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Originally published In Press as doi:10.1074/jbc.M203799200 on July 16, 2002

J. Biol. Chem., Vol. 277, Issue 38, 34708-34716, September 20, 2002
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Proteomic Analysis Reveals Alterations in the Renal Kallikrein Pathway during Hypoxia-Induced Hypertension*

Visith Thongboonkerdabc, Evelyne Gozalde, Leroy R. Sachleben Jr.d, John M. Arthurf, William M. Piercee, Jian Caie, Julie Chaog, Michael Baderh, Joao B. Pesquerohi, David Gozalde, and Jon B. Kleinajk

From the a Core Proteomics Laboratory, Kidney Disease Program, Department of Medicine, the d Kosair Children's Hospital Research Institute, Department of Pediatrics, and the Departments of e Pharmacology and Toxicology and j Biochemistry and Molecular Biology, University of Louisville, Louisville, Kentucky 40202; the h Max-Delbrück-Center for Molecular Medicine, Berlin-Buch, Germany; the i Department of Biophysics, Escola Paulista de Medicina, São Paolo, Brazil; the Departments of f Medicine and g Biochemistry and Molecular Biology, The Medical University of South Carolina, Charleston, South Carolina 29425; and the k Veterans Affairs Medical Center, Louisville, Kentucky 40202

Obstructive sleep apnea syndrome (OSAS), a disorder characterized by episodic hypoxia (EH) during sleep, is associated with systemic hypertension. We used proteomic analysis to examine differences in rat kidney protein expression during EH, and their potential relationship to EH-induced hypertension. Young male Sprague-Dawley rats were exposed to either EH or sustained hypoxia (SH) for 14 (EH14/SH14) and 30 (EH30/SH30) days. Mean arterial blood pressure was significantly increased only in EH30 (p < 0.0002). Kidney proteins were resolved by two-dimensional-PAGE and were identified by MALDI-MS. Renal expression of kallistatin, a potent vasodilator, was down-regulated in all animals. Expression of alpha -1-antitrypsin, an inhibitor of kallikrein activation, was up-regulated in EH but down-regulated in SH. Western blotting showed significant elevation of B2-bradykinin receptor expression in all normotensive animals but remained unchanged in hypertensive animals. Proteins relevant to vascular hypertrophy, such as smooth muscle myosin and protein-disulfide isomerase were up-regulated in EH30 but were down-regulated in SH30. These data indicate that EH induces changes in renal protein expression consistent with impairment of vasodilation mediated by the kallikrein-kallistatin pathway and vascular hypertrophy. In contrast, SH-induced changes suggest the kallikrein- and bradykinin-mediated compensatory mechanisms for prevention of hypertension and vascular remodeling. To test the hypothesis suggested by the proteomic data, we measured the effect of EH on blood pressure in transgenic hKLK1 rats that overexpress human kallikrein. Transgenic hKLK1 animals were protected from EH-induced hypertension. We conclude that EH-induced hypertension may result, at least in part, from altered regulation of the renal kallikrein system.

* This work was supported by Grants HL66358, HL63912, HL65270, P-20, and RR15576 from the National Institutes of Health, from the American Heart Association AHA-0050442, and from the Department of Veterans Affairs.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

b To whom correspondence should be addressed: Core Proteomics Laboratory, Kidney Disease Program, University of Louisville, 570 South Preston St., Louisville, KY 40202. Tel.: 502-852-2366; Fax: 502-852-4384; E-mail: visith.thongboonkerd@louisville.edu.

c Recipient of the International Fellowship Training Award from the International Society of Nephrology and from the Kidney Foundation of Thailand.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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