The effects of vanadium compounds on the activation of adenylate cyclase from rat adrenal membrane.

In rat adrenal membrane, vanadyl sulfate, but not vanadate, inhibits the nonhydrolyzable GTP analogs-, forskolin- and NaF-stimulated activation process of adenylate cyclase. In these reactions, the half-maximum concentration of vanadyl for inhibition was approx. 0.3 mM. The binding of [3H]guanyl-5'-yl imidodiphosphate to the membrane (Kd = 2 microM) was not affected by vanadyl sulfate under the conditions in which the vanadyl sulfate inhibits the activation process. Also, the binding of ACTH to its receptor was inhibited by neither vanadyl sulfate nor vanadate, and the catalytic unit of adenylate cyclase appears to be unaffected by vanadyl sulfate. When the activation by nonhydrolyzable GTP analog was enhanced by Ca2+, vanadyl sulfate strongly inhibited the activation of adenylate cyclase.