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Journal of Cell Science, Vol 114, Issue 10 1847-1859, Copyright © 2001 by Company of Biologists
JOURNAL ARTICLES |
S Alais, N Allioli, C Pujades, JL Duband, O Vainio, BA Imhof and D Dunon
UMR-CNRS 7622, Universite Pierre et Marie Curie, France. dunon@ccr.jussieu.fr
HEMCAM/gicerin, an immunoglobulin superfamily protein, is involved in homophilic and heterophilic adhesion. It interacts with NOF (neurite outgrowth factor), a molecule of the laminin family. Alternative splicing leads to mRNAs coding for HEMCAM with a short (HEMCAM-s) or a long cytoplasmic tail (HEMCAM-l). To investigate the cellular function of these two variants, we stably transfected murine fibroblasts with either form of HEMCAM. Expression of each isoform of this protein in L cells delayed proliferation and modified their adhesion properties to purified extracellular matrix proteins. Expression of either HEMCAM-s or HEMCAM-l inhibited integrin-dependent adhesion and spreading of fibroblasts to laminin 1, showing that this phenomenon did not depend on the cytoplasmic region. By contrast, L-cell adhesion and spreading to fibronectin depended on the HEMCAM isoform expressed. Flow cytometry and immunoprecipitation studies revealed that the expression of HEMCAM downregulated expression of the laminin-binding integrins (&agr;)3 (&bgr;)1, (&agr;)6 (&bgr;)1 and (&agr;)7 (&bgr;)1, and fibronectin receptor (&agr;)5 (&bgr;)1 from the cell surface. Semi-quantitative PCR and northern blot experiments showed that the expression of (&agr;)6 (&bgr;)1 integrin modified by HEMCAM occurred at a translation or maturation level. Thus, our data demonstrate that HEMCAM regulates fibroblast adhesion by controlling (&bgr;)1 integrin expression. http://www.biologists.com/JCS/movies/jcs1886.html
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