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Human, bovine, canine, and rabbit lenses were found to contain proteins which cross-react with anti-4.1 serum and which have molecular weights similar to erythrocyte proteins 4.1a and 4.1b (approximately 80 kd). Additionally, bovine, canine, and rabbit lenses contain a 4.1-like protein of approximately 125 kd which is absent from human lens. Proteins which(More)
Bovine lens epithelium, cortex and nucleus were screened for the presence of red-cell-membrane band 4.1-like proteins by using an immunoblot method. Lens epithelial cells were found to contain proteins of Mr 78 000 and higher (approximately 150 000) that cross-reacted with anti-(protein 4.1) sera. Fibre cells of the superficial cortex were also found to(More)
Chick lens fiber cell gap junctions were isolated to homogeneity by the urea-deoxycholate method, characterized ultrastructurally and biochemically, and their lipid composition determined by quantitative thin layer chromatography (TLC). The junctions were estimated to comprise about 52% of the lens fiber plasma membrane. Unlike the junctions of other(More)
The superficial cortical fiber cells of the bovine lens contain membrane-associated proteins of 150,000, 80,000, and 78,000 D that cross-react with antisera prepared against red blood cell (RBC) protein 4.1 (Aster, J. C., G. J. Brewer, S. M. Hanash, and H. Maisel, 1984, Biochem. J., 224:609-616). To further study their relationship to protein 4.1, these(More)
Although immunological homologues of erythrocyte membrane proteins have been individually discovered in a wide variety of tissues and cultured cells, the major structural components of the membrane have not yet been demonstrated simultaneously in the same cell type. Thus, considerable uncertainty continues to exist concerning whether the red cell homologues(More)
We examined 9 cataracts from maturity onset diabetics and 4 senile posterior subcapsular cataracts by scanning electron microscopy, transmission electron microscopy, immunofluorescence for crystallin proteins and actin, histochemical methods and x-ray diffraction. The cataractous regions contained spherical globules up to 20 mu in diameter, often in a(More)
The surface morphology of lens fibers in embryonic and adult chicken lenses has been studied by scanning electron microscopy. As the elongating epithelial cells enter into a state of terminal differentiation they elaborate a number of cellular processes interconnecting neighboring fibers. The interlocking devices take the shapes of balls on a short stalk,(More)
A biochemically active conjugate of calmodulin and tetramethylrhodamine isothiocyanate (CaM-RITC) was synthesized. When incubated with sections of chick lens, this conjugate bound to the surface membranes of lens fiber cells in the presence of absence of calcium. Incubation of lens sections with antibodies to gap junction protein of lens completely blocked(More)
Insulin and insulin-like growth factor I (IGF-I) play a role in lens cell growth and development. The binding of these hormones to their respective receptors with its concomitant signal transduction is an important step in these cellular processes. Hormone binding to adult chicken lens insulin and IGF-I receptors, partially purified from epithelial and(More)
The following lectins: Con A, WGA, sWGA, PNA, RCA and UEA were used to study developmental changes in the expression of glycoconjugates during chicken lens morphogenesis. Con A, WGA, sWGA binding epitopes were observed in the lens placode and vesicle. Once the fiber mass was formed, the glycoconjugates were mainly found at the epithelial-fiber-cell(More)