Hanley R M, Weinman E J
Department of Internal Medicine, University of Texas Medical School, Houston.
Second Messengers Phosphoproteins. 1991;13(2-3):111-6.
Calcium-calmodulin dependent protein kinase II (CaM-KII) has been implicated in the inhibition of Na(+)-H+ exchange activity in the brush border of the renal proximal convoluted tubule. Conversely, the activity of the antiporter is stimulated in response to phosphorylation by calcium-phospholipid dependent protein kinase (PKC). In these experiments, we explored the potential for direct interaction between these two protein kinases by determining the effect of PKC activation by tumor promoting phorbol esters on the expression of mRNA for CaM-KII in the rabbit renal proximal tubule. The results indicate that activation of PKC reduced the steady-state levels of the mRNA for the alpha subunit of CaM-KII in a dose and time dependent manner. This suggests a novel mechanism by which PKC can antagonize the action of CaM-KII in selected tissues.
钙调蛋白依赖性蛋白激酶II(CaM-KII)与肾近端曲管刷状缘中Na(+)-H+交换活性的抑制有关。相反,钙磷脂依赖性蛋白激酶(PKC)磷酸化可刺激该反向转运体的活性。在这些实验中,我们通过确定肿瘤促进佛波酯激活PKC对兔肾近端小管中CaM-KII mRNA表达的影响,探讨了这两种蛋白激酶之间直接相互作用的可能性。结果表明,PKC的激活以剂量和时间依赖性方式降低了CaM-KII α亚基mRNA的稳态水平。这提示了一种新的机制,通过该机制PKC可在特定组织中拮抗CaM-KII的作用。