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Volumn 64, Issue 3, 1997, Pages 387-395

Loss of cytoskeletal proteins and lens cell opacification in the selenite cataract model

Author keywords

Cataract; Cytoskeletal proteins; Lens; Opacification; Panthetine; Proteins; Selenite

Indexed keywords

LENS PROTEIN; PANTETHINE; SODIUM SELENITE;

EID: 0031105495     PISSN: 00144835     EISSN: None     Source Type: Journal    
DOI: 10.1006/exer.1996.0220     Document Type: Article
Times cited : (65)

References (51)
  • 1
    • 0002306564 scopus 로고
    • Biochemistry of lens plasma membrane and cytoskeleton
    • Marcel Dekker: New York, U.S.A.
    • Alcala, J. and Maisel, H. (1985). Biochemistry of lens plasma membrane and cytoskeleton. In The ocular lens. Pp. 169-222. Marcel Dekker: New York, U.S.A.
    • (1985) The Ocular Lens , pp. 169-222
    • Alcala, J.1    Maisel, H.2
  • 2
    • 0027102664 scopus 로고
    • Selenite nuclear cataractogenesis : A scanning electron microscope study
    • Anderson, R. S. and Shearer, T. R. (1992). Selenite nuclear cataractogenesis : a scanning electron microscope study. Curr. Eye Res. 11, 1147-60.
    • (1992) Curr. Eye Res. , vol.11 , pp. 1147-1160
    • Anderson, R.S.1    Shearer, T.R.2
  • 3
    • 0015022316 scopus 로고
    • Theory of transparency of the eye
    • Benedek, G. B. (1971). Theory of transparency of the eye. Appl. Optics 10, 459-73.
    • (1971) Appl. Optics , vol.10 , pp. 459-473
    • Benedek, G.B.1
  • 4
    • 0028837059 scopus 로고
    • Calcium cataract: A model for optical anisotropy fluctuations
    • Bettelheim, F. A., Qin, C. and Zigler, J. S. Jr. (1995). Calcium cataract: a model for optical anisotropy fluctuations. Eye. Eye Res. 60, 153-7.
    • (1995) Eye. Eye Res. , vol.60 , pp. 153-157
    • Bettelheim, F.A.1    Qin, C.2    Zigler Jr., J.S.3
  • 5
    • 0023931244 scopus 로고
    • Proteolysis of tubulin and microtubule-associated proteins 1 and 2 by calpain I and II. Difference in sensitivity of assembled and disassembled microtubules
    • Billger, M., Wallin, M. and Karlsson, J. (1988). Proteolysis of tubulin and microtubule-associated proteins 1 and 2 by calpain I and II. Difference in sensitivity of assembled and disassembled microtubules. Cell Calcium 9, 33-44.
    • (1988) Cell Calcium , vol.9 , pp. 33-44
    • Billger, M.1    Wallin, M.2    Karlsson, J.3
  • 6
    • 0026130860 scopus 로고
    • Disorganization of membranes and abnormal intermediate filament assembly lead to cataract
    • Bloemendal, H. (1991). Disorganization of membranes and abnormal intermediate filament assembly lead to cataract. Invest. Ophthalmol. Vis. Sci. 32, 445-55.
    • (1991) Invest. Ophthalmol. Vis. Sci. , vol.32 , pp. 445-455
    • Bloemendal, H.1
  • 7
    • 0018388019 scopus 로고
    • Age changes in the skeleton of the human lens
    • Bradley, R. H., Ireland, M. E. and Maisel, H. (1979). Age changes in the skeleton of the human lens. Acta Ophthalmol. 57, 461-9.
    • (1979) Acta Ophthalmol. , vol.57 , pp. 461-469
    • Bradley, R.H.1    Ireland, M.E.2    Maisel, H.3
  • 8
    • 0019828022 scopus 로고
    • Biochemical changes associated with selenite-induced cataract in rat
    • Bunce, G. E. and Hess, J. L. (1981). Biochemical changes associated with selenite-induced cataract in rat. Exp. Eye Res. 33, 505-14.
    • (1981) Exp. Eye Res. , vol.33 , pp. 505-514
    • Bunce, G.E.1    Hess, J.L.2
  • 9
    • 78651161333 scopus 로고
    • Oriented microtubules in elongating cells of the developing lens rudiment after induction
    • Byers, B. B. and Porter, K. R. (1964). Oriented microtubules in elongating cells of the developing lens rudiment after induction. Proc. Natl Acad. Sci. U.S.A. 52, 1091-9.
    • (1964) Proc. Natl Acad. Sci. U.S.A. , vol.52 , pp. 1091-1099
    • Byers, B.B.1    Porter, K.R.2
  • 10
    • 0024470306 scopus 로고
    • Over-expression of the vimentin gene in transgenic mice inhibits normal lens cell differentiation
    • Capetanaki, Y., Smith, S. and Heath, J. P. (1989). Over-expression of the vimentin gene in transgenic mice inhibits normal lens cell differentiation. J. Cell Biol. 109, 1653-64.
    • (1989) J. Cell Biol. , vol.109 , pp. 1653-1664
    • Capetanaki, Y.1    Smith, S.2    Heath, J.P.3
  • 11
    • 0028831015 scopus 로고
    • In vitro studies on the assembly properties of the lens proteins CP49, CP115: Coassembly with α-crystallin but not with vimentin
    • Carter, J. M., Hutcheson, A. M. and Quinlan, R. A. (1995). In vitro studies on the assembly properties of the lens proteins CP49, CP115: coassembly with α-crystallin but not with vimentin. Exp. Eye Res. 60, 181-92.
    • (1995) Exp. Eye Res. , vol.60 , pp. 181-192
    • Carter, J.M.1    Hutcheson, A.M.2    Quinlan, R.A.3
  • 12
    • 0026556822 scopus 로고
    • Phase-separation inhibitors and prevention of selenite cataract
    • Clark, J. I and Steele, J. E. (1992). Phase-separation inhibitors and prevention of selenite cataract. Proc. Natl Acad. Sci., U.S.A. 89, 1720-4.
    • (1992) Proc. Natl Acad. Sci., U.S.A. , vol.89 , pp. 1720-1724
    • Clark, J.I.1    Steele, J.E.2
  • 13
    • 0002581224 scopus 로고
    • Development and maintenance of lens transparency
    • W. B. Saunders Company: Philadelphia, U.S.A.
    • Clark, J. I. (1994). Development and maintenance of lens transparency. In Principles and practice of ophthalmology. Pp. 114-23. W. B. Saunders Company: Philadelphia, U.S.A.
    • (1994) Principles and Practice of Ophthalmology , pp. 114-123
    • Clark, J.I.1
  • 14
    • 0028004289 scopus 로고
    • Mice lacking vimentin develop and reproduce without an obvious phenotype
    • Colucci-Guyon, E., Portier, M., Dunia, I., Paulin, D., Pournin, S. and Badinet, C. (1994). Mice lacking vimentin develop and reproduce without an obvious phenotype. Cell 79, 679-94.
    • (1994) Cell , vol.79 , pp. 679-694
    • Colucci-Guyon, E.1    Portier, M.2    Dunia, I.3    Paulin, D.4    Pournin, S.5    Badinet, C.6
  • 15
    • 0027468977 scopus 로고
    • Sequence analysis of lens β-crystallins suggests involvement of calpain in cataract formation
    • David, L. L., Shearer, T. R. and Shih, M. (1993a). Sequence analysis of lens β-crystallins suggests involvement of calpain in cataract formation. J. Biol. Chem. 268, 1937-40.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1937-1940
    • David, L.L.1    Shearer, T.R.2    Shih, M.3
  • 16
    • 0027241969 scopus 로고
    • β-crystallins insolubilized by calpain II in vitro contain cleavage sites similar to β-crystallins insolubilized during cataract
    • David, L. L. and Shearer, T. R. (1993b). β-crystallins insolubilized by calpain II in vitro contain cleavage sites similar to β-crystallins insolubilized during cataract. FEBS Lett. 324, 265-70.
    • (1993) FEBS Lett. , vol.324 , pp. 265-270
    • David, L.L.1    Shearer, T.R.2
  • 17
    • 0028223362 scopus 로고
    • Cataract and the acceleration of calpain-induced β-crystallin insolubilization occurring during normal maturation of rat lens
    • David, L. L., Azuma, M. and Shearer, T. R. (1994). Cataract and the acceleration of calpain-induced β-crystallin insolubilization occurring during normal maturation of rat lens. Invest. Ophthalmol. Vis. Sci. 35, 785-93.
    • (1994) Invest. Ophthalmol. Vis. Sci. , vol.35 , pp. 785-793
    • David, L.L.1    Azuma, M.2    Shearer, T.R.3
  • 20
    • 0003410731 scopus 로고
    • Biochemistry epidemiology and pharmacology
    • Chapman & Hall: New York, U.S.A.
    • Harding, J. (1991). Biochemistry epidemiology and pharmacology. In Cataract. Chapman & Hall: New York, U.S.A.
    • (1991) Cataract
    • Harding, J.1
  • 21
    • 0023253044 scopus 로고
    • Regional distribution of free calcium in selenite cataract: Relation to Calpain II
    • Hightower, K. R., David, L. L. and Shearer, T. R. (1987). Regional distribution of free calcium in selenite cataract: relation to Calpain II. Invest. Ophthalmol. Vis. Sci. 28, 1702-6.
    • (1987) Invest. Ophthalmol. Vis. Sci. , vol.28 , pp. 1702-1706
    • Hightower, K.R.1    David, L.L.2    Shearer, T.R.3
  • 22
    • 0028206498 scopus 로고
    • Selenite-induced damage to lens membranes
    • Hightower, K. and McCready, J. (1994). Selenite-induced damage to lens membranes. Exp. Eye Res. 58, 225-9.
    • (1994) Exp. Eye Res. , vol.58 , pp. 225-229
    • Hightower, K.1    McCready, J.2
  • 23
    • 0028845993 scopus 로고
    • Inhibition of lens opacification during the early stages of cataract formation
    • Hiraoka, T. and Clark, J. I. (1995). Inhibition of lens opacification during the early stages of cataract formation. Invest. Ophthalmol. Vis. Sci. 36, 2550-5.
    • (1995) Invest. Ophthalmol. Vis. Sci. , vol.36 , pp. 2550-2555
    • Hiraoka, T.1    Clark, J.I.2
  • 24
    • 0029874158 scopus 로고    scopus 로고
    • Effect of selected anti-cataract agents on opacification in the selenite cataract model
    • Hiraoka, T., Clark, J. I., Li, X. Y. and Thurston, G. M. (1996). Effect of selected anti-cataract agents on opacification in the selenite cataract model. Exp. Eye Res. 62, 11-9.
    • (1996) Exp. Eye Res. , vol.62 , pp. 11-19
    • Hiraoka, T.1    Clark, J.I.2    Li, X.Y.3    Thurston, G.M.4
  • 25
    • 0021355006 scopus 로고
    • Evidence for a calcium activated protease specific for lens intermediate filaments
    • Ireland, M. and Maisel, H. (1984). Evidence for a calcium activated protease specific for lens intermediate filaments. Curr. Eye Res. 3, 423-9.
    • (1984) Curr. Eye Res. , vol.3 , pp. 423-429
    • Ireland, M.1    Maisel, H.2
  • 26
    • 0008061578 scopus 로고
    • Lens Biochemistry
    • Gower Medical Publishing: New York, U.S.A.
    • Jaffe, N. S. and Horwitz, J. H. (1992). Lens Biochemistry. In Lens and cataract. Pp. 4.1-4.13. Gower Medical Publishing: New York, U.S.A.
    • (1992) Lens and Cataract
    • Jaffe, N.S.1    Horwitz, J.H.2
  • 28
    • 0017197084 scopus 로고
    • Protein changes in the human lens during development of senile nuclear cataract
    • Kramps, H. A., Hoenders, H. J. and Wollensak, J. (1976). Protein changes in the human lens during development of senile nuclear cataract. Biochim. Biophys. Acta. 434, 32-43.
    • (1976) Biochim. Biophys. Acta. , vol.434 , pp. 32-43
    • Kramps, H.A.1    Hoenders, H.J.2    Wollensak, J.3
  • 29
    • 0023813915 scopus 로고
    • Adherens junctions in the ocular lens of various species: Ultrastructural analysis with an improved fixation
    • Lo, W. K. (1988). Adherens junctions in the ocular lens of various species: ultrastructural analysis with an improved fixation. Cell Tissue Res. 254, 31-40.
    • (1988) Cell Tissue Res. , vol.254 , pp. 31-40
    • Lo, W.K.1
  • 32
    • 0027722988 scopus 로고
    • The 47-kD lens-specific protein phakinin is a tailless intermediate filament protein and assembly partner of filensin
    • Merdes, A., Gounari, F. and Georgatos, S. D. (1993). The 47-kD lens-specific protein phakinin is a tailless intermediate filament protein and assembly partner of filensin. J. Cell Biol. 123, 1507-16.
    • (1993) J. Cell Biol. , vol.123 , pp. 1507-1516
    • Merdes, A.1    Gounari, F.2    Georgatos, S.D.3
  • 33
    • 0027985086 scopus 로고
    • Cytoskeletal regulation of membrane transport events
    • Mills, J. W. and Mandel, L. J. (1994). Cytoskeletal regulation of membrane transport events. FASEB 8, 1161-5.
    • (1994) FASEB , vol.8 , pp. 1161-1165
    • Mills, J.W.1    Mandel, L.J.2
  • 34
    • 0028958274 scopus 로고
    • Causes of decreased phase transition temperature in selenite cataract model
    • Mitton, K. P., Hess, J. L. and Bunce, G. E. (1995). Causes of decreased phase transition temperature in selenite cataract model. Invest. Ophthalmol. Vis. Sci. 36, 914-24.
    • (1995) Invest. Ophthalmol. Vis. Sci. , vol.36 , pp. 914-924
    • Mitton, K.P.1    Hess, J.L.2    Bunce, G.E.3
  • 35
    • 0018682160 scopus 로고
    • Actin in the lens: Changes in actin during differentiation of lens epithelial cells in vivo
    • Mousa, G. Y. and Trevithick, J. R. (1979). Actin in the lens: changes in actin during differentiation of lens epithelial cells in vivo. Exp. Eye Res. 29, 71-81.
    • (1979) Exp. Eye Res. , vol.29 , pp. 71-81
    • Mousa, G.Y.1    Trevithick, J.R.2
  • 36
    • 0020490635 scopus 로고
    • 2+-activated proteinase specific for the intermediate filament proteins vimentin and desmin
    • 2+-activated proteinase specific for the intermediate filament proteins vimentin and desmin. J. Biol. Chem. 257, 5544-53.
    • (1982) J. Biol. Chem. , vol.257 , pp. 5544-5553
    • Nelson, W.J.1    Traub, P.2
  • 37
    • 0028176579 scopus 로고
    • Chaperone activity of α-crystallins modulates intermediate filament assembly
    • NichoII, I. D. and Quinlan, R. A. (1994). Chaperone activity of α-crystallins modulates intermediate filament assembly. EMBO J. 13, 945-53.
    • (1994) EMBO J. , vol.13 , pp. 945-953
    • Nichoii, I.D.1    Quinlan, R.A.2
  • 38
    • 0021871113 scopus 로고
    • Electron microscopic study of water-insoluble fractions in normal and cataractous human lens fibers
    • Ozaki, L., Jap, P. and Bloemendal, H. (1985). Electron microscopic study of water-insoluble fractions in normal and cataractous human lens fibers. Ophthalmic Res. 17, 257-61.
    • (1985) Ophthalmic Res. , vol.17 , pp. 257-261
    • Ozaki, L.1    Jap, P.2    Bloemendal, H.3
  • 40
    • 0025018042 scopus 로고
    • Immunocytochemical evidence for an actin-myosin system in lens epithelial cells
    • Rafferty, N. S., Scholz, D., Goldberg, M. and Lewyckyj, M. (1990). Immunocytochemical evidence for an actin-myosin system in lens epithelial cells. Exp. Eye Res. 51, 591-600.
    • (1990) Exp. Eye Res. , vol.51 , pp. 591-600
    • Rafferty, N.S.1    Scholz, D.2    Goldberg, M.3    Lewyckyj, M.4
  • 41
    • 0020562916 scopus 로고
    • Lens calcium activated proteinase: Degradation of vimentin
    • Roy, D., Chiesa, R. and Spector, A. (1983). Lens calcium activated proteinase: degradation of vimentin. Biochem. Biophys. Res. Commun. 116, 204-9.
    • (1983) Biochem. Biophys. Res. Commun. , vol.116 , pp. 204-209
    • Roy, D.1    Chiesa, R.2    Spector, A.3
  • 42
    • 0028905818 scopus 로고
    • Vimentin and CP49/filensin from distinct networks in the lens which are independently modulated during lens fibre cell differentiation
    • Sandilands, A., Prescott, A. R., Carter, J. M., Hutcheson, A. M., Quinlan, R. A., Richards, J. and FitzGerald, P. G. (1995). Vimentin and CP49/filensin from distinct networks in the lens which are independently modulated during lens fibre cell differentiation. J. Cell Sci. 108, 1397-406.
    • (1995) J. Cell Sci. , vol.108 , pp. 1397-1406
    • Sandilands, A.1    Prescott, A.R.2    Carter, J.M.3    Hutcheson, A.M.4    Quinlan, R.A.5    Richards, J.6    FitzGerald, P.G.7
  • 43
    • 0022572215 scopus 로고
    • Selenite decreases phase separation temperature in rat lens
    • Shearer, T. R., David, L. L. and Anderson, R. S. (1986). Selenite decreases phase separation temperature in rat lens. Exp. Eye Res. 42, 503-6.
    • (1986) Exp. Eye Res. , vol.42 , pp. 503-506
    • Shearer, T.R.1    David, L.L.2    Anderson, R.S.3
  • 45
    • 0029050241 scopus 로고
    • Precipitation of crystallins from young rat lens by endogenous calpain
    • Shearer, T. R., Shih, M., Azuma, M. and David, L. L. (1995). Precipitation of crystallins from young rat lens by endogenous calpain. Exp. Eye Res. 61, 141-50.
    • (1995) Exp. Eye Res. , vol.61 , pp. 141-150
    • Shearer, T.R.1    Shih, M.2    Azuma, M.3    David, L.L.4
  • 46
    • 0021359934 scopus 로고
    • The search for a solution to senile cataract
    • Spector, A. (1984). The search for a solution to senile cataract. Invest. Ophthalmol. Vis. Sci. 25, 130-46.
    • (1984) Invest. Ophthalmol. Vis. Sci. , vol.25 , pp. 130-146
    • Spector, A.1
  • 47
    • 0023004105 scopus 로고
    • Cytoskeleton abnormalities in human senile cataract
    • Tagliavini, J. , Gandolfi, S. A. and Maraini, G. (1986). Cytoskeleton abnormalities in human senile cataract. Curr. Eye Res. 5, 903-10.
    • (1986) Curr. Eye Res. , vol.5 , pp. 903-910
    • Tagliavini, J.1    Gandolfi, S.A.2    Maraini, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.