Site of red cell cation leak induced by mercurial sulfhydryl reagents.
It has been suggested that the human red cell anion transport protein, band 3, is the site not only of the cation leak induced in human red cells by treatment with the sulfhydryl reagent pCMBS (p-chloromercuribenzene sulfonate) but is also the site for the inhibition of water flux induced by the same reagent. Our experiments indicate that N-ethylmaleimide, a sulfhydryl reagent that does not inhibit water transport, also does not induce a cation leak. We have found that the profile of inhibition of water transport by mercurial sulfhydryl reagents is closely mirrored by the effect of these same reagents on the induction of the cation leak. In order to determine whether these effects are caused by band 3 we have reconstituted phosphatidylcholine vesicles containing only purified band 3. Control experiments indicate that these band 3 vesicles do not contain (Na+ + K+)-ATPase as measured by ATP dephosphorylation. pCMBS treatment caused a significant increase in the cation leak in this preparation, consistent with the view that the pCMBS-induced cation leak in whole red cells is mediated by band 3.
D001457:Anion Exchange Protein 1, Erythrocyte / Q000378:metabolism*; D002412:Cations; D002463:Cell Membrane Permeability / Q000187:drug effects*; D002729:Chloromercuribenzoates / Q000494:pharmacology; D004910:Erythrocyte Membrane / Q000187:drug effects*; D005033:Ethylmaleimide / Q000494:pharmacology; D006801:Humans; D007473:Ion Channels / Q000187:drug effects; D010662:Phenylmercuric Acetate / Q000031:analogs & derivatives / Q000494:pharmacology; D013439:Sulfhydryl Reagents / Q000494:pharmacology*; D014867:Water / Q000378:metabolism
D001457:Anion Exchange Protein 1, Erythrocyte; D002412:Cations; D002729:Chloromercuribenzoates; D007473:Ion Channels; D013439:Sulfhydryl Reagents; D014867:Water; C010024:4-aminophenylmercuriacetate; D005033:Ethylmaleimide; D010662:Phenylmercuric Acetate