PMID: 11334627May 4, 2001Paper

Protein kinase C-induced phosphorylation modulates the Na(+)-ATPase activity from proximal tubules

Biochimica Et Biophysica Acta
L B RangelC Caruso-Neves

Abstract

This study describes the modulation of the ouabain-insensitive Na(+)-ATPase activity from renal proximal tubule basolateral membranes (BLM) by protein kinase C (PKC). Two PKC isoforms were identified in BLM, one of 75 kDa and the other of 135 kDa. The former correlates with the PKC isoforms described in the literature but the latter seems to be a novel isoform, not yet identified. Both PKC isoforms of BLM are functional since a protein kinase C activator, TPA, increased the total hydroxylamine-resistant 32P(i) incorporation from [gamma-32P]ATP into the BLM. In parallel, TPA stimulated the Na(+)-ATPase activity from BLM in a dose-dependent manner, the effect being reversed by the PKC inhibitor sphingosine. The stimulatory effect of TPA on Na(+)-ATPase involved an increase in the V(max) (from 13.4+/-0.6 nmol P(i) mg(-1) min(-1) to 25.2+/-1.4 nmol P(i) mg(-1) min(-1), in the presence of TPA, P<0.05) but did not change the apparent affinity for Na(+) (K(0.5)=14.5+/-2.1 mM in control and 10.0+/-2.1 mM in the presence of TPA, P>0.07). PKC involvement was further confirmed by stimulation of the Na(+)-ATPase activity by the catalytic subunit of PKC (PKC-M). Finally, the phosphorylation of an approx. 100 kDa protein in the BLM (the sugg...Continue Reading

References

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Citations

May 1, 2012·Pflügers Archiv : European journal of physiology·Miguel A RocafullJesús R del Castillo
May 4, 2007·Experimental Parasitology·Elmo Eduardo de Almeida-AmaralJosé Roberto Meyer-Fernandes
Sep 29, 2019·Archives of Biochemistry and Biophysics·Diogo B PeruchettiCelso Caruso-Neves
Feb 16, 2010·Archives of Biochemistry and Biophysics·Lucienne S LaraCelso Caruso-Neves
Nov 6, 2008·Archives of Biochemistry and Biophysics·Victor Barbosa SaraivaCelso Caruso-Neves

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