Calcium-induced cleavage and breakdown of spectrin in the rat lens.
Incubation of intact rat lenses under conditions that stimulated a net influx of calcium resulted in a pronounced loss of transparency and a major decrease in the levels of spectrin. The progressive loss of this cytoskeletal component coincided with the appearance of polypeptides of approximately 150 kDa which showed immunoreactivity with an antibody raised to spectrin. These bands disappeared on further incubation. It is, therefore, suggested that a calcium-activated protease is present in the lens which is capable of degrading spectrin by the initial removal of approximately 90 kDa fragments. This process calcium-induced proteolysis may be the basis for the cytoskeletal reorganisation observed during the differentiation of lens fibre cells and may be involved in cataract development.
Truscott
R J
RJ
Department of Chemistry, University of Wollongong, N.S.W. Australia.
Marcantonio
J M
JM
Tomlinson
J
J
Duncan
G
G
D000818:Animals; D015153:Blotting, Western; D002118:Calcium / Q000494:pharmacology*; D066298:In Vitro Techniques; D007908:Lens, Crystalline / Q000378:metabolism*; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000378:metabolism; D010449:Peptide Mapping; D051381:Rats; D013049:Spectrin / Q000378:metabolism*; D013997:Time Factors
D013049:Spectrin; D010447:Peptide Hydrolases; D002118:Calcium