Inhibition of Ca++-ATPase of rat erythrocyte membranes by k-opioid agonists.

The effect of various opioid agonists on Ca++, Mg++-ATPase activity of rat erythrocyte membranes was studied. The Ca++-stimulated component of this enzyme (Ca++-ATPase) showed properties similar to those of the Ca++-pumping ATPase of human erythrocyte membranes, that is, high affinity for Ca++, potentiation by calmodulin, and insensitiveness to Na+. Ethylketocyclazocine (EKC) dose-dependently inhibited this Ca++-ATPase activity at a concentration less than one nM without changing basal Mg++-ATPase activity and this action was reversed by the antagonist Win 44,441. Other opioid agonists mimicked this EKC effect and the rank order of potency was dynorphin (1-13) = greater than EKC greater than levorphanol = morphine = B-endorphin = dihydromorphine greater than leu-enkephalin greater than (D-Ala)2-(D-leu)5-enkephalin (DADL) = morphiceptin. It is concluded that rat erythrocyte membranes possess k-type opioid receptors through which the Ca++-pump is inhibited.