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Research Article Free access | 10.1172/JCI116114

Role of protein kinase C in parathyroid hormone stimulation of renal 1,25-dihydroxyvitamin D3 secretion.

M Janulis, V Tembe, and M J Favus

Department of Medicine, University of Chicago Pritzker School of Medicine, Illinois 60637.

Find articles by Janulis, M. in: PubMed | Google Scholar

Department of Medicine, University of Chicago Pritzker School of Medicine, Illinois 60637.

Find articles by Tembe, V. in: PubMed | Google Scholar

Department of Medicine, University of Chicago Pritzker School of Medicine, Illinois 60637.

Find articles by Favus, M. in: PubMed | Google Scholar

Published December 1, 1992 - More info

Published in Volume 90, Issue 6 on December 1, 1992
J Clin Invest. 1992;90(6):2278–2283. https://doi.org/10.1172/JCI116114.
© 1992 The American Society for Clinical Investigation
Published December 1, 1992 - Version history
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Abstract

PTH is a major regulator of renal proximal tubule 1,25(OH)2D3 biosynthesis. However, the intracellular pathways involved in PTH activation of the mitochondrial 25-hydroxyvitamin D3-1 alpha-hydroxylase (1-OHase) remain unknown. PTH can activate both the adenylate cyclase/protein kinase A (PKA) and the plasma membrane phospholipase C/protein kinase C (PKC) pathways. The present study was undertaken to determine whether PKC may mediate PTH activation of renal 25-hydroxyvitamin D3-1 alpha-hydroxylase activity. Rat PTH 1-34 fragment in vitro translocated PKC activity from cytosolic to soluble membrane fraction from freshly prepared rat proximal tubules. Physiologic concentrations (10(-11)-10(-10) M) of rat PTH 1-34 fragment increased PKC translocation three- to fourfold while PKA activity ratio increased at PTH 10(-7) M. PTH stimulation of PKC and PKA was reduced in the presence of staurosporine (10 nM) by 41 and 29%, respectively. Sangivamycin (10 and 50 microM) also reduced PTH-stimulated PKC translocation, but did not alter PKA activity ratio. In vitro perifusion of renal proximal tubules with PTH (10(-11) M) increased 1,25(OH)2D3 steady-state secretion two- to fourfold. Sangivamycin at the same concentration that inhibited PKC translocation by 52% completely inhibited PTH-stimulated 1,25(OH)2D3 secretion. The present studies indicate that the phospholipase C/PKC pathway may mediate PTH stimulation of mammalian renal proximal tubule 1,25(OH)2D3 secretion.

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