Cytoskeletal proteins of the aging human lens
- 1 January 1984
- journal article
- research article
- Published by Taylor & Francis in Current Eye Research
- Vol. 3 (2), 369-381
- https://doi.org/10.3109/02713688408997222
Abstract
The cytoskeletal proteins of the human lens were studied by SDS-PAGE, 2-D electrophoresis and immunologically. Spectrin, vimentin and actin were identified in the superficial fiber cells of human lenses even to age 87 years. These proteins are lost from the deeper cortical and nuclear fiber cells, where a broad zone of acidic protein (36–42 Kd) emerges even in the transparent normal lens. Age-related changes in the water-soluble fraction include the increased prominence of proteins of 56 Kd and 36 Kd in the cortex, and of 38 Kd in the nucleus.This publication has 29 references indexed in Scilit:
- Normal and Cataractous Human Eye Lens CrystallinsPublished by S. Karger AG ,2015
- Studies on the low molecular weight proteins of human lensExperimental Eye Research, 1981
- Human β-crystallinExperimental Eye Research, 1980
- AGE CHANGES IN THE SKELETON OF THE HUMAN LENSActa Ophthalmologica, 1979
- Racemization in human lens: evidence of rapid insolubilization of specific polypeptides in cataract formation.Proceedings of the National Academy of Sciences, 1978
- The molecular distribution, weight determination and concentration variation of the total water soluble proteins of the human lensExperimental Eye Research, 1978
- Human insoluble lens protein II. Isolation and characterization of a 9600 dalton polypeptideExperimental Eye Research, 1978
- Human insoluble lens protein I. Separation and partial characterization of polypeptidesExperimental Eye Research, 1978
- Absence of low-molecular-weight alpha crystallin in nuclear region of old human lenses.Proceedings of the National Academy of Sciences, 1976
- Studies on the structural proteins of the human lensExperimental Eye Research, 1969