Plasma membrane-cytoskeleton complex in the normal and cataractous lens

Cytoskeleton: A Multi-Volume Treatise

Volumn 3, Issue C, 1996, Pages 451-517

  Benedetti, E L ^a   Dunia, I ^a   Dufier, J L ^b   Seng, Yit Kim ^c   Bloemendal, H ^d  

^a INSTITUT JACQUES MONOD   (France)

^b HÔPITAL NECKER ENFANTS MALADES   (France)

^c Ministry of Health Cambodia   (Cambodia)

^d RADBOUD UNIVERSITY MEDICAL CENTER   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0038592374     PISSN: 18746020     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1874-6020(96)80017-6     Document Type: Review

References (237)

1. Allen D.P., Low P.S., Dola A., and Maisel H. 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. Comm. 149 (1987) 266-275
2. Anderson D.J., Mostov K.E., and Blobel G. Mechanisms of integration of de novo-synthesized polypeptides into membranes: Signal-recognition particle is required for integration into microsomal membranes of calcium ATPase and of lens MP26 but not cytochrome b5. Proc. Natl. Acad. Sci. USA 80 (1983) 7249-7253
3. Aster J.C., Brewer G.J., and Maisel H. 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 (1986) 115-122
4. Atreya P.L., and Maisel H. In vitro translation of cytoskeletal beaded-chain filament proteins from chicken lens mRNA. Biochem. Biophys. Res. Comm. 163 (1989) 589-598
5. Bagchi M., Caporale M.J., Wetcher R.S., and Maisel H. Vimentin synthesis by ocular lens cells. Exp. Eye Res. 40 (1985) 385-392
6. Balkan W., Klintworth G.K., Bock C.B., and Linney E. Transgenic mice expressing a constitutively active retinoic acid receptor in the lens exhibit ocular defects. Dev. Biol. 151 (1992) 622-625
7. Benedetti E.L., and Dunia I. Differentiation patterns in eye lens fibers. In: Obrecht G., and Stark L. (Eds). New Researches in Presbyopia: From Molecular Biology to Visual Adaptation (1990), Plenum Press 21-31
8. Benedetti E.L., Zweers A., and Bloemendal H. Structural aspects of eye lens polyribosomes. Biochem. J. 108 (1968) 765-770
9. Benedetti E.L., Dunia I., and Bloemendal H. Development of junctions during differentiation of lens fibers. Proc. Natl. Acad. Sci. USA 71 (1974) 5073-5078
10. Benedetti E.L., Dunia I., Ramaekers F.C.S., and Kibbelaar M.A. Lenticular plasma membranes and cytoskeleton. In: Bloemendal H. (Ed). Molecular and Cellular Biology of the Eye Lens (1981), John Wiley and Sons, New York 137-184
11. NATO ASI Series. Benedetti E.L., Dunia I., Manenti S., and Bloemendal H. Biochemical and structural properties of the protein constituent of junctional domains in eye lens fiber plasma membranes. In: Robards, and Lucas (Eds). Communication and Signalling via Cell to Cell Junctions in Plants and Animals (1989), Springer Verlag, New York 35-52
12. Bennett V. The membrane skeleton of human erythrocytes and its implications for more complex cells. Annu. Rev. Biochem. 54 (1985) 273-304
13. Bennett V., and Gilligan D. The spectrin-based membrane skeleton and micron-scale organization of the plasma membrane. Annu. Rev. Cell Biol. 9 (1993) 27-66
14. Beyer E.C. Gap junctions. Int. Rev. Cytol. 137C (1993) 1-37
15. Beyer E.C., and Steinberg T.H. Evidence that the gap junction protein connexin-43 is the ATP-induced pore of mouse macrophages. J. Biol. Chem. 266 (1991) 7971-7974
16. Bloemendal H. Biosynthesis of lens crystallins. In: Bloemendal H. (Ed). Molecular and Cellular Biology of the Eye Lens (1981), John Wiley and Sons 189-220
17. Bloemendal H. The lens proteins. In: Bloemendal H. (Ed). Molecular and Cellular Biology of the Eye Lens (1981), John Wiley and Sons, New York 1-47
18. Bloemendal H. Lens Research: From protein to gene. Exp. Eye Res. 41 (1985) 429-448
19. Bloemendal H. Disorganization of membranes and abnormal intermediate filament assembly lead to cataract. Invest. Ophthal. & Vis. Sci. 32 (1991) 445-455
20. Bloemendal H., Vermorken A.J.M., Kibbelaar M., Dunia I., and Benedetti E.L. Nomenclature for the polypetide chains of lens plasma membranes. Exp. Eye Res. 24 (1977) 413-416
21. Bloemendal H., Benedetti E.L., and Dunia I. Transgenic mice: Models for the study of cataractogenesis. Ophthalmic Res. (1996)
22. Boyer S., Maunoury R., Gomes D., De Nechaud B., Hill A.M., and Dupouey P. Expression of glial fibrillary acidic protein and vimentin in mouse lens epithelial cells during development in vivo and during proliferation and differentiation in vitro: Comparison with the developmental appearance of GFAP in the mouse central nervous system. J. Neurosci. Res. 27 (1990) 55-64
23. Boyer S., Montagutelli X., Gomes D., Simon-Chazottes D., Guenet J.L., and Dupouey P. Recent evolutionary origin of the expression of the glial fibrillary acidic protein (GFAP) in lens epithelial cells. A molecular and genetic analysis of various mouse species. Mol. Brain Res. 10 (1991) 159-166
24. Breitman M.L., Bryce D.M., Giddens E., Clapoff S., Goring D., Tsui L.-Ch., Klintworth G.K., and Bernstein A. Analysis of the lens cell fate and eye morphogenesis in transgenic mice ablated for cells of the lens lineage. Development 106 (1990) 457-463
25. Broekhuyse R.M., Kuhlmann E.D., and Winkens H.J. Lens membrane VII. MIP is an immunological specific component of lens fiber membranes and is identical with 26K band protein. Exp. Eye Res. 29 (1979) 303-314
26. Brunkener M., and Georgatos S.D. Membrane-binding properties of filensin, a cytoskeletal protein of the lens fiber cells. J. Cell Sci. 103 (1992) 709-718
27. Bruzzone R., White T.W., and Paul D.L. Connexions with connexins: The molecular basis of direct intercellular signaling. Eur. J. Biochem. 238 (1996) 1-27
28. Burridge K., Fath K., Kelly T., Nuckolls G., and Turner C. Focal adhesions: Transmembrane junctions between the extracellular matrix and the cytoskeleton. Annu. Rev. Cell Biol. 4 (1988) 487-525
29. Capetanaki Y., Smith S., and Heath J.P. Overexpression of the vimentin gene in transgenic mice inhibits normal lens cell differentiation. J. Cell Biol. 109 (1989) 1653-1664
30. Cartaud A., Jasmin B.J., Changeux J.P., and Cartaud J. Direct involvement of lamin-B-related (54 kDa) protein in the association of intermediate filaments with the post-synaptic membrane of Torpedo marmorata electrocyte. J. Cell Sci. 108 (1995) 153-160
31. Carter J.M., Hutcheson A.M., and Quinlan R.A. 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 (1995) 181-192
32. Cenedella R.J. Regional distribution of lipids and phospholipase A2 activity in normal and cataractous rat lens. Curr. Eye Res. 4 (1985) 113-120
33. Chambers C., and Russell P. Deletion mutation in an eye lens β-crystallin. J. Biol. Chem. 266 (1991) 6742-6746
34. Chevez-Barrios P., Schaffner D.L., Barrios R., Overbeek P.A., Leibovitz R.M., and Lieberman M.W. Expression of the rat TG oncogene in the ciliary body pigment epithelium results in hyperplasia, adenoma and adenocarcinoma. Am. J. Pathol. 143 (1993) 20-28
35. Chepelinsky A.B. The MIP transmembrane channel family. In: Peracchia C. (Ed). Handbook of Membrane Channels: Molecular and Cellular Physiology (1994) 413-432
36. Chrispeels M.J., and Agre P. Aquaporins: Water channel proteins of plant and animal cells. TIBS 19 (1994) 421-425
37. Colucci-Guyon E., Portier M.-M., Dunia I., Paulin D., Pournin S., and Babinet Ch. Mice lacking vimentin develop and reproduce without an obvious phenotype. Cell 79 (1994) 679-694
38. Cooper K., Mathias R.T., and Rae J.L. The physiology of lens junctions. In: Peracchia C. (Ed). Biophysics of Gap-Junction Channels (1991), CRC Press, New York 57-74
39. Costello M.J., MCintosh T.J., and Robertson D. Distribution of gap junctions and square array junctions in the mammalian lens. Invest. Ophthalm. & Vis. Sci. 30 (1989) 975-989
40. Costello M.J., Oliver T.N., and Cobo L.M. Cellular architecture in age related human nuclear cataract. Invest. Ophthalm. & Vis. Sci. 33 (1992) 3209-3227
41. De Jong W.W., Hoekman W.A., Mulders J.W.M., and Bloemendal H. Heat shock response of the rat lens. J. Cell Biol. 102 (1986) 104-111
42. De Jong W., Lubsen N., and Kraft H.J. Molecular evolution of the eye lens. Progress in Ret. Eye Res. 13 (1994) 391-442
43. Delaye M., and Tardieu A. Short-range order of crystallin proteins account for eye lens transparency. Nature (London) 302 (1983) 415-417
44. Denker B.M., Smith B.L., Kuhajda F.P., and Agre P. Identification, purification and partial characterization of a novel Mr28,000 integral membrane protein from erythrocytes and renal tubules. J. Biol. Chem. 263 (1988) 15634-15642
45. Djabali K., Portier M.-M., Gros F., Blobel G., and Georgatos S.D. Network antibodies identify nuclear lamin B as a physiological attachment site for peripherin intermediate filaments. Cell 64 (1991) 109-121
46. Donaldson P., and Kistler J. Reconstitution of channels from preparations enriched in lens gap junction protein MP70. J. Membrane Biol. 129 (1992) 155-165
47. Do Ngoc L., Paroutaud P., Dunia I., Benedetti E.L., and Hoebeke J. Sequence analysis of peptide fragments from the intrinsic protein of calf lens fibers MP26 and its natural maturation product MP22. FEBS Let. 181 (1985) 74-78
48. Duncan G., Stewart S., Prescott A.R., and Warn R.M. Membrane and junctional properties of the isolated frog lens epithelium. J. Membr. Biol. 102 (1988) 195-204
49. Duncan G., Williams M.R., and Riach R.A. Calcium cell signaling and cataract. Progress in Retinal and Eye Research 13 (1994) 623-652
50. Dunia I., Do Ngoc L., Manenti S., and Benedetti E.L. Dilemmas of the structural and biochemical organization of lens membranes during differentiation and aging. Cur. Eye Res. 4 (1985) 1219-1234
51. Dunia I., Manenti S., Rousselet A., and Benedetti E.L. Electron microscopic observations of reconstituted proteoliposomes with the purified major intrinsic membrane protein of eye lens fibers. J. Cell Biol. 105 (1987) 1679-1689
52. Dunia I., Pieper F., Manenti S., Van Der Kemp A., Devilliers G., Benedetti E.L., and Bloemendal H. Plasma membrane-cytoskeleton damage in eye lenses of transgenic mice expressing desmin. Eur. J. Cell Biol. 53 (1990) 59-74
53. Dunia I., Van Der Kemp A., Pieper F., Bloemendal H., and Benedetti E.L. Eye lens structural abnormalities in mice expressing transgenes affecting the organization of intermediate filaments. In: Vrensen G.F.J.M., and Clauwaert J. (Eds). Eye Lens Membrane and Aging. Topics in Aging Research in Europe Vol. 15 (1991), EURAGE, Boca Raton, FL 145-159
54. Dunia I., Smit J.J.M., van der Walk M.A., Bloemendal H., Borst P., and Benedetti E.L. Human MDR3-P-Glycoprotein expression in transgenic mice induces lens membrane alterations leading to cataract. J. Cell Biol. 132 (1996) 701-716
55. Ebihara L. Gap junction proteins in the lens. In: Peracchia C. (Ed). Handbook of Membrane Channels: Molecular and Cellular Physiology (1994), Academic Press, Leiden 403-410
56. Ebihara L.V., Berthoud M., and Beyer E.C. Distinct behavior of Connexin 56 and Connexin 46 ap junctional channels can be predicted from the behavior of their hemi-gap-junctional channels. Biophysical J. 68 (1995) 1796-1803
57. Edelman G.M. Cell adhesion molecules in the regulation of animal form and tissue pattern. Ann. Rev. Cell Biol. 2 (1986) 81-116
58. Edidin M. Patches, posts and fences: Proteins and plasma membrane domains. Trends Cell Biol. 2 (1992) 376-380
59. Edstrôm L., Thornell L.E., and Eriksson A. A new type of hereditary distal myopathy with characteristic sarcoplasmic bodies and intermediate (skeletin) filaments. J. Neurol. Sci. 47 (1980) 171-190
60. Egwuagu C.E., Sztein J., Chi-Chao C., Mahdi R., Nussenblatt R.B., and Chepelinsky A. γ interferon expression disrupts lens and retinal differentiation in transgenic mice. Develop. Biol. 166 (1994) 557-568
61. Ehring G.R., Zampighi G.A., and Hall J.E. Does MIP play a role in cell-cell communication?. In: Hall J.E., Zampighi G.A., and Davis R.M. (Eds). Progress in Cell Research (1993), Elsevier Science Publishers, B.V. 153-162
62. Ellis M., Alousi S., Lawniczak J., Maisel H., and Welsh M. Studies on lens vimentin. Exp. Eye Res. 38 (1984) 195-202
63. Emptage N.G., Duncan G., and Croghan P.C. Internal acidification modulates membrane and junctional resistance in the isolated lens of the frog Exp. Eye Res. 54 (1992) 33-39
64. Evans C.W., Eastwood S., Rains J., Gruijters W.T.M., Bullivant S., and Kistler J. Gap junction formation during development of the mouse. Eur. J. Cell Biol. 60 (1992) 243-249
65. Falk M., Kumar N., and Gilula N.B. Membrane insertion of gap junction connexins: polytopic channel forming membrane proteins. J. Cell Biol. 127 (1994) 343-355
66. Faquin W.C., Husain A., Hung J., and Branton D. An immunoreactive form of erythrocyte protein 4.9 is present in non-erythroid cells. Eur. J. Cell Biol. 46 (1988) 168-175
67. FitzGerald P.G., and Casselman J. Immunological conservation of the fiber cell beaded filament. Curr. Eye Res. 10 (1991) 471-478
68. FitzGerald P.G., and Gottlieb W. The Mr.115kd fiber cell-specific protein is a component of the lens cytoskeleton. Curr. Eye Res. 8 (1989) 801-811
69. FitzGerald P.G., and Graham D. Ultrastructural localization of αA-crystallin to the bovine lens fiber cell cytoskeleton. Curr. Eye Res. 10 (1991) 417-436
70. Fleschner C.R., and Cenedella R.J. Specific restriction of cholesterol from cortical lens gap junctional membrane in the U18666A cataract. Curr. Eye Res. 7 (1988) 1029-1034
71. Fleschner C.R., and Cenedella R.J. Lipid composition of lens plasma membrane fractions enriched in fiber junctions. J. Lipid Res. 32 (1991) 45-53
72. Foisner R., Leichtfried F.E., Herrmann H., Small J.V., Lawson D., and Wiche G. Cytoskeleton-associated plectin: In situ localization, in vitro reconstitution and binding to immobilized intermediate filament proteins. J. Cell Biol. 106 (1988) 723-733
73. Franke W.W., Kapprell H.P., and Cowin P. Plakoglobin is a component of the filamentous subplasmalemmal coat of lens cells. Eur. J. Cell Biol. 43 (1987) 301-315
74. Fuchs E. Keratin genes, epidermal differentiation and animal models for the study of human skin diseases. Bioch. Soc. Trans. 19 (1991) 12-15
75. Fujimoto K. Freeze-fracture replica electron microscopy combined with SDS digestion for cytochemical labeling of integral membrane proteins. Application to the immunogold labeling of intercellular junctional complexes. J. Cell Sci. 108 (1995) 3443-3449
76. Fukui H.N., Merola L.O., and Kinoshita H. A possible cataractogenic factor in the Nakano mouse lens. Exp. Eye Res. 26 (1978) 477-485
77. Gadiparthi N.R., Gutekunst K.A., and Church R.L. Bovine lens 23, 21 and 19 kDa intrinsic membrane proteins have an identical amino-terminal amino acid sequence. FEBS Let. 250 (1989) 483-486
78. Galvan A., Lampe P.D., Chung Hur K., Howard J.B., Eccleston E.D., Arneson M., and Louis C.F. Structural organization of the lens fiber cell plasma membrane protein MP18. J. Biol. Chem. 264 (1989) 19974-19978
79. Garner M.H., and Horwitz J. Catalytic subunit isoforms of mammalian lens Na,K-ATPase. Curr. Eye Res. 13 (1994) 65-77
80. Geiger B. Cytoskeleton-associated cell contacts. Curr. Opi. Cell Biol. 1 (1989) 103-109
81. Geiger K., Howes E., Galfins M., Huang X.J., Travis G.H., and Sarvetnick N. Transgenic mice expressing INTγ in the retina develop inflammation of the eye and photoreceptor loss. Invest. Opthalm. & Vis. Sci. 35 (1994) 2667-2681
82. Georgatos S.D., and Blobel G. Two distinct attachment sites for vimentin along the plasma membrane and the nuclear envelope in avian erythrocytes: A basis for a vectorial assembly of intermediate filaments. J. Cell Biol. 105 (1987) 105-115
83. Georgatos S.D., and Blobel G. Lamin B constitutes an intermediate filament attachment site at the nuclear envelope. J. Cell Biol. 105 (1987) 117-125
84. Georgatos S.D., Gounari F., and Remington S. The beaded intermediate filaments and their potential functions in eye lens. BioEssays 16 (1994) 413-418
85. Gilula N.B., Nishi M., and Kumar N. Gap junctional communication during mouse development. In: Wassarman P.M. (Ed). Advances in Developmental Biology (1992), JAI Press Inc. 163-182
86. Goodenough D.A. The crystalline lens. A system networked by gap junctional intercellular communication. Sem. Cell Biol. 3 (1992) 49-58
87. Goodenough D.A., Dick J.S.B., and Lyons J.E. Lens metabolic cooperation: A study of mouse lens transport and permeability visualized with freeze-substitution, autoradiography and electron microscopy. J. Cell Biol. 86 (1980) 576-589
88. Gorin M.B., Yancey S.B., Cline J., Revel J.P., and Horwitz J. The major intrinsic protein (MIP) of the bovine lens fiber membrane: Characterization and structure based on cDNA cloning. Cell 39 (1984) 49-59
89. Götz W., Theuring F., Favor J., and Herken R. Eye pathology in transgenic mice carrying a MSV-SV 40 large T-construct. Exp. Eye Res. 52 (1991) 41-50
90. Goulielmos G., Gounari F., Remington S., Mmller S., Häner M., Aebi U., and Georgatos S. Filensin and phakinin form a novel type of beaded intermediate filaments and coassemble de novo in cultured cells. J. Cell Biol. 132 (1996) 643-655
91. Gounari F., Merdes A., Quinlan R., Hess J., Fitzgerald P., Ouzounis C.A., and Georgatos S.D. Bovine filensin possesses primary and secondary structure similarity to intermediate filament proteins. J. Cell Biol. 121 (1993) 847-853
92. Groth-Vasselli B., Repke K.B., and Farnsworth P. Regional variations in electrolytes related to resistivity during bovine lens maturation. Exp. Eye Res. 54 (1992) 797-801
93. Gruijters W.T.M. A non-connexon protein (MIP) is involved in eye lens gap-junction formation. J. Cell Sci. 93 (1989) 509-513
94. Gupta V.K., Berthoud V.M., Atal N., Jarillo J.A., Barrio L.C., and Beyer E.C. Bovine Connexin 44, a lens gap junction protein: molecular cloning, immunological characterization and functional expression. Investig. Ophthalmol. & Vis. Sci. 35 (1994) 3747-3758
95. Hamai Y., Fukui N., and Kuwabara T. Morphology of hereditary mouse cataract 18 (1974) 537-546
96. Harding J. Cataract, Biochemistry, Epidemiology and Pharmacology (1991), Chapman & Hall, Greenwich, CT
97. Heins S., and Aebi U. Making heads and tails of intermediate filament assembly, dynamics and networks. Curr. Opi. Cell Biol. 6 (1994) 25-33
98. Hentzen P.C., Bessem C.C., Sorgente N., and Bekhor I. Total poly(A+)-Messenger RNA from bovine lens cofractionates with sucrose purified fiber plasma membrane. Exp. Eye Res. 39 (1984) 51-60
99. Hess J.F., Casselman J.T., and Fitzgerald P.G. cDNA analysis of the 49 kDa lens fiber cell cytoskeletal protein: a new, lens-specific member of the intermediate filament family?. Curr. Eye Res. 12 (1993) 77-88
100. Higgins C.F. ABC transporters: from microorganisms to man. Annu. Rev. Cell Biol. 8 (1992) 67-113
101. Horkovics-Kovats S., and Traub P. Specific interaction of the intermediate filament protein vimentin and its isolated N-terminus with negatively charged phospholipids as determined by vesicle aggregation, fusion, and leakage measurements. Biochemistry 29 (1990) 8652-8657
102. Horwitz J., and Bok D. Conformational properties of the main intrinsic polypeptide (MIP26) isolated from lens plasma membranes. Biochemistry 26 (1987) 8092-8098
103. Ireland M., and Maisel H. Identification of native actin filaments in chick lens fiber cells. Exp. Eye Res. 36 (1983) 531-536
104. Ireland M., and Maisel H. A cytoskeletal protein unique to lens fiber cell differentiation. Exp. Eye Res. 38 (1984) 637-645
105. Ireland M., Lieska N., and Maisel H. Lens actin: Purification and localization. Exp. Eye Res. 37 (1983) 393-408
106. Jarvis L.J., Kumar N., and Louis C.F. The developmental expression of three mammalian lens fiber cell membrane proteins. Investig. Ophthal. & Visual Sci. 34 (1993) 613-621
107. Jiang J.X., and Goodenough D.A. Heteromeric connexons in lens gap junction channels. Proc. Natl. Acad. Sci. USA 93 (1996) 1287-1291
108. Jiang J.X., White T.W., Goodenough D.A., and Paul D. Molecular cloning and functional characterization of chicken lens fiber connexin 45.6. Molec. Biol. Cell 5 (1994) 363-373
109. Jiang J.X., White T.W., and Goodenough D.A. Changes in connexin expression and distribution during chick lens development. Dev. Biol. 168 (1995) 649-661
110. Johnson K.R., Lampe P.D., Chung Hur K., Louis C.F., and Johnson R.G. A lens intercellular junction protein, MP26, is a phosphoprotein. J. Cell Biol. 102 (1986) 1334-1343
111. Kasper M., and Vlebahn Ch. Cytokeratin expression and early lens development. Anat. Embryol. 186 (1992) 285-290
112. Kibbelaar M.A., Selten-Versteegen A.M.E., Dunia I., Benedetti E.L., and Bloemendal H. Actin in mammalian lens. Eur. J. Biochem. 95 (1979) 543-549
113. Kibbelaar M.A., Ramaekers F.C.M., Ringens P.G., Selten-Versteegen A.M.E., Poels L.G., Jap P.H.K., Rossum A.L., Feltkamp T.E.W., and Bloemendal H. Is actin in eye lens a possible factor in visual accommodation?. Nature 285 (1980) 506-508
114. Kistler J., and Bullivant S. Structural and molecular biology of the eye lens membranes. CRC Crit. Rev. Biochem. 24 (1989) 151-181
115. Kistler J., Christie D., and Bullivant S. Homologies between gap junction proteins in lens heart and liver. Nature 331 (1988) 721-723
116. Kistler J., Schaller J., and Sigrist H. MP 38 contains the membrane-embedded domain of the lens fiber gap junction protein MP70. J. Biol. Chem. 265 (1990) 13357-13361
117. Kistler J., Bond J., Donaldson P., and Engel A. Two distinct levels of gap junctional assembly in vitro. J. Struct. Biol. 110 (1993) 28-38
118. Kistler J., Goldie K., Donaldson P., and Engel A. Reconstitution of native-type noncrystalline lens fiber gap junctions from isolated hemichannels. J. Cell Biol. 126 (1994) 1047-1058
119. Klymkowsky M.W., Bachant J.B., and Domingo A. Functions of intermediate filaments. Cell motility. Cytoskeleton 14 (1989) 309-333
120. Kobayashi S., Kasuya M., and Itoi M. Changes in lens proteins induced at the early stage of cataractogenesis in cac (Nakano) mice. Exp. Eye Res. 49 (1989) 553-559
121. Konig N., and Zampighi G.A. Purification of bovine lens cell-to-cell channels composed of connexin 44 and connexin 50. J. Cell Sci. 108 (1995) 3091-3098
122. Kovac M., Geist S.T., Westphale E.M., Kemendy A.E., Civitelli R., Beyer E.C., and Steinberg T.H. Transfected connexin 45 alters gap junction permeability in cells expressing endogenous connexin 43. J. Cell Biol. 130 (1995) 987-995
123. Krimpenfort P.J., Schaart G., Pieper F.R., Ramaekers F.C., Cuypers H.T., Van Den Heuvel R.M., Vree-Egberts W.T., Van Eys G.J., Berns A., and Bloemendal H. Tissue-specific expression of a vimentin-desmin hybrid gene in transgenic mice. EMBO J. 7 (1988) 941-947
124. Kumar N., and Gilula N.B. Molecular biology and genetics of gap junctions channels. Sem. Cell Biol. 3 (1992) 3-16
125. Kumar N., and Gilula N.B. The gap junction communication channel. Cell 84 (1996) 381-388
126. Kumar N., Jarvis L.G., Tenbroek E., and Louis C.F. Cloning and expression of a major rat lens membrane protein MP20. Exp. Eye Res. 56 (1993) 35-43
127. Kuszak J.R. The ultrastructure of epithelial and fiber cells in the crystalline lens. Int. Rev. Cell Cytol. 163 (1995) 306-350
128. Kuszak J.R., Alcala J., and Maisel H. Evidence for sequencial replacement of gap junctions in chick lens development. Exp. Eye Res. 34 (1982) 455-466
129. Lakso M., Sauer B., Mosinger Jr. B., Lee E.J., Manning R.W., Yu S.H., Muldor K.I., and Westphal H. Targeted oncogene activation by site-specific recombination in transgenic mice. Proc. Natl. Acad. Sci. USA 89 (1992) 6232-6236
130. Lampe P.D., Bazzi M.D., Nelsestuen G.L., and Johnson R.G. Eur. J. Biochem. 156 (1986) 351-357
131. Lampe P.D., Kistler J., Hefti A., Bond J., Muller S., Johnson R., and Engel A. In vitro assembly of gap junctions. J. Struct. Biol. 107 (1991) 281-289
132. Lee A.Y.W., Chung S.K., and Chung S.S.M. Demonstration that polyol accumulation is responsible for diabetic cataract by the use of transgenic mice expressing the aldose reductase gene in the lens. Proc. Natl. Acad. Sci. USA 92 (1995) 2780-2784
133. Liang J.J.N., and Xiao-Yan L. Spectroscopic studies on the interaction of calf lens membranes with crystallins. Exp. Eye Res. 54 (1992) 719-724
134. Lieska N., Hsi-Yuan Y., and Maisel H. Reconstitution of the filamentous backbone of lens beaded-chain filaments from a purified 49 kDa polypeptide. Curr. Eye Res. 10 (1991) 1037-1048
135. Lo W.K., Shaw A.P., Takemoto L., Grossniklaus H.E., and Tigges M. Gap junction structures and distribution patterns of immunoreactive connexins 46 and 50 in lens regrowths of Rhesus monkeys. Exp. Eye Res. 62 (1996) 171-180
136. Luna E.J., and Hitt A.L. Cytoskeleton-plasma membrane interactions. Science 258 (1992) 955-964
137. Maisel H., and Ellis M. Cytoskeletal proteins of the aging human lens. Curr. Eye Res. 3 (1984) 369-381
138. Maisel H., and Perry M. Electron microscope observations on some structural proteins of the chick lens. Exp. Eye Res. 14 (1972) 7-12
139. Maisel H., Harding J., Alcala C.V., Kuszac J.R., and Bradley R. The morphology of the lens. In: Bloemendal H. (Ed). Molecular and Cellular Biology of the Eye Lens (1981), John Wiley and Sons, London 49-84
140. Malewicz B., Kumar N.V., Johnson R.J., and Baumann J.W. Lipids in gap junction assembly and function. Lipids 25 (1990) 419-427
141. Manenti S., Dunia I., Le Maire M., and Benedetti E.L. High-performance liquid chromatography of the main polypeptide (MP26) of lens fiber plasma membranes solubilized with n-octyl β-D-glucopyranoside. FEBS Lett. 233 (1988) 148-152
142. Manenti S., Dunia I., and Benedetti E.L. Fatty acid acylation of lens fiber plasma membrane proteins, MP26 and α crystallin are palmitoylated. FEBS Lett. 262 (1990) 356-358
143. Marcantonio J.M. Susceptibility of the bovine lens 115 kDa beaded filament protein to degradation by calcium and calpain. Curr. Eye Res. 11 (1992) 103-108
144. Marcantonio J.M. The effect of Calmodulin on the degradation of lens spectrin and Calpain. In: Vrensen G.F.J.M., and Clauwaert J. (Eds). Eye Lens Membrane and Aging. Topics in Aging Research in Europe Vol. 15 (1991), EURAGE, New York 161-170
145. Martin W.D., Egan R.M., Stevens J.L., and Woodward J.G. Lens-specific expression of a major histocompatibility complex class I molecule disrupts normal lens development and induces cataracts in transgenic mice. Invest. Ophthal. & Visual Sci. 36 (1995) 1144-1154
146. Masaki S., and Watanabe T. cDNA sequence analysis of CP94: Rat lens fiber cell beaded-filament structural protein shows homology to cytokeratins. Biochem. Biophys. Res. Comm. 186 (1992) 190-198
147. Masaki S., Tamai K., Shoji R., and Watanabe T. Defect of a fiber cell-specific 94 kDa-protein in the lens of inherited microphthalmic mutant mouse Elo. Biochem. Biophys. Res. Commun. 179 (1991) 1175-1180
148. Mathias R.T., and Rae J.L. Transport properties of the lens. Am. J. Physiol. 249 (1985) C181-C190
149. Mathias R.T., and Rae J.L. Cell to cell communication in the lens. In: Sperelakis, and Cole W.C. (Eds). Cell Interactions and Gap Junctions (1989), CRC Press, Leiden 29-50
150. McAvoy J.W. Induction of the eye lens. Differentiation 17 (1980) 137-149
151. Merck K.B., Groenen P.J.T.A., Voorter C.E.M., De Haard-Hoekman W.A., Horwitz J., Bloemendal H., and De Jong W.W. Structural and functional similarities of bovine α crystallin and mouse small heat-shock protein. A family of chaperones. J. Biol. Chem. 268 (1993) 1046-1052
152. Merdes A., Brunkener M., Horstmann H., and Georgatos S.D. Filensin: A new vimentin-binding, polymerization-competent, and membrane-associated protein of the lens fiber cell. J. Cell Biol. 115 (1991) 397-410
153. Merdes A., Gounari F., and Georgatos S.D. The 47-kD lens-specific protein Phakinin is a tailess intermediate filament protein and an assembly partner of Filensin. J. Cell Biol. 123 (1993) 1507-1516
154. Michea L.F., De La Fuente M., and Lagos N. Lens major intrinsic protein (MIP) promotes adhesion when reconstituted into large unilamellar liposomes. Biochemistry 33 (1994) 7663-7669
155. Miller T.M., and Goodenough D.A. Gap junctions structures after experimental alteration of junctional channel conductance. J. Cell Biol. 101 (1985) 1741-1748
156. Miller T.M., and Goodenough D.A. Evidence for two physiologically distinct gap junctions expressed by the chick lens epithelial cells. J. Cell Biol. 102 (1986) 194-199
157. Monteiro M.J., and Cleveland D.W. Expression of NF-L and NF-M in fibroblasts reveals coassembly of neurofilaments and vimentin subunits. J. Cell Biol. 108 (1989) 579-593
158. Montiero M.J., Hoffman P.N., Gearhart J.D., and Cleveland D.W. Expression of NF-L in both neuronal and non-neuronal cells of transgenic mice: Increased neurofilament density in exons without affecting caliber. J. Cell Biol. 111 (1990) 1543-1557
159. Morrow J.S., Cianci C.D., Kennedy S.P., and Warren S.L. Polarized assembly of spectrin and ankyrin in epithelial cells. Curr. Top. Membr. 38 (1991) 227-244
160. Fr) mouse congenital cataract. Gen. Res. 49 (1987) 235-238
161. Mulders J.W.M., Stokkermans J., Leunissen J.A.M., Benedetti E.L., Bloemendal H., and De Jong W.W. Interaction of α crystallin with lens plasma membrane. Eur. J. Biochem. 152 (1985) 721-728
162. Mulders S.M., Preston G.M., Deen P.M.T., Guggino W.B., Van Os C.H., and Agre P. Water channel properties of major intrinsic protein of lens. J. Biol. Chem. 270 (1995) 1-7
163. Musil L.S., and Goodenough D.A. Biochemical analysis of Connexin43 intracellular transport, phosphorylation and assembly into gap junctional plaques. J. Cell Biol. 115 (1991) 1357-1374
164. Musil L.S., and Goodenough D.A. Multisubunit assembly of an integral plasma membrane channel protein, gap junction connexin 43, occurs after exit from the ER. Cell 74 (1993) 1065-1077
165. Musil L.S., Beyer E.C., and Goodenough D.A. Expression of the gap junction protein Connexin43 in embryonic chick lens: molecular cloning, ultrastructural localization and post-translational phosphorylation. J. Membr. Biol. 116 (1990) 163-175
166. Nelson W.J., Granger B.L., and Lazarides E. Avian lens spectrin: Subunit composition compared with erythrocyte and brain spectrin. J. Cell Biol. 97 (1983) 1271-1276
167. Ngai J., Coleman T.R., and Lazarides E. Localization of newly synthesized vimentin subunits reveal a novel mechanism of intermediate filament assembly. Cell 60 (1990) 415-427
168. Nicholl I.D., and Quinlan R.A. Chaperone activity of α-crystallins modulates intermediate filament assembly. EMBO J. 13 (1994) 945-953
169. Nielsen S., Smith B.L., Christensen E.I., and Agre P. Distribution of the aquaporin CHIP in secretory and resorptive epithelia and capillary endothelia. Proc. Natl. Acad. Sci. USA 90 (1993) 7275-7279
170. Orii H., Agata K., Sawada K., Eguchi G., and Maisel H. Evidence that the chick lens cytoskeletal protein CP49, belongs to the family of intermediate filament proteins. Curr. Eye Res. 12 (1993) 583-588
171. Pan H., and Griep A.E. Altered cell cycle regulation in the lens of HPV-16 E6 or E7 transgenic mice: Implications for tumor supressor gene function in development. Gen. Dev. 8 (1994) 1285-1299
172. Paul D.L., and Goodenough D. In vitro synthesis and membrane insertion of bovine MP26 an integral protein from lens fiber plasma membrane. J. Cell Biol. 96 (1983) 636-638
173. Paul D.L., Ebihara L., Takemoto L.J., Swenson K.I., and Goodenough D.A. Connexin46, a novel lens gap junction protein induces voltage-gated currents in non-junctional plasma membrane of Xenopus oocytes. J. Cell Biol. 115 (1991) 1077-1089
174. Pelissier J.F., Pouget J., Charpin C., and Figarella D. Myopathy associated with desmin type intermediate filaments, an immunoelectron microscopic study. J. Neurol. Sci. 89 (1989) 49-61
175. Peracchia C., and Girsch S.J. Functional modulation of cell coupling: Evidence for a calmodulin-driven channel gate. Am. J. Physiol. 248 (1985) H765-H782
176. Peracchia C., and Glrsch S.J. Calmodulin site at the C-terminus of the putative lens gap junction protein MIP26. Eye Toxic Res. 6 (1989) 613-621
177. Perez-Castro A.V., Tran V.T., and Nguyen-Huu M.C. Defective lens fiber differentiation and pancreatic tumorigenesis caused by ectopic expression of the cellular retinoic acid-binding protein. J. Development. 119 (1993) 363-375
178. Pieper F.R., Schaart G., Krimpenfort P.J., Henderik J.B., Moshage H.J., Van der Kemp A., Ramaekers F.C., Berns A., and Bloemendal H. Transgenic expression of the muscle-specific intermediate filament protein desmin in nonmuscle cells. J. Cell Biol. 108 (1989) 1009-1024
179. Pieper F.R., Raats J.M.H., Schaarts G., Dunia I., Van der Kemp A., Benedetti E.L., Ramaekers F.C.S., and Bloemendal H. Disruption of vimentin intermediate filaments in transgenic mice by expression of a dominant negative mutant desmin subunit Eur. J. Cell Biol. 68 (1995) 355-368
180. Pisano M.M., and Chepelinsky A. Genomic cloning, complete nucleotide sequence and structure of the human gene encoding the major intrinsic protein (MIP) of the lens. Genomics 11 (1991) 981-990
181. Porte A., Stoeckel M.E., Sacrez A., and Batzenschlager A. Unusual familial cardiomyopathy with storage of intermediate filaments in the cardiac muscular cells. Virchows Arch. A Path. Anat. and Histol. 386 (1981) 43-58
182. Prescott A.R., Duncan G., Rawlins D., and Shaw P.J. Dye communication properties in three regions of the intact frog lens. In: Vrensen G.F.J.M., and Clauwaert J. (Eds). Eye Lens Membrane and Aging. Topics in Aging Research in Europe Vol. 15 (1991), EURAGE, Boca Raton, FL 59-72
183. Quinlan R. The soluble plasma membrane-cytoskeleton complexes and aging in the lens. In: Vrensen G.F.J.M., and Clauwaert J. (Eds). Eye Lens Membrane and Aging. Topics in Aging Research in Europe Vol. 15 (1991), EURAGE, Leiden 171-184
184. Quinlan R.A., Carter J.M., Sandilands A., and Prescott A.R. The beaded filament of the eye lens: An unexpected key to intermediate filament structure and function. Trends. Cell Biol. 6 (1996) 123-126
185. Raats J.M.H., Henderik J.B.J., Verdijk M., Van Oort F.L.G., Gerards W.L.H., Ramaekers F.C.S., and Bloemendal H. Assembly of carboxy-terminally deleted desmin in vimentin-free cells. Eur. J. Cell Biol. 56 (1991) 84-103
186. Rae J. Physiology of the lens. In: Albert D.M., and Jakobiec F. (Eds). Principles and Practice of Ophthalmology: Basic Science (1994), W. Saunders Company, Leiden 82-92
187. Ramaekers F.C.S., Selten-Versteegen A.M.E., Benedetti E.L., Dunia I., and Bloemendal H. In vitro synthesis of the major lens membrane protein. Proc. Natl. Acad. Sci. 77 (1980) 725-729
188. Ramaekers F.C.S., Boomkens T.R., and Bloemendal H. Cytoskeletal and contractile structures in bovine lens cell differentiation. Exp. Eye Res. 135 (1981) 454-461
189. Ramaekers F.C.S., Benedetti E.L., Dunia I., Vorstenbosch P., and Bloemendal H. Polyribosomes associated with microfilaments in cultured lens cells. Biochem. Biophys. Acta 740 (1983) 441-448
190. Rup D.M., Veenstra R.D., Wang H.Z., Brink P.R., and Beyer E.C. Chick connexin-56, a novel lens gap junction protein. Molecular cloning and functional expression. J. Biol. Chem. 268 (1993) 706-712
191. Sandilands A., Prescott A.R., Hutcheson A.M., Quinlan R.A., Casselman J.T., and Fitzgerald P.G. Filensin is proteolytically processed during lens fiber cell differentiation by multiple independent pathways. Eur. J. Cell Biol. 67 (1995) 238-253
192. Sandilands A., Prescott A.R., Carter J.M., Hutcheson A.M., Quinlan R.A., Richards J., and Fitzgerald P.G. Vimentin and CP49/filensin form distinct networks in the lens which are independently modulated during lens fibre cell differentiation. J. Cell Sci. 108 (1995) 1397-1406
193. ins, the first vertebrate cytoplasmic intermediate filament protein with a lamin-like insertion in helix 1B. Cur. Eye Res. 13 (1994) 545-553
194. Sax C.M., Farrell F.X., Zehner Z.E., and Piatigorsky J. Regulation of vimentin gene expression in the ocular lens. Dev. Biol. 136 (1990) 56-64
195. Schinkel A.H., and Borst P. Multidrug resistance mediated by P-glycoproteins. Semin. Cancer Biol. 2 (1991) 213-226
196. Schinkel A.H., Roelofs M.E.M., and Borst P. Characterization of the human MDR3 P-glycoprotein and its recognition by P-glycoprotein-specific monoclonal antibodies. Cancer Res. 51 (1991) 2628-2635
197. 2-treatment with development. J. Cell Biol. 92 (1982) 694-705
198. Shen L., Shrager P., Girsch J.L., Donaldson P.G., and Peracchia C. Channel reconstitution in liposomes and planar lipid bilayers with HPLC-purified MIP26 of bovine lens. J. Membr. Biol. 124 (1991) 21-32
199. Shiels A., and Griffin C.S. In situ hybridisation localises the gene for the major intrinsic protein of eye-lens-fibre cell membranes to human chromosome 12q14. Cytogenet. Cell Genet. 61 (1992) 8-9
200. Shiels A., and Griffin C.S. Localisation of the gene for the major intrinsic protein of eye-lens-fibre cell membranes to mouse chromosome 10 by in situ hybridisation. Cytogenet. Cell Genet. 59 (1992) 300-302
201. Shiels A., and Griffin C.S. Aberrant expression of the gene for lens major intrinsic protein in the CAT mouse. Curr. Eye Res. 12 (1993) 913-921
202. Shiels A., Griffin C.S., and Muggleton-Harris A.L. Immunochemical comparison of the major intrinsic protein of eye-lens fibre cell membranes in mice with hereditary cataracts. Biochem. Biophys. Acta 1097 (1991) 81-85
203. Shiels A., Griffin C.S., and Muggleton-Harris A.L. Restriction fragments length polymorphisms associated with the gene for the major intrinsic protein of eye-lens fibre cell membranes in mice with hereditary cataracts. Biochem. Biophys. Acta 1097 (1991) 318-324
204. Smelser G.K. Embryology and morphology of the lens. Invest. Opht. 4 (1965) 398-410
205. Smit J.J.M., Schinkel A.H., Oude Elferink R.P.J., Groen A.K., Wagenaar E., Van Deemter L., Mol C.A.A.M., Ottenhoff R., Van Der Lugt N.M.T., Van Roon M.A., Van Der Valk M.A., Offerhaus G.J.A., Berns A.J.M., and Borst P. Homozygous disruption of the murine mdr2 P-glycoprotein gene leads to a complete absence of phospholipid from bile and to liver disease. Cell 75 (1993) 451-462
206. Smit J.J.M., Schinkel A.H., Mol C.A.A.M., Majoor D., Mooi W.J., Jongsma A.P.M., Lincke C.R., and Borst P. The tissue distribution of the human MDR3 P-glycoprotein. Lab. Invest. 71 (1994) 638-649
207. Smith A.J., Timmermans-Hereijgers J.L.P.M., Roelofsen B., Wirtz K.W.A., Van Blitterswijk W.J., Smith J.J.M., Schinkel A.H., and Borst P. The human MDR3 P-glycoprotein promotes translocation of phosphatidylcholine through the plasma membrane of fibroblasts from transgenic mice. FEBS Lett. 354 (1994) 263-266
208. Smith B.L., and Agre P. Erythrocyte Mr28,000 transmembrane protein exists as a multisubunit oligomer similar to channel proteins. J. Biol. Chem. 266 (1991) 6407-6415
209. Stauffer K., Kumar N.M., Gilula N.B., and Unwin N. Isolation and purification of gap junctional channels. J. Cell Biol. 115 (1991) 141-150
210. Stoeckel M.E., Osborn M., Porte A., Sacrez A., Batzenschlager A., and Weber K. An unusual familial cardiomyopathy characterized by aberrant accumulations of desmin-type intermediate filaments. Virchows Arch. 393 (1981) 53-60
211. Swenson K., Jordan J.R., Beyer E.C., and Paul D. Formation of gap junctions by expression of connexins in Xenopus oocyte pairs. Cell 57 (1989) 145-155
212. Takemoto L., and Boyle D. Molecular chaperone properties of the high molecular weight aggregate from aged lens. Curr. Eye Res. 12 (1993) 35-44
213. Tassin A.M., Pincon-Raymond M., Paulin D., and Rieger F. Unusual organization of desmin intermediate filaments in muscular dysgenesis and TTX-treated myotubes. Dev. Biol. 129 (1988) 37-47
214. Tekehana M. Hereditary cataract of the Nakano mouse. Exp. Eye Res. 50 (1990) 671-676
215. TenBroek E., Anderson M., Jarvis L., and Louis C. The distribution of the fiber cell intrinsic membrane proteins MP20 and connexin 46 in the bovine lens. J. Cell Sci. 103 (1992) 245-257
216. TenBroek E., Johnson R., and Louis C. Cell-to-cell communication in a differentiating ovine lens culture system. Investig. Ophthalmol. & Vis. Sci. 35 (1994) 215-228
217. Traub P., Perides G., Schimmel H., and Scherbarth A. Interaction of in vitro non-epithlial intermediate filament proteins with total cellular lipids, individual phospholipids, and a phospholipid mixture. J. Biol. Chem. 261 (1986) 10558-10568
218. Tripathi B.J., Tripathi R.C., Borisuth N.S.C., Dhaliwal R., and Dhaliwal D. Rodent models of congenital and hereditary cataract in man. Lens & Toxi. Res. 30 (1984) 74-100
219. Tripathi B.J., Tripathi R.C., Borisuth N.S.C., Dhaliwal R., and Dhaliwal D. Rodent models of congenital and hereditary cataract in man. Lens and Eye Toxicity Res. 8 (1991) 373-413
220. Truscott R.J.W., Marcantonio J., Tomlinson J., and Duncan G. Calcium-induced cleavage and breakdown of spectrin in the rat lens. Biochem. Biophys. Res. Commun. 162 (1989) 1472-1477
221. Unwin N. Is there a common design for cell membrane channels?. Nature 323 (1986) 12-13
222. Vajsar J., Becker L.E., Freedom R.M., and Murphy E.G. Familial desminopathy: Myopathy with accumulation of desmin-type intermediate filaments. J. Neurol. Neurosur. Psy. 56 (1993) 644-648
223. Van Hoek A.N., and Verkman A.S. Functional reconstitution of the isolated erythrocyte water channel CHIP28. J. Biol. Chem. 267 (1992) 18267-18269
224. Van Marle J., Vrensen G., and Van Veen H. Maturing human eye lens fiber membranes and filipin. In: Vrensen G.F.J.M., and Clauwaert J. (Eds). Eye Lens Membrane and Aging. Topics in Aging Research in Europe Vol. 15 (1991), EURAGE, Philadelphia 123-136
225. Van Os C.H., Deen P.M.T., and Dempster J.A. Aquaporins: Water selective channels in biological membranes. Molecular structure and tissue distribution. Biophys. Biochem. Acta 1197 (1994) 291-309
226. Verbavatz J.M., Brown D., Sabolic I., Valenti G., Ausiello D.A., Van Hoek A.N., Tonghui M.A., and Verkman A.S. Tetrameric assembly of CHIP28 water channels in liposomes and cell membranes: A freeze-fracture study. J. Cell Biol. 123 (1993) 605-618
227. White T.W., Bruzzone R., Goodenough D.A., and Paul D. Mouse Cx50 a functional member of the connexin family of gap junction proteins is the lens fiber protein MP70. Mol. Biol. Cell 3 (1992) 711-720
228. White W.T., Bruzzone R., Wolfram S., Paul D., and Goodenough D. Selective interactions among the multiple connexin proteins expressed in the vertebrate lens: The second extracellular domain is a determinant of compatibility between connexins. J. Cell Biol. 125 (1994) 879-892
229. White T.W., Paul D., Goodenough D.A., and Bruzzone R. Functional analysis of selective interactions among rodent connexins. Mol. Biol. Cell 6 (1995) 459-470
230. Watanabe M., Kobayashi H., Rutishauser U., Katar M., Alcala J., and Maisel H. NCAM in the differentiation of embryonic lens tissue. Develop. Biol. 135 (1989) 414-423
231. Weitzer G., and Wiche G. Plectin from bovine lenses. Eur. J. Biochem. 169 (1987) 41-52
232. Wistow G.J., and Piatigorsky J. Lens crystallins: The evolution and expression of proteins for a highly specialized tissue. Ann. Rev. Biochem. 57 (1988) 479-504
233. Yancey S.B., Koh K., Chung J., and Revel J.P. Expression of the gene for Main Intrinsic Polypeptide (MIP): Separate spatial distributions of MIP and β-crystallin gene transcripts in rat lens development. J. Cell Biol. 106 (1988) 705-714
234. Yancey S.B., Biswal S., and Revel J.P. Spatial and temporal patterns of distribution of the gap junction protein connexin 43 during mouse gastrulation and organogenesis. Development 114 (1992) 203-212
235. Zampighi G.A., Hall J.E., Ehring J.R., and Simon S.A. The structural organization and protein composition of lens fiber junctions. J. Cell Biol. 108 (1989) 2255-2275
236. Zampighi G.A., Kreman M., Boorer K.J., Loo D.D.F., Bezanilla F., Chandy G., Hall J.E., and Wright E.M. A method for determining the unitary functional capacity of cloned channels and transporters expressed in Xenopus laevis oocytes. J. Membrane Biol. 148 (1995) 65-78
237. Zigler J.S. Animal models for the study of maturity-onset and hereditary cataract. Exp. Eye Res. 50 (1990) 651-657