Carboxyl methylation of human erythrocyte band 3 in intact cells. Relation to anion transport activity.
The anion transport protein of the human erythrocyte membrane, band 3, is reversibly methylated by an endogenous protein carboxyl methyltransferase. The physiological consequence of this modification was studied by measuring the rate of phosphate transport by intact erythrocytes incubated under conditions where protein methylation reactions are inhibited. No change in phosphate transport was detected when cells were treated with either methionine-free media or cycloleucine, whereas cells incubated with adenosine and homocysteine thiolactone displayed a marginally slower rate of transport, which was not reversed by subsequent remethylation of the membrane proteins. These results suggest that erythrocyte protein carboxyl methylation does not directly regulate this activity of band 3.
D000241:Adenosine / Q000494:pharmacology; D001457:Anion Exchange Protein 1, Erythrocyte / Q000378:metabolism*; D000838:Anions / Q000097:blood*; D001692:Biological Transport / Q000187:drug effects; D003515:Cycloleucine / Q000494:pharmacology; D004912:Erythrocytes / Q000187:drug effects / Q000378:metabolism*; D006710:Homocysteine / Q000031:analogs & derivatives / Q000494:pharmacology; D006801:Humans; D008745:Methylation; D010710:Phosphates / Q000097:blood
D001457:Anion Exchange Protein 1, Erythrocyte; D000838:Anions; D010710:Phosphates; D006710:Homocysteine; D003515:Cycloleucine; C007957:homocysteine thiolactone; D000241:Adenosine