HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) All Versions of this Article: 290/3/C764    most recent 00285.2005v1 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 ISI Web of Science 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 ISI Web of Science (6) Citing Articles via Google Scholar Google Scholar Articles by Vainionpää, N. Articles by Virtanen, I. Search for Related Content PubMed PubMed Citation Articles by Vainionpää, N. Articles by Virtanen, I.

EXTRACELLULAR MATRIX, CELL INTERACTIONS

Laminin-10 and Lutheran blood group glycoproteins in adhesion of human endothelial cells

¹Institute of Biomedicine/Anatomy, University of Helsinki, Helsinki, Finland; ²Department of Pathophysiology, Cancer Research Institute, Sapporo Medical University School of Medicine, Chuo-ku, Sapporo, Japan; ³Laboratory of Electronics Production Technology, Helsinki University of Technology, Espoo, Finland; ⁴Renal Division, Washington University School of Medicine, St. Louis, Missouri; and ⁵Institut de Biologie et Chimie des Protéines, Unité Mixte de Recherche 5086, Institut Fédératif de Recherche 128 BioSciences Lyon-Gerland, Lyon, France

Submitted 14 June 2005 ; accepted in final form 11 October 2005

Laminin 5-chain, a constituent of laminins-10 and -11, is expressed in endothelial basement membranes. In this study we evaluated the roles of 5 laminins and Lutheran blood group glycoproteins (Lu), recently identified receptors of the laminin 5-chain, in the adhesion of human dermal microvascular and pulmonary artery endothelial cells. Field emission scanning electron microscopy and immunohistochemistry showed that the endothelial cells spread on laminin-10 and formed fibronectin-positive fibrillar adhesion structures. Immunoprecipitation results suggested that the cells produced fibronectin, which they could use as adhesion substratum, during the adhesion process. When the protein synthesis during the adhesion was inhibited with cycloheximide, the formation of fibrillar adhesions on laminin-10 was abolished, suggesting that laminin-10 does not stimulate the formation of any adhesion structures. Northern and Western blot analyses showed that the cells expressed M_r 78,000 and 85,000 isoforms of Lu. Quantitative cell adhesion assays showed that in the endothelial cell adhesion to laminin-10, Lu acted in concert with integrins ₁ and _v3, whereas in the adhesion to laminin-10/11, Lu and integrin ₁ were involved. In the cells adhering to the 5 laminins, Lu and the integrins showed uniform cell surface distribution. These findings indicate that 5 laminins stimulate endothelial cell adhesion but not the formation of fibrillar or focal adhesions. Lu mediates the adhesion of human endothelial cells to 5 laminins in collaboration with integrins ₁ and _v3.

integrin; cycloheximide

This article has been cited by other articles:

				M.-P. Wautier, W. El Nemer, P. Gane, J.-D. Rain, J.-P. Cartron, Y. Colin, C. Le Van Kim, and J.-L. Wautier Increased adhesion to endothelial cells of erythrocytes from patients with polycythemia vera is mediated by laminin {alpha}5 chain and Lu/BCAM Blood, August 1, 2007; 110(3): 894 - 901. [Abstract] [Full Text] [PDF]