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Volumn 217, Issue 3, 2000, Pages 257-270

Stabilization and remodeling of the membrane skeleton during lens fiber cell differentiation and maturation

Author keywords

Actin; Lens cytoskeleton; Spectrin; Tropomodulin; Tropomyosin

Indexed keywords

ACTIN; ACTIN BINDING PROTEIN; SPECTRIN; TROPOMODULIN; TROPOMYOSIN;

EID: 0034007480     PISSN: 10588388     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0177(200003)217:3<257::AID-DVDY4>3.0.CO;2-5     Document Type: Article
Times cited : (78)

References (76)
  • 1
    • 0031546410 scopus 로고    scopus 로고
    • Light microscopic variation of fiber cell size, shape and ordering in the equatorial plane of bovine and human lenses
    • Al-Ghoul KJ, Costello MJ. 1997. Light microscopic variation of fiber cell size, shape and ordering in the equatorial plane of bovine and human lenses. Mol Vis 3:2.
    • (1997) Mol Vis , vol.3 , pp. 2
    • Al-Ghoul, K.J.1    Costello, M.J.2
  • 2
    • 0023668669 scopus 로고
    • Band 3 and ankyrin homologues are present in eye lens: Evidence for all major erythrocyte membrane components in same non-erythroid cell
    • Allen DP, Low PS, Dola A, Maisel H. 1987. Band 3 and ankyrin homologues are present in eye lens: evidence for all major erythrocyte membrane components in same non-erythroid cell. Biochem Biophys Res Commun 149:266-275.
    • (1987) Biochem Biophys Res Commun , vol.149 , pp. 266-275
    • Allen, D.P.1    Low, P.S.2    Dola, A.3    Maisel, H.4
  • 3
    • 0033214493 scopus 로고    scopus 로고
    • Identification of a novel tropomodulin isoform, skeletal tropomodulin, that caps actin filament pointed ends in fast skeletal muscle
    • Almenar-Queralt A, Lee A, Conley C, de Pouplana LR, Fowler V. 1999. Identification of a novel tropomodulin isoform, skeletal tropomodulin, that caps actin filament pointed ends in fast skeletal muscle. J Biol Chem 274:28466-28475.
    • (1999) J Biol Chem , vol.274 , pp. 28466-28475
    • Almenar-Queralt, A.1    Lee, A.2    Conley, C.3    De Pouplana, L.R.4    Fowler, V.5
  • 4
    • 0022486518 scopus 로고
    • The 4.1-like proteins of the bovine lens: Spectrin-binding proteins closely related in structure to red blood cell protein 4.1
    • Aster JC, Brewer GJ, Maisel H. 1986. The 4.1-like proteins of the bovine lens: spectrin-binding proteins closely related in structure to red blood cell protein 4.1. J Cell Biol 103:115-22.
    • (1986) J Cell Biol , vol.103 , pp. 115-122
    • Aster, J.C.1    Brewer, G.J.2    Maisel, H.3
  • 5
    • 0026774623 scopus 로고
    • Coincident loss of mitochondria and nuclei during lens fiber cell differentiation
    • Bassnett S, Beebe DC. 1992. Coincident loss of mitochondria and nuclei during lens fiber cell differentiation. Dev Dyn 194:85-93.
    • (1992) Dev Dyn , vol.194 , pp. 85-93
    • Bassnett, S.1    Beebe, D.C.2
  • 6
    • 0032820553 scopus 로고    scopus 로고
    • Molecular architecture of the lens fiber cell basal membrane complex
    • Bassnett S, Missey H, Vucemilo I. 1999. Molecular architecture of the lens fiber cell basal membrane complex. J Cell Sci 112:2155-2165.
    • (1999) J Cell Sci , vol.112 , pp. 2155-2165
    • Bassnett, S.1    Missey, H.2    Vucemilo, I.3
  • 7
    • 0024798108 scopus 로고
    • Cytochalasin prevents cell elongation and increases potassium efflux from embryonic lens epithelial cells: Implications for the mechanism of lens fiber cell elongation
    • Beebe DC, Cerrelli S. 1989. Cytochalasin prevents cell elongation and increases potassium efflux from embryonic lens epithelial cells: implications for the mechanism of lens fiber cell elongation. Lens Eye Toxic Res 6:589-601.
    • (1989) Lens Eye Toxic Res , vol.6 , pp. 589-601
    • Beebe, D.C.1    Cerrelli, S.2
  • 8
    • 0024990463 scopus 로고
    • Spectrin-based membrane skeleton: A multipotential adaptor between plasma membrane and cytoplasm
    • Bennett V. 1990. Spectrin-based membrane skeleton: a multipotential adaptor between plasma membrane and cytoplasm. Physiol Rev 70:1029-1065.
    • (1990) Physiol Rev , vol.70 , pp. 1029-1065
    • Bennett, V.1
  • 10
    • 0021337080 scopus 로고
    • Physical change in cytoplasmic messenger ribonucleoproteins in cells treated with inhibitors of mRNA transcription
    • Dreyfuss G, Adam S, Choi Y-D. 1984. Physical change in cytoplasmic messenger ribonucleoproteins in cells treated with inhibitors of mRNA transcription. Mol Cell Biol 4:415-423.
    • (1984) Mol Cell Biol , vol.4 , pp. 415-423
    • Dreyfuss, G.1    Adam, S.2    Choi, Y.-D.3
  • 11
    • 0023992619 scopus 로고
    • An immunoreactive form of erythrocyte protein 4.9 is present in non-erythroid cells
    • Faquin WC, Husain A, Hung J, Branton D. 1988. An immunoreactive form of erythrocyte protein 4.9 is present in non-erythroid cells. Eur J Cell Biol 46:168-175.
    • (1988) Eur J Cell Biol , vol.46 , pp. 168-175
    • Faquin, W.C.1    Husain, A.2    Hung, J.3    Branton, D.4
  • 12
    • 0033985955 scopus 로고    scopus 로고
    • Tropomodulin and tropomyosin help to reorganize the actin cytoskeleton during lens cell morphogenesis
    • Fischer R, Lee A, Fowler V. 2000. Tropomodulin and tropomyosin help to reorganize the actin cytoskeleton during lens cell morphogenesis. Invest Ophthal Vis Sci 41:166-174.
    • (2000) Invest Ophthal Vis Sci , vol.41 , pp. 166-174
    • Fischer, R.1    Lee, A.2    Fowler, V.3
  • 13
    • 0024210122 scopus 로고
    • Age-related changes in a fiber cell-specific extrinsic membrane protein
    • FitzGerald P. 1988. Age-related changes in a fiber cell-specific extrinsic membrane protein. Curr Eye Res 7:1255-1262.
    • (1988) Curr Eye Res , vol.7 , pp. 1255-1262
    • FitzGerald, P.1
  • 14
    • 0025314680 scopus 로고
    • Tropomodulin: A cytoskeletal protein that binds to the end of erythrocyte tropomyosin and inhibits tropomyosin binding to actin
    • Fowler VM. 1990. Tropomodulin: a cytoskeletal protein that binds to the end of erythrocyte tropomyosin and inhibits tropomyosin binding to actin. J Cell Biol 111:471-481.
    • (1990) J Cell Biol , vol.111 , pp. 471-481
    • Fowler, V.M.1
  • 15
    • 0030021105 scopus 로고    scopus 로고
    • Regulation of actin filament length in erythrocytes and striated muscle
    • Fowler VM. 1996. Regulation of actin filament length in erythrocytes and striated muscle. Curr Opin Cell Biol 8:86-96.
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 86-96
    • Fowler, V.M.1
  • 16
    • 0030949077 scopus 로고    scopus 로고
    • Capping actin filament growth: Tropomodulin in muscle and nonmuscle cells
    • Fowler VM. 1997. Capping actin filament growth: tropomodulin in muscle and nonmuscle cells. Soc Gen Physiol Ser 52:79-89.
    • (1997) Soc Gen Physiol Ser , vol.52 , pp. 79-89
    • Fowler, V.M.1
  • 17
    • 0027102134 scopus 로고
    • Spectrin redistributes to the cytosol and is phosphorylated during mitosis in cultured cells
    • Fowler VM, Adam EJ. 1992. Spectrin redistributes to the cytosol and is phosphorylated during mitosis in cultured cells. J Cell Biol 119: 1559-1572.
    • (1992) J Cell Biol , vol.119 , pp. 1559-1572
    • Fowler, V.M.1    Adam, E.J.2
  • 18
    • 0030802113 scopus 로고    scopus 로고
    • Expression of Cdk5, p35, and Cdk5-associated kinase activity in the developing rat lens
    • Gao CY, Zakeri Z, Zhu Y, He H, Zelenka PS. 1997. Expression of Cdk5, p35, and Cdk5-associated kinase activity in the developing rat lens. Dev Genet 20:267-275.
    • (1997) Dev Genet , vol.20 , pp. 267-275
    • Gao, C.Y.1    Zakeri, Z.2    Zhu, Y.3    He, H.4    Zelenka, P.S.5
  • 19
    • 0014421023 scopus 로고
    • Lens soluble proteins: Correlation with the cytological differentiation in the young adult organ of the chick
    • Genis-Galvez JM, Castro JM, Battaner E. 1968. Lens soluble proteins: correlation with the cytological differentiation in the young adult organ of the chick. Nature 217:652-654.
    • (1968) Nature , vol.217 , pp. 652-654
    • Genis-Galvez, J.M.1    Castro, J.M.2    Battaner, E.3
  • 20
    • 0030717391 scopus 로고    scopus 로고
    • To bead or not to bead? Lens-specific intermediate filaments revisited
    • Georgatos SD, Gounari F, Goulielmos G, Aebi U. 1997. To bead or not to bead? Lens-specific intermediate filaments revisited. J Cell Sci 110:2629-2634.
    • (1997) J Cell Sci , vol.110 , pp. 2629-2634
    • Georgatos, S.D.1    Gounari, F.2    Goulielmos, G.3    Aebi, U.4
  • 21
    • 0026815368 scopus 로고
    • The crystalline lens: A system networked by gap junctional intercellular communication
    • Goodenough DA. 1992. The crystalline lens: a system networked by gap junctional intercellular communication. Semin Cell Biol 3:49-58.
    • (1992) Semin Cell Biol , vol.3 , pp. 49-58
    • Goodenough, D.A.1
  • 22
    • 0028914944 scopus 로고
    • Mechanisms of thin filament assembly in embryonic chick cardiac myocytes: Tropomodulin requires tropomyosin for assembly
    • Gregorio CC, Fowler VM. 1995. Mechanisms of thin filament assembly in embryonic chick cardiac myocytes: tropomodulin requires tropomyosin for assembly. J Cell Biol 129:683-695.
    • (1995) J Cell Biol , vol.129 , pp. 683-695
    • Gregorio, C.C.1    Fowler, V.M.2
  • 23
    • 0029166140 scopus 로고
    • Requirement of pointed-end capping by tropomodulin to maintain actin filament length in embryonic chick cardiac myocytes
    • Gregorio CC, Weber A, Bondad M, Pennise CR, Fowler VM. 1995. Requirement of pointed-end capping by tropomodulin to maintain actin filament length in embryonic chick cardiac myocytes. Nature 377:83-86.
    • (1995) Nature , vol.377 , pp. 83-86
    • Gregorio, C.C.1    Weber, A.2    Bondad, M.3    Pennise, C.R.4    Fowler, V.M.5
  • 24
    • 0025239385 scopus 로고
    • Calmodulin and calcium-dependent protease I coordinately regulate the interaction of fodrin with actin
    • Harris AS, Morrow JS. 1990. Calmodulin and calcium-dependent protease I coordinately regulate the interaction of fodrin with actin. Proc Natl Acad Sci USA 87:3009-3013.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 3009-3013
    • Harris, A.S.1    Morrow, J.S.2
  • 25
    • 0026646876 scopus 로고
    • Contrasting patterns of c-myc and N-myc expression in proliferating, quiescent, and differentiating cells of the embryonic chicken lens
    • Harris LL, Talian JC, Zelenka PS. 1992. Contrasting patterns of c-myc and N-myc expression in proliferating, quiescent, and differentiating cells of the embryonic chicken lens. Development 115: 813-820.
    • (1992) Development , vol.115 , pp. 813-820
    • Harris, L.L.1    Talian, J.C.2    Zelenka, P.S.3
  • 27
    • 0028917316 scopus 로고
    • Expression of functional domains of beta G-spectrin disrupts epithelial morphology in cultured cells
    • Hu R, Moorthy S, Bennett V. 1995. Expression of functional domains of beta G-spectrin disrupts epithelial morphology in cultured cells. J Cell Biol 128:1069-1080.
    • (1995) J Cell Biol , vol.128 , pp. 1069-1080
    • Hu, R.1    Moorthy, S.2    Bennett, V.3
  • 28
    • 0025955448 scopus 로고
    • In vitro proteolysis of brain spectrin by calpain I inhibits association of spectrin with ankyrin-independent membrane binding site(s)
    • Hu R-J, Bennett V. 1991. In vitro proteolysis of brain spectrin by calpain I inhibits association of spectrin with ankyrin-independent membrane binding site(s). J Biol Chem 266:18200-18205.
    • (1991) J Biol Chem , vol.266 , pp. 18200-18205
    • Hu, R.-J.1    Bennett, V.2
  • 29
    • 0021035990 scopus 로고
    • Lens actin: Purification and localization
    • Ireland M, Lieska N, Maisel H. 1983. Lens actin: purification and localization. Exp Eye Res 37:393-408.
    • (1983) Exp Eye Res , vol.37 , pp. 393-408
    • Ireland, M.1    Lieska, N.2    Maisel, H.3
  • 30
    • 0024344616 scopus 로고
    • Adducin: Ca+ +-dependent association with sites of cell-cell contact
    • Kaiser HW, O'Keefe E, Bennett V. 1989. Adducin: Ca+ +-dependent association with sites of cell-cell contact. J Cell Biol 109:557-569.
    • (1989) J Cell Biol , vol.109 , pp. 557-569
    • Kaiser, H.W.1    O'Keefe, E.2    Bennett, V.3
  • 32
    • 0019194787 scopus 로고
    • The surface morphology of embryonic and adult chick lens-fiber cells
    • Kuszak J, Alcala J, Maisel H. 1980. The surface morphology of embryonic and adult chick lens-fiber cells. Am J Anat 159:395-410.
    • (1980) Am J Anat , vol.159 , pp. 395-410
    • Kuszak, J.1    Alcala, J.2    Maisel, H.3
  • 33
  • 34
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli1
  • 35
    • 0027756154 scopus 로고
    • Cell shape and interaction defects in alpha-spectrin mutants in Drosophila melanogaster
    • Lee J, Coyne R, Dubreuil R, Goldstein L, Branton D. 1993. Cell shape and interaction defects in alpha-spectrin mutants in Drosophila melanogaster. J Cell Biol 123:1797-1809.
    • (1993) J Cell Biol , vol.123 , pp. 1797-1809
    • Lee, J.1    Coyne, R.2    Dubreuil, R.3    Goldstein, L.4    Branton, D.5
  • 36
    • 0032407540 scopus 로고    scopus 로고
    • Defining actin filament length in striated muscle: Rulers and caps or dynamic stability?
    • Littlefield R, Fowler VM. 1998. Defining actin filament length in striated muscle: rulers and caps or dynamic stability? Annu Rev Cell Dev Biol 14:487-525.
    • (1998) Annu Rev Cell Dev Biol , vol.14 , pp. 487-525
    • Littlefield, R.1    Fowler, V.M.2
  • 37
    • 0030665258 scopus 로고    scopus 로고
    • Actin filament bundles in cortical fiber cells of the rat lens
    • Lo WK, Shaw AP, Wen XJ. 1997. Actin filament bundles in cortical fiber cells of the rat lens. Exp Eye Res 65:691-701.
    • (1997) Exp Eye Res , vol.65 , pp. 691-701
    • Lo, W.K.1    Shaw, A.P.2    Wen, X.J.3
  • 38
    • 0003147477 scopus 로고
    • Disorders of the red cell membrane
    • Handin RI, editor. Philadelphia: JB Lippincott
    • Lux SE, Palek J. 1995. Disorders of the red cell membrane. In: Handin RI, editor. Blood: principles and practice of hematology. Philadelphia: JB Lippincott. p 1701-1817.
    • (1995) Blood: Principles and Practice of Hematology , pp. 1701-1817
    • Lux, S.E.1    Palek, J.2
  • 39
    • 0021353557 scopus 로고
    • Cytoskeletal proteins of the aging human lens
    • Maisel H, Ellis M. 1984. Cytoskeletal proteins of the aging human lens. Curr Eye Res 3:369-381.
    • (1984) Curr Eye Res , vol.3 , pp. 369-381
    • Maisel, H.1    Ellis, M.2
  • 42
    • 0031014473 scopus 로고    scopus 로고
    • Physiological properties of the normal lens
    • Mathias RT, Rae JL, Baldo GJ. 1997. Physiological properties of the normal lens. Physiol Rev 77:21-50.
    • (1997) Physiol Rev , vol.77 , pp. 21-50
    • Mathias, R.T.1    Rae, J.L.2    Baldo, G.J.3
  • 43
    • 0028126085 scopus 로고
    • Organization and function of the cytoskeleton in polarized epithelial cells: A component of the protein sorting machinery
    • Mays RW, Beck KA, Nelson WJ. 1994. Organization and function of the cytoskeleton in polarized epithelial cells: a component of the protein sorting machinery. Curr Opin Cell Biol 6:16-24.
    • (1994) Curr Opin Cell Biol , vol.6 , pp. 16-24
    • Mays, R.W.1    Beck, K.A.2    Nelson, W.J.3
  • 44
    • 0021237343 scopus 로고
    • Chicken embryo lens cultures mimic differentiation in the lens
    • Menko AS, Klukas KA, Johnson RG. 1984. Chicken embryo lens cultures mimic differentiation in the lens. Dev Biol 103:129-141.
    • (1984) Dev Biol , vol.103 , pp. 129-141
    • Menko, A.S.1    Klukas, K.A.2    Johnson, R.G.3
  • 45
    • 0028978094 scopus 로고
    • Beta 1 integrins in epithelial tissues: A unique distribution in the lens
    • Menko AS, Philp NJ. 1995. Beta 1 integrins in epithelial tissues: a unique distribution in the lens. Exp Cell Res 218:516-521.
    • (1995) Exp Cell Res , vol.218 , pp. 516-521
    • Menko, A.S.1    Philp, N.J.2
  • 46
    • 0017707029 scopus 로고
    • Differentiation of rat lens epithelial cells in tissue culture. II. Effects of cytochalasins B and D on actin organization and differentiation
    • Mousa GY, Trevithick JR. 1977. Differentiation of rat lens epithelial cells in tissue culture. II. Effects of cytochalasins B and D on actin organization and differentiation. Dev Biol 60:14-25.
    • (1977) Dev Biol , vol.60 , pp. 14-25
    • Mousa, G.Y.1    Trevithick, J.R.2
  • 47
    • 0018682160 scopus 로고
    • Actin in the lens: Changes in actin during differentiation of lens epithelial cells in vivo
    • Mousa GY, Trevithick JR. 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
  • 48
    • 0018922519 scopus 로고
    • Regional differences in the composition of the bovine lens urea-soluble protein
    • Nasser S. 1980. Regional differences in the composition of the bovine lens urea-soluble protein. Exp Eye Res 30:109-113.
    • (1980) Exp Eye Res , vol.30 , pp. 109-113
    • Nasser, S.1
  • 49
    • 0025502464 scopus 로고
    • Involvement of the membrane-cytoskeleton in development of epithelial cell polarity
    • Nelson W, Hammerton R, Wang A, Shore E. 1990. Involvement of the membrane-cytoskeleton in development of epithelial cell polarity. Semin Cell Biol 1:359-371.
    • (1990) Semin Cell Biol , vol.1 , pp. 359-371
    • Nelson, W.1    Hammerton, R.2    Wang, A.3    Shore, E.4
  • 50
    • 0020633830 scopus 로고
    • Avian lens spectrin: Subunit composition compared with erythrocyte and brain spectrin
    • Nelson WJ, Granger BL, Lazarides E. 1983. Avian lens spectrin: subunit composition compared with erythrocyte and brain spectrin. J Cell Biol 97:1271-1276.
    • (1983) J Cell Biol , vol.97 , pp. 1271-1276
    • Nelson, W.J.1    Granger, B.L.2    Lazarides, E.3
  • 51
    • 0024349323 scopus 로고
    • Lens crystallins and their genes: Diversity and tissue-specific expression
    • Piatigorsky J. 1989. Lens crystallins and their genes: diversity and tissue-specific expression. FASEB J 3:1933-1940.
    • (1989) FASEB J , vol.3 , pp. 1933-1940
    • Piatigorsky, J.1
  • 52
    • 0029929571 scopus 로고    scopus 로고
    • The intermediate filament cytoskeleton of the lens: An ever changing network through development and differentiation. A minireview
    • Prescott A, Sandilands A, Hutcheson AM, Carter JM, Quinlan RA. 1996. The intermediate filament cytoskeleton of the lens: an ever changing network through development and differentiation. A minireview. Ophthalmic Res 28 Suppl 1:58-61.
    • (1996) Ophthalmic Res , vol.28 , Issue.SUPPL. 1 , pp. 58-61
    • Prescott, A.1    Sandilands, A.2    Hutcheson, A.M.3    Carter, J.M.4    Quinlan, R.A.5
  • 53
    • 0030004555 scopus 로고    scopus 로고
    • The beaded filament of the eye lens: An unexpected key to intermediate filament structure and function
    • Quinlan RA, Carter JM, Sandilands A, Prescott AR. 1996. The beaded filament of the eye lens: an unexpected key to intermediate filament structure and function. Trends Cell Biol 6:123-126.
    • (1996) Trends Cell Biol , vol.6 , pp. 123-126
    • Quinlan, R.A.1    Carter, J.M.2    Sandilands, A.3    Prescott, A.R.4
  • 55
    • 0019833489 scopus 로고
    • Cytoskeletal and contractile structures in bovine lens cell differentiation
    • Ramaekers FC, Boomkens TR, Bloemendal H. 1981. Cytoskeletal and contractile structures in bovine lens cell differentiation. Exp Cell Res 135:454-461.
    • (1981) Exp Cell Res , vol.135 , pp. 454-461
    • Ramaekers, F.C.1    Boomkens, T.R.2    Bloemendal, H.3
  • 56
    • 0027182464 scopus 로고
    • Chicken filensin: A lens fiber cell protein that exhibits sequence similarity to intermediate filament proteins
    • Remington S. 1993. Chicken filensin: a lens fiber cell protein that exhibits sequence similarity to intermediate filament proteins. J Cell Sci 105:1057-1068.
    • (1993) J Cell Sci , vol.105 , pp. 1057-1068
    • Remington, S.1
  • 57
    • 0020156264 scopus 로고
    • Widespread occurrence of avian spectrin in nonerythroid cells
    • Repasky E, Granger B, Lazarides E. 1982. Widespread occurrence of avian spectrin in nonerythroid cells. Cell 29:821-833.
    • (1982) Cell , vol.29 , pp. 821-833
    • Repasky, E.1    Granger, B.2    Lazarides, E.3
  • 58
    • 0028905818 scopus 로고
    • Vimentin and CP49/filensin form distinct networks in the lens which are independently modulated during lens fibre cell differentiation
    • Sandilands A, Prescott A, Carter J, Hutcheson A, Quinlan R, Richards J, FitzGerald P. 1995a. Vimentin and CP49/filensin form distinct networks in the lens which are independently modulated during lens fibre cell differentiation. J Cell Sci 107:1397-1406.
    • (1995) J Cell Sci , vol.107 , pp. 1397-1406
    • Sandilands, A.1    Prescott, A.2    Carter, J.3    Hutcheson, A.4    Quinlan, R.5    Richards, J.6    FitzGerald, P.7
  • 59
    • 0029148358 scopus 로고
    • Filensin is proteolytically processed during lens fiber cell differentiation by multiple independent pathways
    • Sandilands A, Prescott A, Hutcheson A, Quinlan R, Casselman J, FitzGerald P. 1995b. Filensin is proteolytically processed during lens fiber cell differentiation by multiple independent pathways. Eur J Cell Biol 67:238-253.
    • (1995) Eur J Cell Biol , vol.67 , pp. 238-253
    • Sandilands, A.1    Prescott, A.2    Hutcheson, A.3    Quinlan, R.4    Casselman, J.5    FitzGerald, P.6
  • 60
    • 0020625987 scopus 로고
    • Differences in the stress fibers between fibroblasts and epithelial cells
    • Sanger J, Sanger J, Jockusch BM. 1983. Differences in the stress fibers between fibroblasts and epithelial cells. J Cell Biol 96:961-969.
    • (1983) J Cell Biol , vol.96 , pp. 961-969
    • Sanger, J.1    Sanger, J.2    Jockusch, B.M.3
  • 61
    • 0024185459 scopus 로고
    • The actin cytoskeleton
    • Small J. 1988. The actin cytoskeleton. Electron Microsc Rev 1:155-174.
    • (1988) Electron Microsc Rev , vol.1 , pp. 155-174
    • Small, J.1
  • 62
    • 0030696042 scopus 로고    scopus 로고
    • Immunodetection of membrane skeletal protein 4.2 in bovine and chicken eye lenses and erythrocytes
    • Sung LA, Lo W-K. 1997. Immunodetection of membrane skeletal protein 4.2 in bovine and chicken eye lenses and erythrocytes. Curr Eye Res 16:1127-1133.
    • (1997) Curr Eye Res , vol.16 , pp. 1127-1133
    • Sung, L.A.1    Lo, W.-K.2
  • 66
    • 0026008318 scopus 로고
    • Calpactin I in the differentiating embryonic chicken lens: MRNA levels and protein distribution
    • Talian JC, Zelenka PS. 1991. Calpactin I in the differentiating embryonic chicken lens: mRNA levels and protein distribution. Dev Biol 143:68-77.
    • (1991) Dev Biol , vol.143 , pp. 68-77
    • Talian, J.C.1    Zelenka, P.S.2
  • 67
    • 0031880461 scopus 로고    scopus 로고
    • Distinct localizations of tropomyosin isoforms in LLC-PK1 epithelial cells suggests specialized function at cell-cell adhesions
    • Temm-Grove C, Jockusch B, Weinberger R, Schevzov G, Helfman D. 1998. Distinct localizations of tropomyosin isoforms in LLC-PK1 epithelial cells suggests specialized function at cell-cell adhesions. Cell Motil Cytoskel 40:397-407.
    • (1998) Cell Motil Cytoskel , vol.40 , pp. 397-407
    • Temm-Grove, C.1    Jockusch, B.2    Weinberger, R.3    Schevzov, G.4    Helfman, D.5
  • 68
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T, Gordon J. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 76:4350-4354.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 69
    • 0028246498 scopus 로고
    • Immunolocalization of tropomodulin, tropomyosin and actin in spread human erythrocyte skeletons
    • Ursitti JA, Fowler VM. 1994. Immunolocalization of tropomodulin, tropomyosin and actin in spread human erythrocyte skeletons. J Cell Sci 107:1633-1639.
    • (1994) J Cell Sci , vol.107 , pp. 1633-1639
    • Ursitti, J.A.1    Fowler, V.M.2
  • 70
    • 0033563308 scopus 로고    scopus 로고
    • Alpha6 integrin is regulated with lens cell differentiation by linkage to the cytoskeleton and isoform switching
    • Walker J, Menko A. 1999. Alpha6 integrin is regulated with lens cell differentiation by linkage to the cytoskeleton and isoform switching. Dev Biol 210:497-511.
    • (1999) Dev Biol , vol.210 , pp. 497-511
    • Walker, J.1    Menko, A.2
  • 72
    • 0028233519 scopus 로고
    • Identification and characterization of tropomodulin and tropomyosin in the adult rat lens
    • Woo MK, Fowler VM. 1994. Identification and characterization of tropomodulin and tropomyosin in the adult rat lens. J Cell Sci 107:1359-1367.
    • (1994) J Cell Sci , vol.107 , pp. 1359-1367
    • Woo, M.K.1    Fowler, V.M.2
  • 73
    • 0033198370 scopus 로고    scopus 로고
    • Members of the Bcl-2 and caspase families regulate nuclear degeneration during chick lens fibre differentiation
    • Wride MA, Parker E, Sanders EJ. 1999. Members of the Bcl-2 and caspase families regulate nuclear degeneration during chick lens fibre differentiation. Dev Biol 213:142-156.
    • (1999) Dev Biol , vol.213 , pp. 142-156
    • Wride, M.A.1    Parker, E.2    Sanders, E.J.3
  • 75
    • 0018682298 scopus 로고
    • Developmental changes in proteins of purified membranes of chicken lenses and evidence for contamination by cytoplasmic delta-crystallin
    • Zelenka P, Reszelbach R, Piatigorsky J. 1979. Developmental changes in proteins of purified membranes of chicken lenses and evidence for contamination by cytoplasmic delta-crystallin. Biochim Biophys Acta 556:447-456
    • (1979) Biochim Biophys Acta , vol.556 , pp. 447-456
    • Zelenka, P.1    Reszelbach, R.2    Piatigorsky, J.3
  • 76
    • 84984087137 scopus 로고
    • Lens-specific antigens and cytodifferentiation in the developing lens
    • Zwaan J. 1968. Lens-specific antigens and cytodifferentiation in the developing lens. J. Cell Physiol 72 (Suppl.1):47-72.
    • (1968) J. Cell Physiol , vol.72 , Issue.SUPPL. 1 , pp. 47-72
    • Zwaan, J.1


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