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Volumn 85, Issue 4, 2007, Pages 473-481

Status of caveolin-1 in various membrane domains of the bovine lens

Author keywords

caveolae; caveolin 1; lens epithelial cell membranes; lens fiber cell membranes; lipid vesicles; lipid like rafts; peripheral protein; plasma membrane

Indexed keywords

CAVEOLIN 1; CHOLESTEROL; DETERGENT; LIPID; MEMBRANE PROTEIN; SCAFFOLD PROTEIN; SPHINGOMYELIN; UREA;

EID: 34948812546     PISSN: 00144835     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.exer.2007.05.011     Document Type: Article
Times cited : (8)

References (48)
  • 1
    • 0842304654 scopus 로고    scopus 로고
    • Smooth muscle raft-like membranes
    • Baron C.B., and Coburn R.F. Smooth muscle raft-like membranes. J. Lipid Res. 45 (2004) 41-53
    • (2004) J. Lipid Res. , vol.45 , pp. 41-53
    • Baron, C.B.1    Coburn, R.F.2
  • 2
    • 0030771954 scopus 로고    scopus 로고
    • Fiber cell denucleation in the primate lens
    • Bassnett S. Fiber cell denucleation in the primate lens. Invest. Ophthalmol. Vis. Sci. 38 (1997) 1678-1687
    • (1997) Invest. Ophthalmol. Vis. Sci. , vol.38 , pp. 1678-1687
    • Bassnett, S.1
  • 3
    • 0019433250 scopus 로고
    • Studies on the source of urinary cholesterol in the normal human male
    • Cenedella R.J., and Belis J.A. Studies on the source of urinary cholesterol in the normal human male. J. Lipid Res. 22 (1981) 122-130
    • (1981) J. Lipid Res. , vol.22 , pp. 122-130
    • Cenedella, R.J.1    Belis, J.A.2
  • 4
    • 0027208037 scopus 로고
    • Apparent coordination of plasma membrane component synthesis in the lens
    • Cenedella R.J. Apparent coordination of plasma membrane component synthesis in the lens. Invest. Ophthalmol. Vis. Sci. 34 (1993) 2186-2194
    • (1993) Invest. Ophthalmol. Vis. Sci. , vol.34 , pp. 2186-2194
    • Cenedella, R.J.1
  • 5
    • 31044454146 scopus 로고    scopus 로고
    • Multiple forms of 22 kDa caveolin-1 alpha present in bovine lens cells could reflect variable palmitoylation
    • Cenedella R.J., Neely A.R., and Sexton P. Multiple forms of 22 kDa caveolin-1 alpha present in bovine lens cells could reflect variable palmitoylation. Exp. Eye Res. 82 (2006) 229-235
    • (2006) Exp. Eye Res. , vol.82 , pp. 229-235
    • Cenedella, R.J.1    Neely, A.R.2    Sexton, P.3
  • 6
    • 0031105338 scopus 로고    scopus 로고
    • Properties of α-crystallin bound to lens membrane: probing organization at the membrane surface
    • Chandrasekher G., and Cenedella R.J. Properties of α-crystallin bound to lens membrane: probing organization at the membrane surface. Exp. Eye Res. 64 (1997) 423-430
    • (1997) Exp. Eye Res. , vol.64 , pp. 423-430
    • Chandrasekher, G.1    Cenedella, R.J.2
  • 7
    • 0037080002 scopus 로고    scopus 로고
    • Alpha-crystallin chaperone-like activity and membrane binding in age-related cataracts
    • Cobb B.A., and Petrash J.M. Alpha-crystallin chaperone-like activity and membrane binding in age-related cataracts. Biochemistry 41 (2002) 483-490
    • (2002) Biochemistry , vol.41 , pp. 483-490
    • Cobb, B.A.1    Petrash, J.M.2
  • 8
    • 0029560256 scopus 로고
    • Caveolin cycles between plasma membrane caveolae and the Golgi complex by microtubule-dependent and microtubule-independent steps
    • Conrad P.A., Smart E.J., Ying Y.-S., Anderson R.G.W., and Bloom G.S. Caveolin cycles between plasma membrane caveolae and the Golgi complex by microtubule-dependent and microtubule-independent steps. J. Cell Biol. 131 (1995) 1421-1433
    • (1995) J. Cell Biol. , vol.131 , pp. 1421-1433
    • Conrad, P.A.1    Smart, E.J.2    Ying, Y.-S.3    Anderson, R.G.W.4    Bloom, G.S.5
  • 9
    • 0037959071 scopus 로고    scopus 로고
    • The state of lipid rafts: from model membranes to cells
    • Edidin M. The state of lipid rafts: from model membranes to cells. Annu. Rev. Biophys. Biomol. Struct. 32 (2003) 257-283
    • (2003) Annu. Rev. Biophys. Biomol. Struct. , vol.32 , pp. 257-283
    • Edidin, M.1
  • 11
    • 0026815368 scopus 로고
    • The crystalline lens. A system networked by gap junctional intercellular communications
    • Goodenough D.A. The crystalline lens. A system networked by gap junctional intercellular communications. Semin. Cell Biol. 3 (1992) 49-58
    • (1992) Semin. Cell Biol. , vol.3 , pp. 49-58
    • Goodenough, D.A.1
  • 12
    • 32444437957 scopus 로고    scopus 로고
    • Caveolins in vascular smooth muscle: form organizing functions
    • Hardin C.D., and Vallejo J. Caveolins in vascular smooth muscle: form organizing functions. Cardiovasc. Res. 69 (2006) 808-815
    • (2006) Cardiovasc. Res. , vol.69 , pp. 808-815
    • Hardin, C.D.1    Vallejo, J.2
  • 13
    • 0022396961 scopus 로고
    • Absolute rates of sterol synthesis estimated from [3H] water for bovine lens epithelial cells in culture
    • Hitchener W.R., and Cenedella R.J. Absolute rates of sterol synthesis estimated from [3H] water for bovine lens epithelial cells in culture. J. Lipid Res. 26 (1985) 1455-1463
    • (1985) J. Lipid Res. , vol.26 , pp. 1455-1463
    • Hitchener, W.R.1    Cenedella, R.J.2
  • 14
    • 0030475794 scopus 로고    scopus 로고
    • 2+ channel essential for phosphoinositide-mediated photoreception, forms a signaling complex with NorpA, Inac and Inad
    • 2+ channel essential for phosphoinositide-mediated photoreception, forms a signaling complex with NorpA, Inac and Inad. EMBO J. 15 (1996) 7036-7045
    • (1996) EMBO J. , vol.15 , pp. 7036-7045
    • Huber, A.1    Sander, P.2    Gobert, A.3    Bahner, M.4    Hermann, R.5    Paulsen, R.6
  • 15
    • 0034654036 scopus 로고    scopus 로고
    • Caveolin internalization by heat shock or hyperosmotic shock
    • Kang Y.S., Ko Y.G., and Seo J.S. Caveolin internalization by heat shock or hyperosmotic shock. Exp. Cell Res. 255 (2000) 221-228
    • (2000) Exp. Cell Res. , vol.255 , pp. 221-228
    • Kang, Y.S.1    Ko, Y.G.2    Seo, J.S.3
  • 17
    • 0344971186 scopus 로고
    • Modification of the Lowry procedure for analysis of proteolipid protein
    • Lees M.B., and Paxman S. Modification of the Lowry procedure for analysis of proteolipid protein. Anal. Biochem. 227 (1972) 680-685
    • (1972) Anal. Biochem. , vol.227 , pp. 680-685
    • Lees, M.B.1    Paxman, S.2
  • 19
    • 0035031405 scopus 로고    scopus 로고
    • Cell-specific targeting of caveolin-1 to caveolae, secretory vesicles, cytoplasm or mitochondria
    • Li W.-P., Lui P., Pilcher B.K., and Anderson R.G.W. Cell-specific targeting of caveolin-1 to caveolae, secretory vesicles, cytoplasm or mitochondria. J. Cell. Sci. 114 (2001) 1397-1408
    • (2001) J. Cell. Sci. , vol.114 , pp. 1397-1408
    • Li, W.-P.1    Lui, P.2    Pilcher, B.K.3    Anderson, R.G.W.4
  • 20
    • 0035282064 scopus 로고    scopus 로고
    • Selective inactivation of guanine-nucleotide-binding regulatory protein (G-protein) α and βγ subunits by urea
    • Lim W.K., and Neubig R.R. Selective inactivation of guanine-nucleotide-binding regulatory protein (G-protein) α and βγ subunits by urea. Biochem. J. 354 (2001) 337-344
    • (2001) Biochem. J. , vol.354 , pp. 337-344
    • Lim, W.K.1    Neubig, R.R.2
  • 21
    • 0344420042 scopus 로고    scopus 로고
    • Protein kinase Cgamma regulation of gap junction activity through caveolin-1-containing lipid rafts
    • Lin D., Zhou J., Zelenka P.S., and Takemoto D.J. Protein kinase Cgamma regulation of gap junction activity through caveolin-1-containing lipid rafts. Invest. Ophthalmol. Vis. Sci. 44 (2003) 5259-5268
    • (2003) Invest. Ophthalmol. Vis. Sci. , vol.44 , pp. 5259-5268
    • Lin, D.1    Zhou, J.2    Zelenka, P.S.3    Takemoto, D.J.4
  • 23
    • 17144369501 scopus 로고    scopus 로고
    • Oxidative activation of protein Cgamma through the C1 domain. Effects of gap junctions
    • Lin D., and Takemoto D.J. Oxidative activation of protein Cgamma through the C1 domain. Effects of gap junctions. J. Biol. Chem. 280 (2005) 13682-13693
    • (2005) J. Biol. Chem. , vol.280 , pp. 13682-13693
    • Lin, D.1    Takemoto, D.J.2
  • 24
    • 4544299036 scopus 로고    scopus 로고
    • Identification of caveolae and their signature proteins caveolin 1 and 2 in the lens
    • Lo W.-K., Zhou C.-J., and Reddan J. Identification of caveolae and their signature proteins caveolin 1 and 2 in the lens. Exp. Eye Res. 79 (2004) 487-498
    • (2004) Exp. Eye Res. , vol.79 , pp. 487-498
    • Lo, W.-K.1    Zhou, C.-J.2    Reddan, J.3
  • 25
    • 0031470628 scopus 로고    scopus 로고
    • Platelet derived growth factor activates mitogen- activated protein kinase in isolated caveolae
    • Lui P., Ying Y., and Anderson R.G. Platelet derived growth factor activates mitogen- activated protein kinase in isolated caveolae. Proc. Natl. Acad. Sci. 94 (1997) 13666-13670
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 13666-13670
    • Lui, P.1    Ying, Y.2    Anderson, R.G.3
  • 26
    • 0036830114 scopus 로고    scopus 로고
    • Multiple functions of caveolin-1
    • Lui P., Rudick M., and Anderson R.G.W. Multiple functions of caveolin-1. J. Biol. Chem. 277 (2002) 41295-41298
    • (2002) J. Biol. Chem. , vol.277 , pp. 41295-41298
    • Lui, P.1    Rudick, M.2    Anderson, R.G.W.3
  • 27
    • 22244469306 scopus 로고    scopus 로고
    • A simplified method for the preparation of detergent-free lipid rafts
    • Macdonald J.L., and Pike L.J. A simplified method for the preparation of detergent-free lipid rafts. J. Lipid Res. 46 (2005) 1061-1067
    • (2005) J. Lipid Res. , vol.46 , pp. 1061-1067
    • Macdonald, J.L.1    Pike, L.J.2
  • 29
    • 15844431258 scopus 로고    scopus 로고
    • Localization of epidermal growth factor-stimulated ras/raf-1 interactions to caveolae membrane
    • Mineo C., James G.L., Smart E.J., and Anderson R.G. Localization of epidermal growth factor-stimulated ras/raf-1 interactions to caveolae membrane. J. Biol. Chem. 271 (1996) 11930-11935
    • (1996) J. Biol. Chem. , vol.271 , pp. 11930-11935
    • Mineo, C.1    James, G.L.2    Smart, E.J.3    Anderson, R.G.4
  • 31
    • 33748699989 scopus 로고    scopus 로고
    • Caveolin-1 is upregulated in transdifferentiated lens epithelial cells but minimal in normal and murine lenses
    • Perdue N., and Yan Q. Caveolin-1 is upregulated in transdifferentiated lens epithelial cells but minimal in normal and murine lenses. Exp. Eye Res. 83 (2006) 1154-1161
    • (2006) Exp. Eye Res. , vol.83 , pp. 1154-1161
    • Perdue, N.1    Yan, Q.2
  • 32
    • 0035809933 scopus 로고    scopus 로고
    • A caveolin dominant negative mutant associates with lipid bodies and induces intracellular cholesterol imbalance
    • Pol A., Luetterforst R., Lindsay M., Heino S., Ikonen E., and Parton R.G. 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
  • 33
    • 4143084213 scopus 로고    scopus 로고
    • Lipids partition caveolin-1 from ER membranes into lipid droplets: updating the model of lipid droplet biogenesis
    • Robenek M.J., Severs N.J., Schlattmann K., Plenz G., Zimmer K.-P., Troyer D., and Robenek H. Lipids partition caveolin-1 from ER membranes into lipid droplets: updating the model of lipid droplet biogenesis. FASEB J. 18 (2004) 866-868
    • (2004) FASEB J. , vol.18 , pp. 866-868
    • Robenek, M.J.1    Severs, N.J.2    Schlattmann, K.3    Plenz, G.4    Zimmer, K.-P.5    Troyer, D.6    Robenek, H.7
  • 34
    • 0037378889 scopus 로고    scopus 로고
    • Isolation and lipid characterization of cholesterol-enriched fractions in cortical and nuclear human lens fibers
    • Rujoi M., Jin J., Borchman D., Tang D., and Yappert M.C. Isolation and lipid characterization of cholesterol-enriched fractions in cortical and nuclear human lens fibers. Invest. Ophthalmol. Vis. Sci. 44 (2004) 1634-1642
    • (2004) Invest. Ophthalmol. Vis. Sci. , vol.44 , pp. 1634-1642
    • Rujoi, M.1    Jin, J.2    Borchman, D.3    Tang, D.4    Yappert, M.C.5
  • 35
    • 0019435458 scopus 로고
    • A new method for rapid isolation of the intrinsic membrane proteins from lens
    • Russell P. A new method for rapid isolation of the intrinsic membrane proteins from lens. Exp. Eye Res. 32 (1981) 511-516
    • (1981) Exp. Eye Res. , vol.32 , pp. 511-516
    • Russell, P.1
  • 36
    • 0037035519 scopus 로고    scopus 로고
    • Connexin family members target to lipid raft domains and interact with caveolin-1
    • Schubert A.-L., Schubert W., Spray D.C., and Lisanti M.P. Connexin family members target to lipid raft domains and interact with caveolin-1. Biochemistry 41 (2002) 5754-5764
    • (2002) Biochemistry , vol.41 , pp. 5754-5764
    • Schubert, A.-L.1    Schubert, W.2    Spray, D.C.3    Lisanti, M.P.4
  • 37
    • 0345550316 scopus 로고    scopus 로고
    • Distribution of caveolin-1 in bovine lens and redistribution in cultured bovine lens epithelial cells upon confluence
    • Sexton P.S., Neely A.R., and Cenedella R.J. Distribution of caveolin-1 in bovine lens and redistribution in cultured bovine lens epithelial cells upon confluence. Exp. Eye Res. 78 (2004) 75-82
    • (2004) Exp. Eye Res. , vol.78 , pp. 75-82
    • Sexton, P.S.1    Neely, A.R.2    Cenedella, R.J.3
  • 38
    • 0028125208 scopus 로고
    • Caveolin moves from caveolae to the Golgi apparatus in response to cholesterol oxidation
    • Smart E.J., Ying Y.-S., Donzell W.C., and Anderson R.G.W. 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    Donzell, W.C.3    Anderson, R.G.W.4
  • 39
    • 0028820041 scopus 로고
    • A detergent-free method for purifying membrane from tissue cultured cells
    • Smart E.J., Ying Y.S., Mineo C., and Anderson R.G. A detergent-free method for purifying membrane from tissue cultured cells. Proc. Natl. Acad. Sci. USA 92 (1995) 10104-10108
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10104-10108
    • Smart, E.J.1    Ying, Y.S.2    Mineo, C.3    Anderson, R.G.4
  • 40
    • 0029799891 scopus 로고    scopus 로고
    • A role for caveolin in the transport of cholesterol from endoplasmic reticulum to plasma membrane
    • Smart E.J., Ying Y.-S., Conrad P.A., and Anderson R.G.W. A role for caveolin in the transport of cholesterol from endoplasmic reticulum to plasma membrane. J. Biol. Chem. 271 (1996) 29427-29435
    • (1996) J. Biol. Chem. , vol.271 , pp. 29427-29435
    • Smart, E.J.1    Ying, Y.-S.2    Conrad, P.A.3    Anderson, R.G.W.4
  • 42
    • 29144534595 scopus 로고    scopus 로고
    • Structure of caveolae
    • Stan R.V. Structure of caveolae. Biochem. Biophys. Acta 1746 (2005) 334-348
    • (2005) Biochem. Biophys. Acta , vol.1746 , pp. 334-348
    • Stan, R.V.1
  • 43
    • 0036975880 scopus 로고    scopus 로고
    • Caveolin-1 redistribution in human endothelial cells induced by laminar flow and cytokine
    • Sun R.J., Mueller S., Zhaung F.Y., Stoltz J.F., and Wang X. Caveolin-1 redistribution in human endothelial cells induced by laminar flow and cytokine. Biorheology 40 (2003) 31-39
    • (2003) Biorheology , vol.40 , pp. 31-39
    • Sun, R.J.1    Mueller, S.2    Zhaung, F.Y.3    Stoltz, J.F.4    Wang, X.5
  • 44
    • 0034682847 scopus 로고    scopus 로고
    • Palmitoylation of caveolin-1 is required for cholesterol binding, chaperone complex formation, and rapid transport of cholesterol to caveolae
    • Uittenbogaard A., and Smart E.J. Palmitoylation of caveolin-1 is required for cholesterol binding, chaperone complex formation, and rapid transport of cholesterol to caveolae. J. Biol. Chem. 275 (2000) 25595-25599
    • (2000) J. Biol. Chem. , vol.275 , pp. 25595-25599
    • Uittenbogaard, A.1    Smart, E.J.2
  • 45
    • 0033018603 scopus 로고    scopus 로고
    • Visualization of caveolin-1, a caveolar marker protein, in living cells using green fluorescent protein (GFP) chimeras. The subcellular distribution of caveolin-1 is modulated by cell-cell contact
    • Volonte D., Galhiati F., and Lisanti M.P. Visualization of caveolin-1, a caveolar marker protein, in living cells using green fluorescent protein (GFP) chimeras. The subcellular distribution of caveolin-1 is modulated by cell-cell contact. FEBS Lett. 445 (1999) 431-439
    • (1999) FEBS Lett. , vol.445 , pp. 431-439
    • Volonte, D.1    Galhiati, F.2    Lisanti, M.P.3
  • 46
    • 0027483048 scopus 로고
    • Cooperative binding of the retinal rod protein, transducin, to the light activated rhodopsin
    • Willardson B.M., Pou B., Yoshida T., and Bitenshy M.W. Cooperative binding of the retinal rod protein, transducin, to the light activated rhodopsin. J. Biol. Chem. 268 (1993) 6371-6382
    • (1993) J. Biol. Chem. , vol.268 , pp. 6371-6382
    • Willardson, B.M.1    Pou, B.2    Yoshida, T.3    Bitenshy, M.W.4
  • 48
    • 27244457253 scopus 로고    scopus 로고
    • Regulation of lens cell-to-cell communication by activation of PKCgamma and disassembly of Cx50 channels
    • Zampighi G.A., Planells A.M., Lin D., and Takemoto D. Regulation of lens cell-to-cell communication by activation of PKCgamma and disassembly of Cx50 channels. Invest. Ophthamol. Vis. Sci. 46 (2005) 3247-3255
    • (2005) Invest. Ophthamol. Vis. Sci. , vol.46 , pp. 3247-3255
    • Zampighi, G.A.1    Planells, A.M.2    Lin, D.3    Takemoto, D.4


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