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Original Article

Amino Acid Transport and Protein Synthesis in Human Normal and Cataractous Lenses

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Pages 1299-1308 | Received 02 Jul 1987, Accepted 30 Sep 1987, Published online: 02 Jul 2009

References

  • Harding J. J., Crabbe M. J.C. The lens: development, proteins, metabolism and cataract. The Eye, H. Davson. Academic Press, LondonUK 1984; Vol lb: 205–492
  • Hightower K. R., Kinsey V. E. Transport and bioelectric properties in post mortem lenses. Exp. Eye Res. 1980; 30: 19–28
  • Maraini G., Pasino M. Active and passive Rubidium influx in normal human lenses and senile cataracts. Exp. Eye Res. 1983; 36: 543–550
  • Lucas V. A., Duncan G., Davies P. D. Membrane permeability characteristics of perfused human senile cataractous lenses. Exp. Eye Res. 1986; 42: 151–165
  • Duncan G., Jacob T. J.C. Calcium and the physiology of cataract. Human Cataract Formation, J. Nugent, J. Whelan. Ciba Foundation. 1984; 132–152, Symposium 106
  • Hightower K. R., Farnum R. Calcium induces opacities in cultured human lenses. Exp. Eye Res. 1985; 41: 565–568
  • Hightower K. R., Harrison S. E. Valinomycin cataract: the relative role of calcium and sodium accumulation. Exp. Eye Res. 1982; 34: 941–943
  • Boutros G., Koch H.-R., Jansen R., Jacob T. J.C., Duncan G. Effect of 8-methoxypsoralen on rat lens cations, membrane potential and protein levels. Exp. Eye Res. 1984; 38: 509–513
  • Shearer T. R., David L. L. Role of calcium in selenium cataract. Curr. Eye Res. 1983; 2: 777–784
  • Marcantonio J. M., Duncan G. Calcium-induced opacification and loss of protein in the organ-cultured bovine lens. Exp. Eye Res. 1986; 42: 617–630
  • Jedziniak J. A., Kinoshita J. H., Yates E. M., Hocker L. O., Benedek G. B. Calcium-induced aggregation of bovine lens alpha crystallins. Invest. Ophthalmol. 1972; 11: 905–915
  • Spector A., Adams D., Krul K. Calcium and high molecular weight protein aggregates in human cataract Invest. Ophthalmol. 1974; 13: 982–990
  • Giblin F. J., Hightower K. R., Ragatzki P. A., Reddy V. N. Calcium-induced high molecular weight proteins in the intact rabbit lens. Exp. Eye Res. 1984; 39: 9–17
  • Hightower K. R. The influence of calcium on protein synthesis in the rabbit lens. Invest. Ophthalmol. Vis. Sci. 1983; 24: 1422–1426
  • Marcantonio J. M., Duncan G. Amino acid transport and crystallin synthesis in the bovine lens. Exp. Eye Res. 1983; 36: 429–440
  • Marcantonio J. M., Marainz G. Amino acid transport and protein synthesis in the rabbit lens: absence of cryoprobe effect. Curr. Eye Res. 1984; 3: 667–671
  • Pirie A. Colour and solubility of the proteins of human cataracts. Invest. Ophthalmol. 1968; 7: 634–642
  • Marcantonio J. M., Duncan G., Davies P. D., Bushell A. R. Classification of human senile cataracts by nuclear colour and sodium content. Exp. Eye Res. 1980; 31: 227–237
  • Van Heyningen R. C. The human lens. 1. A comparison of cataracts extracted in Oxford and Shikarpur. Exp. Eye Res. 1972; 13: 136–147
  • Duncan G., Bushell A. R. Ion analysis of human cataractous lenses. Exp. Eye Res. 1975; 20: 223–230
  • Kinoshita J. H., Kern H. L., Merolo L. O. Factors affecting the cation transport of calf lens. Biochim. Biophys. Acta. 1961; 47: 458–466
  • Cotlier E., Beaty C. The role of Na+ ion in the transport of AIB and other amino acids into the lens. Invest. Ophthalmol. 1967; 6: 64–75
  • Maraini G., Carta F., Pescatori A., Prosperi L. Protein metabolism in human senile cataract. Exp. Eye Res. 1971; 11: 83–88
  • Kinoshita J. H., Merolo L. O., Hayman S. Osmotic effects on the amino acid-concentrating mechanism in the rabbit lens. J. Biol. Chem. 1965; 240: 310–315
  • Thomson J. A., Augusteyn R. C. Ontogeny of human lens crystallins. Exp. Eye Res. 1985; 40: 393–410
  • Ringens P. J., Hoenders H. J., Bloemendal H. Biosynthesis of human lens proteins in organ culture. Exp. Eye Res. 1982; 34: 825–830
  • Yoshida H., Murachi T., Tsukahara I. Limited proteolysis of bovine lens α-crystallin by calpain, a Ca++ -dependent cysteine proteinase, isolated from the same tissue. Biochim. et Biophys. Acta. 1984; 798: 252–259
  • Yoshida H., Yumoto N., Tsukahara I., Murachi T. The degradation of α-crystallin at its carboxyl-terminal portion by calpain in bovine lens. Invest. Ophthalmol. Vis. Sci. 1986; 27: 1269–1273
  • Spector A., Rothschild C. The effect of calcium upon the re-aggregation of bovine α-crystallin. Invest. Ophthalmol. 1973; 12: 225–231
  • Hightower K. R. Cytotoxic effects of internal calcium on lens physiology: a review. Curr. Eye Res. 1985; 4: 453–459
  • Shearer T. R., David L. L., Anderson R. S. Selenite cataract: a review. Curr. Eye Res. 1987; 6: 289–300
  • Mathias R. T., Rae J. L., Riquelme G. Modulation of intercellular communication in the frog lens. Proceedings of the International Society for Eye Research 1986; 4: 129
  • Harding C. V., Unakar N. J., Bobrowski W. F., Dang L., Tsui J. Y., Harding D. Elemental analysis of the rat galactose cataract. Suppl. to Invest. Ophthal. Vis. Sci. 1987; 28: 88
  • Bekhor I., Hsu M.-Y., Davis C., Unakar N. J. Crystallin mRNA product levels in lens undergoing reversal and inhibition of cataracts. Suppl. to Invest. Ophthalmol. Vis. Sci. 1987; 28: 282
  • Maraini G., Mangili R. Differences in proteins and in the water balance of the lens in nuclear and cortical types of senile cataract. The Human Lens in Relation to Cataract. Assoc. Scientific Pub., Amsterdam 1973; 79–95, CIBA Symposium 19

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