Oxidation of thiol in the vimentin cytoskeleton.
Sublethal doses of H2O2, which induces oxidative stress, cause substantial alteration to the vimentin cytoskeleton in various cell types. We have used a thiol-blot assay to assess thiol status in individual proteins from cell extracts. Vimentin thiol is oxidized in preference to other cytoskeleton proteins. Immunoblot analysis also demonstrated a loss of reactivity to an anti-vimentin monoclonal antibody under non-reducing conditions, possibly due to thiol-group oxidation. During induced oxidative stress a number of proteins become associated with the cytoskeleton extracts.
Rogers
K R
KR
Inflammation Group, London Hospital Medical College, U.K.
Morris
C J
CJ
Blake
D R
DR
D002478:Cells, Cultured; D003599:Cytoskeleton / Q000187:drug effects / Q000378:metabolism*; D005033:Ethylmaleimide / Q000494:pharmacology; D006801:Humans; D006861:Hydrogen Peroxide / Q000494:pharmacology; D015151:Immunoblotting; D010084:Oxidation-Reduction; D013438:Sulfhydryl Compounds / Q000378:metabolism*; D013583:Synovial Membrane / Q000648:ultrastructure; D014746:Vimentin / Q000378:metabolism*
D013438:Sulfhydryl Compounds; D014746:Vimentin; D006861:Hydrogen Peroxide; D005033:Ethylmaleimide