Biological action and binding sites for vasopressin on the mesenteric artery from normal and sodium-depleted rats.

We have recently demonstrated specific binding for 3H-arginine8-vasopressin (3H-AVP) to high affinity sites on membranes of rat mesenteric arteries. We have now measured the biological activity of this peptide (AVP) and analogues on the perfused rat mesenteric artery. There was a close relationship between the ED50 of agonists or the pA2 of antagonists on the perfused tissue and the relative potency (IC50) of analogues for displacing 3H-AVP from the membrane preparation. The ED50 measured was 67 +/- 7 ng for AVP and 7.2 +/- 1.1 microgram for oxytocin. In sodium-depleted rats we have observed an increase (27%) of the maximal response to AVP with no significant change in ED50 (from 2.8 +/- 1.0 X 10(-8) M to 1.3 +/- 0.2 X 10(-8) M). On the membrane preparation, the number of binding sites for 3H-AVP was increased from 71 +/- 17 fmole/mg protein (Kd 3.5 +/- 0.5 nM) to 115 +/- 10 fmole/mg protein (Kd 4.8 +/- 0.3 nM) in the sodium-depleted rat by comparison to control animals. These results suggest that AVP and its analogues interact in a similar manner in the in vitro perfused rat mesenteric artery and with the membrane receptors isolated from the same tissue. Receptors for AVP are increased in the mesenteric vascular bed by sodium depletion.