Lateral mobility of beta-receptors involved in adenylate cyclase activation.
Cationized ferritin was found to inhibit the lateral mobility of intramembrane proteins in turkey erythrocyte membranes and the activation of adenylate cyclase by the (--)-epinephrine-bound beta-adrenergic receptor. It was observed that cationized ferritin has only a small direct effect on the beta-receptor and on the adenylate cyclase moiety. It is concluded that the cationized ferritin-induced inhibition of the hormone-dependent cyclase activity results from the inhibition of the lateral mobility of the receptor and therefore a decrease in the bimolecular rate of interaction between the receptor and the enzyme.
D000262:Adenylyl Cyclases / Q000097:blood*; D000818:Animals; D004837:Epinephrine / Q000097:blood*; D004910:Erythrocyte Membrane / Q000187:drug effects / Q000378:metabolism* / Q000648:ultrastructure; D004912:Erythrocytes / Q000378:metabolism*; D005293:Ferritins / Q000494:pharmacology; D005613:Freeze Etching; D007700:Kinetics; D011941:Receptors, Adrenergic / Q000378:metabolism*; D011943:Receptors, Adrenergic, beta / Q000187:drug effects / Q000378:metabolism*; D014422:Turkeys
D011941:Receptors, Adrenergic; D011943:Receptors, Adrenergic, beta; D005293:Ferritins; D000262:Adenylyl Cyclases; D004837:Epinephrine