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Vasopressin stimulates, in a dose-dependent manner, the phosphorylation of a 47-kDa protein in the mouse ileum and binds to a 47-kDa phosphotyrosine protein in the mouse ileum.
The regulation of inositol phosphate metabolism by arginine-vasopressin (AVP) was studied in mouse ileum smooth muscle. AVP stimulated inositol phosphate formation in a dose-dependent manner. This response was abolished by pretreatment of the tissue with trifluoperazine (TFP), a calmodulin antagonist. AVP (3 x 10(-12) M) treatment increased the phosphorylation of a 47-kDa protein present in mouse ileum plasma membranes. Similarly, treatment of the tissue with 12.5 microM AVP for 5 min increased the phosphorylation of a 47-kDa protein. 125I-AVP and 125I-arginine-vasopressin (3H-AVP) bound to this protein in crude mouse ileum membrane preparations. Anti-AVP serum inhibited in vitro binding of 125I-AVP and 125I-arginine-vasopressin, but not 125I-angiotensin II, to the 47-kDa phosphotyrosine protein in mouse ileum membranes. Anti-AVP serum did not block the capacity of AVP to induce the phosphorylation of the 47-kDa protein. AVP (3 x 10(-10) M), AVP (1 x 10(-7) M), and oxytocin (1 x 10(-6) M) were equipotent in inducing the phosphorylation of the 47-kDa protein. The binding capacity of AVP to the 47-kDa phosphotyrosine protein was different from that of oxytocin, since AVP was 1000-fold more potent than oxytocin to induce the phosphorylation of the 47-kDa protein in mouse ile
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