AJP - Renal Physiology, Vol 261, Issue 4 679-F687, Copyright © 1991 by American Physiological Society

ARTICLES

Biochemical and immunological characterization of renal protein kinase C

L. Q. Dong, J. L. Stevens and S. Jaken
W. Alton Jones Cell Science Center, Lake Placid, New York 12946.

Protein kinase C (PKC) plays an important role in regulation of renal transport and metabolic function. To understand the role of a specific PKC isozyme in renal homeostasis, alpha-PKC content, regulation, and localization have been characterized. Immunoadsorption assays were used to determine that 34% of the total rat kidney PKC (measured as phorbol ester receptors) was alpha-PKC. Immunohistochemical staining with alpha-PKC-specific monoclonal antibodies determined that alpha-PKC was present throughout the nephron and was especially concentrated in proximal tubules and papillary collecting ducts. In general, the S3 segment of the proximal tubule stained more intensely than the S1-S2 segments. Cortical collecting ducts stained poorly for alpha-PKC. Interstitial cells of the papilla also stained for alpha-PKC. Subcellular distribution of alpha-PKC could not be determined in tissue sections; however, in cultured proximal tubule epithelial cells, alpha-PKC was localized not only in cytoplasm but also in cell-cell borders and focal contacts. Chromatography of rat kidney soluble fraction revealed two endogenous kinase inhibitors, one which is PKC specific and one which is a more general kinase inhibitor. The presence of negative regulators of PKC activity suggests that both activation and inactivation of PKC are important for normal renal function.

This article has been cited by other articles:

				R. A. Fenton and M. A. Knepper Mouse Models and the Urinary Concentrating Mechanism in the New Millennium Physiol Rev, October 1, 2007; 87(4): 1083 - 1112. [Abstract] [Full Text] [PDF]

				W.-Y. Kim, J.-H. Jung, E.-Y. Park, C.-W. Yang, H. Kim, S. Nielsen, K. M. Madsen, and J. Kim Expression of protein kinase C isoenzymes {alpha}, betaI, and {delta} in subtypes of intercalated cells of mouse kidney Am J Physiol Renal Physiol, November 1, 2006; 291(5): F1052 - F1060. [Abstract] [Full Text] [PDF]

				S. Redling, I. L. Pfaff, M. Leitges, and V. Vallon Immunolocalization of protein kinase C isoenzymes {alpha}, {beta}I, {beta}II, {delta}, and {varepsilon} in mouse kidney Am J Physiol Renal Physiol, August 1, 2004; 287(2): F289 - F298. [Abstract] [Full Text] [PDF]

				L. Yao, D.-Y. Huang, I. L. Pfaff, X. Nie, M. Leitges, and V. Vallon Evidence for a role of protein kinase C-{alpha} in urine concentration Am J Physiol Renal Physiol, August 1, 2004; 287(2): F299 - F304. [Abstract] [Full Text] [PDF]

				I. L. PFAFF, H.-J. WAGNER, and V. VALLON Immunolocalization of Protein Kinase C Isoenzymes {alpha}, {beta}I and {beta}II in Rat Kidney J. Am. Soc. Nephrol., September 1, 1999; 10(9): 1861 - 1873. [Abstract] [Full Text]

				V. Rybin and S. F. Steinberg Thyroid Hormone Represses Protein Kinase C Isoform Expression and Activity in Rat Cardiac Myocytes Circ. Res., September 1, 1996; 79(3): 388 - 398. [Abstract] [Full Text]