PMID: 8471634Apr 16, 1993Paper

Differential effects of activation of protein kinase C and cyclic-AMP-dependent protein kinase on sodium-dependent phosphate uptake in NIH 3T3 cells

Biochimica Et Biophysica Acta
Z OlahW B Anderson

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 (Pi) 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+/Pi transport. Activation of either PKC or PKA did not change the Vmax of Pi uptake. However, activation of PKC did result in an increase, while activation of PKA caused a decrease, in the affinity for Pi. These results indicate that there is differential regulation of Na+/Pi 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 Pi.

References

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May 2, 2006·Proceedings of the National Academy of Sciences of the United States of America·Cyrille SageZheng-Yi Chen

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Citations

Apr 5, 2002·Journal of Virology·Christine SalaünJean Michel Heard
Sep 17, 2002·Molecular Therapy : the Journal of the American Society of Gene Therapy·Thomas RelanderJohan Richter
Mar 6, 1999·The Journal of Biological Chemistry·Z JobbagyW B Anderson

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