid bodies
    • S. Martin, and R.G. Parton Caveolin, cholesterol, and lipid bodies Semin. Cell Dev. Biol. 16 2005 163 174
    • (2005) Semin. Cell Dev. Biol. , vol.16 , pp. 163-174
    • Martin, S.1    Parton, R.G.2
  • 61
    • 4544233451 scopus 로고    scopus 로고
    • Loss of caveolin-1 expression is associated with disruption of muscarinic cholinergic activities in the urinary bladder
    • H.H. Lai, T.B. Boone, G. Yang, C.P. Smith, S. Kiss, T.C. Thompson, and G.T. Somogyi Loss of caveolin-1 expression is associated with disruption of muscarinic cholinergic activities in the urinary bladder Neurochem. Int. 45 2004 1185 1193
    • (2004) Neurochem. Int. , vol.45 , pp. 1185-1193
    • Lai, H.H.1    Boone, T.B.2    Yang, G.3    Smith, C.P.4    Kiss, S.5    Thompson, T.C.6    Somogyi, G.T.7
  • 62
    • 0036082492 scopus 로고    scopus 로고
    • Relationships between caveolae and eNOS: Everything in proximity and the proximity of everything
    • M.S. Goligorsky, H. Li, S. Brodsky, and J. Chen Relationships between caveolae and eNOS: everything in proximity and the proximity of everything Am. J. Physiol., Renal. Physiol. 283 2002 F1 F10
    • (2002) Am. J. Physiol., Renal. Physiol. , vol.283
    • Goligorsky, M.S.1    Li, H.2    Brodsky, S.3    Chen, J.4
  • 63
    • 0029901663 scopus 로고    scopus 로고
    • Targeting of nitric oxide synthase to endothelial cell caveolae via palmitoylation: Implications for nitric oxide signaling
    • G. Garcia-Cardena, P. Oh, J. Liu, J.E. Schnitzer, and W.C. Sessa Targeting of nitric oxide synthase to endothelial cell caveolae via palmitoylation: implications for nitric oxide signaling Proc. Natl. Acad. Sci. U. S. A. 93 1996 6448 6453
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 6448-6453
    • Garcia-Cardena, G.1    Oh, P.2    Liu, J.3    Schnitzer, J.E.4    Sessa, W.C.5
  • 65
    • 0034529950 scopus 로고    scopus 로고
    • In vivo delivery of the caveolin-1 scaffolding domain inhibits nitric oxide synthesis and reduces inflammation
    • M. Bucci, J.P. Gratton, R.D. Rudic, L. Acevedo, F. Roviezzo, G. Cirino, and W.C. Sessa In vivo delivery of the caveolin-1 scaffolding domain inhibits nitric oxide synthesis and reduces inflammation Nat. Med. 6 2000 1362 1367
    • (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    Sessa, W.C.7
  • 66
    • 0030953208 scopus 로고    scopus 로고
    • Reciprocal regulation of endothelial nitric-oxide synthase by Ca2+-calmodulin and caveolin
    • J.B. Michel, O. Feron, D. Sacks, and T. Michel Reciprocal regulation of endothelial nitric-oxide synthase by Ca2+-calmodulin and caveolin J. Biol. Chem. 272 1997 15583 15586
    • (1997) J. Biol. Chem. , vol.272 , pp. 15583-15586
    • Michel, J.B.1    Feron, O.2    Sacks, D.3    Michel, T.4
  • 67
  • 68
  • 69
    • 0037155864 scopus 로고    scopus 로고
    • Caveolin-1 expression enhances endothelial capillary tubule formation
    • J. Liu, X.B. Wang, D.S. Park, and M.P. Lisanti Caveolin-1 expression enhances endothelial capillary tubule formation J. Biol. Chem. 277 2002 10661 10668
    • (2002) J. Biol. Chem. , vol.277 , pp. 10661-10668
    • Liu, J.1    Wang, X.B.2    Park, D.S.3    Lisanti, M.P.4
  • 72
  • 74
    • 0033965898 scopus 로고    scopus 로고
    • Caveolin 1-mediated regulation of receptor tyrosine kinase-associated phosphatidylinositol 3-kinase activity by ceramide
    • W. Zundel, L.M. Swiersz, and A. Giaccia Caveolin 1-mediated regulation of receptor tyrosine kinase-associated phosphatidylinositol 3-kinase activity by ceramide Mol. Cell. Biol. 20 2000 1507 1514
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1507-1514
    • Zundel, W.1    Swiersz, L.M.2    Giaccia, A.3
  • 76
    • 0032538790 scopus 로고    scopus 로고
    • Targeted downregulation of caveolin-1 is sufficient to drive cell transformation and hyperactivate the p42/44 MAP kinase cascade
    • F. Galbiati, D. Volonte, J.A. Engelman, G. Watanabe, R. Burk, R.G. Pestell, and M.P. Lisanti Targeted downregulation of caveolin-1 is sufficient to drive cell transformation and hyperactivate the p42/44 MAP kinase cascade EMBO J. 17 1998 6633 6648
    • (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    Lisanti, M.P.7
  • 77
    • 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
    • J.A. Engelman, C. Chu, A. Lin, H. Jo, T. Ikezu, T. Okamoto, D.S. Kohtz, and M.P. Lisanti Caveolin-mediated regulation of signaling along the p42/44 MAP kinase cascade in vivo. A role for the caveolin-scaffolding domain FEBS Lett. 428 1998 205 211
    • (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    Kohtz, D.S.7    Lisanti, M.P.8
  • 78
    • 0031470628 scopus 로고    scopus 로고
    • Platelet-derived growth factor activates mitogen-activated protein kinase in isolated caveolae
    • P. Liu, Y. Ying, and R.G. Anderson Platelet-derived growth factor activates mitogen-activated protein kinase in isolated caveolae Proc. Natl. Acad. Sci. U. S. A. 94 1997 13666 13670
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 13666-13670
    • Liu, P.1    Ying, Y.2    Anderson, R.G.3
  • 79
    • 0024317054 scopus 로고
    • Tyrosine phosphorylation of a 22-kDa protein is correlated with transformation by Rous sarcoma virus
    • J.R. Glenney Jr. Tyrosine phosphorylation of a 22-kDa protein is correlated with transformation by Rous sarcoma virus J. Biol. Chem. 264 1989 20163 20166
    • (1989) J. Biol. Chem. , vol.264 , pp. 20163-20166
    • Glenney Jr., J.R.1
  • 81
    • 13644266312 scopus 로고    scopus 로고
    • Caveolin-1 in oncogenic transformation, cancer, and metastasis
    • T.M. Williams, and M.P. Lisanti Caveolin-1 in oncogenic transformation, cancer, and metastasis Am. J. Physiol., Cell Physiol. 288 2005 C494 C506
    • (2005) Am. J. Physiol., Cell Physiol. , vol.288
    • Williams, T.M.1    Lisanti, M.P.2
  • 83
    • 0038751964 scopus 로고    scopus 로고
    • Absence of caveolin-1 sensitizes mouse skin to carcinogen-induced epidermal hyperplasia and tumor formation
    • F. Capozza, T.M. Williams, W. Schubert, S. McClain, B. Bouzahzah, F. Sotgia, and M.P. Lisanti Absence of caveolin-1 sensitizes mouse skin to carcinogen-induced epidermal hyperplasia and tumor formation Am. J. Pathol. 162 2003 2029 2039
    • (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    Lisanti, M.P.7
  • 86
    • 19944366937 scopus 로고    scopus 로고
    • Caveolin-1 gene disruption promotes mammary tumorigenesis and dramatically enhances lung metastasis in vivo. Role of Cav-1 in cell invasiveness and matrix metalloproteinase (MMP-2/9) secretion
    • T.M. Williams, F. Medina, I. Badano, R.B. Hazan, J. Hutchinson, W.J. Muller, N.G. Chopra, P.E. Scherer, R.G. Pestell, and M.P. Lisanti Caveolin-1 gene disruption promotes mammary tumorigenesis and dramatically enhances lung metastasis in vivo. Role of Cav-1 in cell invasiveness and matrix metalloproteinase (MMP-2/9) secretion J. Biol. Chem. 279 2004 51630 51646
    • (2004) J. Biol. Chem. , vol.279 , pp. 51630-51646
    • Williams, T.M.1    Medina, F.2    Badano, I.3    Hazan, R.B.4    Hutchinson, J.5    Muller, W.J.6    Chopra, N.G.7    Scherer, P.E.8    Pestell, R.G.9    Lisanti, M.P.10
  • 87
    • 0032831879 scopus 로고    scopus 로고
    • Caveolin-1, a metastasis-related gene that promotes cell survival in prostate cancer
    • T.C. Thompson, T.L. Timme, L. Li, and A. Goltsov Caveolin-1, a metastasis-related gene that promotes cell survival in prostate cancer Apoptosis 4 1999 233 237
    • (1999) Apoptosis , vol.4 , pp. 233-237
    • Thompson, T.C.1    Timme, T.L.2    Li, L.3    Goltsov, A.4
  • 88
    • 21644452110 scopus 로고    scopus 로고
    • Caveolin-1 promotes tumor progression in an autochthonous mouse model of prostate cancer: Genetic ablation of Cav-1 delays advanced prostate tumor development in TRAMP mice
    • (in press).
    • T.M. Williams, G.S. Hassan, J. Li, A.W. Cohen, F. Medina, P.G. Frank, R.G. Pestell, D. Di Vizio, M. Loda, M.P. Lisanti, Caveolin-1 promotes tumor progression in an autochthonous mouse model of prostate cancer: genetic ablation of Cav-1 delays advanced prostate tumor development in TRAMP mice, J. Biol. Chem. (in press).
    • J. Biol. Chem.
    • Williams, T.M.1    Hassan, G.S.2    Li, J.3    Cohen, A.W.4    Medina, F.5    Frank, P.G.6    Pestell, R.G.7    Di Vizio, D.8    Loda, M.9    Lisanti, M.P.10
  • 90
    • 0032546319 scopus 로고    scopus 로고
    • Tumor cell growth inhibition by caveolin re-expression in human breast cancer cells
    • S.W. Lee, C.L. Reimer, P. Oh, D.B. Campbell, and J.E. Schnitzer Tumor cell growth inhibition by caveolin re-expression in human breast cancer cells Oncogene 16 1998 1391 1397
    • (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
  • 92
    • 0034617296 scopus 로고    scopus 로고
    • Caveolin-1 inhibits epidermal growth factor-stimulated lamellipod extension and cell migration in metastatic mammary adenocarcinoma cells (MTLn3). Transformation suppressor effects of adenovirus-mediated gene delivery of caveolin-1
    • W. Zhang, B. Razani, Y. Altschuler, B. Bouzahzah, K.E. Mostov, R.G. Pestell, and M.P. Lisanti Caveolin-1 inhibits epidermal growth factor-stimulated lamellipod extension and cell migration in metastatic mammary adenocarcinoma cells (MTLn3). Transformation suppressor effects of adenovirus-mediated gene delivery of caveolin-1 J. Biol. Chem. 275 2000 20717 20725
    • (2000) J. Biol. Chem. , vol.275 , pp. 20717-20725
    • Zhang, W.1    Razani, B.2    Altschuler, Y.3    Bouzahzah, B.4    Mostov, K.E.5    Pestell, R.G.6    Lisanti, M.P.7
  • 93
    • 0035930547 scopus 로고    scopus 로고
    • Prolactin negatively regulates caveolin-1 gene expression in the mammary gland during lactation, via a Ras-dependent mechanism
    • D.S. Park, H. Lee, C. Riedel, J. Hulit, P.E. Scherer, R.G. Pestell, and M.P. Lisanti Prolactin negatively regulates caveolin-1 gene expression in the mammary gland during lactation, via a Ras-dependent mechanism J. Biol. Chem. 276 2001 48389 48397
    • (2001) J. Biol. Chem. , vol.276 , pp. 48389-48397
    • Park, D.S.1    Lee, H.2    Riedel, C.3    Hulit, J.4    Scherer, P.E.5    Pestell, R.G.6    Lisanti, M.P.7
  • 94
    • 0036798278 scopus 로고    scopus 로고
    • Caveolin-1-deficient mice show accelerated mammary gland development during pregnancy, premature lactation, and hyperactivation of the Jak-2/STAT5a signaling cascade
    • D.S. Park, H. Lee, P.G. Frank, B. Razani, A.V. Nguyen, A.F. Parlow, R.G. Russell, J. Hulit, R.G. Pestell, and M.P. Lisanti Caveolin-1-deficient mice show accelerated mammary gland development during pregnancy, premature lactation, and hyperactivation of the Jak-2/STAT5a signaling cascade Mol. Biol. Cell 13 2002 3416 3430
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3416-3430
    • Park, D.S.1    Lee, H.2    Frank, P.G.3    Razani, B.4    Nguyen, A.V.5    Parlow, A.F.6    Russell, R.G.7    Hulit, J.8    Pestell, R.G.9    Lisanti, M.P.10
  • 98
    • 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 mutant and rescues wild-type caveolin-3
    • F. Galbiati, D. Volonte, C. Minetti, D.B. Bregman, and M.P. Lisanti 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 mutant and rescues wild-type caveolin-3 J. Biol. Chem. 275 2000 37702 37711
    • (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
  • 99
    • 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
    • F. Galbiati, D. Volonte, C. Minetti, J.B. Chu, and M.P. Lisanti 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. 274 1999 25632 25641
    • (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
  • 100
    • 1342267006 scopus 로고    scopus 로고
    • Caveolinopathies: Mutations in caveolin-3 cause four distinct autosomal dominant muscle diseases
    • S.E. Woodman, F. Sotgia, F. Galbiati, C. Minetti, and M.P. Lisanti Caveolinopathies: mutations in caveolin-3 cause four distinct autosomal dominant muscle diseases Neurology 62 2004 538 543
    • (2004) Neurology , vol.62 , pp. 538-543
    • Woodman, S.E.1    Sotgia, F.2    Galbiati, F.3    Minetti, C.4    Lisanti, M.P.5
  • 101
    • 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
    • F. Sotgia, G. Bonuccelli, C. Minetti, S.E. Woodman, F. Capozza, R.G. Kemp, P.E. Scherer, and M.P. Lisanti 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. 163 2003 2619 2634
    • (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    Scherer, P.E.7    Lisanti, M.P.8
  • 104
    • 0032504045 scopus 로고    scopus 로고
    • Increased caveolin-3 levels in mdx mouse muscles
    • P.L. Vaghy, J. Fang, W. Wu, and L.P. Vaghy Increased caveolin-3 levels in mdx mouse muscles FEBS Lett. 431 1998 125 127
    • (1998) FEBS Lett. , vol.431 , pp. 125-127
    • Vaghy, P.L.1    Fang, J.2    Wu, W.3    Vaghy, L.P.4
  • 105
    • 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
    • K.S. Song, P.E. Scherer, Z. Tang, T. Okamoto, S. Li, M. Chafel, C. Chu, D.S. Kohtz, and M.P. Lisanti 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. 271 1996 15160 15165
    • (1996) J. Biol. Chem. , vol.271 , pp. 15160-15165
    • Song, K.S.1    Scherer, P.E.2    Tang, Z.3    Okamoto, T.4    Li, S.5    Chafel, M.6    Chu, C.7    Kohtz, D.S.8    Lisanti, M.P.9
  • 108
    • 1342268582 scopus 로고    scopus 로고
    • Overexpression of P104L mutant caveolin-3 in mice develops hypertrophic cardiomyopathy with enhanced contractility in association with increased endothelial nitric oxide synthase activity
    • Y. Ohsawa, H. Toko, M. Katsura, K. Morimoto, H. Yamada, Y. Ichikawa, T. Murakami, S. Ohkuma, I. Komuro, and Y. Sunada Overexpression of P104L mutant caveolin-3 in mice develops hypertrophic cardiomyopathy with enhanced contractility in association with increased endothelial nitric oxide synthase activity Hum. Mol. Genet. 13 2004 151 157
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 151-157
    • Ohsawa, Y.1    Toko, H.2    Katsura, M.3    Morimoto, K.4    Yamada, H.5    Ichikawa, Y.6    Murakami, T.7    Ohkuma, S.8    Komuro, I.9    Sunada, Y.10
  • 109
    • 0014312862 scopus 로고
    • Formation of elaborate networks of T-system tubules in cultured skeletal muscle with special reference to the T-system formation
    • H. Ishikawa Formation of elaborate networks of T-system tubules in cultured skeletal muscle with special reference to the T-system formation J. Cell Biol. 38 1968 51 66
    • (1968) J. Cell Biol. , vol.38 , pp. 51-66
    • Ishikawa, H.1
  • 110
    • 0031030664 scopus 로고    scopus 로고
    • Caveolin-3 associates with developing T-tubules during muscle differentiation
    • R.G. Parton, M. Way, N. Zorzi, and E. Stang Caveolin-3 associates with developing T-tubules during muscle differentiation J. Cell Biol. 136 1997 137 154
    • (1997) J. Cell Biol. , vol.136 , pp. 137-154
    • Parton, R.G.1    Way, M.2    Zorzi, N.3    Stang, E.4
  • 111
    • 0141429991 scopus 로고    scopus 로고
    • Modulation of myoblast fusion by caveolin-3 in dystrophic skeletal muscle cells: Implications for Duchenne muscular dystrophy and limb-girdle muscular dystrophy-1C
    • D. Volonte, A.J. Peoples, and F. Galbiati Modulation of myoblast fusion by caveolin-3 in dystrophic skeletal muscle cells: implications for Duchenne muscular dystrophy and limb-girdle muscular dystrophy-1C Mol. Biol. Cell 14 2003 4075 4088
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4075-4088
    • Volonte, D.1    Peoples, A.J.2    Galbiati, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.