Abstract
Characteristics of signal transduction systems mediated by protein kinase-C (Ca2+/phospholipid-dependent protein kinase) and estradiol receptors in cow placenta and caruncle were conducted by evaluating protein kinase-C activity and estradiol receptor concentrations and by exploring substrate proteins for the enzyme. The enzyme activity was detected in cytosolic and total particulate fractions of both tissues. The activity levels in these fractions were comparable to those in other cow tissues such as liver and mammary gland. The enzyme activity was inhibited by palmitoylcarnitine, gossypol and adriamycin, known phospholipid-interacting inhibitors of the enzyme. Phosphorylation by the enzyme and subsequent autoradiography revealed that only 125K protein in placental cytosol and two low molecular weight proteins in caruncular cytosol were found to be substrates for protein kinase-C. Ca2+ acts as inhibitor of the phosphorylation of several phosphoproteins other than the substrates. Estradiol receptor concentrations in cytosolic and nuclear fractions were similar in both tissues, and the cytosolic concentrations were also comparable to those in pregnant uterus. However, the nuclear concentrations were extremely low when compared to those in the uterus. The signal transduction systems mediated by protein kinase-C and by estradiol receptors seem to be concertedly suppressed in cow placenta and caruncle.
