Functional evidence for distinct interaction of hydrophobic arylisothiocyanates with the erythrocyte anion transport protein.
Human erythrocytes were treated with various hydrophobic arylisothiocyanates under conditions which favor modification of distinct proteinaceous nucleophiles. The morphological appearance of phenylisothiocyanate-treated cells was discoid and membrane-bound hydrolases (human acetylcholinesterase, sheep phospholipase A2) were fully active following membrane modification. Noncharged hydrophobic arylisothiocyanates, including phenylisothiocyanate, beta-naphthylisothiocyanate and heterobifunctional azidoarylisothiocyanates inhibited [35S]-sulfate efflux irreversibly. Protection against modification-induced inhibition of sulfate transport was attained by the simultaneous presence of the specific reversible anion transport inhibitor 4,4'-dinitrostilbene-2,2'-disulfonate. Selective protection of a functionally relevant domain of band 3 is concluded to occur based on the above-derived information.
D015058:1-Naphthylisothiocyanate / Q000494:pharmacology; D000110:Acetylcholinesterase / Q000097:blood; D001457:Anion Exchange Protein 1, Erythrocyte / Q000097:blood; D027321:Anion Transport Proteins; D002352:Carrier Proteins / Q000097:blood*; D004910:Erythrocyte Membrane / Q000187:drug effects* / Q000201:enzymology / Q000648:ultrastructure; D006801:Humans; D017879:Isothiocyanates; D010741:Phospholipases A / Q000097:blood; D054467:Phospholipases A2; D013267:Stilbenes / Q000494:pharmacology; D013431:Sulfates / Q000097:blood; D013861:Thiocyanates / Q000494:pharmacology*
D001457:Anion Exchange Protein 1, Erythrocyte; D027321:Anion Transport Proteins; D002352:Carrier Proteins; D017879:Isothiocyanates; D013267:Stilbenes; D013431:Sulfates; D013861:Thiocyanates; C005441:phenylisothiocyanate; D015058:1-Naphthylisothiocyanate; C022306:4,4'-dinitro-2,2'-stilbenedisulfonic acid; D010741:Phospholipases A; D054467:Phospholipases A2; D000110:Acetylcholinesterase; C031287:2-naphthylisothiocyanate