Biochemical evidence for membrane disintegration in human cataracts.
- 1 March 1981
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 78 (3) , 1892-1895
- https://doi.org/10.1073/pnas.78.3.1892
Abstract
Biochemical evidence is presented for the disintegration of the lens fiber plasma membrane in human cataracts. The intrinsic membrane proteins are found in both the water-soluble and water-insoluble nonmembrane fractions of the cataract lens but not in the normal tissue. Furthermore, in contrast to the normal lens, not all of the lipid found in the cataractous lens is isolated with the membrane fraction. In cataracts, both the membrane and membrane fragments are involved in covalent high molecular weight aggregates with an extrinsic membrane protein (43,000 daltons) and a cytoplasmic protein (gamma-crystallin).This publication has 25 references indexed in Scilit:
- Ultrastructural changes during the development and reversal of galactose cataractsExperimental Eye Research, 1978
- Regulation of protein synthesis, intracellular electrolytes and cataract formation in vitroNature, 1977
- Anterior polar and posterior subcapsular cataract in a patient with retinitis pigmentosa: a light-microscopic and ultrastructural studyExperimental Eye Research, 1976
- X-ray induced cataract in rabbit lensExperimental Eye Research, 1975
- Ion analyses of human cataractous lensesExperimental Eye Research, 1975
- [Scanning electron microscopic studies on the normal and senile cataractous human lenses (author's transl)].1973
- Changes in the lens related to the reduction of transparencyExperimental Eye Research, 1973
- Electrophoretic analysis of the major polypeptides of the human erythrocyte membraneBiochemistry, 1971
- Hydrolysis of phenylthiohydantoins of amino acidsBiochemical and Biophysical Research Communications, 1964
- [INVESTIGATIONS ON LENS PROTEIN AND MICROELECTROPHORESIS OF HYDROSOLUBLE PROTEIN IN SENILE CATARACT].1963