메뉴 건너뛰기




Volumn 129, Issue 1, 2004, Pages 1-20

Sphingolipids in human lens membranes: An update on their composition and possible biological implications

Author keywords

Cholesterol; Dihydrosphingomyelins; Growth; Human lens membranes; Sphingolipids

Indexed keywords

CHOLESTEROL; DIHYDROSPHINGOMYELIN; HYDROXYL GROUP; PHOSPHOLIPID; SPHINGOMYELIN; UNCLASSIFIED DRUG;

EID: 1442299372     PISSN: 00093084     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chemphyslip.2003.12.003     Document Type: Review
Times cited : (71)

References (239)
  • 1
    • 0025333990 scopus 로고
    • Hydrodynamic characterization of the major intrinsic protein from the bovine lens fiber membranes. Extraction in n-octyl-beta-D-glucopyranoside and evidence for a tetrameric structure
    • Aerts T., Xia J.Z., Slegers H., de Block J., Clauwaert J. Hydrodynamic characterization of the major intrinsic protein from the bovine lens fiber membranes. Extraction in n-octyl-beta-D-glucopyranoside and evidence for a tetrameric structure. J. Biol. Chem. 265:1990;8675-8680.
    • (1990) J. Biol. Chem. , vol.265 , pp. 8675-8680
    • Aerts, T.1    Xia, J.Z.2    Slegers, H.3    De Block, J.4    Clauwaert, J.5
  • 3
    • 0020960731 scopus 로고
    • Lipid composition of chick lens fiber cell gap junctions
    • Alcala J., Katar M., Maisel H. Lipid composition of chick lens fiber cell gap junctions. Curr. Eye Res. 2:1982;569-578.
    • (1982) Curr. Eye Res. , vol.2 , pp. 569-578
    • Alcala, J.1    Katar, M.2    Maisel, H.3
  • 5
    • 0014694228 scopus 로고
    • Lipids of ocular tissues. I. The phospholipids of mature rabbit and bovine lens
    • Anderson R.E., Maude M.B., Feldman G.L. Lipids of ocular tissues. I. The phospholipids of mature rabbit and bovine lens. Biochim. Biophys. Acta. 187:1969;345-353.
    • (1969) Biochim. Biophys. Acta , vol.187 , pp. 345-353
    • Anderson, R.E.1    Maude, M.B.2    Feldman, G.L.3
  • 6
    • 0021924483 scopus 로고
    • Abnormalities in gangliosides and other lipids of monkey, rabbit and human brains with chronic organic mercury intoxication
    • Ando S., Toyoda Y., Nagai Y., Ikuta F. Abnormalities in gangliosides and other lipids of monkey, rabbit and human brains with chronic organic mercury intoxication. Jpn. J. Exp. Med. 55:1985;1-6.
    • (1985) Jpn. J. Exp. Med. , vol.55 , pp. 1-6
    • Ando, S.1    Toyoda, Y.2    Nagai, Y.3    Ikuta, F.4
  • 9
    • 0026555973 scopus 로고
    • Na,K-ATPase and phospholipid degradation in bovine and human lenses
    • Baghieri S., Garner M.H. Na,K-ATPase and phospholipid degradation in bovine and human lenses. Curr. Eye Res. 11:1992;459-467.
    • (1992) Curr. Eye Res. , vol.11 , pp. 459-467
    • Baghieri, S.1    Garner, M.H.2
  • 10
    • 0017075610 scopus 로고
    • A calorimetric study of the thermotropic behavior of aqueous dispersions of natural and synthetic sphingomyelins
    • Barenholz Y., Suurkuusk J., Mountcastle D., Thompson T.E., Biltonen R.L. A calorimetric study of the thermotropic behavior of aqueous dispersions of natural and synthetic sphingomyelins. Biochemistry. 15:1976;2441-2447.
    • (1976) Biochemistry , vol.15 , pp. 2441-2447
    • Barenholz, Y.1    Suurkuusk, J.2    Mountcastle, D.3    Thompson, T.E.4    Biltonen, R.L.5
  • 12
    • 0029127167 scopus 로고
    • The fate of the Golgi apparatus and the endoplasmic reticulum during lens fiber cell differentiation
    • Bassnett S. The fate of the Golgi apparatus and the endoplasmic reticulum during lens fiber cell differentiation. Invest. Ophthalmol. Vis. Sci. 36:1995;1793-1803.
    • (1995) Invest. Ophthalmol. Vis. Sci. , vol.36 , pp. 1793-1803
    • Bassnett, S.1
  • 13
  • 14
    • 0036672240 scopus 로고    scopus 로고
    • Bone morphogenetic protein signaling and the initiation of lens fiber cell differentiation
    • Belecky-Adams T.L., Adler R., Beebe D.C. Bone morphogenetic protein signaling and the initiation of lens fiber cell differentiation. Development. 129:2002;3795-3802.
    • (2002) Development , vol.129 , pp. 3795-3802
    • Belecky-Adams, T.L.1    Adler, R.2    Beebe, D.C.3
  • 16
    • 0028290620 scopus 로고
    • Assessment of oxidative stress to eye in animal model for cataract
    • Bhuyan D.K., Bhuyan K.C. Assessment of oxidative stress to eye in animal model for cataract. Meth. Enzym. 233:1994;630-639.
    • (1994) Meth. Enzym. , vol.233 , pp. 630-639
    • Bhuyan, D.K.1    Bhuyan, K.C.2
  • 17
    • 0030582557 scopus 로고    scopus 로고
    • Crosslinking of aminophospholipids in cellular membranes of lens by oxidative stress in vitro
    • Bhuyan D.K., Master R.W., Bhuyan K.C. Crosslinking of aminophospholipids in cellular membranes of lens by oxidative stress in vitro. Biochim. Biophys. Acta. 1285:1996;21-28.
    • (1996) Biochim. Biophys. Acta , vol.1285 , pp. 21-28
    • Bhuyan, D.K.1    Master, R.W.2    Bhuyan, K.C.3
  • 18
    • 84907037268 scopus 로고
    • Free radical enhancer xenobiotic is an inducer of cataract in rabbit
    • Bhuyan K.C., Bhuyan D.K., Podos S.M. Free radical enhancer xenobiotic is an inducer of cataract in rabbit. Free Radic. Res. Commun. 12/13(Pt 2):1991;609-620.
    • (1991) Free Radic. Res. Commun. , vol.1213 , Issue.PT 2 , pp. 609-620
    • Bhuyan, K.C.1    Bhuyan, D.K.2    Podos, S.M.3
  • 19
    • 0015355244 scopus 로고
    • The plasma membranes of eye lens fibres. Biochemical and structural characterization
    • Bloemendal H., Zweers A., Vermorken F., Dunia I., Benedetti E.L. The plasma membranes of eye lens fibres. Biochemical and structural characterization. Cell Differ. 1:1972;91-106.
    • (1972) Cell Differ. , vol.1 , pp. 91-106
    • Bloemendal, H.1    Zweers, A.2    Vermorken, F.3    Dunia, I.4    Benedetti, E.L.5
  • 20
    • 0019075644 scopus 로고
    • Intermolecular hydrogen bonding between lipids: Influence on organization and function of lipids in membranes
    • Boggs J.M. Intermolecular hydrogen bonding between lipids: influence on organization and function of lipids in membranes. Can. J. Biochem. 58:1980;755-770.
    • (1980) Can. J. Biochem. , vol.58 , pp. 755-770
    • Boggs, J.M.1
  • 21
    • 0023239664 scopus 로고
    • Lipid intermolecular hydrogen bonding: Influence on structural organization and membrane function
    • Boggs J.M. Lipid intermolecular hydrogen bonding: influence on structural organization and membrane function. Biochim. Biophys. Acta. 906:1987;353-404.
    • (1987) Biochim. Biophys. Acta , vol.906 , pp. 353-404
    • Boggs, J.M.1
  • 22
    • 0028097372 scopus 로고
    • Regional and age-dependent differences in the phospholipid composition of human lens membranes
    • Borchman D., Byrdwell W.C., Yappert M.C. Regional and age-dependent differences in the phospholipid composition of human lens membranes. Invest. Ophthalmol. Vis. Sci. 35:1994;3938-3942.
    • (1994) Invest. Ophthalmol. Vis. Sci. , vol.35 , pp. 3938-3942
    • Borchman, D.1    Byrdwell, W.C.2    Yappert, M.C.3
  • 23
    • 0030004999 scopus 로고    scopus 로고
    • Thermodynamic phase transition parameters of human lens dihydrosphingomyelin
    • Borchman D., Byrdwell W.C., Yappert M.C. Thermodynamic phase transition parameters of human lens dihydrosphingomyelin. Ophthalmic Res. 28(Suppl. 1):1996a;81-85.
    • (1996) Ophthalmic Res. , vol.28 , Issue.SUPPL. 1 , pp. 81-85
    • Borchman, D.1    Byrdwell, W.C.2    Yappert, M.C.3
  • 24
    • 0029921307 scopus 로고    scopus 로고
    • Role of cholesterol in the structural order of lens membrane lipids
    • Borchman D., Cenedella R.J., Lamba O.P. Role of cholesterol in the structural order of lens membrane lipids. Exp. Eye Res. 62:1996b;191-197.
    • (1996) Exp. Eye Res. , vol.62 , pp. 191-197
    • Borchman, D.1    Cenedella, R.J.2    Lamba, O.P.3
  • 25
    • 0024804753 scopus 로고
    • Studies on the distribution of cholesterol, phospholipid, and protein in the human and bovine lens
    • Borchman D., Delamere N.A., McCauley L.A., Paterson C.A. Studies on the distribution of cholesterol, phospholipid, and protein in the human and bovine lens. Lens Eye Toxic Res. 6:1989;703-724.
    • (1989) Lens Eye Toxic Res. , vol.6 , pp. 703-724
    • Borchman, D.1    Delamere, N.A.2    McCauley, L.A.3    Paterson, C.A.4
  • 30
    • 0019142554 scopus 로고
    • Lens membranes. XII. Age-related changes in polypeptide composition of bovine lens fiber membranes
    • Bouman A.A., de Leeuw A.L., Broekhuyse R.M. Lens membranes. XII. Age-related changes in polypeptide composition of bovine lens fiber membranes. Exp. Eye Res. 31:1980;495-503.
    • (1980) Exp. Eye Res. , vol.31 , pp. 495-503
    • Bouman, A.A.1    De Leeuw, A.L.2    Broekhuyse, R.M.3
  • 31
    • 0019426515 scopus 로고
    • Lens membranes. XV. Comparative study of membrane and cytoplasmic proteins from human, monkey and other animal lenses
    • Bouman A.A., de Leeuw A.L., Kuhlmann E.D., Broekhuyse R.M. Lens membranes. XV. Comparative study of membrane and cytoplasmic proteins from human, monkey and other animal lenses. Exp. Eye Res. 33:1981;309-314.
    • (1981) Exp. Eye Res. , vol.33 , pp. 309-314
    • Bouman, A.A.1    De Leeuw, A.L.2    Kuhlmann, E.D.3    Broekhuyse, R.M.4
  • 32
    • 0018677390 scopus 로고
    • Lens membranes. VI. Some characteristics of the EDTA-extractable protein (EEP) from bovine lens fiber membranes
    • Bouman A.A., de Leeuw A.L., Tolhuizen E.F., Broekhuyse R.M. Lens membranes. VI. Some characteristics of the EDTA-extractable protein (EEP) from bovine lens fiber membranes. Exp. Eye Res. 29:1979;83-93.
    • (1979) Exp. Eye Res. , vol.29 , pp. 83-93
    • Bouman, A.A.1    De Leeuw, A.L.2    Tolhuizen, E.F.3    Broekhuyse, R.M.4
  • 33
    • 0014950774 scopus 로고
    • Lipids in tissues of the eye. IV. Influence of age and species differences on the phospholipid composition of the lens
    • Broekhuyse R.M. Lipids in tissues of the eye. IV. Influence of age and species differences on the phospholipid composition of the lens. Biochim. Biophys. Acta. 218:1970;546-548.
    • (1970) Biochim. Biophys. Acta , vol.218 , pp. 546-548
    • Broekhuyse, R.M.1
  • 35
    • 0016140680 scopus 로고
    • Lens membranes. I. Composition of urea-treated plasma membranes from calf lens
    • Broekhuyse R.M., Kuhlmann E.D. Lens membranes. I. Composition of urea-treated plasma membranes from calf lens. Exp. Eye Res. 19:1974;297-302.
    • (1974) Exp. Eye Res. , vol.19 , pp. 297-302
    • Broekhuyse, R.M.1    Kuhlmann, E.D.2
  • 36
    • 0017861922 scopus 로고
    • Lens membranes. IV. Preparative isolation and characterization of membranes and various membrane proteins from calf lens
    • Broekhuyse R.M., Kuhlmann E.D. Lens membranes. IV. Preparative isolation and characterization of membranes and various membrane proteins from calf lens. Exp. Eye Res. 26:1978;305-320.
    • (1978) Exp. Eye Res. , vol.26 , pp. 305-320
    • Broekhuyse, R.M.1    Kuhlmann, E.D.2
  • 37
    • 0018864331 scopus 로고
    • Lens membranes XI. Some properties of human lens main intrinsic protein (MIP) and its enzymatic conversion into a 22000 Dalton polypeptide
    • Broekhuyse R.M., Kuhlmann E.D. Lens membranes XI. Some properties of human lens main intrinsic protein (MIP) and its enzymatic conversion into a 22000 Dalton polypeptide. Exp. Eye Res. 30:1980;305-310.
    • (1980) Exp. Eye Res. , vol.30 , pp. 305-310
    • Broekhuyse, R.M.1    Kuhlmann, E.D.2
  • 38
    • 0017798851 scopus 로고
    • Lens membranes. III. Freeze fracture morphology and composition of bovine lens fibre membranes in relation to ageing
    • Broekhuyse R.M., Kuhlmann E.D., Bijvelt J., Verkleij A.J., Ververgaert P.H. Lens membranes. III. Freeze fracture morphology and composition of bovine lens fibre membranes in relation to ageing. Exp. Eye Res. 26:1978;147-156.
    • (1978) Exp. Eye Res. , vol.26 , pp. 147-156
    • Broekhuyse, R.M.1    Kuhlmann, E.D.2    Bijvelt, J.3    Verkleij, A.J.4    Ververgaert, P.H.5
  • 39
    • 0018615178 scopus 로고
    • Lens membranes. VII. MIP is an immunologically specific component of lens fiber membranes and is identical with 26K band protein
    • Broekhuyse R.M., Kuhlmann E.D., Winkens H.J. Lens membranes. VII. MIP is an immunologically specific component of lens fiber membranes and is identical with 26K band protein. Exp. Eye Res. 29:1979;303-313.
    • (1979) Exp. Eye Res. , vol.29 , pp. 303-313
    • Broekhuyse, R.M.1    Kuhlmann, E.D.2    Winkens, H.J.3
  • 40
    • 0016201791 scopus 로고
    • Lipids in tissues of the eye. X. Molecular species of sphingomyelins from different parts of calf lens in relation to differentiation and aging
    • Broekhuyse R.M., Roelfzema H., Breimer M.E., Karlsson K.A. Lipids in tissues of the eye. X. Molecular species of sphingomyelins from different parts of calf lens in relation to differentiation and aging. Exp. Eye Res. 19:1974;477-484.
    • (1974) Exp. Eye Res. , vol.19 , pp. 477-484
    • Broekhuyse, R.M.1    Roelfzema, H.2    Breimer, M.E.3    Karlsson, K.A.4
  • 41
    • 0031558768 scopus 로고    scopus 로고
    • Structure of detergent-resistant membrane domains: Does phase separation occur in biological membranes?
    • Brown D.A., London E. 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
  • 42
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • Brown D.A., London E. Functions of lipid rafts in biological membranes. Annu. Rev. Cell Dev. Biol. 14:1998;111-136.
    • (1998) Annu. Rev. Cell Dev. Biol. , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 43
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • Brown D.A., Rose J.K. Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell. 68:1992;533-544.
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.2
  • 45
    • 0031965054 scopus 로고    scopus 로고
    • Sphingolipid organization in biomembranes: What physical studies of model membranes reveal
    • Brown R.E. Sphingolipid organization in biomembranes: what physical studies of model membranes reveal. J. Cell. Sci. 111:1998;1-9.
    • (1998) J. Cell. Sci. , vol.111 , pp. 1-9
    • Brown, R.E.1
  • 46
    • 0023849544 scopus 로고
    • Conformation of the polar headgroup of sphingomyelin and its analogues
    • Bruzik K.S. Conformation of the polar headgroup of sphingomyelin and its analogues. Biochim. Biophys. Acta. 939:1988;315-326.
    • (1988) Biochim. Biophys. Acta , vol.939 , pp. 315-326
    • Bruzik, K.S.1
  • 47
    • 0031915441 scopus 로고    scopus 로고
    • Dual parallel mass spectrometers for analysis of sphingolipid, glycerophospholipid and plasmalogen molecular species
    • Byrdwell W.C. Dual parallel mass spectrometers for analysis of sphingolipid, glycerophospholipid and plasmalogen molecular species. Rapid Commun. Mass Spectrom. 12:1998;256-272.
    • (1998) Rapid Commun. Mass Spectrom. , vol.12 , pp. 256-272
    • Byrdwell, W.C.1
  • 49
    • 0018405887 scopus 로고
    • Sphingomyelin - Lecithin bilayers and their interaction with cholesterol
    • Calhoun W.I., Shipley G.G. Sphingomyelin - lecithin bilayers and their interaction with cholesterol. Biochemistry. 18:1979;1717-1722.
    • (1979) Biochemistry , vol.18 , pp. 1717-1722
    • Calhoun, W.I.1    Shipley, G.G.2
  • 50
    • 0027162454 scopus 로고
    • Protein kinase C activity and its relationship to myo-inositol uptake during hyperglycemic conditions in cultured bovine lens epithelial cells
    • Cammarata P.R., Fan W., Jin Y., Yorio T. Protein kinase C activity and its relationship to myo-inositol uptake during hyperglycemic conditions in cultured bovine lens epithelial cells. Curr. Eye Res. 12:1993;403-412.
    • (1993) Curr. Eye Res. , vol.12 , pp. 403-412
    • Cammarata, P.R.1    Fan, W.2    Jin, Y.3    Yorio, T.4
  • 51
    • 0021927657 scopus 로고
    • Regional distribution of lipids and phospholipase A2 activity in normal and cataractous rat lens
    • Cenedella R.J. Regional distribution of lipids and phospholipase A2 activity in normal and cataractous rat lens. Curr. Eye Res. 4:1985;113-120.
    • (1985) Curr. Eye Res. , vol.4 , pp. 113-120
    • Cenedella, R.J.1
  • 52
    • 0023201812 scopus 로고
    • Direct chemical measurement of DNA synthesis and net rates of differentiation of rat lens epithelial cells in vivo: Applied to the selenium cataract
    • Cenedella R.J. Direct chemical measurement of DNA synthesis and net rates of differentiation of rat lens epithelial cells in vivo: applied to the selenium cataract. Exp. Eye Res. 44:1987;677-690.
    • (1987) Exp. Eye Res. , vol.44 , pp. 677-690
    • Cenedella, R.J.1
  • 53
    • 0024566191 scopus 로고
    • Aging and rates of lens-cell differentiation in vivo, measured by a chemical approach
    • Cenedella R.J. Aging and rates of lens-cell differentiation in vivo, measured by a chemical approach. Invest. Ophthalmol. Vis. Sci. 30:1989a;575-579.
    • (1989) Invest. Ophthalmol. Vis. Sci. , vol.30 , pp. 575-579
    • Cenedella, R.J.1
  • 54
    • 0024547714 scopus 로고
    • Cell cycle specific effects of selenium on the lens epithelium studied in vivo by the direct chemical approach
    • Cenedella R.J. Cell cycle specific effects of selenium on the lens epithelium studied in vivo by the direct chemical approach. Curr. Eye Res. 8:1989b;429-433.
    • (1989) Curr. Eye Res. , vol.8 , pp. 429-433
    • Cenedella, R.J.1
  • 55
    • 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
  • 56
    • 0030026343 scopus 로고    scopus 로고
    • Cholesterol and cataracts
    • Cenedella R.J. Cholesterol and cataracts. Surv. Ophthalmol. 40:1996;320-337.
    • (1996) Surv. Ophthalmol. , vol.40 , pp. 320-337
    • Cenedella, R.J.1
  • 57
    • 0030694454 scopus 로고    scopus 로고
    • Myelin contains neutral sphingomyelinase activity that is stimulated by tumor necrosis factor-alpha
    • Chakraborty G., Ziemba S., Drivas A., Ledeen R.W. Myelin contains neutral sphingomyelinase activity that is stimulated by tumor necrosis factor-alpha. J. Neurosci. Res. 50:1997;466-476.
    • (1997) J. Neurosci. Res. , vol.50 , pp. 466-476
    • Chakraborty, G.1    Ziemba, S.2    Drivas, A.3    Ledeen, R.W.4
  • 58
    • 0027349865 scopus 로고
    • Neutral sphingomyelinase
    • Chatterjee S. Neutral sphingomyelinase. Adv. Lipid Res. 26:1993;25-48.
    • (1993) Adv. Lipid Res. , vol.26 , pp. 25-48
    • Chatterjee, S.1
  • 60
    • 0034009392 scopus 로고    scopus 로고
    • Characterization of alpha-crystallin-plasma membrane binding
    • [Erratum appears in J. Biol. Chem. 277 (2) (2002) 1628]
    • Cobb B.A., Petrash J.M. Characterization of alpha-crystallin-plasma membrane binding. J. Biol. Chem. 275:2000;6664-6672. [Erratum appears in J. Biol. Chem. 277 (2) (2002) 1628].
    • (2000) J. Biol. Chem. , vol.275 , pp. 6664-6672
    • Cobb, B.A.1    Petrash, J.M.2
  • 61
    • 0037080002 scopus 로고    scopus 로고
    • Alpha-Crystallin chaperone-like activity and membrane binding in age-related cataracts
    • Cobb B.A., Petrash J.M. alpha-Crystallin chaperone-like activity and membrane binding in age-related cataracts. Biochemistry. 41:2002a;483-490.
    • (2002) Biochemistry , vol.41 , pp. 483-490
    • Cobb, B.A.1    Petrash, J.M.2
  • 62
    • 0036974373 scopus 로고    scopus 로고
    • Factors influencing alpha-crystallin association with phospholipid vesicles
    • Cobb B.A., Petrash J.M. Factors influencing alpha-crystallin association with phospholipid vesicles. Mol. Vis. 8:2002b;85-93.
    • (2002) Mol. Vis. , vol.8 , pp. 85-93
    • Cobb, B.A.1    Petrash, J.M.2
  • 63
    • 0032486433 scopus 로고    scopus 로고
    • Teratogen-mediated inhibition of target tissue response to Shh signaling [see comments]
    • Cooper M.K., Porter J.A., Young K.E., Beachy P.A. Teratogen-mediated inhibition of target tissue response to Shh signaling [see comments]. Science. 280:1998;1603-1607.
    • (1998) Science , vol.280 , pp. 1603-1607
    • Cooper, M.K.1    Porter, J.A.2    Young, K.E.3    Beachy, P.A.4
  • 64
    • 0018164774 scopus 로고
    • Cholesterol and phospholipids in protein fractions of human lens and senile cataract
    • Cotlier E., Obara Y., Toftness B. Cholesterol and phospholipids in protein fractions of human lens and senile cataract. Biochim. Biophys. Acta. 530:1978;267-278.
    • (1978) Biochim. Biophys. Acta , vol.530 , pp. 267-278
    • Cotlier, E.1    Obara, Y.2    Toftness, B.3
  • 65
    • 0037203316 scopus 로고    scopus 로고
    • Sphingosine in apoptosis signaling
    • Cuvillier O. Sphingosine in apoptosis signaling. Biochim. Biophys. Act. 1585:2002;153-162.
    • (2002) Biochim. Biophys. Act. , vol.1585 , pp. 153-162
    • Cuvillier, O.1
  • 66
    • 0031918326 scopus 로고    scopus 로고
    • An apical-type trafficking pathway is present in cultured oligodendrocytes but the sphingolipid-enriched myelin membrane is the target of a basolateral-type pathway
    • de Vries H., Schrage C., Hoekstra D. An apical-type trafficking pathway is present in cultured oligodendrocytes but the sphingolipid-enriched myelin membrane is the target of a basolateral-type pathway. Mol. Biol. Cell. 9:1998;599-609.
    • (1998) Mol. Biol. Cell. , vol.9 , pp. 599-609
    • De Vries, H.1    Schrage, C.2    Hoekstra, D.3
  • 67
    • 0017615489 scopus 로고
    • The preferential interaction of cholesterol with different classes of phospholipids
    • Demel R.A., Jansen J.W., van Dijck P.W., van Deenen L.L. The preferential interaction of cholesterol with different classes of phospholipids. Biochim. Biophys. Acta. 465:1977;1-10.
    • (1977) Biochim. Biophys. Acta , vol.465 , pp. 1-10
    • Demel, R.A.1    Jansen, J.W.2    Van Dijck, P.W.3    Van Deenen, L.L.4
  • 68
    • 0026524746 scopus 로고
    • Effect of osmotic stress on phosphorylcholine efflux and turnover in rat lenses
    • Desouky M.A., Geller A.M., Jernigan H.M. Jr. Effect of osmotic stress on phosphorylcholine efflux and turnover in rat lenses. Exp. Eye Res. 54:1992;269-276.
    • (1992) Exp. Eye Res. , vol.54 , pp. 269-276
    • Desouky, M.A.1    Geller, A.M.2    Jernigan, H.M.Jr.3
  • 69
    • 0025119208 scopus 로고
    • Evidence for a role of phosphatidylcholine-hydrolysing phospholipase C in the regulation of protein kinase C by ras and src oncogenes
    • Diaz-Laviada I., Larrodera P., Diaz-Meco M.T., Cornet M.E., Guddal P.H., Johansen T., Moscat J. Evidence for a role of phosphatidylcholine-hydrolysing phospholipase C in the regulation of protein kinase C by ras and src oncogenes. EMBO J. 9:1990;3907-3912.
    • (1990) EMBO J. , vol.9 , pp. 3907-3912
    • Diaz-Laviada, I.1    Larrodera, P.2    Diaz-Meco, M.T.3    Cornet, M.E.4    Guddal, P.H.5    Johansen, T.6    Moscat, J.7
  • 70
    • 0037071871 scopus 로고    scopus 로고
    • Sphingolipid functions in Saccharomyces cerevisiae
    • Dickson R.C., Lester R.L. Sphingolipid functions in Saccharomyces cerevisiae. Biochim. Biophys. Acta. 1583:2002;13-25.
    • (2002) Biochim. Biophys. Acta , vol.1583 , pp. 13-25
    • Dickson, R.C.1    Lester, R.L.2
  • 72
    • 0029050618 scopus 로고
    • New approach to assess the cholesterol distribution in the eye lens: Confocal Raman microspectroscopy and filipin cytochemistry
    • Duindam H.J., Vrensen G.F., Otto C., Puppels G.J., Greve J. New approach to assess the cholesterol distribution in the eye lens: confocal Raman microspectroscopy and filipin cytochemistry. J. Lipid Res. 36:1995;1139-1146.
    • (1995) J. Lipid Res. , vol.36 , pp. 1139-1146
    • Duindam, H.J.1    Vrensen, G.F.2    Otto, C.3    Puppels, G.J.4    Greve, J.5
  • 73
    • 0029986547 scopus 로고    scopus 로고
    • Aging affects the conformation of cholesterol in the human eye lens
    • Duindam J.J., Vrensen G.F., Otto C., Greve J. Aging affects the conformation of cholesterol in the human eye lens. Ophthalmic. Res. 28(Suppl. 1):1996;86-91.
    • (1996) Ophthalmic. Res. , vol.28 , Issue.SUPPL. 1 , pp. 86-91
    • Duindam, J.J.1    Vrensen, G.F.2    Otto, C.3    Greve, J.4
  • 74
    • 0031975419 scopus 로고    scopus 로고
    • Cholesterol, phospholipid, and protein changes in focal opacities in the human eye lens
    • Duindam J.J., Vrensen G.F., Otto C., Greve J. Cholesterol, phospholipid, and protein changes in focal opacities in the human eye lens. Invest. Ophthalmol. Vis. Sci. 39:1998;94-103.
    • (1998) Invest. Ophthalmol. Vis. Sci. , vol.39 , pp. 94-103
    • Duindam, J.J.1    Vrensen, G.F.2    Otto, C.3    Greve, J.4
  • 75
    • 0033786113 scopus 로고    scopus 로고
    • Overexpression of PAX6(5a) in lens fiber cells results in cataract and upregulation of (alpha)5(beta)1 integrin expression
    • Duncan M.K., Kozmik Z., Cveklova K., Piatigorsky J., Cvekl A. Overexpression of PAX6(5a) in lens fiber cells results in cataract and upregulation of (alpha)5(beta)1 integrin expression. J. Cell. Sci. 113:2000;3173-3185.
    • (2000) J. Cell. Sci. , vol.113 , pp. 3173-3185
    • Duncan, M.K.1    Kozmik, Z.2    Cveklova, K.3    Piatigorsky, J.4    Cvekl, A.5
  • 76
    • 0037165460 scopus 로고    scopus 로고
    • Cooperative hydrogen- and πh-bonded interactions involving water and the ethylenic double bond
    • DuPré D.B., Yappert M.C. Cooperative hydrogen- and πH-bonded interactions involving water and the ethylenic double bond. J. Phys. Chem. Part A. 106:2002;567-574.
    • (2002) J. Phys. Chem. Part a , vol.106 , pp. 567-574
    • Dupré, D.B.1    Yappert, M.C.2
  • 77
    • 0028070290 scopus 로고
    • Rat lens choline and ethanolamine kinases: Independent kinetics in intact tissue-competition in homogenates
    • Ekambaram M.C., Jernigan H.M. Jr. Rat lens choline and ethanolamine kinases: independent kinetics in intact tissue-competition in homogenates. Biochim. Biophys. Acta. 1213:1994;289-294.
    • (1994) Biochim. Biophys. Acta , vol.1213 , pp. 289-294
    • Ekambaram, M.C.1    Jernigan, H.M.Jr.2
  • 78
    • 0023205581 scopus 로고
    • Relationship of cholesterolgenesis to DNA synthesis and proliferation by lens epithelial cells in culture
    • el-Sayed G.N., Cenedella R.J. Relationship of cholesterolgenesis to DNA synthesis and proliferation by lens epithelial cells in culture. Exp. Eye Res. 45:1987;443-451.
    • (1987) Exp. Eye Res. , vol.45 , pp. 443-451
    • El-Sayed, G.N.1    Cenedella, R.J.2
  • 79
    • 0038637713 scopus 로고    scopus 로고
    • Cholesterol in bilayers of sphingomyelin or dihydrosphingomyelin at concentrations found in ocular lens membranes
    • Epand R.M. Cholesterol in bilayers of sphingomyelin or dihydrosphingomyelin at concentrations found in ocular lens membranes. Biophys. J. 84:2003;3102-3110.
    • (2003) Biophys. J. , vol.84 , pp. 3102-3110
    • Epand, R.M.1
  • 80
    • 0014101583 scopus 로고
    • Human ocular lipids: Their analysis and distribution
    • Feldman G.L. Human ocular lipids: their analysis and distribution. Surv. Ophthalmol. 12:1967;207-243.
    • (1967) Surv. Ophthalmol. , vol.12 , pp. 207-243
    • Feldman, G.L.1
  • 81
    • 0029745714 scopus 로고    scopus 로고
    • Confirmation of the identity of the major phospholipid in human lens membranes
    • Ferguson S.R., Borchman D., Yappert M.C. Confirmation of the identity of the major phospholipid in human lens membranes. Invest. Ophthalmol. Vis. Sci. 37:1996;1703-1706.
    • (1996) Invest. Ophthalmol. Vis. Sci. , vol.37 , pp. 1703-1706
    • Ferguson, S.R.1    Borchman, D.2    Yappert, M.C.3
  • 83
    • 0034630316 scopus 로고    scopus 로고
    • N-Cadherin function is required for differentiation-dependent cytoskeletal reorganization in lens cells in vitro
    • Ferreira-Cornwell M.C., Veneziale R.W., Grunwald G.B., Menko A.S. N-Cadherin function is required for differentiation-dependent cytoskeletal reorganization in lens cells in vitro. Exp. Cell Res. 256:2000;237-247.
    • (2000) Exp. Cell Res. , vol.256 , pp. 237-247
    • Ferreira-Cornwell, M.C.1    Veneziale, R.W.2    Grunwald, G.B.3    Menko, A.S.4
  • 84
    • 0031706594 scopus 로고    scopus 로고
    • Caveolin is present in intestinal cells: Role in cholesterol trafficking?
    • Field F.J., Born E., Murthy S., Mathur S.N. Caveolin is present in intestinal cells: role in cholesterol trafficking? J. Lipid Res. 39:1998;1938-1950.
    • (1998) J. Lipid Res. , vol.39 , pp. 1938-1950
    • Field, F.J.1    Born, E.2    Murthy, S.3    Mathur, S.N.4
  • 85
    • 0030809601 scopus 로고    scopus 로고
    • Intracellular cholesterol transport
    • Fielding C.J., Fielding P.E. Intracellular cholesterol transport. J. Lipid Res. 38:1997;1503-1521.
    • (1997) J. Lipid Res. , vol.38 , pp. 1503-1521
    • Fielding, C.J.1    Fielding, P.E.2
  • 86
    • 0023685315 scopus 로고
    • Specific restriction of cholesterol from cortical lens gap junctional membrane in the U18666A cataract
    • Fleschner C.R., Cenedella R.J. Specific restriction of cholesterol from cortical lens gap junctional membrane in the U18666A cataract. Curr. Eye Res. 7:1988;1029-1034.
    • (1988) Curr. Eye Res. , vol.7 , pp. 1029-1034
    • Fleschner, C.R.1    Cenedella, R.J.2
  • 87
    • 0025959169 scopus 로고
    • Lipid composition of lens plasma membrane fractions enriched in fiber junctions
    • Fleschner C.R., Cenedella R.J. Lipid composition of lens plasma membrane fractions enriched in fiber junctions. J. Lipid Res. 32:1991;45-53.
    • (1991) J. Lipid Res. , vol.32 , pp. 45-53
    • Fleschner, C.R.1    Cenedella, R.J.2
  • 88
    • 0026640588 scopus 로고
    • Examination of a lens 'native' plasma membrane fraction and its associated crystallins
    • Fleschner C.R., Cenedella R.J. Examination of a lens 'native' plasma membrane fraction and its associated crystallins. Curr. Eye Res. 11:1992;739-752.
    • (1992) Curr. Eye Res. , vol.11 , pp. 739-752
    • Fleschner, C.R.1    Cenedella, R.J.2
  • 89
    • 0027285778 scopus 로고
    • Isolation of a non-sedimenting membrane fraction from the water soluble fraction of bovine lens
    • Fleschner C.R., Cenedella R.J. Isolation of a non-sedimenting membrane fraction from the water soluble fraction of bovine lens. Exp. Eye Res. 56:1993;649-657.
    • (1993) Exp. Eye Res. , vol.56 , pp. 649-657
    • Fleschner, C.R.1    Cenedella, R.J.2
  • 90
    • 0030937605 scopus 로고    scopus 로고
    • Neutral lipids of the plasma membrane: Composition of plasma membrane fractions isolated from ocular lens
    • Fleschner C.R., Cenedella R.J. Neutral lipids of the plasma membrane: composition of plasma membrane fractions isolated from ocular lens. Curr. Eye Res. 16:1997;263-269.
    • (1997) Curr. Eye Res. , vol.16 , pp. 263-269
    • Fleschner, C.R.1    Cenedella, R.J.2
  • 92
    • 0032516835 scopus 로고    scopus 로고
    • Cholesterol depletion of caveolae causes hyperactivation of extracellular signal-related kinase (ERK)
    • Furuchi T., Anderson R.G. Cholesterol depletion of caveolae causes hyperactivation of extracellular signal-related kinase (ERK). J. Biol. Chem. 273:1998;21099-21104.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21099-21104
    • Furuchi, T.1    Anderson, R.G.2
  • 93
    • 0032508379 scopus 로고    scopus 로고
    • Purification and characterization of ceramide-activated protein phosphatases
    • Galadari S., Kishikawa K., Kamibayashi C., Mumby M.C., Hannun Y.A. Purification and characterization of ceramide-activated protein phosphatases. Biochemistry. 37:1998;11232-11238.
    • (1998) Biochemistry , vol.37 , pp. 11232-11238
    • Galadari, S.1    Kishikawa, K.2    Kamibayashi, C.3    Mumby, M.C.4    Hannun, Y.A.5
  • 95
    • 1442266178 scopus 로고    scopus 로고
    • DNA repair and cellular resistance to alkylating agents in chronic lymphocytic leukemia
    • Giblin F.J., Lin L.R., Chakrapani B., Muller M.R. DNA repair and cellular resistance to alkylating agents in chronic lymphocytic leukemia. Invest. Ophthalmol. Vis. Sci. 39:1998;344-350.
    • (1998) Invest. Ophthalmol. Vis. Sci. , vol.39 , pp. 344-350
    • Giblin, F.J.1    Lin, L.R.2    Chakrapani, B.3    Muller, M.R.4
  • 96
    • 0032078787 scopus 로고    scopus 로고
    • Cholesterol oxides accumulate in human cataracts
    • Girao H., Mota M.C., Ramalho J., Pereira P. Cholesterol oxides accumulate in human cataracts. Exp. Eye Res. 66:1998;645-652.
    • (1998) Exp. Eye Res. , vol.66 , pp. 645-652
    • Girao, H.1    Mota, M.C.2    Ramalho, J.3    Pereira, P.4
  • 98
    • 0029609895 scopus 로고
    • Functional role of glycosphingolipids in cell recognition and signaling
    • Hakomori S., Igarashi Y. Functional role of glycosphingolipids in cell recognition and signaling. J. Biochem. (Tokyo). 118:1995;1091-1103.
    • (1995) J. Biochem. (Tokyo) , vol.118 , pp. 1091-1103
    • Hakomori, S.1    Igarashi, Y.2
  • 99
    • 0031928904 scopus 로고    scopus 로고
    • Signal transduction through glyco(sphingo)lipids. Introduction and recent studies on glyco(sphingo)lipid-enriched microdomains
    • Hakomori S., Yamamura S., Handa A.K. Signal transduction through glyco(sphingo)lipids. Introduction and recent studies on glyco(sphingo)lipid- enriched microdomains. Ann. N.Y. Acad. Sci. 845:1998;1-10.
    • (1998) Ann. N.Y. Acad. Sci. , vol.845 , pp. 1-10
    • Hakomori, S.1    Yamamura, S.2    Handa, A.K.3
  • 100
    • 0027994349 scopus 로고
    • The sphingomyelin cycle and the second messenger function of ceramide
    • Hannun Y.A. The sphingomyelin cycle and the second messenger function of ceramide. J. Biol. Chem. 269:1994;3125-3128.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3125-3128
    • Hannun, Y.A.1
  • 101
    • 0030448021 scopus 로고    scopus 로고
    • Functions of ceramide in coordinating cellular responses to stress
    • Hannun Y.A. Functions of ceramide in coordinating cellular responses to stress. Science. 274:1996;1855-1859.
    • (1996) Science , vol.274 , pp. 1855-1859
    • Hannun, Y.A.1
  • 102
    • 0027762512 scopus 로고
    • Sphingolipid breakdown products: Anti-proliferative and tumor-suppressor lipids
    • Hannun Y.A., Linardic C.M. Sphingolipid breakdown products: anti-proliferative and tumor-suppressor lipids. Biochim. Biophys. Acta. 1154:1993;223-236.
    • (1993) Biochim. Biophys. Acta , vol.1154 , pp. 223-236
    • Hannun, Y.A.1    Linardic, C.M.2
  • 103
    • 0022974603 scopus 로고
    • Sphingosine inhibition of protein kinase C activity and of phorbol dibutyrate binding in vitro and in human platelets
    • Hannun Y.A., Loomis C.R., Merrill A.H. Jr., Bell R.M. Sphingosine inhibition of protein kinase C activity and of phorbol dibutyrate binding in vitro and in human platelets. J. Biol. Chem. 261:1986;12604-12609.
    • (1986) J. Biol. Chem. , vol.261 , pp. 12604-12609
    • Hannun, Y.A.1    Loomis, C.R.2    Merrill, A.H.Jr.3    Bell, R.M.4
  • 104
    • 0028855405 scopus 로고
    • Ceramide: An intracellular signal for apoptosis
    • Hannun Y.A., Obeid L.M. Ceramide: an intracellular signal for apoptosis. Trends Biochem. Sci. 20:1995;73-77.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 73-77
    • Hannun, Y.A.1    Obeid, L.M.2
  • 105
    • 0031750335 scopus 로고    scopus 로고
    • Lipid domain structure of the plasma membrane revealed by patching of membrane components
    • Harder T., Scheiffele P., Verkade P., Simons K. Lipid domain structure of the plasma membrane revealed by patching of membrane components. J. Cell Biol. 141:1998;929-942.
    • (1998) J. Cell Biol. , vol.141 , pp. 929-942
    • Harder, T.1    Scheiffele, P.2    Verkade, P.3    Simons, K.4
  • 106
    • 0030878573 scopus 로고    scopus 로고
    • Caveolae, DIGs, and the dynamics of sphingolipid-cholesterol microdomains
    • Harder T., Simons K. Caveolae, DIGs, and the dynamics of sphingolipid-cholesterol microdomains. Curr. Opin. Cell Biol. 9:1997;534-542.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 534-542
    • Harder, T.1    Simons, K.2
  • 107
    • 0022396961 scopus 로고
    • Absolute rates of sterol synthesis estimated from [3H]water for bovine lens epithelial cells in culture
    • Hitchener W.R., 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
  • 108
    • 0023394806 scopus 로고
    • HMG CoA reductase activity of lens epithelial cells: Compared with true rates of sterol synthesis
    • Hitchener W.R., Cenedella R.J. HMG CoA reductase activity of lens epithelial cells: compared with true rates of sterol synthesis. Curr. Eye Res. 6:1987;1045-1049.
    • (1987) Curr. Eye Res. , vol.6 , pp. 1045-1049
    • Hitchener, W.R.1    Cenedella, R.J.2
  • 109
    • 0028330335 scopus 로고
    • The effect of age on glutathione peroxidase and glutathione reductase activities in lenses of Old World simians and prosimians
    • Holleschau A.M., Rathbun W.B. The effect of age on glutathione peroxidase and glutathione reductase activities in lenses of Old World simians and prosimians. Curr. Eye Res. 13:1994;331-336.
    • (1994) Curr. Eye Res. , vol.13 , pp. 331-336
    • Holleschau, A.M.1    Rathbun, W.B.2
  • 110
    • 0033055564 scopus 로고    scopus 로고
    • Detergent-insoluble glycosphingolipid/cholesterol-rich membrane domains, lipid rafts and caveolae (review)
    • Hooper N.M. Detergent-insoluble glycosphingolipid/cholesterol-rich membrane domains, lipid rafts and caveolae (review). Mol. Membr. Biol. 16:1999;145-156.
    • (1999) Mol. Membr. Biol. , vol.16 , pp. 145-156
    • Hooper, N.M.1
  • 111
    • 0023607231 scopus 로고
    • Conformational properties of the main intrinsic polypeptide (MIP26) isolated from lens plasma membranes
    • Horwitz J., Bok D. Conformational properties of the main intrinsic polypeptide (MIP26) isolated from lens plasma membranes. Biochemistry. 26:1987;8092-8098.
    • (1987) Biochemistry , vol.26 , pp. 8092-8098
    • Horwitz, J.1    Bok, D.2
  • 112
    • 0024340465 scopus 로고
    • Differential binding of alpha-crystallins to bovine lens membrane
    • Ifeanyi F., Takemoto L. Differential binding of alpha-crystallins to bovine lens membrane. Exp. Eye Res. 49:1989;143-147.
    • (1989) Exp. Eye Res. , vol.49 , pp. 143-147
    • Ifeanyi, F.1    Takemoto, L.2
  • 113
    • 0025095434 scopus 로고
    • Alpha crystallin from human cataractous versus normal lenses: Change in binding to lens membrane
    • Ifeanyi F., Takemoto L. Alpha crystallin from human cataractous versus normal lenses: change in binding to lens membrane. Exp. Eye Res. 50:1990a;113-116.
    • (1990) Exp. Eye Res. , vol.50 , pp. 113-116
    • Ifeanyi, F.1    Takemoto, L.2
  • 114
    • 0025374422 scopus 로고
    • Specificity of alpha crystallin binding to the lens membrane
    • Ifeanyi F., Takemoto L. Specificity of alpha crystallin binding to the lens membrane. Curr. Eye Res. 9:1990b;259-265.
    • (1990) Curr. Eye Res. , vol.9 , pp. 259-265
    • Ifeanyi, F.1    Takemoto, L.2
  • 115
    • 0025909564 scopus 로고
    • Interaction of lens crystallins with lipid vesicles
    • Ifeanyi F., Takemoto L. Interaction of lens crystallins with lipid vesicles. Exp. Eye Res. 52:1991;535-538.
    • (1991) Exp. Eye Res. , vol.52 , pp. 535-538
    • Ifeanyi, F.1    Takemoto, L.2
  • 116
    • 0030911667 scopus 로고    scopus 로고
    • Molecular mechanisms of intracellular cholesterol transport
    • Ikonen E. Molecular mechanisms of intracellular cholesterol transport. Curr. Opin. Lipidol. 8:1997;60-64.
    • (1997) Curr. Opin. Lipidol. , vol.8 , pp. 60-64
    • Ikonen, E.1
  • 117
    • 0031723219 scopus 로고    scopus 로고
    • The teratogenic Veratrum alkaloid cyclopamine inhibits sonic hedgehog signal transduction
    • Incardona J.P., Gaffield W., Kapur R.P., Roelink H. The teratogenic Veratrum alkaloid cyclopamine inhibits sonic hedgehog signal transduction. Development. 125:1998;3553-3562.
    • (1998) Development , vol.125 , pp. 3553-3562
    • Incardona, J.P.1    Gaffield, W.2    Kapur, R.P.3    Roelink, H.4
  • 120
    • 0028146621 scopus 로고
    • Coordination of membrane phospholipid synthesis with the cell cycle
    • Jackowski S. Coordination of membrane phospholipid synthesis with the cell cycle. J. Biol. Chem. 269:1994;3858-3867.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3858-3867
    • Jackowski, S.1
  • 121
    • 0029786402 scopus 로고    scopus 로고
    • Cell cycle regulation of membrane phospholipid metabolism
    • Jackowski S. Cell cycle regulation of membrane phospholipid metabolism. J. Biol. Chem. 271:1996;20219-20222.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20219-20222
    • Jackowski, S.1
  • 122
    • 0033615688 scopus 로고    scopus 로고
    • Direct evidence for immiscible cholesterol domains in human ocular lens fiber cell plasma membranes
    • Jacob R.F., Cenedella R.J., Mason R.P. Direct evidence for immiscible cholesterol domains in human ocular lens fiber cell plasma membranes. J. Biol. Chem. 274:1999;31613-31618.
    • (1999) J. Biol. Chem. , vol.274 , pp. 31613-31618
    • Jacob, R.F.1    Cenedella, R.J.2    Mason, R.P.3
  • 123
    • 0035957941 scopus 로고    scopus 로고
    • Evidence for distinct cholesterol domains in fiber cell membranes from cataractous human lenses
    • Jacob R.F., Cenedella R.J., Mason R.P. Evidence for distinct cholesterol domains in fiber cell membranes from cataractous human lenses. J. Biol. Chem. 276:2001;13573-13578.
    • (2001) J. Biol. Chem. , vol.276 , pp. 13573-13578
    • Jacob, R.F.1    Cenedella, R.J.2    Mason, R.P.3
  • 124
    • 0029156287 scopus 로고
    • Purification and oligomeric state of the major lens fiber cell membrane proteins
    • Jarvis L.J., Louis C.F. Purification and oligomeric state of the major lens fiber cell membrane proteins. Curr. Eye Res. 14:1995;799-808.
    • (1995) Curr. Eye Res. , vol.14 , pp. 799-808
    • Jarvis, L.J.1    Louis, C.F.2
  • 126
    • 0027518611 scopus 로고
    • Efflux and hydrolysis of phosphorylethanolamine and phosphorylcholine in stressed cultured rat lenses
    • Jernigan H.M. Jr., Desouky M.A., Geller A.M., Blum P.S., Ekambaram M.C. Efflux and hydrolysis of phosphorylethanolamine and phosphorylcholine in stressed cultured rat lenses. Exp. Eye Res. 56:1993;25-33.
    • (1993) Exp. Eye Res. , vol.56 , pp. 25-33
    • Jernigan, H.M.Jr.1    Desouky, M.A.2    Geller, A.M.3    Blum, P.S.4    Ekambaram, M.C.5
  • 128
    • 0024351562 scopus 로고
    • Phosphorylcholine and phosphorylethanolamine in human and rhesus monkey lenses
    • Jernigan H.M. Jr., Zigler J.S. Jr. Phosphorylcholine and phosphorylethanolamine in human and rhesus monkey lenses. Exp. Eye Res. 49:1989;901-909.
    • (1989) Exp. Eye Res. , vol.49 , pp. 901-909
    • Jernigan, H.M.Jr.1    Zigler, J.S.Jr.2
  • 129
    • 0025941734 scopus 로고
    • Interaction of cholesterol with sphingomyelin in bilayer membranes: Evidence that the hydroxy group of sphingomyelin does not modulate the rate of cholesterol exchange between vesicles
    • Kan C.C., Ruan Z.S., Bittman R. Interaction of cholesterol with sphingomyelin in bilayer membranes: evidence that the hydroxy group of sphingomyelin does not modulate the rate of cholesterol exchange between vesicles. Biochemistry. 30:1991;7759-7766.
    • (1991) Biochemistry , vol.30 , pp. 7759-7766
    • Kan, C.C.1    Ruan, Z.S.2    Bittman, R.3
  • 130
    • 0033564253 scopus 로고    scopus 로고
    • TNF-alpha-mediated apoptosis is initiated in caveolae-like domains
    • Ko Y.G., Lee J.S., Kang Y.S., Ahn J.H., Seo J.S. TNF-alpha-mediated apoptosis is initiated in caveolae-like domains. J. Immunol. 162:1999;7217-7223.
    • (1999) J. Immunol. , vol.162 , pp. 7217-7223
    • Ko, Y.G.1    Lee, J.S.2    Kang, Y.S.3    Ahn, J.H.4    Seo, J.S.5
  • 131
    • 0023871074 scopus 로고
    • Characterization of disulfide-linked crystallins associated with human cataractous lens membranes
    • Kodama T., Takemoto L. Characterization of disulfide-linked crystallins associated with human cataractous lens membranes. Invest. Ophthalmol. Vis. Sci. 29:1988;145-149.
    • (1988) Invest. Ophthalmol. Vis. Sci. , vol.29 , pp. 145-149
    • Kodama, T.1    Takemoto, L.2
  • 134
    • 0035033848 scopus 로고    scopus 로고
    • Membrane properties of D-erythro-N-acyl sphingomyelins and their corresponding dihydro species
    • Kuikka M., Ramstedt B., Ohvo-Rekila H., Tuuf J., Slotte J.P. Membrane properties of D-erythro-N-acyl sphingomyelins and their corresponding dihydro species. Biophys. J. 80:2001;2327-2337.
    • (2001) Biophys. J. , vol.80 , pp. 2327-2337
    • Kuikka, M.1    Ramstedt, B.2    Ohvo-Rekila, H.3    Tuuf, J.4    Slotte, J.P.5
  • 136
    • 0038765831 scopus 로고    scopus 로고
    • Scanning electron micrographs
    • Phelps Brown, N.A., Bron, A.J. (Eds.). Butterworth-Heinemann, Oxford
    • Kuszak, J.R., 1996. Scanning electron micrographs. In: Phelps Brown, N.A., Bron, A.J. (Eds.), Lens Disorders. Butterworth-Heinemann, Oxford, p. 41.
    • (1996) Lens Disorders , pp. 41
    • Kuszak, J.R.1
  • 137
    • 0022459258 scopus 로고
    • Phosphorylation of lens intrinsic membrane proteins by protein kinase C
    • Lampe P.D., Bazzi M.D., Nelsestuen G.L., Johnson R.G. Phosphorylation of lens intrinsic membrane proteins by protein kinase C. Eur. J. Biochem. 156:1986;351-357.
    • (1986) Eur. J. Biochem. , vol.156 , pp. 351-357
    • Lampe, P.D.1    Bazzi, M.D.2    Nelsestuen, G.L.3    Johnson, R.G.4
  • 138
    • 0038089272 scopus 로고
    • Eye lens weight and age in African elephants
    • Laws R.M. Eye lens weight and age in African elephants. E. Afric. Wild. J. 5:1967;46-52.
    • (1967) E. Afric. Wild. J. , vol.5 , pp. 46-52
    • Laws, R.M.1
  • 139
    • 0035827604 scopus 로고    scopus 로고
    • Caspase remodeling of the spectrin membrane skeleton during lens development and aging
    • Lee A., Morrow J.S., Fowler V.M. Caspase remodeling of the spectrin membrane skeleton during lens development and aging. J. Biol. Chem. 276:2001;20735-20742.
    • (2001) J. Biol. Chem. , vol.276 , pp. 20735-20742
    • Lee, A.1    Morrow, J.S.2    Fowler, V.M.3
  • 140
    • 0028002620 scopus 로고
    • Signal transduction in vascular smooth muscle: Diacylglycerol second messengers and PKC action
    • Lee M.W., Severson D.L. Signal transduction in vascular smooth muscle: diacylglycerol second messengers and PKC action. Am. J. Physiol. 267:1994;C659-C678.
    • (1994) Am. J. Physiol. , vol.267 , pp. 659-C678
    • Lee, M.W.1    Severson, D.L.2
  • 141
    • 0032532276 scopus 로고    scopus 로고
    • The rate of sphingomyelin synthesis de novo is influenced by the level of cholesterol in cultured human skin fibroblasts
    • Leppimaki P., Kronqvist R., Slotte J.P. The rate of sphingomyelin synthesis de novo is influenced by the level of cholesterol in cultured human skin fibroblasts. Biochem. J. 335:1998;285-291.
    • (1998) Biochem. J. , vol.335 , pp. 285-291
    • Leppimaki, P.1    Kronqvist, R.2    Slotte, J.P.3
  • 142
    • 0036214899 scopus 로고    scopus 로고
    • Conformational characterization of ceramides by nuclear magnetic resonance spectroscopy
    • Li L., Tang X., Taylor K.G., DuPre D.B., Yappert M.C. Conformational characterization of ceramides by nuclear magnetic resonance spectroscopy. Biophys. J. 82:2002;2067-2080.
    • (2002) Biophys. J. , vol.82 , pp. 2067-2080
    • Li, L.1    Tang, X.2    Taylor, K.G.3    Dupre, D.B.4    Yappert, M.C.5
  • 143
    • 0023111375 scopus 로고
    • Age dependent lipid and protein changes in individual bovine lenses
    • Li L.K., So L. Age dependent lipid and protein changes in individual bovine lenses. Curr. Eye Res. 6:1987;599-605.
    • (1987) Curr. Eye Res. , vol.6 , pp. 599-605
    • Li, L.K.1    So, L.2
  • 144
    • 0021798840 scopus 로고
    • Membrane cholesterol and phospholipid in consecutive concentric sections of human lenses
    • Li L.K., So L., Spector A. Membrane cholesterol and phospholipid in consecutive concentric sections of human lenses. J. Lipid Res. 26:1985;600-609.
    • (1985) J. Lipid Res. , vol.26 , pp. 600-609
    • Li, L.K.1    So, L.2    Spector, A.3
  • 145
    • 0023070521 scopus 로고
    • Age-dependent changes in the distribution and concentration of human lens cholesterol and phospholipids
    • Li L.K., So L., Spector A. Age-dependent changes in the distribution and concentration of human lens cholesterol and phospholipids. Biochim. Biophys. Acta. 917:1987;112-120.
    • (1987) Biochim. Biophys. Acta , vol.917 , pp. 112-120
    • Li, L.K.1    So, L.2    Spector, A.3
  • 147
    • 0038647272 scopus 로고    scopus 로고
    • Effects of cataractogenesis on the CDP-choline pathway: Changes in ATP concentration and phosphocholine synthesis during and after exposure of rat lenses to sugars in vitro and in vivo
    • Liu Y., Blum P.S., Pabst D.M., Chakrabarti I., Jernigan H.M. Jr. Effects of cataractogenesis on the CDP-choline pathway: changes in ATP concentration and phosphocholine synthesis during and after exposure of rat lenses to sugars in vitro and in vivo. Ophthal. Res. 35:2003;185-191.
    • (2003) Ophthal. Res. , vol.35 , pp. 185-191
    • Liu, Y.1    Blum, P.S.2    Pabst, D.M.3    Chakrabarti, I.4    Jernigan, H.M.Jr.5
  • 148
    • 0036346918 scopus 로고    scopus 로고
    • Lens epithelium-derived growth factor: Increased survival and decreased DNA breakage of human RPE cells induced by oxidative stress
    • Lou M.F., Matsui H. Lens epithelium-derived growth factor: increased survival and decreased DNA breakage of human RPE cells induced by oxidative stress. Exp. Eye Res. 74:2002;113-122.
    • (2002) Exp. Eye Res. , vol.74 , pp. 113-122
    • Lou, M.F.1    Matsui, H.2
  • 149
    • 0030932229 scopus 로고    scopus 로고
    • Expression of FGF-1 and FGF-2 mRNA during lens morphogenesis, differentiation and growth
    • Lovicu F.J., de Longh R.U., McAvoy J.W. Expression of FGF-1 and FGF-2 mRNA during lens morphogenesis, differentiation and growth. Curr. Eye Res. 16:1997;222-230.
    • (1997) Curr. Eye Res. , vol.16 , pp. 222-230
    • Lovicu, F.J.1    De Longh, R.U.2    McAvoy, J.W.3
  • 150
    • 0035691974 scopus 로고    scopus 로고
    • FGF-induced lens cell proliferation and differentiation is dependent on MAPK (ERK1/2) signalling
    • Lovicu F.J., McAvoy J.W. FGF-induced lens cell proliferation and differentiation is dependent on MAPK (ERK1/2) signalling. Development. 128:2001;5075-5084.
    • (2001) Development , vol.128 , pp. 5075-5084
    • Lovicu, F.J.1    McAvoy, J.W.2
  • 152
    • 0034659737 scopus 로고    scopus 로고
    • Spatial and temporal regulation of protein kinase D (PKD)
    • Matthews S.A., Iglesias T., Rozengurt E., Cantrell D. Spatial and temporal regulation of protein kinase D (PKD). EMBO J. 19:2000a;2935-2945.
    • (2000) EMBO J. , vol.19 , pp. 2935-2945
    • Matthews, S.A.1    Iglesias, T.2    Rozengurt, E.3    Cantrell, D.4
  • 153
    • 0034686420 scopus 로고    scopus 로고
    • Protein kinase D. A selective target for antigen receptors and a downstream target for protein kinase C in lymphocytes
    • Matthews S.A., Rozengurt E., Cantrell D. Protein kinase D. A selective target for antigen receptors and a downstream target for protein kinase C in lymphocytes. J. Exp. Med. 191:2000b;2075-2082.
    • (2000) J. Exp. Med. , vol.191 , pp. 2075-2082
    • Matthews, S.A.1    Rozengurt, E.2    Cantrell, D.3
  • 154
    • 0026721034 scopus 로고
    • Interbilayer interactions between sphingomyelin and sphingomyelin/ cholesterol bilayers
    • McIntosh T.J., Simon S.A., Needham D., Huang C.H. Interbilayer interactions between sphingomyelin and sphingomyelin/cholesterol bilayers. Biochemistry. 31:1992a;2020-2024.
    • (1992) Biochemistry , vol.31 , pp. 2020-2024
    • McIntosh, T.J.1    Simon, S.A.2    Needham, D.3    Huang, C.H.4
  • 155
    • 0026740396 scopus 로고
    • Structure and cohesive properties of sphingomyelin/cholesterol bilayers
    • McIntosh T.J., Simon S.A., Needham D., Huang C.H. Structure and cohesive properties of sphingomyelin/cholesterol bilayers. Biochemistry. 31:1992b;2012-2020.
    • (1992) Biochemistry , vol.31 , pp. 2012-2020
    • McIntosh, T.J.1    Simon, S.A.2    Needham, D.3    Huang, C.H.4
  • 156
    • 0025020325 scopus 로고
    • Comparison of membrane phospholipids of the rabbit and pig crystalline lens
    • Meneses P., Greiner J.V., Glonek T. Comparison of membrane phospholipids of the rabbit and pig crystalline lens. Exp. Eye Res. 50:1990;235-240.
    • (1990) Exp. Eye Res. , vol.50 , pp. 235-240
    • Meneses, P.1    Greiner, J.V.2    Glonek, T.3
  • 157
    • 0031970687 scopus 로고    scopus 로고
    • Integrins and development: How might these receptors regulate differentiation of the lens
    • Menko S., Philp N., Veneziale B., Walker J. Integrins and development: how might these receptors regulate differentiation of the lens. Ann. N.Y. Acad. Sci. 842:1998;36-41.
    • (1998) Ann. N.Y. Acad. Sci. , vol.842 , pp. 36-41
    • Menko, S.1    Philp, N.2    Veneziale, B.3    Walker, J.4
  • 158
    • 0036448293 scopus 로고    scopus 로고
    • Lens epithelial cell differentiation
    • Menko S. Lens epithelial cell differentiation. Exp. Eye Res. 75:2002;485-490.
    • (2002) Exp. Eye Res. , vol.75 , pp. 485-490
    • Menko, S.1
  • 160
    • 0025283928 scopus 로고
    • An update of the enzymology and regulation of sphingomyelin metabolism
    • Merrill A.H. Jr., Jones D.D. An update of the enzymology and regulation of sphingomyelin metabolism. Biochim. Biophys. Acta. 1044:1990;1-12.
    • (1990) Biochim. Biophys. Acta , vol.1044 , pp. 1-12
    • Merrill, A.H.Jr.1    Jones, D.D.2
  • 161
    • 0029031099 scopus 로고
    • Sphingolipid biosynthesis de novo by rat hepatocytes in culture. Ceramide and sphingomyelin are associated with, but not required for, very low density lipoprotein secretion
    • Merrill A.H. Jr., Lingrell S., Wang E., Nikolova-Karakashian M., Vales T.R., Vance D.E. Sphingolipid biosynthesis de novo by rat hepatocytes in culture. Ceramide and sphingomyelin are associated with, but not required for, very low density lipoprotein secretion. J. Biol. Chem. 270:1995;13834-13841.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13834-13841
    • Merrill, A.H.Jr.1    Lingrell, S.2    Wang, E.3    Nikolova-Karakashian, M.4    Vales, T.R.5    Vance, D.E.6
  • 162
    • 0030963660 scopus 로고    scopus 로고
    • Characterization of ceramide synthesis. A dihydroceramide desaturase introduces the 4,5-trans-double bond of sphingosine at the level of dihydroceramide
    • Michel C., van Echten-Deckert G., Rother J., Sandhoff K., Wang E., Merrill A.H. Jr. Characterization of ceramide synthesis. A dihydroceramide desaturase introduces the 4,5-trans-double bond of sphingosine at the level of dihydroceramide. J. Biol. Chem. 272:1997;22432-22437.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22432-22437
    • Michel, C.1    Van Echten-Deckert, G.2    Rother, J.3    Sandhoff, K.4    Wang, E.5    Merrill, A.H.Jr.6
  • 163
    • 0037343133 scopus 로고    scopus 로고
    • Hydrogen-bonding propensities of sphingomyelin in solution and in a bilayer assembly: A molecular dynamics study
    • Mombelli E., Morris R., Taylor W., Fraternali F. Hydrogen-bonding propensities of sphingomyelin in solution and in a bilayer assembly: a molecular dynamics study. Biophys. J. 84:2003;1507-1517.
    • (2003) Biophys. J. , vol.84 , pp. 1507-1517
    • Mombelli, E.1    Morris, R.2    Taylor, W.3    Fraternali, F.4
  • 164
    • 0037304544 scopus 로고    scopus 로고
    • Properties of palmitoyl phosphatidylcholine, sphingomyelin, and dihydrosphingomyelin bilayer membranes as reported by different fluorescent reporter molecules
    • Nyholm T., Nylund M., Soderholm A., Slotte J.P. Properties of palmitoyl phosphatidylcholine, sphingomyelin, and dihydrosphingomyelin bilayer membranes as reported by different fluorescent reporter molecules. Biophys. J. 84:2003;987-997.
    • (2003) Biophys. J. , vol.84 , pp. 987-997
    • Nyholm, T.1    Nylund, M.2    Soderholm, A.3    Slotte, J.P.4
  • 165
    • 0029055676 scopus 로고
    • Ceramide: A stress signal and mediator of growth suppression and apoptosis
    • Obeid L.M., Hannun Y.A. Ceramide: a stress signal and mediator of growth suppression and apoptosis. J. Cell Biochem. 58:1995;191-198.
    • (1995) J. Cell Biochem. , vol.58 , pp. 191-198
    • Obeid, L.M.1    Hannun, Y.A.2
  • 167
    • 0037390139 scopus 로고    scopus 로고
    • Effect of sphingomyelin versus dipalmitoyl-phosphatidylcholine on the extent of lipid oxidation
    • Oborina E.M., Yappert M.C. Effect of sphingomyelin versus dipalmitoyl-phosphatidylcholine on the extent of lipid oxidation. Chem. Phys. Lip. 123:2003;223-232.
    • (2003) Chem. Phys. Lip. , vol.123 , pp. 223-232
    • Oborina, E.M.1    Yappert, M.C.2
  • 168
    • 1442339663 scopus 로고    scopus 로고
    • Effect of the trans double bond in the interfacial region of sphingophospholipids on the extent of stearoyl-arachidonoyl phosphatidylcholine oxidation
    • submitted for publication
    • Oborina, E.M., Yappert, M.C., 2004. Effect of the trans double bond in the interfacial region of sphingophospholipids on the extent of stearoyl-arachidonoyl phosphatidylcholine oxidation. Chem. Phys. Lip., submitted for publication.
    • (2004) Chem. Phys. Lip.
    • Oborina, E.M.1    Yappert, M.C.2
  • 169
    • 0032238017 scopus 로고    scopus 로고
    • Implication of glycolipids in lens fiber development
    • Ogiso M. Implication of glycolipids in lens fiber development. Acta Biochim. Pol. 45:1998;501-507.
    • (1998) Acta Biochim. Pol. , vol.45 , pp. 501-507
    • Ogiso, M.1
  • 171
    • 0028934580 scopus 로고
    • Age-related changes in ganglioside composition in human lens
    • Ogiso M., Komoto M., Okinaga T., Koyota S., Hoshi M. Age-related changes in ganglioside composition in human lens. Exp. Eye Res. 60:1995a;317-323.
    • (1995) Exp. Eye Res. , vol.60 , pp. 317-323
    • Ogiso, M.1    Komoto, M.2    Okinaga, T.3    Koyota, S.4    Hoshi, M.5
  • 172
    • 0028817127 scopus 로고
    • Characterization of neutral glycosphingolipids in rat lens
    • Ogiso M., Ohta M., Irie A., Hoshi M., Komoto M. Characterization of neutral glycosphingolipids in rat lens. Exp. Eye Res. 60:1995b;193-198.
    • (1995) Exp. Eye Res. , vol.60 , pp. 193-198
    • Ogiso, M.1    Ohta, M.2    Irie, A.3    Hoshi, M.4    Komoto, M.5
  • 173
  • 174
    • 0032497837 scopus 로고    scopus 로고
    • The role of ceramide in cell signaling
    • Perry D.K., Hannun Y.A. The role of ceramide in cell signaling. Biochim. Biophys. Acta. 1436:1998;233-243.
    • (1998) Biochim. Biophys. Acta , vol.1436 , pp. 233-243
    • Perry, D.K.1    Hannun, Y.A.2
  • 175
    • 1442266183 scopus 로고    scopus 로고
    • A study on lens epithelial cell DNA damage induced by hydrogen peroxide in rat and its repair
    • Qin H., Zhao G., Wu H. A study on lens epithelial cell DNA damage induced by hydrogen peroxide in rat and its repair. Acta Soc. Ophthalmol. Jpn. 101:1997;40-45.
    • (1997) Acta Soc. Ophthalmol. Jpn. , vol.101 , pp. 40-45
    • Qin, H.1    Zhao, G.2    Wu, H.3
  • 176
    • 0033584968 scopus 로고    scopus 로고
    • Lens-specific regulation of the thioredoxin-1 gene, but not thioredoxin-2, upon in vivo photochemical oxidative stress in the Emory mouse
    • Reddy P.G., Bhuyan D.K., Bhuyan K.C. Lens-specific regulation of the thioredoxin-1 gene, but not thioredoxin-2, upon in vivo photochemical oxidative stress in the Emory mouse. Biochem. Biophys. Res. Commun. 265:1999;345-349.
    • (1999) Biochem. Biophys. Res. Commun. , vol.265 , pp. 345-349
    • Reddy, P.G.1    Bhuyan, D.K.2    Bhuyan, K.C.3
  • 177
    • 0018082756 scopus 로고
    • Cholesterol-lipid interactions in membranes. The saturation concentration of cholesterol in bilayers of various lipids
    • Reiber H. Cholesterol-lipid interactions in membranes. The saturation concentration of cholesterol in bilayers of various lipids. Biochim. Biophys. Acta. 512:1978;72-83.
    • (1978) Biochim. Biophys. Acta , vol.512 , pp. 72-83
    • Reiber, H.1
  • 178
    • 0031740079 scopus 로고    scopus 로고
    • The differential miscibility of lipids as the basis for the formation of functional membrane rafts
    • Rietveld A., Simons K. The differential miscibility of lipids as the basis for the formation of functional membrane rafts. Biochim. Biophys. Acta. 1376:1998;467-479.
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 467-479
    • Rietveld, A.1    Simons, K.2
  • 180
    • 0016194986 scopus 로고
    • Subcellular distribution of sphingomyelinase and other acid hydrolases in different parts of the calf lens
    • Roelfzema H., Broekhuyse R.M., Veerkamp J.H. Subcellular distribution of sphingomyelinase and other acid hydrolases in different parts of the calf lens. Exp. Eye Res. 18:1974;579-594.
    • (1974) Exp. Eye Res. , vol.18 , pp. 579-594
    • Roelfzema, H.1    Broekhuyse, R.M.2    Veerkamp, J.H.3
  • 181
    • 0017117766 scopus 로고
    • Lipids in tissues of the eye. XI. Synthesis of sphingomyelin in the calf lens
    • Roelfzema H., Broekhuyse R.M., Veerkamp J.H. Lipids in tissues of the eye. XI. Synthesis of sphingomyelin in the calf lens. Exp. Eye Res. 22:1976;85-94.
    • (1976) Exp. Eye Res. , vol.22 , pp. 85-94
    • Roelfzema, H.1    Broekhuyse, R.M.2    Veerkamp, J.H.3
  • 182
    • 0019975413 scopus 로고
    • Lens plasma membrane: Isolation and biochemical characterization
    • Roy D., Rosenfeld L., Spector A. Lens plasma membrane: isolation and biochemical characterization. Exp. Eye Res. 35:1982;113-129.
    • (1982) Exp. Eye Res. , vol.35 , pp. 113-129
    • Roy, D.1    Rosenfeld, L.2    Spector, A.3
  • 183
    • 0029558776 scopus 로고
    • Protein kinase D (PKD): A novel target for diacylglycerol and phorbol esters
    • Rozengurt E., Sinnett-Smith J., Van Lint J., Valverde A.M. Protein kinase D (PKD): a novel target for diacylglycerol and phorbol esters. Mut. Res. 333:1995;153-160.
    • (1995) Mut. Res. , vol.333 , pp. 153-160
    • Rozengurt, E.1    Sinnett-Smith, J.2    Van Lint, J.3    Valverde, A.M.4
  • 184
    • 0036114438 scopus 로고    scopus 로고
    • Interactions of Ca(2+) with sphingomyelin and dihydrosphingomyelin
    • Rujoi M., Borchman D., DuPre D.B., Yappert M.C. Interactions of Ca(2+) with sphingomyelin and dihydrosphingomyelin. Biophys. J. 82:2002;3096-3104.
    • (2002) Biophys. J. , vol.82 , pp. 3096-3104
    • Rujoi, M.1    Borchman, D.2    Dupre, D.B.3    Yappert, M.C.4
  • 185
    • 1442339662 scopus 로고    scopus 로고
    • In situ MALDI-TOF MS regional analysis of neutral phospholipids in lens tissue
    • in press
    • Rujoi, M., Estrada, R., Yappert, M.C., 2004. In situ MALDI-TOF MS regional analysis of neutral phospholipids in lens tissue. Anal. Chem., in press.
    • (2004) Anal. Chem.
    • Rujoi, M.1    Estrada, R.2    Yappert, M.C.3
  • 186
    • 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., Yappert M.C. Isolation and lipid characterization of cholesterol-enriched fractions in cortical and nuclear human lens fibers. Invest. Ophthalmol. Vis. Sci. 44:2003;1634-1642.
    • (2003) 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
  • 187
    • 0000965942 scopus 로고
    • Growth in mass and volume of the human lens in postnatal life
    • Scammon R.E., Hesdorffer M.B. Growth in mass and volume of the human lens in postnatal life. Arch. Ophthalmol. 17:1937;104-112.
    • (1937) Arch. Ophthalmol. , vol.17 , pp. 104-112
    • Scammon, R.E.1    Hesdorffer, M.B.2
  • 188
    • 0035656189 scopus 로고    scopus 로고
    • Regulation of c-fos induction in lens epithelial cells by 12(S)HETE-dependent activation of PKC
    • Seth R.K., Haque M.S., Zelenka P.S. Regulation of c-fos induction in lens epithelial cells by 12(S)HETE-dependent activation of PKC. Invest. Ophthalmol. Vis. Sci. 42:2001;3239-3246.
    • (2001) Invest. Ophthalmol. Vis. Sci. , vol.42 , pp. 3239-3246
    • Seth, R.K.1    Haque, M.S.2    Zelenka, P.S.3
  • 189
    • 0344588823 scopus 로고    scopus 로고
    • Membrane-destabilizing properties of C2-ceramide may be responsible for its ability to inhibit platelet aggregation
    • Simon C.G. Jr., Gear A.R. Membrane-destabilizing properties of C2-ceramide may be responsible for its ability to inhibit platelet aggregation. Biochemistry. 37:1998;2059-2069.
    • (1998) Biochemistry , vol.37 , pp. 2059-2069
    • Simon, C.G.Jr.1    Gear, A.R.2
  • 190
    • 0029870940 scopus 로고    scopus 로고
    • Fatty acid composition of membrane phospholipids of cataractous human lenses
    • Simonelli F., Libondi T., Romano N., Nunziata G., D'Aloia A., Rinaldi E. Fatty acid composition of membrane phospholipids of cataractous human lenses. Ophthal. Res. 28(Suppl. 1):1996;101-104.
    • (1996) Ophthal. Res. , vol.28 , Issue.SUPPL. 1 , pp. 101-104
    • Simonelli, F.1    Libondi, T.2    Romano, N.3    Nunziata, G.4    D'Aloia, A.5    Rinaldi, E.6
  • 191
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K., Ikonen E. Functional rafts in cell membranes. Nature. 387:1997;569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 192
    • 0023788823 scopus 로고
    • Lipid sorting in epithelial cells
    • Simons K., van Meer G. Lipid sorting in epithelial cells. Biochemistry. 27:1988;6197-6202.
    • (1988) Biochemistry , vol.27 , pp. 6197-6202
    • Simons, K.1    Van Meer, G.2
  • 193
    • 0029799891 scopus 로고    scopus 로고
    • A role for caveolin in transport of cholesterol from endoplasmic reticulum to plasma membrane
    • Smart E.J., Ying Y., Donzell W.C., Anderson R.G. A role for caveolin in 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.2    Donzell, W.C.3    Anderson, R.G.4
  • 194
    • 0034781755 scopus 로고    scopus 로고
    • The effect of aging on glutathione peroxidase-i knockout mice-resistance of the lens to oxidative stress
    • Spector A., Kuszak J.R., Ma W., Wang R.R. The effect of aging on glutathione peroxidase-i knockout mice-resistance of the lens to oxidative stress. Exp. Eye Res. 72:2001;533-545.
    • (2001) Exp. Eye Res. , vol.72 , pp. 533-545
    • Spector, A.1    Kuszak, J.R.2    Ma, W.3    Wang, R.R.4
  • 195
    • 0035988177 scopus 로고    scopus 로고
    • 2 and tertiary butyl hydroperoxide upon a murine immortal lens epithelial cell line, alphaTN4-1
    • 2 and tertiary butyl hydroperoxide upon a murine immortal lens epithelial cell line, alphaTN4-1. Exp. Eye Res. 75:2002;573-582.
    • (2002) Exp. Eye Res. , vol.75 , pp. 573-582
    • Spector, A.1    Ma, W.2    Sun, F.3    Li, D.4    Kleiman, N.J.5
  • 196
    • 0036569034 scopus 로고    scopus 로고
    • Sphingosine 1-phosphate signaling: Providing cells with a sense of direction
    • Spiegel S., English D., Milstien S. Sphingosine 1-phosphate signaling: providing cells with a sense of direction. Trends Cell Biol. 12:2002;236-242.
    • (2002) Trends Cell Biol. , vol.12 , pp. 236-242
    • Spiegel, S.1    English, D.2    Milstien, S.3
  • 197
    • 0017795845 scopus 로고
    • Lipid and fatty acid composition of human cerebral myelin during
    • Svennerholm L., Vanier M.T. Lipid and fatty acid composition of human cerebral myelin during development. Adv. Exp. Med. Biol. 100:1978;27-41.
    • (1978) Adv. Exp. Med. Biol. , vol.100 , pp. 27-41
    • Svennerholm, L.1    Vanier, M.T.2
  • 198
    • 0023255659 scopus 로고
    • Quantitation of membrane-associated crystallins from aging and cataractous human lenses
    • Takehana M., Takemoto L. Quantitation of membrane-associated crystallins from aging and cataractous human lenses. Invest. Ophthalmol. Vis. Sci. 28:1987;780-784.
    • (1987) Invest. Ophthalmol. Vis. Sci. , vol.28 , pp. 780-784
    • Takehana, M.1    Takemoto, L.2
  • 199
    • 0022978546 scopus 로고
    • Major intrinsic polypeptide (MIP26K) from human lens membrane: Characterization of low-molecular-weight forms in the aging human lens
    • Takemoto L., Takehana M. Major intrinsic polypeptide (MIP26K) from human lens membrane: characterization of low-molecular-weight forms in the aging human lens. Exp. Eye Res. 43:1986;661-667.
    • (1986) Exp. Eye Res. , vol.43 , pp. 661-667
    • Takemoto, L.1    Takehana, M.2
  • 200
    • 0021634188 scopus 로고
    • High molecular weight aggregates from human cataracts: Characterization by Western blot analysis
    • Takemoto L.J., Hansen J.S., Horwitz J. High molecular weight aggregates from human cataracts: characterization by Western blot analysis. Biochem. Biophys. Res. Commun. 122:1984;1028-1033.
    • (1984) Biochem. Biophys. Res. Commun. , vol.122 , pp. 1028-1033
    • Takemoto, L.J.1    Hansen, J.S.2    Horwitz, J.3
  • 202
    • 13044311394 scopus 로고    scopus 로고
    • Alpha-crystallin/lens lipid interactions using resonance energy transfer
    • Tang D., Borchman D., Yappert M.C. Alpha-crystallin/lens lipid interactions using resonance energy transfer. Ophthal. Res. 31:1999;452-462.
    • (1999) Ophthal. Res. , vol.31 , pp. 452-462
    • Tang, D.1    Borchman, D.2    Yappert, M.C.3
  • 203
    • 0032077957 scopus 로고    scopus 로고
    • Influence of cholesterol on the interaction of alpha-crystallin with phospholipids
    • Tang D., Borchman D., Yappert M.C., Cenedella R.J. Influence of cholesterol on the interaction of alpha-crystallin with phospholipids. Exp. Eye Res. 66:1998;559-567.
    • (1998) Exp. Eye Res. , vol.66 , pp. 559-567
    • Tang, D.1    Borchman, D.2    Yappert, M.C.3    Cenedella, R.J.4
  • 205
    • 0037407654 scopus 로고    scopus 로고
    • Influence of age, diabetes, and cataract on calcium, lipid-calcium, and protein-calcium relationships in human lenses
    • Tang D., Borchman D., Yappert M.C., Vrensen G.F., Rasi V. Influence of age, diabetes, and cataract on calcium, lipid-calcium, and protein-calcium relationships in human lenses. Invest. Ophthalmol. Vis. Sci. 44:2003b;2059-2066.
    • (2003) Invest. Ophthalmol. Vis. Sci. , vol.44 , pp. 2059-2066
    • Tang, D.1    Borchman, D.2    Yappert, M.C.3    Vrensen, G.F.4    Rasi, V.5
  • 206
    • 0016708202 scopus 로고
    • Ceramides of human normal and cataractous lens
    • Tao R.V., Cotlier E. Ceramides of human normal and cataractous lens. Biochim. Biophys. Acta. 409:1975;329-341.
    • (1975) Biochim. Biophys. Acta , vol.409 , pp. 329-341
    • Tao, R.V.1    Cotlier, E.2
  • 207
    • 0020282887 scopus 로고
    • Isolation and partial characterization of fucose- and N-acetylglucosamine-containing neutral glycosphingolipids from human senile cataracts
    • Tao R.V., Kovathana N., Shen Y.W. Isolation and partial characterization of fucose- and N-acetylglucosamine-containing neutral glycosphingolipids from human senile cataracts. Curr. Eye Res. 2:1982;427-434.
    • (1982) Curr. Eye Res. , vol.2 , pp. 427-434
    • Tao, R.V.1    Kovathana, N.2    Shen, Y.W.3
  • 208
    • 0023605949 scopus 로고
    • Occurrence of an unusual amount of an odd-numbered fatty acid in glycosphingolipids from human cataracts
    • Tao R.V., Lee B.C., Hsieh T.C., Laine R.A. Occurrence of an unusual amount of an odd-numbered fatty acid in glycosphingolipids from human cataracts. Curr. Eye Res. 6:1987;1361-1367.
    • (1987) Curr. Eye Res. , vol.6 , pp. 1361-1367
    • Tao, R.V.1    Lee, B.C.2    Hsieh, T.C.3    Laine, R.A.4
  • 209
    • 0020606717 scopus 로고
    • A new family of fucose-containing gangliosides isolated from human senile cataracts
    • Tao R.V., Shen Y.W., Kovathana N., Cotlier E. A new family of fucose-containing gangliosides isolated from human senile cataracts. Biochim. Biophys. Acta. 753:1983;89-96.
    • (1983) Biochim. Biophys. Acta , vol.753 , pp. 89-96
    • Tao, R.V.1    Shen, Y.W.2    Kovathana, N.3    Cotlier, E.4
  • 213
    • 0018384817 scopus 로고
    • Negatively charged phospholipids and their position in the cholesterol affinity sequence
    • van Dijck P.W. Negatively charged phospholipids and their position in the cholesterol affinity sequence. Biochim. Biophys. Acta. 555:1979;89-101.
    • (1979) Biochim. Biophys. Acta , vol.555 , pp. 89-101
    • Van Dijck, P.W.1
  • 214
    • 0038765817 scopus 로고
    • The biochemistry of the lens - Selected topics
    • Perkins, E.S., Hill, D.W. (Eds.). Heinemann, London
    • van Heynigen, R., 1977. The biochemistry of the lens - selected topics. In: Perkins, E.S., Hill, D.W. (Eds.), Scientific Foundations of Ophthalmology. Heinemann, London, p. 44.
    • (1977) Scientific Foundations of Ophthalmology , pp. 44
    • Van Heynigen, R.1
  • 216
    • 0029933091 scopus 로고    scopus 로고
    • Incorporation of 12(S)-hydroxyeicosatetraenoic acid into phospholipids and active diacylglycerols in rat liver epithelial cells: Effects on DNA synthesis
    • Vernhet L., Hichami A., Hamon L., Cochet M.F., Legrand A.B. Incorporation of 12(S)-hydroxyeicosatetraenoic acid into phospholipids and active diacylglycerols in rat liver epithelial cells: effects on DNA synthesis. J. Lipid Mediat. Cell Signal. 13:1996;233-248.
    • (1996) J. Lipid Mediat. Cell Signal , vol.13 , pp. 233-248
    • Vernhet, L.1    Hichami, A.2    Hamon, L.3    Cochet, M.F.4    Legrand, A.B.5
  • 217
    • 0024521789 scopus 로고
    • Evidence for the presence of phosphoinositide cycle and its involvement in cellular signal transduction in the rabbit lens
    • Vivekanandan S., Lou M.F. Evidence for the presence of phosphoinositide cycle and its involvement in cellular signal transduction in the rabbit lens. Curr. Eye Res. 8:1989;101-111.
    • (1989) Curr. Eye Res. , vol.8 , pp. 101-111
    • Vivekanandan, S.1    Lou, M.F.2
  • 218
    • 0004053611 scopus 로고
    • Wiley, New York
    • Voet, D., Voet, J.G., 1995a. Biochemistry. Wiley, New York, p. 1287-1290.
    • (1995) Biochemistry , pp. 1287-1290
    • Voet, D.1    Voet, J.G.2
  • 219
  • 221
    • 0037204333 scopus 로고    scopus 로고
    • Hydrogen bonding in monomers and dimers of 2-aminoethanol
    • Vorobyov I., Yappert M.C., DuPré D.B. Hydrogen bonding in monomers and dimers of 2-aminoethanol. J. Phys. Chem. Part A. 106:2002;668-679.
    • (2002) J. Phys. Chem. Part a , vol.106 , pp. 668-679
    • Vorobyov, I.1    Yappert, M.C.2    Dupré, D.B.3
  • 222
    • 0029143223 scopus 로고
    • Mechanism of farnesol cytotoxicity: Further evidence for the role of PKC-dependent signal transduction in farnesol-induced apoptotic cell death
    • Voziyan P.A., Haug J.S., Melnykovych G. Mechanism of farnesol cytotoxicity: further evidence for the role of PKC-dependent signal transduction in farnesol-induced apoptotic cell death. Biochem. Biophys. Res. Commun. 212:1995;479-486.
    • (1995) Biochem. Biophys. Res. Commun. , vol.212 , pp. 479-486
    • Voziyan, P.A.1    Haug, J.S.2    Melnykovych, G.3
  • 223
    • 0029115937 scopus 로고
    • Aging of the human eye lens - A morphological point of view
    • Vrensen G.F. Aging of the human eye lens - a morphological point of view. Comp. Biochem. Physiol. Part A: Physiol. 111:1995;519-532.
    • (1995) Comp. Biochem. Physiol. Part A: Physiol. , vol.111 , pp. 519-532
    • Vrensen, G.F.1
  • 224
    • 1442290619 scopus 로고    scopus 로고
    • Response of lens epithelial cells to hydrogen peroxide stress and the protective effect of caloric restriction
    • Vrensen G.F., van Marle J., Gan L., Soderberg P.G., Li Y. Response of lens epithelial cells to hydrogen peroxide stress and the protective effect of caloric restriction. Invest. Ophthalmol. Vis. Sci. 39:1998;2681-2687.
    • (1998) Invest. Ophthalmol. Vis. Sci. , vol.39 , pp. 2681-2687
    • Vrensen, G.F.1    Van Marle, J.2    Gan, L.3    Soderberg, P.G.4    Li, Y.5
  • 225
    • 0033015540 scopus 로고    scopus 로고
    • Phosphorylation-dependent protein kinase D activation
    • Waldron R.T., Iglesias T., Rozengurt E. Phosphorylation-dependent protein kinase D activation. Electrophoresis. 20:1999;382-390.
    • (1999) Electrophoresis , vol.20 , pp. 382-390
    • Waldron, R.T.1    Iglesias, T.2    Rozengurt, E.3
  • 226
    • 0034595789 scopus 로고    scopus 로고
    • Oxidative stress induces protein kinase D activation in intact cells. Involvement of Src and dependence on protein kinase C
    • Waldron R.T., Rozengurt E. Oxidative stress induces protein kinase D activation in intact cells. Involvement of Src and dependence on protein kinase C. J. Biol. Chem. 275:2000;17114-17121.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17114-17121
    • Waldron, R.T.1    Rozengurt, E.2
  • 227
    • 0035986741 scopus 로고    scopus 로고
    • A signaling sole for the uncleaved form of alpha 6 integrin in differentiating lens fiber cells
    • Walker J.L., Zhang L., Menko A.S. A signaling sole for the uncleaved form of alpha 6 integrin in differentiating lens fiber cells. Dev. Biol. 251:2002;195-205.
    • (2002) Dev. Biol. , vol.251 , pp. 195-205
    • Walker, J.L.1    Zhang, L.2    Menko, A.S.3
  • 228
    • 1442315140 scopus 로고    scopus 로고
    • DNA repair and survival in human lens epithelial cells with extended lifespan
    • Wang R.R., Ma W., Kleiman N.J., Andley U.P. DNA repair and survival in human lens epithelial cells with extended lifespan. Invest. Ophthalmol. Vis. Sci. 41:2000;832-843.
    • (2000) Invest. Ophthalmol. Vis. Sci. , vol.41 , pp. 832-843
    • Wang, R.R.1    Ma, W.2    Kleiman, N.J.3    Andley, U.P.4
  • 229
    • 0028122397 scopus 로고
    • Role of ceramide-activated protein phosphatase in ceramide-mediated signal transduction
    • Wolff R.A., Dobrowsky R.T., Bielawska A., Obeid L.M., Hannun Y.A. Role of ceramide-activated protein phosphatase in ceramide-mediated signal transduction. J. Biol. Chem. 269:1994;19605-19609.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19605-19609
    • Wolff, R.A.1    Dobrowsky, R.T.2    Bielawska, A.3    Obeid, L.M.4    Hannun, Y.A.5
  • 230
    • 0029730560 scopus 로고    scopus 로고
    • Cellular and molecular features of lens differentiation: A review of recent advances
    • Wride M.A. Cellular and molecular features of lens differentiation: a review of recent advances. Differentiation. 61:1996;77-93.
    • (1996) Differentiation , vol.61 , pp. 77-93
    • Wride, M.A.1
  • 232
    • 0038667898 scopus 로고    scopus 로고
    • Glycero- versus sphingo-phospholipids: Correlations with human and non-human mammalian lens growth
    • Yappert M.C., Rujoi M., Borchman D., Vorobyov I., Estrada R. Glycero- versus sphingo-phospholipids: correlations with human and non-human mammalian lens growth. Exp. Eye Res. 76:2003b;725-734.
    • (2003) Exp. Eye Res. , vol.76 , pp. 725-734
    • Yappert, M.C.1    Rujoi, M.2    Borchman, D.3    Vorobyov, I.4    Estrada, R.5
  • 233
    • 0017660967 scopus 로고
    • Phospholipid head-group conformations intermolecular interactions and cholesterol effects
    • Yeagle P.L., Hutton W.C., Huang C., Martin R.B. Phospholipid head-group conformations intermolecular interactions and cholesterol effects. Biochemistry. 16:1977;4344-4349.
    • (1977) Biochemistry , vol.16 , pp. 4344-4349
    • Yeagle, P.L.1    Hutton, W.C.2    Huang, C.3    Martin, R.B.4
  • 234
    • 0018893516 scopus 로고
    • Changes in phosphatidylinositol metabolism during differentiation of lens epithelial cells into lens fiber cells in the embryonic chick
    • Zelenka P.S. Changes in phosphatidylinositol metabolism during differentiation of lens epithelial cells into lens fiber cells in the embryonic chick. J. Biol. Chem. 255:1980;1296-1300.
    • (1980) J. Biol. Chem. , vol.255 , pp. 1296-1300
    • Zelenka, P.S.1
  • 235
    • 0021106143 scopus 로고
    • Phosphatidylcholine and phosphatidylethanolamine metabolism during lens fiber cell formation
    • Zelenka P.S. Phosphatidylcholine and phosphatidylethanolamine metabolism during lens fiber cell formation. Biochim. Biophys. Acta. 752:1983;145-152.
    • (1983) Biochim. Biophys. Acta , vol.752 , pp. 145-152
    • Zelenka, P.S.1
  • 236
  • 237
    • 0020062972 scopus 로고
    • Phosphorylcholine and phosphorylethanolamine concentrations in the lens
    • Zelenka P.S., Jernigan H.M. Jr. Phosphorylcholine and phosphorylethanolamine concentrations in the lens. Exp. Eye Res. 34:1982;209-217.
    • (1982) Exp. Eye Res. , vol.34 , pp. 209-217
    • Zelenka, P.S.1    Jernigan, H.M.Jr.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.