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Originally published In Press as doi:10.1074/jbc.M204694200 on August 20, 2002

J. Biol. Chem., Vol. 277, Issue 44, 41342-41351, November 1, 2002
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Complement C5b-9 Membrane Attack Complex Increases Expression of Endoplasmic Reticulum Stress Proteins in Glomerular Epithelial Cells*

Andrey V. CybulskyDagger §, Tomoko TakanoDagger ||, Joan PapillonDagger , Abdelkrim KhadirDagger , Jianhong LiuDagger §**, and Hongwei PengDagger Dagger Dagger

From the Dagger  Department of Medicine, McGill University Health Centre, and § Department of Physiology, McGill University, Montreal, Quebec H3A 1A1, Canada

In the passive Heymann nephritis (PHN) model of membranous nephropathy, complement C5b-9 induces glomerular epithelial cell (GEC) injury, proteinuria, and activation of cytosolic phospholipase A2 (cPLA2). This study addresses the role of endoplasmic reticulum (ER) stress proteins (bip, grp94) in GEC injury. GEC that overexpress cPLA2 (produced by transfection) and "neo" GEC (which expresses cPLA2 at a lower level) were incubated with complement (40 min), and leakage of constitutively expressed bip and grp94 from ER into cytosol was measured to monitor ER injury. Greater leakage of bip and grp94 occurred in complement-treated GEC that overexpress cPLA2, as compared with neo, implying that cPLA2 activation perturbed ER membrane integrity. After chronic incubation (4-24 h), C5b-9 increased bip and grp94 mRNAs and proteins, and the increases were dependent on cPLA2. Expression of bip-antisense mRNA reduced stimulated bip protein expression and enhanced complement-dependent GEC injury. Glomerular bip and grp94 proteins were up-regulated in proteinuric rats with PHN, as compared with normal control. Pretreatment of rats with tunicamycin or adriamycin, which increase ER stress protein expression, reduced proteinuria in PHN. Thus, C5b-9 injures the ER and enhances ER stress protein expression, in part, via activation of cPLA2. ER stress protein induction is a novel mechanism of protection from complement attack.

* This work was supported in part by research grants from the Canadian Institutes of Health Research (CIHR) and the Kidney Foundation of Canada.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.

Holds a Scholarship from the Fonds de la Recherche en Santé du Québec. To whom correspondence should be addressed: Division of Nephrology, Royal Victoria Hospital, 687 Pine Ave. West, Montreal, Quebec H3A 1A1, Canada. Tel.: 514-398-8148; Fax: 514-982-0897; E-mail: andrey.cybulsky@mcgill.ca.

|| Holds a CIHR Scholarship.

** Recipient of a CIHR Studentship.

Dagger Dagger Recipient of a Fellowship from the McGill University Health Centre Research Institute.

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