2007 JASN IMPACT FACTOR 7.111	HOME   AUTHOR INFO   EDITORIAL BOARD   SUBSCRIBE   FEEDBACK   ALERTS   HELP
advanced	CURRENT ISSUE	ARCHIVES	JASN Express	ONLINE SUBMISSION

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by KAPADIA, R. Articles by AMSLER, K. Search for Related Content PubMed PubMed Citation Articles by KAPADIA, R. Articles by AMSLER, K.

Binding of the Renal Epithelial Cell Line LLC-PK₁ to Laminin Is Regulated by Protein Kinase C

RINA KAPADIA^*, PETER D. YURCHENCO and KURT AMSLER^*

^* Department of Physiology and Biophysics, University of Medicine and Dentistry of New Jersey, Robert Wood Johnson Medical School, Piscataway, New Jersey.
Department of Pathology, University of Medicine and Dentistry of New Jersey, Robert Wood Johnson Medical School, Piscataway, New Jersey.

Correspondence to Dr. Kurt Amsler, Department of Physiology and Biophysics, University of Medicine and Dentistry of New Jersey-Robert Wood Johnson Medical School, 675 Hoes Lane, Piscataway, NJ 08854-5635. Phone: 732-235-4605; Fax: 732-235-5038; E-mail: amsler{at}umdnj.edu

Abstract. The 6ß1 integrin heterodimer has been implicated in the mediation of renal epithelial cell binding to laminin, and it has been suggested that this binding is important for renal morphogenesis and development. Studies of nonrenal cells have suggested that the functional activity of 6ß1 integrin is regulated by protein kinase C (PKC) activity. In this study, the binding of a renal epithelial cell line, LLC-PK₁, to laminin was characterized and the role of PKC activity in the modulation of binding was investigated. LLC-PK₁ cells bound to laminin-coated surfaces in a time- and laminin concentration-dependent manner. Binding was strongly inhibited by anti-ß1 integrin antibodies and by anti-6 integrin antibodies. Antibodies against 2 integrin and 3 integrin had little inhibitory effect. Cells bound to both whole laminin and laminin fragment E8, i.e., the fragment to which the 6ß1 integrin heterodimer binds. Exposure of cells to PKC activators for as little as 2 h enhanced cell binding to laminin approximately twofold, in a protein synthesis-dependent manner. PKC inhibitors antagonized this effect. PKC-stimulated binding was also inhibited by anti-ß1 integrin and anti-6 integrin antibodies. PKC activation did not alter expression of ß1 integrin subunits at the cell surface after short time periods (2 to 4 h), but expression was increased after longer time periods (24 h). These results indicate that the renal epithelial cell line LLC-PK₁ binds to laminin via the 6ß1 integrin heterodimer and binding is enhanced by PKC activation. The PKC-mediated enhancement of binding requires protein synthesis and is mediated in part by activation of surface 6ß1 integrin.

This article has been cited by other articles:

				D.-Y. Wu, J.-Q. Zheng, M. A. McDonald, B. Chang, and J. L. Twiss PKC Isozymes in the Enhanced Regrowth of Retinal Neurites after Optic Nerve Injury Invest. Ophthalmol. Vis. Sci., June 1, 2003; 44(6): 2783 - 2790. [Abstract] [Full Text] [PDF]

Copyright © 2008 by the American Society of Nephrology. Online ISSN: 1533-3450 Print ISSN: 1046-6673