Abstract
Activation of protein kinase C (PKC) by phorbol ester (PMA), or by diacylglycerol analogue (OAG) treatment of NIH 3T3 cells resulted in the rapid (within 2–5 min) stimulation (approx. 2-fold) of sodium-dependent phosphate (P i) transport. Conversely, preincubation of these cells with forskolin and cholera toxin, or incubation with 8-bromo-cAMP, to activate cAMP-dependent protein kinase (PKA), resulted in a decrease in Na + P i transport. Activation of either PKC or PKA did not change the V max of P i uptake. However, activation of PKC did result in an increase, while activation of PKA caused a decrease, in the affinity for P i. These results indicate that there is differential regulation of Na + P i uptake in NIH 3T3 cells by activators of PKC (stimulated) and PKA (inhibited) as a consequence of changes in the affinity of the transporter for P i.
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