Pedemont C H, Bertorello A M
Department of Pharmacological and Pharmaceutical Sciences, College of Pharmacy, University of Houston, Texas 77204-5515, USA.
J Bioenerg Biomembr. 2001 Oct;33(5):439-47. doi: 10.1023/a:1010675708820.
In different species and tissues, a great variety of hormones modulate Na+,K+-ATPase activity in a short-term fashion. Such regulation involves the activation of distinct intracellular signaling networks that are often hormone- and tissue-specific. This minireview focuses on our own experimental observations obtained by studying the regulation of the rodent proximal tubule Na+,K+-ATPase. We discuss evidence that hormones responsible for regulating kidney proximal tubule sodium reabsorption may not affect the intrinsic catalytic activity of the Na+,K+-ATPase, but rather the number of active units within the plasma membrane due to shuttling Na+,K+-ATPase molecules between intracellular compartments and the plasma membrane. These processes are mediated by different isoforms of protein kinase C and depend largely on variations in intracellular sodium concentrations.
在不同的物种和组织中,多种激素以短期方式调节钠钾ATP酶的活性。这种调节涉及激活不同的细胞内信号网络,这些网络通常具有激素和组织特异性。本综述聚焦于我们通过研究啮齿动物近端小管钠钾ATP酶的调节所获得的实验观察结果。我们讨论了证据,即负责调节肾脏近端小管钠重吸收的激素可能不会影响钠钾ATP酶的内在催化活性,而是由于钠钾ATP酶分子在细胞内区室和质膜之间穿梭,从而影响质膜内活性单位的数量。这些过程由蛋白激酶C的不同同工型介导,并且在很大程度上取决于细胞内钠浓度的变化。