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Volumn 1746, Issue 3, 2005, Pages 334-348

Structure of caveolae

Author keywords

[No Author keywords available]

Indexed keywords

CAVEOLIN 1; CELL MARKER; LIPID;

EID: 29144534595     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2005.08.008     Document Type: Review
Times cited : (225)

References (168)
  • 1
    • 0000855817 scopus 로고
    • Fine structure of blood capillaries
    • G.E. Palade Fine structure of blood capillaries J. Appl. Phys. 24 1953 1424
    • (1953) J. Appl. Phys. , vol.24 , pp. 1424
    • Palade, G.E.1
  • 2
    • 77049234363 scopus 로고
    • The fine structure of the gall bladder epithelium of the mouse
    • E. Yamada The fine structure of the gall bladder epithelium of the mouse J. Biophys. Biochem. Cytol. 1 1955 445 457
    • (1955) J. Biophys. Biochem. Cytol. , vol.1 , pp. 445-457
    • Yamada, E.1
  • 4
    • 0028926204 scopus 로고
    • Glycolipid-anchored proteins in neuroblastoma cells form detergent-resistant complexes without caveolin
    • A. Gorodinsky, and D.A. Harris Glycolipid-anchored proteins in neuroblastoma cells form detergent-resistant complexes without caveolin J. Cell Biol. 129 1995 619 627
    • (1995) J. Cell Biol. , vol.129 , pp. 619-627
    • Gorodinsky, A.1    Harris, D.A.2
  • 5
    • 0029818694 scopus 로고    scopus 로고
    • Detergent-resistant membrane microdomains from Caco-2 cells do not contain caveolin
    • C. Mirre, L. Monlauzeur, M. Garcia, M.H. Delgrossi, and A. Le Bivic Detergent-resistant membrane microdomains from Caco-2 cells do not contain caveolin Am. J. Physiol. 271 1996 C887 C894
    • (1996) Am. J. Physiol. , vol.271
    • Mirre, C.1    Monlauzeur, L.2    Garcia, M.3    Delgrossi, M.H.4    Le Bivic, A.5
  • 8
    • 4544375506 scopus 로고    scopus 로고
    • Caveolin-stabilized membrane domains as multifunctional transport and sorting devices in endocytic membrane traffic
    • L. Pelkmans, T. Burli, M. Zerial, and A. Helenius Caveolin-stabilized membrane domains as multifunctional transport and sorting devices in endocytic membrane traffic Cell 118 2004 767 780
    • (2004) Cell , vol.118 , pp. 767-780
    • Pelkmans, L.1    Burli, T.2    Zerial, M.3    Helenius, A.4
  • 9
    • 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
  • 10
    • 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
  • 11
    • 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
  • 12
    • 3042696866 scopus 로고    scopus 로고
    • Endothelial endocytic pathways: Gates for vascular drug delivery
    • S. Muro, M. Koval, and V. Muzykantov Endothelial endocytic pathways: gates for vascular drug delivery Curr. Vasc. Pharmacol. 2 2004 281 299
    • (2004) Curr. Vasc. Pharmacol. , vol.2 , pp. 281-299
    • Muro, S.1    Koval, M.2    Muzykantov, V.3
  • 14
    • 0036017680 scopus 로고    scopus 로고
    • Clathrin-dependent or not: Is it still the question?
    • L. Johannes, and C. Lamaze Clathrin-dependent or not: is it still the question? Traffic 3 2002 443 451
    • (2002) Traffic , vol.3 , pp. 443-451
    • Johannes, L.1    Lamaze, C.2
  • 15
    • 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
  • 17
    • 0036232040 scopus 로고    scopus 로고
    • GPI-anchored proteins are delivered to recycling endosomes via a distinct cdc42-regulated, clathrin-independent pinocytic pathway
    • S. Sabharanjak, P. Sharma, R.G. Parton, and S. Mayor GPI-anchored proteins are delivered to recycling endosomes via a distinct cdc42-regulated, clathrin-independent pinocytic pathway Dev. Cell 2 2002 411 423
    • (2002) Dev. Cell , vol.2 , pp. 411-423
    • Sabharanjak, S.1    Sharma, P.2    Parton, R.G.3    Mayor, S.4
  • 18
    • 0014283669 scopus 로고
    • Studies on blood capillaries: II. Transport of ferritin molecules across the wall of muscle capillaries
    • R.R. Bruns, and G.E. Palade Studies on blood capillaries: II. Transport of ferritin molecules across the wall of muscle capillaries J. Cell Biol. 37 1968 277 299
    • (1968) J. Cell Biol. , vol.37 , pp. 277-299
    • Bruns, R.R.1    Palade, G.E.2
  • 19
    • 0014289538 scopus 로고
    • Studies on blood capillaries. I. General organization of blood capillaries in muscle
    • R.R. Bruns, and G.E. Palade Studies on blood capillaries. I. General organization of blood capillaries in muscle J. Cell Biol. 37 1968 244 276
    • (1968) J. Cell Biol. , vol.37 , pp. 244-276
    • Bruns, R.R.1    Palade, G.E.2
  • 20
    • 0014301569 scopus 로고
    • Structural modulations of plasmalemmal vesicles
    • G.E. Palade, and R.R. Bruns Structural modulations of plasmalemmal vesicles J. Cell Biol. 37 1968 633 649
    • (1968) J. Cell Biol. , vol.37 , pp. 633-649
    • Palade, G.E.1    Bruns, R.R.2
  • 21
    • 0015952652 scopus 로고
    • Morphometric data on the endothelium of blood capillaries
    • M. Simionescu, N. Simionescu, and G.E. Palade Morphometric data on the endothelium of blood capillaries J. Cell Biol. 60 1974 128 152
    • (1974) J. Cell Biol. , vol.60 , pp. 128-152
    • Simionescu, M.1    Simionescu, N.2    Palade, G.E.3
  • 22
    • 0017327698 scopus 로고
    • Cell membrane structure of vascular smooth muscle of circle of Willis
    • E. Tani, S. Yamagata, and Y. Ito Cell membrane structure of vascular smooth muscle of circle of Willis Cell Tissue Res. 179 1977 131 142
    • (1977) Cell Tissue Res. , vol.179 , pp. 131-142
    • Tani, E.1    Yamagata, S.2    Ito, Y.3
  • 23
    • 0018122985 scopus 로고
    • Inpocketings of the cell membrane (caveolae) in the rat myocardium
    • G. Gabella Inpocketings of the cell membrane (caveolae) in the rat myocardium J. Ultrastruct. Res. 65 1978 135 147
    • (1978) J. Ultrastruct. Res. , vol.65 , pp. 135-147
    • Gabella, G.1
  • 24
    • 0017807025 scopus 로고
    • High resolution scanning electron microscopy of frog sartorius muscle
    • H. Sawada, H. Ishikawa, and E. Yamada High resolution scanning electron microscopy of frog sartorius muscle Tissue Cell 10 1978 179 190
    • (1978) Tissue Cell , vol.10 , pp. 179-190
    • Sawada, H.1    Ishikawa, H.2    Yamada, E.3
  • 25
    • 0018969929 scopus 로고
    • Structure of the freeze-fractured sarcolemma in the normal and anoxic rabbit myocardium
    • J.S. Frank, S. Beydler, M. Kreman, and E.E. Rau Structure of the freeze-fractured sarcolemma in the normal and anoxic rabbit myocardium Circ. Res. 47 1980 131 143
    • (1980) Circ. Res. , vol.47 , pp. 131-143
    • Frank, J.S.1    Beydler, S.2    Kreman, M.3    Rau, E.E.4
  • 26
    • 0019782120 scopus 로고
    • Plasma membrane cholesterol in myocardial muscle and capillary endothelial cells. Distribution of filipin-induced deformations in freeze-fracture
    • N.J. Severs Plasma membrane cholesterol in myocardial muscle and capillary endothelial cells. Distribution of filipin-induced deformations in freeze-fracture Eur J. Cell Biol. 25 1981 289 299
    • (1981) Eur J. Cell Biol. , vol.25 , pp. 289-299
    • Severs, N.J.1
  • 27
    • 0022364832 scopus 로고
    • Endothelial plasmalemmal vesicles have a characteristic striped bipolar surface structure
    • K.R. Peters, W.W. Carley, and G.E. Palade Endothelial plasmalemmal vesicles have a characteristic striped bipolar surface structure J. Cell Biol. 101 1985 2233 2238
    • (1985) J. Cell Biol. , vol.101 , pp. 2233-2238
    • Peters, K.R.1    Carley, W.W.2    Palade, G.E.3
  • 28
    • 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
  • 29
    • 0023938560 scopus 로고
    • Striped structures on the cytoplasmic surface membranes of the endothelial vesicles of the rat aorta revealed by quick-freeze, deep-etching replicas
    • T. Izumi, Y. Shibata, and T. Yamamoto Striped structures on the cytoplasmic surface membranes of the endothelial vesicles of the rat aorta revealed by quick-freeze, deep-etching replicas Anat. Rec. 220 1988 225 232
    • (1988) Anat. Rec. , vol.220 , pp. 225-232
    • Izumi, T.1    Shibata, Y.2    Yamamoto, T.3
  • 30
    • 0033756726 scopus 로고    scopus 로고
    • Isoforms of caveolin-1 and caveolar structure
    • T. Fujimoto, H. Kogo, R. Nomura, and T. Une Isoforms of caveolin-1 and caveolar structure J. Cell Sci. 113 Pt. 19 2000 3509 3517
    • (2000) J. Cell Sci. , vol.113 , Issue.19 PART , pp. 3509-3517
    • Fujimoto, T.1    Kogo, H.2    Nomura, R.3    Une, T.4
  • 32
    • 0036473056 scopus 로고    scopus 로고
    • Sites of Ca(2+) wave initiation move with caveolae to the trailing edge of migrating cells
    • M. Isshiki, J. Ando, K. Yamamoto, T. Fujita, Y. Ying, and R.G. Anderson Sites of Ca(2+) wave initiation move with caveolae to the trailing edge of migrating cells J. Cell Sci. 115 2002 475 484
    • (2002) J. Cell Sci. , vol.115 , pp. 475-484
    • Isshiki, M.1    Ando, J.2    Yamamoto, K.3    Fujita, T.4    Ying, Y.5    Anderson, R.G.6
  • 33
    • 0041969715 scopus 로고    scopus 로고
    • Differential caveolin-1 polarization in endothelial cells during migration in two and three dimensions
    • M.O. Parat, B. Anand-Apte, and P.L. Fox Differential caveolin-1 polarization in endothelial cells during migration in two and three dimensions Mol. Biol. Cell 14 2003 3156 3168
    • (2003) Mol. Biol. Cell , vol.14 , pp. 3156-3168
    • Parat, M.O.1    Anand-Apte, B.2    Fox, P.L.3
  • 34
    • 10044219518 scopus 로고    scopus 로고
    • A role for caveolae in cell migration
    • A. Navarro, B. Anand-Apte, and M.O. Parat A role for caveolae in cell migration FASEB. J. 18 2004 1801 1811
    • (2004) FASEB. J. , vol.18 , pp. 1801-1811
    • Navarro, A.1    Anand-Apte, B.2    Parat, M.O.3
  • 35
    • 0001254013 scopus 로고
    • Transport in quanta across endothelium in blood capillaries
    • G.E. Palade Transport in quanta across endothelium in blood capillaries Anat. Rec. 136 1960 254
    • (1960) Anat. Rec. , vol.136 , pp. 254
    • Palade, G.E.1
  • 36
    • 0001281220 scopus 로고
    • Blood capillaries of the heart and other organs
    • G.E. Palade Blood capillaries of the heart and other organs Circulation 24 1961 368 388
    • (1961) Circulation , vol.24 , pp. 368-388
    • Palade, G.E.1
  • 37
    • 0041110797 scopus 로고
    • Endothelial plasmalemmal vesicles as elements in a system of branching invaginations from the cell surface
    • M. Bundgaard, J. Frokjaer-Jensen, and C. Crone Endothelial plasmalemmal vesicles as elements in a system of branching invaginations from the cell surface Proc. Natl. Acad. Sci. U. S. A. 76 1979 6439 6442
    • (1979) Proc. Natl. Acad. Sci. U. S. A. , vol.76 , pp. 6439-6442
    • Bundgaard, M.1    Frokjaer-Jensen, J.2    Crone, C.3
  • 38
    • 0020530055 scopus 로고
    • The three-dimensional organization of plasmalemmal vesicular profiles in the endothelium of rat heart capillaries
    • M. Bundgaard, P. Hagman, and C. Crone The three-dimensional organization of plasmalemmal vesicular profiles in the endothelium of rat heart capillaries Microvasc. Res. 25 1983 358 368
    • (1983) Microvasc. Res. , vol.25 , pp. 358-368
    • Bundgaard, M.1    Hagman, P.2    Crone, C.3
  • 39
    • 0019274075 scopus 로고
    • Three-dimensional organization of plasmalemmal vesicles in endothelial cells. An analysis by serial sectioning of frog mesenteric capillaries
    • J. Frokjaer-Jensen Three-dimensional organization of plasmalemmal vesicles in endothelial cells. An analysis by serial sectioning of frog mesenteric capillaries J. Ultrastruct. Res. 73 1980 9 20
    • (1980) J. Ultrastruct. Res. , vol.73 , pp. 9-20
    • Frokjaer-Jensen, J.1
  • 40
    • 0021369116 scopus 로고
    • The plasmalemmal vesicular system in striated muscle capillaries and in pericytes
    • J. Frokjaer-Jensen The plasmalemmal vesicular system in striated muscle capillaries and in pericytes Tissue Cell 16 1984 31 42
    • (1984) Tissue Cell , vol.16 , pp. 31-42
    • Frokjaer-Jensen, J.1
  • 41
    • 0025996847 scopus 로고
    • The endothelial vesicle system in cryofixed frog mesenteric capillaries analysed by ultrathin serial sectioning
    • J. Frokjaer-Jensen The endothelial vesicle system in cryofixed frog mesenteric capillaries analysed by ultrathin serial sectioning J. Electron Microsc. Tech. 9 1991 291 304
    • (1991) J. Electron Microsc. Tech. , vol.9 , pp. 291-304
    • Frokjaer-Jensen, J.1
  • 42
    • 0024097293 scopus 로고
    • Three-dimensional organization of the plasmalemmal vesicular system in directly frozen capillaries of the rete mirabile in the swim bladder of the eel
    • J. Frokjaer-Jensen, R.C. Wagner, S.B. Andrews, P. Hagman, and T.S. Reese Three-dimensional organization of the plasmalemmal vesicular system in directly frozen capillaries of the rete mirabile in the swim bladder of the eel Cell Tissue Res. 254 1988 17 24
    • (1988) Cell Tissue Res. , vol.254 , pp. 17-24
    • Frokjaer-Jensen, J.1    Wagner, R.C.2    Andrews, S.B.3    Hagman, P.4    Reese, T.S.5
  • 43
    • 0031980371 scopus 로고    scopus 로고
    • Expression of caveolin-1 and polarized formation of invaginated caveolae in Caco-2 and MDCK II cells
    • U. Vogel, K. Sandvig, and B. van Deurs Expression of caveolin-1 and polarized formation of invaginated caveolae in Caco-2 and MDCK II cells J. Cell Sci. 111 Pt. 6 1998 825 832
    • (1998) J. Cell Sci. , vol.111 , Issue.6 PART , pp. 825-832
    • Vogel, U.1    Sandvig, K.2    Van Deurs, B.3
  • 44
    • 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
    • (1968) J. Cell Biol. , vol.38 , pp. 51
    • Ishikawa, H.1
  • 45
    • 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
  • 47
    • 0016640970 scopus 로고
    • Permeability of muscle capillaries to small heme-peptides. Evidence for the existence of patent transendothelial channels
    • N. Simionescu, M. Siminoescu, and G.E. Palade Permeability of muscle capillaries to small heme-peptides. Evidence for the existence of patent transendothelial channels J. Cell Biol. 64 1975 586 607
    • (1975) J. Cell Biol. , vol.64 , pp. 586-607
    • Simionescu, N.1    Siminoescu, M.2    Palade, G.E.3
  • 48
    • 0036605843 scopus 로고    scopus 로고
    • Ultrastructural studies define soluble macromolecular, particulate, and cellular transendothelial cell pathways in venules, lymphatic vessels, and tumor-associated microvessels in man and animals
    • D. Feng, J.A. Nagy, H.F. Dvorak, and A.M. Dvorak Ultrastructural studies define soluble macromolecular, particulate, and cellular transendothelial cell pathways in venules, lymphatic vessels, and tumor-associated microvessels in man and animals Microsc. Res. Tech. 57 2002 289 326
    • (2002) Microsc. Res. Tech. , vol.57 , pp. 289-326
    • Feng, D.1    Nagy, J.A.2    Dvorak, H.F.3    Dvorak, A.M.4
  • 49
    • 0003665179 scopus 로고
    • Adipose tissue. Morphological changes associated with lipid mobilization
    • J.R. Williamson Adipose tissue. Morphological changes associated with lipid mobilization J. Cell Biol. 20 1964 57 74
    • (1964) J. Cell Biol. , vol.20 , pp. 57-74
    • Williamson, J.R.1
  • 51
    • 0032710815 scopus 로고    scopus 로고
    • Tubular invaginations with caveolae and coated pits in the sinus endothelial cells of the rat spleen
    • K. Uehara, and M. Miyoshi Tubular invaginations with caveolae and coated pits in the sinus endothelial cells of the rat spleen Histochem. Cell Biol. 112 1999 351 358
    • (1999) Histochem. Cell Biol. , vol.112 , pp. 351-358
    • Uehara, K.1    Miyoshi, M.2
  • 52
    • 0028057494 scopus 로고
    • Ultrastructural localization of gangliosides; GM1 is concentrated in caveolae
    • R.G. Parton Ultrastructural localization of gangliosides; GM1 is concentrated in caveolae J. Histochem. Cytochem. 42 1994 155 166
    • (1994) J. Histochem. Cytochem. , vol.42 , pp. 155-166
    • Parton, R.G.1
  • 53
    • 0037135573 scopus 로고    scopus 로고
    • Caveolin-associated filamentous actin (Cav-actin) defines a novel F-actin structure in adipocytes
    • M. Kanzaki, and J.E. Pessin Caveolin-associated filamentous actin (Cav-actin) defines a novel F-actin structure in adipocytes J. Biol. Chem. 277 2002 25867 25869
    • (2002) J. Biol. Chem. , vol.277 , pp. 25867-25869
    • Kanzaki, M.1    Pessin, J.E.2
  • 54
    • 0037195870 scopus 로고    scopus 로고
    • Characterization of a distinct plasma membrane macrodomain in differentiated adipocytes
    • R.G. Parton, J.C. Molero, M. Floetenmeyer, K.M. Green, and D.E. James Characterization of a distinct plasma membrane macrodomain in differentiated adipocytes J. Biol. Chem. 277 2002 46769 46778
    • (2002) J. Biol. Chem. , vol.277 , pp. 46769-46778
    • Parton, R.G.1    Molero, J.C.2    Floetenmeyer, M.3    Green, K.M.4    James, D.E.5
  • 55
    • 0344443664 scopus 로고    scopus 로고
    • Intersectin regulates fission and internalization of caveolae in endothelial cells
    • S.A. Predescu, D.N. Predescu, B.K. Timblin, R.V. Stan, and A.B. Malik Intersectin regulates fission and internalization of caveolae in endothelial cells Mol. Biol. Cell 14 2003 4997 5010
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4997-5010
    • Predescu, S.A.1    Predescu, D.N.2    Timblin, B.K.3    Stan, R.V.4    Malik, A.B.5
  • 57
    • 0020525293 scopus 로고
    • Morphology of rapidly frozen aortic endothelial cells. Glutaraldehyde fixation increases the number of caveolae
    • P.G. McGuire, and T.A. Twietmeyer Morphology of rapidly frozen aortic endothelial cells. Glutaraldehyde fixation increases the number of caveolae Circ. Res. 53 1983 424 429
    • (1983) Circ. Res. , vol.53 , pp. 424-429
    • McGuire, P.G.1    Twietmeyer, T.A.2
  • 58
    • 0023179230 scopus 로고
    • Endothelial vesicular system in rapid-frozen muscle capillaries revealed by serial sectioning and deep etching
    • Y. Noguchi, Y. Shibata, and T. Yamamoto Endothelial vesicular system in rapid-frozen muscle capillaries revealed by serial sectioning and deep etching Anat. Rec. 217 1987 355 360
    • (1987) Anat. Rec. , vol.217 , pp. 355-360
    • Noguchi, Y.1    Shibata, Y.2    Yamamoto, T.3
  • 59
    • 0022836273 scopus 로고
    • Rapidly-frozen, cultured, human endothelial cells: An ultrastructural and morphometric comparison between freshly-frozen and glutaraldehyde prefixed cells
    • M.R. Wood, R.C. Wagner, S.B. Andrews, D.A. Greener, and S.K. Williams Rapidly-frozen, cultured, human endothelial cells: an ultrastructural and morphometric comparison between freshly-frozen and glutaraldehyde prefixed cells Microcirc. Endothel. Lymphat. 3 1986 323 358
    • (1986) Microcirc. Endothel. Lymphat. , vol.3 , pp. 323-358
    • Wood, M.R.1    Wagner, R.C.2    Andrews, S.B.3    Greener, D.A.4    Williams, S.K.5
  • 60
    • 0141631549 scopus 로고
    • Observations on the morphology of adipose tissue: I. the fine structure of cells from fasted and diabetic rats
    • H. Sheldon, C.H. Hollenberg, and A.I. Winegrad Observations on the morphology of adipose tissue: I. The fine structure of cells from fasted and diabetic rats Diabetes 11 1962 378 387
    • (1962) Diabetes , vol.11 , pp. 378-387
    • Sheldon, H.1    Hollenberg, C.H.2    Winegrad, A.I.3
  • 62
    • 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
  • 63
    • 0015184456 scopus 로고
    • Sarcoplasmic reticulum and the temperature-dependent contraction of smooth muscle in calcium-free solutions
    • A.P. Somlyo, C.E. Devine, A.V. Somlyo, and S.R. North Sarcoplasmic reticulum and the temperature-dependent contraction of smooth muscle in calcium-free solutions J. Cell Biol. 51 1971 722 741
    • (1971) J. Cell Biol. , vol.51 , pp. 722-741
    • Somlyo, A.P.1    Devine, C.E.2    Somlyo, A.V.3    North, S.R.4
  • 64
    • 0024521599 scopus 로고
    • The cytoplasmic surface structures of uncoated vesicles in various tissues of rat as revealed by quick-freeze, deep-etching replicas
    • T. Izumi, Y. Shibata, and T. Yamamoto The cytoplasmic surface structures of uncoated vesicles in various tissues of rat as revealed by quick-freeze, deep-etching replicas J. Electron. Microsc. (Tokyo) 38 1989 47 53
    • (1989) J. Electron. Microsc. (Tokyo) , vol.38 , pp. 47-53
    • Izumi, T.1    Shibata, Y.2    Yamamoto, T.3
  • 65
    • 0025946167 scopus 로고
    • Quick-freeze, deep-etch studies of endothelial components, with special reference to cytoskeletons and vesicle structures
    • T. Izumi, Y. Shibata, and T. Yamamoto Quick-freeze, deep-etch studies of endothelial components, with special reference to cytoskeletons and vesicle structures J. Electron Microsc. Tech. 19 1991 316 326
    • (1991) J. Electron Microsc. Tech. , vol.19 , pp. 316-326
    • Izumi, T.1    Shibata, Y.2    Yamamoto, T.3
  • 67
    • 0024047352 scopus 로고
    • Caveolae: Static inpocketings of the plasma membrane, dynamic vesicles or plain artifact?
    • N.J. Severs Caveolae: static inpocketings of the plasma membrane, dynamic vesicles or plain artifact? J. Cell Sci. 90 1988 341 348
    • (1988) J. Cell Sci. , vol.90 , pp. 341-348
    • Severs, N.J.1
  • 68
    • 0242529783 scopus 로고    scopus 로고
    • Membrane structure of caveolae and isolated caveolin-rich vesicles
    • M. Westermann, H. Leutbecher, and H.W. Meyer Membrane structure of caveolae and isolated caveolin-rich vesicles Histochem. Cell Biol. 111 1999 71 81
    • (1999) Histochem. Cell Biol. , vol.111 , pp. 71-81
    • Westermann, M.1    Leutbecher, H.2    Meyer, H.W.3
  • 69
    • 23744484015 scopus 로고    scopus 로고
    • Belt-like localisation of caveolin in deep caveolae and its re-distribution after cholesterol depletion
    • M. Westermann, F. Steiniger, and W. Richter Belt-like localisation of caveolin in deep caveolae and its re-distribution after cholesterol depletion Histochem. Cell Biol. 123 6 2005 Jun. 613 620
    • (2005) Histochem. Cell Biol. , vol.123 , Issue.6 , pp. 613-620
    • Westermann, M.1    Steiniger, F.2    Richter, W.3
  • 71
    • 0030561979 scopus 로고    scopus 로고
    • M-caveolin, a muscle-specific caveolin-related protein [corrected and republished in FEBS. Lett. 1996 Jan 2;378(1):108-12]
    • M. Way, and R.G. Parton M-caveolin, a muscle-specific caveolin-related protein [corrected and republished in FEBS. Lett. 1996 Jan 2;378(1):108-12] FEBS Lett. 376 1995 Jan. 108 112
    • (1995) FEBS Lett. , vol.376 , pp. 108-112
    • Way, M.1    Parton, R.G.2
  • 72
    • 0028177422 scopus 로고
    • VIP21-Caveolin, a protein of the trans-Golgi network and caveolae
    • T.V. Kurzchalia, P. Dupree, and S. Monier VIP21-Caveolin, a protein of the trans-Golgi network and caveolae FEBS Lett. 346 1994 88 91
    • (1994) FEBS Lett. , vol.346 , pp. 88-91
    • Kurzchalia, T.V.1    Dupree, P.2    Monier, S.3
  • 75
    • 0030561979 scopus 로고    scopus 로고
    • M-caveolin, a muscle-specific caveolin-related protein
    • M. Way, and R.G. Parton M-caveolin, a muscle-specific caveolin-related protein FEBS Lett. 376 1995 108 112
    • (1995) FEBS Lett. , vol.376 , pp. 108-112
    • Way, M.1    Parton, R.G.2
  • 76
    • 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
    • J.R. Glenney Jr., and D. Soppet 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. U. S. A. 89 1992 10517 10521
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 10517-10521
    • Glenney Jr., J.R.1    Soppet, D.2
  • 77
    • 0026499749 scopus 로고
    • The sequence of human caveolin reveals identity with VIP21, a component of transport vesicles
    • J.R. Glenney Jr. The sequence of human caveolin reveals identity with VIP21, a component of transport vesicles FEBS Lett. 314 1992 45 48
    • (1992) FEBS Lett. , vol.314 , pp. 45-48
    • Glenney Jr., J.R.1
  • 78
    • 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
  • 79
    • 2942595764 scopus 로고    scopus 로고
    • Cell type-specific occurrence of caveolin-1alpha and -1beta in the lung caused by expression of distinct mRNAs
    • H. Kogo, T. Aiba, and T. Fujimoto Cell type-specific occurrence of caveolin-1alpha and -1beta in the lung caused by expression of distinct mRNAs J. Biol. Chem. 279 2004 25574 25581
    • (2004) J. Biol. Chem. , vol.279 , pp. 25574-25581
    • Kogo, H.1    Aiba, T.2    Fujimoto, T.3
  • 80
    • 0033976055 scopus 로고    scopus 로고
    • Caveolin-1 isoforms are encoded by distinct mRNAs. Identification of mouse caveolin-1 mRNA variants caused by alternative transcription initiation and splicing
    • H. Kogo, and T. Fujimoto Caveolin-1 isoforms are encoded by distinct mRNAs. Identification Of mouse caveolin-1 mRNA variants caused by alternative transcription initiation and splicing FEBS Lett. 465 2000 119 123
    • (2000) FEBS Lett. , vol.465 , pp. 119-123
    • Kogo, H.1    Fujimoto, T.2
  • 81
    • 0028889719 scopus 로고
    • Hormonal regulation of caveolae internalization
    • E.J. Smart, Y.S. Ying, and R.G. Anderson Hormonal regulation of caveolae internalization J. Cell Biol. 131 1995 929 938
    • (1995) J. Cell Biol. , vol.131 , pp. 929-938
    • Smart, E.J.1    Ying, Y.S.2    Anderson, R.G.3
  • 83
    • 0033429208 scopus 로고    scopus 로고
    • Calcium signal transduction from caveolae
    • M. Isshiki, and R.G. Anderson Calcium signal transduction from caveolae Cell Calcium 26 1999 201 208
    • (1999) Cell Calcium , vol.26 , pp. 201-208
    • Isshiki, M.1    Anderson, R.G.2
  • 84
    • 0030067984 scopus 로고    scopus 로고
    • Phosphorylation of caveolin by src tyrosine kinases. the alpha-isoform of caveolin is selectively phosphorylated by v-Src in vivo
    • S. Li, R. Seitz, and M.P. Lisanti Phosphorylation of caveolin by src tyrosine kinases. The alpha-isoform of caveolin is selectively phosphorylated by v-Src in vivo J. Biol. Chem. 271 1996 3863 3868
    • (1996) J. Biol. Chem. , vol.271 , pp. 3863-3868
    • Li, S.1    Seitz, R.2    Lisanti, M.P.3
  • 85
    • 0030798998 scopus 로고    scopus 로고
    • Gp60 activation mediates albumin transcytosis in endothelial cells by tyrosine kinase-dependent pathway
    • C. Tiruppathi, W. Song, M. Bergenfeldt, P. Sass, and A.B. Malik Gp60 activation mediates albumin transcytosis in endothelial cells by tyrosine kinase-dependent pathway J. Biol. Chem. 272 1997 25968 25975
    • (1997) J. Biol. Chem. , vol.272 , pp. 25968-25975
    • Tiruppathi, C.1    Song, W.2    Bergenfeldt, M.3    Sass, P.4    Malik, A.B.5
  • 86
  • 87
    • 0032911042 scopus 로고    scopus 로고
    • Tyrosine-phosphorylated caveolin-1: Immunolocalization and molecular characterization
    • R. Nomura, and T. Fujimoto Tyrosine-phosphorylated caveolin-1: immunolocalization and molecular characterization Mol. Biol. Cell 10 1999 975 986
    • (1999) Mol. Biol. Cell , vol.10 , pp. 975-986
    • Nomura, R.1    Fujimoto, T.2
  • 88
    • 0033573098 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of caveolin-1 in the endothelium
    • T. Aoki, R. Nomura, and T. Fujimoto Tyrosine phosphorylation of caveolin-1 in the endothelium Exp. Cell Res. 253 1999 629 636
    • (1999) Exp. Cell Res. , vol.253 , pp. 629-636
    • Aoki, T.1    Nomura, R.2    Fujimoto, T.3
  • 89
    • 10644229956 scopus 로고    scopus 로고
    • Src-mediated tyrosine phosphorylation of caveolin-1 induces its association with membrane type 1 matrix metalloproteinase
    • L. Labrecque, C. Nyalendo, S. Langlois, Y. Durocher, C. Roghi, G. Murphy, D. Gingras, and R. Beliveau Src-mediated tyrosine phosphorylation of caveolin-1 induces its association with membrane type 1 matrix metalloproteinase J. Biol. Chem. 279 2004 52132 52140
    • (2004) J. Biol. Chem. , vol.279 , pp. 52132-52140
    • Labrecque, L.1    Nyalendo, C.2    Langlois, S.3    Durocher, Y.4    Roghi, C.5    Murphy, G.6    Gingras, D.7    Beliveau, R.8
  • 90
    • 0037119387 scopus 로고    scopus 로고
    • The insulin receptor catalyzes the tyrosine phosphorylation of caveolin-1
    • A. Kimura, S. Mora, S. Shigematsu, J.E. Pessin, and A.R. Saltiel The insulin receptor catalyzes the tyrosine phosphorylation of caveolin-1 J. Biol. Chem. 277 2002 30153 30158
    • (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
  • 91
    • 0036033549 scopus 로고    scopus 로고
    • Caveolin-1 phosphorylation in human squamous and epidermoid carcinoma cells: Dependence on ErbB1 expression and Src activation
    • Y.N. Kim, P. Dam, and P.J. Bertics Caveolin-1 phosphorylation in human squamous and epidermoid carcinoma cells: dependence on ErbB1 expression and Src activation Exp. Cell Res. 280 2002 134 147
    • (2002) Exp. Cell Res. , vol.280 , pp. 134-147
    • Kim, Y.N.1    Dam, P.2    Bertics, P.J.3
  • 92
    • 0037088672 scopus 로고    scopus 로고
    • A phosphotyrosine-dependent protein interaction screen reveals a role for phosphorylation of caveolin-1 on tyrosine 14: Recruitment of C-terminal Src kinase
    • H. Cao, W.E. Courchesne, and C.C. Mastick A phosphotyrosine-dependent protein interaction screen reveals a role for phosphorylation of caveolin-1 on tyrosine 14: recruitment of C-terminal Src kinase J. Biol. Chem. 277 2002 8771 8774
    • (2002) J. Biol. Chem. , vol.277 , pp. 8771-8774
    • Cao, H.1    Courchesne, W.E.2    Mastick, C.C.3
  • 93
    • 0035896560 scopus 로고    scopus 로고
    • Cellular stress induces the tyrosine phosphorylation of caveolin-1 (Tyr(14)) via activation of p38 mitogen-activated protein kinase and c-Src kinase. Evidence for caveolae, the actin cytoskeleton, and focal adhesions as mechanical sensors of osmotic stress
    • D. Volonte, F. Galbiati, R.G. Pestell, and M.P. Lisanti Cellular stress induces the tyrosine phosphorylation of caveolin-1 (Tyr(14)) via activation of p38 mitogen-activated protein kinase and c-Src kinase. Evidence for caveolae, the actin cytoskeleton, and focal adhesions as mechanical sensors of osmotic stress J. Biol. Chem. 276 2001 8094 8103
    • (2001) J. Biol. Chem. , vol.276 , pp. 8094-8103
    • Volonte, D.1    Galbiati, F.2    Pestell, R.G.3    Lisanti, M.P.4
  • 94
    • 0035378664 scopus 로고    scopus 로고
    • Tyrosine-phosphorylated caveolin is a physiological substrate of the low M(r) protein-tyrosine phosphatase
    • A. Caselli, M.L. Taddei, G. Manao, G. Camici, and G. Ramponi Tyrosine-phosphorylated caveolin is a physiological substrate of the low M(r) protein-tyrosine phosphatase J. Biol. Chem. 276 2001 18849 18854
    • (2001) J. Biol. Chem. , vol.276 , pp. 18849-18854
    • Caselli, A.1    Taddei, M.L.2    Manao, G.3    Camici, G.4    Ramponi, G.5
  • 95
    • 0028920139 scopus 로고
    • Caveolin is palmitoylated on multiple cysteine residues. Palmitoylation is not necessary for localization of caveolin to caveolae
    • D.J. Dietzen, W.R. Hastings, and D.M. Lublin Caveolin is palmitoylated on multiple cysteine residues. Palmitoylation is not necessary for localization of caveolin to caveolae J. Biol. Chem. 270 1995 6838 6842
    • (1995) J. Biol. Chem. , vol.270 , pp. 6838-6842
    • Dietzen, D.J.1    Hastings, W.R.2    Lublin, D.M.3
  • 96
    • 0035844253 scopus 로고    scopus 로고
    • Palmitoylation of caveolin-1 in endothelial cells is post-translational but irreversible
    • M.O. Parat, and P.L. Fox Palmitoylation of caveolin-1 in endothelial cells is post-translational but irreversible J. Biol. Chem. 276 2001 15776 15782
    • (2001) J. Biol. Chem. , vol.276 , pp. 15776-15782
    • Parat, M.O.1    Fox, P.L.2
  • 97
    • 0032497835 scopus 로고    scopus 로고
    • Signalling functions of protein palmitoylation
    • J.T. Dunphy, and M.E. Linder Signalling functions of protein palmitoylation Biochim. Biophys. Acta 1436 1998 245 261
    • (1998) Biochim. Biophys. Acta , vol.1436 , pp. 245-261
    • Dunphy, J.T.1    Linder, M.E.2
  • 98
    • 7444255626 scopus 로고    scopus 로고
    • Membrane targeting of lipid modified signal transduction proteins
    • M.D. Resh Membrane targeting of lipid modified signal transduction proteins Subcell. Biochem. 37 2004 217 232
    • (2004) Subcell. Biochem. , vol.37 , pp. 217-232
    • Resh, M.D.1
  • 99
    • 0030591426 scopus 로고    scopus 로고
    • Oligomerization of VIP21-caveolin in vitro is stabilized by long chain fatty acylation or cholesterol
    • S. Monier, D.J. Dietzen, W.R. Hastings, D.M. Lublin, and T.V. Kurzchalia Oligomerization of VIP21-caveolin in vitro is stabilized by long chain fatty acylation or cholesterol FEBS Lett. 388 1996 143 149
    • (1996) FEBS Lett. , vol.388 , pp. 143-149
    • Monier, S.1    Dietzen, D.J.2    Hastings, W.R.3    Lublin, D.M.4    Kurzchalia, T.V.5
  • 101
    • 0035830831 scopus 로고    scopus 로고
    • Caveolin-1 binding to endoplasmic reticulum membranes and entry into the regulated secretory pathway are regulated by serine phosphorylation. Protein sorting at the level of the endoplasmic reticulum
    • A. Schlegel, P. Arvan, and M.P. Lisanti Caveolin-1 binding to endoplasmic reticulum membranes and entry into the regulated secretory pathway are regulated by serine phosphorylation. Protein sorting at the level of the endoplasmic reticulum J. Biol. Chem. 276 2001 4398 4408
    • (2001) J. Biol. Chem. , vol.276 , pp. 4398-4408
    • Schlegel, A.1    Arvan, P.2    Lisanti, M.P.3
  • 102
    • 0033612537 scopus 로고    scopus 로고
    • Molecular characterization of caveolin association with the Golgi complex: Identification of a cis-Golgi targeting domain in the caveolin molecule
    • R. Luetterforst, E. Stang, N. Zorzi, A. Carozzi, M. Way, and R.G. Parton Molecular characterization of caveolin association with the Golgi complex: identification of a cis-Golgi targeting domain in the caveolin molecule J. Cell Biol. 145 1999 1443 1459
    • (1999) J. Cell Biol. , vol.145 , pp. 1443-1459
    • Luetterforst, R.1    Stang, E.2    Zorzi, N.3    Carozzi, A.4    Way, M.5    Parton, R.G.6
  • 103
    • 4644286390 scopus 로고    scopus 로고
    • Conformational defects slow Golgi exit, block oligomerization, and reduce raft affinity of caveolin-1 mutant proteins
    • X. Ren, A.G. Ostermeyer, L.T. Ramcharan, Y. Zeng, D.M. Lublin, and D.A. Brown Conformational defects slow Golgi exit, block oligomerization, and reduce raft affinity of caveolin-1 mutant proteins Mol. Biol. Cell 15 2004 4556 4567
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4556-4567
    • Ren, X.1    Ostermeyer, A.G.2    Ramcharan, L.T.3    Zeng, Y.4    Lublin, D.M.5    Brown, D.A.6
  • 104
    • 0036578575 scopus 로고    scopus 로고
    • Identification of a splice variant of mouse caveolin-2 mRNA encoding an isoform lacking the C-terminal domain
    • H. Kogo, K. Ishiguro, S. Kuwaki, and T. Fujimoto Identification of a splice variant of mouse caveolin-2 mRNA encoding an isoform lacking the C-terminal domain Arch. Biochem. Biophys. 401 2002 108 114
    • (2002) Arch. Biochem. Biophys. , vol.401 , pp. 108-114
    • Kogo, H.1    Ishiguro, K.2    Kuwaki, S.3    Fujimoto, T.4
  • 105
    • 0038313015 scopus 로고    scopus 로고
    • The phosphorylation of caveolin-2 on serines 23 and 36 modulates caveolin-1-dependent caveolae formation
    • G. Sowa, M. Pypaert, D. Fulton, and W.C. Sessa The phosphorylation of caveolin-2 on serines 23 and 36 modulates caveolin-1-dependent caveolae formation Proc. Natl. Acad. Sci. U. S. A. 100 2003 6511 6516
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 6511-6516
    • Sowa, G.1    Pypaert, M.2    Fulton, D.3    Sessa, W.C.4
  • 106
    • 7244258688 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of caveolin-2 at residue 27: Differences in the spatial and temporal behavior of phospho-Cav-2 (pY19 and pY27)
    • X.B. Wang, H. Lee, F. Capozza, S. Marmon, F. Sotgia, J.W. Brooks, R. Campos-Gonzalez, and M.P. Lisanti Tyrosine phosphorylation of caveolin-2 at residue 27: differences in the spatial and temporal behavior of phospho-Cav-2 (pY19 and pY27) Biochemistry 43 2004 13694 13706
    • (2004) Biochemistry , vol.43 , pp. 13694-13706
    • Wang, X.B.1    Lee, H.2    Capozza, F.3    Marmon, S.4    Sotgia, F.5    Brooks, J.W.6    Campos-Gonzalez, R.7    Lisanti, M.P.8
  • 108
    • 0030561979 scopus 로고    scopus 로고
    • M-caveolin, a muscle-specific caveolin-related protein
    • M. Way, and R.G. Parton M-caveolin, a muscle-specific caveolin-related protein FEBS Lett. 378 1996 108 112
    • (1996) FEBS Lett. , vol.378 , pp. 108-112
    • Way, M.1    Parton, R.G.2
  • 110
    • 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
  • 111
    • 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
  • 113
    • 0036208765 scopus 로고    scopus 로고
    • Localization of caveolin-3 in the sinus endothelial cells of the rat spleen
    • K. Uehara, and M. Miyoshi Localization of caveolin-3 in the sinus endothelial cells of the rat spleen Cell Tissue Res. 307 2002 329 336
    • (2002) Cell Tissue Res. , vol.307 , pp. 329-336
    • Uehara, K.1    Miyoshi, M.2
  • 119
    • 2942685631 scopus 로고    scopus 로고
    • Caveolae and caveolins in the cardiovascular system
    • J.P. Gratton, P. Bernatchez, and W.C. Sessa Caveolae and caveolins in the cardiovascular system Circ. Res. 94 2004 1408 1417
    • (2004) Circ. Res. , vol.94 , pp. 1408-1417
    • Gratton, J.P.1    Bernatchez, P.2    Sessa, W.C.3
  • 121
    • 13044275816 scopus 로고    scopus 로고
    • Caveolin is necessary and sufficient for caveolae formation
    • K.N. Chung, P.C. Elwood, and J.E. Heuser Caveolin is necessary and sufficient for caveolae formation Mol. Biol. Cell 7 1996 276a
    • (1996) Mol. Biol. Cell , vol.7
    • Chung, K.N.1    Elwood, P.C.2    Heuser, J.E.3
  • 124
    • 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
  • 128
    • 0028998554 scopus 로고
    • VIP21-caveolin, a membrane protein constituent of the caveolar coat, oligomerizes in vivo and in vitro
    • S. Monier, R.G. Parton, F. Vogel, J. Behlke, A. Henske, and T.V. Kurzchalia VIP21-caveolin, a membrane protein constituent of the caveolar coat, oligomerizes in vivo and in vitro Mol. Biol. Cell 6 1995 911 927
    • (1995) Mol. Biol. Cell , vol.6 , pp. 911-927
    • Monier, S.1    Parton, R.G.2    Vogel, F.3    Behlke, J.4    Henske, A.5    Kurzchalia, T.V.6
  • 129
    • 0027414646 scopus 로고
    • Caveolae and sorting in the trans-Golgi network of epithelial cells
    • P. Dupree, R.G. Parton, G. Raposo, T.V. Kurzchalia, and K. Simons Caveolae and sorting in the trans-Golgi network of epithelial cells EMBO J. 12 1993 1597 1605
    • (1993) EMBO J. , vol.12 , pp. 1597-1605
    • Dupree, P.1    Parton, R.G.2    Raposo, G.3    Kurzchalia, T.V.4    Simons, K.5
  • 130
    • 0029757511 scopus 로고    scopus 로고
    • GPI-anchored proteins, glycosphingolipids, and sphingomyelin are sequestered to caveolae only after crosslinking
    • T. Fujimoto GPI-anchored proteins, glycosphingolipids, and sphingomyelin are sequestered to caveolae only after crosslinking J. Histochem. Cytochem. 44 1996 929 941
    • (1996) J. Histochem. Cytochem. , vol.44 , pp. 929-941
    • Fujimoto, T.1
  • 131
    • 0026064541 scopus 로고
    • Cryosputtering-a combined freeze-drying and sputtering method for high-resolution electron microscopy
    • M. Lindroth, B.A. Fredriksson, and P.B. Bell Cryosputtering-a combined freeze-drying and sputtering method for high-resolution electron microscopy J. Microsc. 161 Pt. 2 1991 229 239
    • (1991) J. Microsc. , vol.161 , Issue.2 PART , pp. 229-239
    • Lindroth, M.1    Fredriksson, B.A.2    Bell, P.B.3
  • 132
    • 0024270714 scopus 로고
    • Comparison of the effects of critical point-drying and freeze-drying on cytoskeletons and microtubules
    • M. Lindroth, P.B. Bell Jr., and B.A. Fredriksson Comparison of the effects of critical point-drying and freeze-drying on cytoskeletons and microtubules J. Microsc. 151 Pt. 2 1988 103 114
    • (1988) J. Microsc. , vol.151 , Issue.2 PART , pp. 103-114
    • Lindroth, M.1    Bell Jr., P.B.2    Fredriksson, B.A.3
  • 133
    • 0026703756 scopus 로고
    • Preservation and visualization of molecular structure in detergent-extracted whole mounts of cultured cells
    • M. Lindroth, P.B. Bell Jr., B.A. Fredriksson, and X.D. Liu Preservation and visualization of molecular structure in detergent-extracted whole mounts of cultured cells Microsc. Res. Tech. 22 1992 130 150
    • (1992) Microsc. Res. Tech. , vol.22 , pp. 130-150
    • Lindroth, M.1    Bell Jr., P.B.2    Fredriksson, B.A.3    Liu, X.D.4
  • 135
    • 0037036135 scopus 로고    scopus 로고
    • A role for lipid shells in targeting proteins to caveolae, rafts, and other lipid domains
    • R.G. Anderson, and K. Jacobson A role for lipid shells in targeting proteins to caveolae, rafts, and other lipid domains Science 296 2002 1821 1825
    • (2002) Science , vol.296 , pp. 1821-1825
    • Anderson, R.G.1    Jacobson, K.2
  • 136
    • 0021063738 scopus 로고
    • Rings of membrane sterols surround the openings of vesicles and fenestrae, in capillary endothelium
    • N. Simionescu, F. Lupu, and M. Simionescu Rings of membrane sterols surround the openings of vesicles and fenestrae, in capillary endothelium J. Cell Biol. 97 1983 1592 1600
    • (1983) J. Cell Biol. , vol.97 , pp. 1592-1600
    • Simionescu, N.1    Lupu, F.2    Simionescu, M.3
  • 137
    • 0030865913 scopus 로고    scopus 로고
    • Crosslinked plasmalemmal cholesterol is sequestered to caveolae: Analysis with a new cytochemical probe
    • T. Fujimoto, M. Hayashi, M. Iwamoto, and Y. Ohno-Iwashita Crosslinked plasmalemmal cholesterol is sequestered to caveolae: analysis with a new cytochemical probe J. Histochem. Cytochem. 45 1997 1197 1205
    • (1997) J. Histochem. Cytochem. , vol.45 , pp. 1197-1205
    • Fujimoto, T.1    Hayashi, M.2    Iwamoto, M.3    Ohno-Iwashita, Y.4
  • 139
    • 0030027901 scopus 로고    scopus 로고
    • Expression and characterization of recombinant caveolin. Purification by polyhistidine tagging and cholesterol-dependent incorporation into defined lipid membranes
    • S. Li, K.S. Song, and M.P. Lisanti Expression and characterization of recombinant caveolin. Purification by polyhistidine tagging and cholesterol-dependent incorporation into defined lipid membranes J. Biol. Chem. 271 1996 568 573
    • (1996) J. Biol. Chem. , vol.271 , pp. 568-573
    • Li, S.1    Song, K.S.2    Lisanti, M.P.3
  • 141
    • 0028125208 scopus 로고
    • Caveolin moves from caveolae to the Golgi apparatus in response to cholesterol oxidation
    • E.J. Smart, Y.S. Ying, P.A. Conrad, and R.G. Anderson Caveolin moves from caveolae to the Golgi apparatus in response to cholesterol oxidation J. Cell Biol. 127 1994 1185 1197
    • (1994) J. Cell Biol. , vol.127 , pp. 1185-1197
    • Smart, E.J.1    Ying, Y.S.2    Conrad, P.A.3    Anderson, R.G.4
  • 142
    • 0028878310 scopus 로고
    • NEM inhibits transcytosis, endocytosis, and capillary permeability: Implication of caveolae fusion in endothelia
    • J.E. Schnitzer, J. Allard, and P. Oh NEM inhibits transcytosis, endocytosis, and capillary permeability: implication of caveolae fusion in endothelia Am. J. Physiol. 268 1995 H48 H55
    • (1995) Am. J. Physiol. , vol.268
    • Schnitzer, J.E.1    Allard, J.2    Oh, P.3
  • 143
    • 0028784298 scopus 로고
    • Compartmentalized production of ceramide at the cell surface
    • P. Liu, and R.G. Anderson Compartmentalized production of ceramide at the cell surface J. Biol. Chem. 270 1995 27179 27185
    • (1995) J. Biol. Chem. , vol.270 , pp. 27179-27185
    • Liu, P.1    Anderson, R.G.2
  • 144
    • 0028806694 scopus 로고
    • A photo-reactive derivative of ganglioside GM1 specifically cross-links VIP21-caveolin on the cell surface
    • A.M. Fra, M. Masserini, P. Palestini, S. Sonnino, and K. Simons A photo-reactive derivative of ganglioside GM1 specifically cross-links VIP21-caveolin on the cell surface FEBS Lett. 375 1995 11 14
    • (1995) FEBS Lett. , vol.375 , pp. 11-14
    • Fra, A.M.1    Masserini, M.2    Palestini, P.3    Sonnino, S.4    Simons, K.5
  • 146
    • 0141828502 scopus 로고    scopus 로고
    • Use of detergents to study membrane rafts: The good, the bad, and the ugly
    • H. Shogomori, and D.A. Brown Use of detergents to study membrane rafts: the good, the bad, and the ugly Biol. Chem. 384 2003 1259 1263
    • (2003) Biol. Chem. , vol.384 , pp. 1259-1263
    • Shogomori, H.1    Brown, D.A.2
  • 148
    • 0034625373 scopus 로고    scopus 로고
    • Structure and function of sphingolipid- and cholesterol-rich membrane rafts
    • D.A. Brown, and E. London Structure and function of sphingolipid- and cholesterol-rich membrane rafts J. Biol. Chem. 275 2000 17221 17224
    • (2000) J. Biol. Chem. , vol.275 , pp. 17221-17224
    • Brown, D.A.1    London, E.2
  • 149
    • 0014572124 scopus 로고
    • Intestinal capillaries: II. Structural effects ofEDTA and histamine
    • F. Clementi, and G.E. Palade Intestinal capillaries: II. Structural effects ofEDTA and histamine J. Cell Biol. 42 1969 706 714
    • (1969) J. Cell Biol. , vol.42 , pp. 706-714
    • Clementi, F.1    Palade, G.E.2
  • 150
    • 0014495399 scopus 로고
    • Intestinal capillaries: I. Permeability to peroxidase and ferritin
    • F. Clementi, and G.E. Palade Intestinal capillaries: I. Permeability to peroxidase and ferritin J. Cell Biol. 41 1969 33 58
    • (1969) J. Cell Biol. , vol.41 , pp. 33-58
    • Clementi, F.1    Palade, G.E.2
  • 151
    • 0033553879 scopus 로고    scopus 로고
    • Isolation, cloning, and localization of rat PV-1, a novel endothelial caveolar protein
    • R.V. Stan, L. Ghitescu, B.S. Jacobson, and G.E. Palade Isolation, cloning, and localization of rat PV-1, a novel endothelial caveolar protein J. Cell Biol. 145 1999 1189 1198
    • (1999) J. Cell Biol. , vol.145 , pp. 1189-1198
    • Stan, R.V.1    Ghitescu, L.2    Jacobson, B.S.3    Palade, G.E.4
  • 152
    • 0033539691 scopus 로고    scopus 로고
    • PV-1 is a component of the fenestral and stomatal diaphragms in fenestrated endothelia
    • R.V. Stan, M. Kubitza, and G.E. Palade PV-1 is a component of the fenestral and stomatal diaphragms in fenestrated endothelia Proc. Natl. Acad. Sci. U. S. A. 96 1999 13203 13207
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 13203-13207
    • Stan, R.V.1    Kubitza, M.2    Palade, G.E.3
  • 153
    • 3342972122 scopus 로고    scopus 로고
    • PV1 is a key structural component for the formation of the stomatal and fenestral diaphragms
    • R.V. Stan, E. Tkachenko, and I.R. Niesman PV1 is a key structural component for the formation of the stomatal and fenestral diaphragms Mol. Biol. Cell 15 2004 3615 3630
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3615-3630
    • Stan, R.V.1    Tkachenko, E.2    Niesman, I.R.3
  • 154
    • 1642412447 scopus 로고    scopus 로고
    • Multiple PV1 dimers reside in the same stomatal or fenestral diaphragm
    • R.V. Stan Multiple PV1 dimers reside in the same stomatal or fenestral diaphragm Am. J. Physiol, Heart Circ. Physiol. 286 2004 H1347 H1353
    • (2004) Am. J. Physiol, Heart Circ. Physiol. , vol.286
    • Stan, R.V.1
  • 155
    • 0021972672 scopus 로고
    • Endothelial fenestral diaphragms: A quick-freeze, deep-etch study
    • E.L. Bearer, and L. Orci Endothelial fenestral diaphragms: a quick-freeze, deep-etch study J. Cell Biol. 100 1985 418 428
    • (1985) J. Cell Biol. , vol.100 , pp. 418-428
    • Bearer, E.L.1    Orci, L.2
  • 156
    • 0019792786 scopus 로고
    • Differentiated microdomains on the luminal surface of the capillary endothelium: II. Partial characterization of their anionic sites
    • M. Simionescu, N. Simionescu, J.E. Silbert, and G.E. Palade Differentiated microdomains on the luminal surface of the capillary endothelium: II. Partial characterization of their anionic sites J. Cell Biol. 90 1981 614 621
    • (1981) J. Cell Biol. , vol.90 , pp. 614-621
    • Simionescu, M.1    Simionescu, N.2    Silbert, J.E.3    Palade, G.E.4
  • 157
    • 0019977465 scopus 로고
    • Differentiated microdomains on the luminal surface of capillary endothelium: Distribution of lectin receptors
    • M. Simionescu, N. Simionescu, and G.E. Palade Differentiated microdomains on the luminal surface of capillary endothelium: distribution of lectin receptors J. Cell Biol. 94 1982 406 413
    • (1982) J. Cell Biol. , vol.94 , pp. 406-413
    • Simionescu, M.1    Simionescu, N.2    Palade, G.E.3
  • 158
    • 0036605832 scopus 로고    scopus 로고
    • Structure and function of endothelial caveolae
    • R.V. Stan Structure and function of endothelial caveolae Microsc. Res. Tech. 57 2002 350 364
    • (2002) Microsc. Res. Tech. , vol.57 , pp. 350-364
    • Stan, R.V.1
  • 159
    • 0035074497 scopus 로고    scopus 로고
    • The vesiculo-vacuolar organelle (VVO). a new endothelial cell permeability organelle
    • A.M. Dvorak, and D. Feng The vesiculo-vacuolar organelle (VVO). A new endothelial cell permeability organelle J. Histochem. Cytochem. 49 2001 419 432
    • (2001) J. Histochem. Cytochem. , vol.49 , pp. 419-432
    • Dvorak, A.M.1    Feng, D.2
  • 160
    • 0035868622 scopus 로고    scopus 로고
    • CDNA and protein sequence, genomic organization, and analysis of cis regulatory elements of mouse and human PLVAP genes
    • R.V. Stan, K.C. Arden, and G.E. Palade cDNA and protein sequence, genomic organization, and analysis of cis regulatory elements of mouse and human PLVAP genes Genomics 72 2001 304 313
    • (2001) Genomics , vol.72 , pp. 304-313
    • Stan, R.V.1    Arden, K.C.2    Palade, G.E.3
  • 161
    • 0031562684 scopus 로고    scopus 로고
    • Antibodies specific to the plasma membrane of rat lung microvascular endothelium
    • L.D. Ghitescu, P. Crine, and B.S. Jacobson Antibodies specific to the plasma membrane of rat lung microvascular endothelium Exp. Cell Res. 232 1997 47 55
    • (1997) Exp. Cell Res. , vol.232 , pp. 47-55
    • Ghitescu, L.D.1    Crine, P.2    Jacobson, B.S.3
  • 162
    • 0036936847 scopus 로고    scopus 로고
    • Distribution and characterization of plasmalemma vesicle protein-1 in rat endocrine glands
    • R. Hnasko, M. McFarl, and N. Ben-Jonathan Distribution and characterization of plasmalemma vesicle protein-1 in rat endocrine glands J. Endocrinol. 175 2002 649 661
    • (2002) J. Endocrinol. , vol.175 , pp. 649-661
    • Hnasko, R.1    McFarl, M.2    Ben-Jonathan, N.3
  • 163
    • 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
    • J. Couet, S. Li, T. Okamoto, T. Ikezu, and M.P. Lisanti Identification of peptide and protein ligands for the caveolin-scaffolding domain. Implications for the interaction of caveolin with caveolae-associated proteins J. Biol. Chem. 272 1997 6525 6533
    • (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
  • 164
    • 0030004228 scopus 로고    scopus 로고
    • Prediction and analysis of coiled-coil structures
    • A. Lupas Prediction and analysis of coiled-coil structures Methods Enzymol. 266 1996 513 525
    • (1996) Methods Enzymol. , vol.266 , pp. 513-525
    • Lupas, A.1
  • 165
    • 12144268807 scopus 로고    scopus 로고
    • Developmental regulation of PV-1 in rat lung: Association with the nuclear envelope and limited colocalization with Cav-1
    • R. Hnasko, and N. Ben-Jonathan Developmental regulation of PV-1 in rat lung: association with the nuclear envelope and limited colocalization with Cav-1 Am. J. Physiol., Lung Cell Mol. Physiol. 288 2005 L275 L284
    • (2005) Am. J. Physiol., Lung Cell Mol. Physiol. , vol.288
    • Hnasko, R.1    Ben-Jonathan, N.2
  • 166
    • 34548164863 scopus 로고    scopus 로고
    • Endothelial diaphragms: Nanogates of vascular permeability
    • (in press).
    • R.V. Stan, Endothelial diaphragms: nanogates of vascular permeability. Anat. Rec. (in press).
    • Anat. Rec.
    • Stan, R.V.1
  • 167
    • 0019869405 scopus 로고
    • Differentiated microdomains on the luminal surface of the capillary endothelium. I. Preferential distribution of anionic sites
    • N. Simionescu, M. Simionescu, and G.E. Palade Differentiated microdomains on the luminal surface of the capillary endothelium. I. Preferential distribution of anionic sites J. Cell Biol. 90 1981 605 613
    • (1981) J. Cell Biol. , vol.90 , pp. 605-613
    • Simionescu, N.1    Simionescu, M.2    Palade, G.E.3
  • 168
    • 0015124321 scopus 로고
    • Structure and formation of pores in fenestrated capillaries
    • G.G. Maul Structure and formation of pores in fenestrated capillaries J. Ultrastruct. Res. 36 1971 768 782
    • (1971) J. Ultrastruct. Res. , vol.36 , pp. 768-782
    • Maul, G.G.1


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