IEPA.d55.s139
After protein kinase C activity was functionally depleted by treating cells with phorbol 12-myristate 13-acetate for 24 hours, AVP did not augment IL-1beta-induced NO production
IEPA.d55.s140
The effect of AVP was also inhibited in the presence of the protein kinase C inhibitor calphostin C
IEPA.d55.s141
The addition of AVP increased protein kinase C activity in cardiac myocytes, and its effect was significantly inhibited in the presence of calphostin C
IEPA.d55.s142
These results support the hypothesis that the heart may be a target organ for AVP and that AVP modulates IL-1beta-induced iNOS expression in myocytes through the V1a receptor, which is mediated at least partially via activation of protein kinase C