Oxidative cross-linking of fodrin parallels a membrane conductance increase in the mammalian lens.
An oxidative cross-linking of the lens spectrin-like protein fodrin was induced by incubating WKY-rat lenses in the presence of the SH-reagent diamide. The oxidation of fodrin was paralleled by an increase in lens membrane conductance. The time relationship between these two events as well as the reversibility of both, achieved by incubating the lens in the presence of dithiothreitol, indicate that normal permeability characteristics of the lens membranes require the integrity of the membrane attached cytoskeleton.
Gandolfi
S A
SA
Istituto di Oftalmologia, Università di Parma, Italy.
Tagliavini
J
J
Belpoliti
M
M
Duncan
G
G
Maraini
G
G
D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism*; D003432:Cross-Linking Reagents / Q000494:pharmacology; D003958:Diamide / Q000494:pharmacology; D004553:Electric Conductivity; D007908:Lens, Crystalline / Q000378:metabolism / Q000502:physiology*; D008566:Membranes / Q000502:physiology; D008840:Microfilament Proteins / Q000378:metabolism*; D010084:Oxidation-Reduction; D051381:Rats; D011919:Rats, Inbred Strains; D013049:Spectrin
D002352:Carrier Proteins; D003432:Cross-Linking Reagents; D003958:Diamide; D008840:Microfilament Proteins; D013049:Spectrin