IOVS
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Lin, L.
Right arrow Articles by Kurpakus-Wheater, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lin, L.
Right arrow Articles by Kurpakus-Wheater, M.
(Investigative Ophthalmology and Visual Science. 2002;43:2615-2621.)
© 2002 by The Association for Research in Vision and Ophthalmology, Inc.

Laminin {alpha}5 Chain Adhesion and Signaling in Conjunctival Epithelial Cells

Lin Lin and Michelle Kurpakus-Wheater

From the Department of Anatomy and Cell Biology, Wayne State University School of Medicine, Detroit, Michigan.

PURPOSE. To identify peptides of the LG4 module of the laminin {alpha}5 chain that mediate human conjunctival epithelial cell adhesion to the laminin-10 isoform.

METHODS. A peptide corresponding to a major heparin- and cell-binding domain of the LG4 module of the laminin {alpha}5 chain was analyzed. The attachment of conjunctival epithelial cells to the peptide compared with laminin-10 was determined by colorimetric adhesion assay. The role of glycosaminoglycans in mediating adhesion to the peptide was determined by altering their function at the cell surface and by blocking adhesion with exogenous glycosaminoglycans. The role of syndecan-4 in cell adhesion to the peptide was examined by adhesion assay. The role of the peptide in cell signaling was examined by phosphotyrosine Western blot analysis.

RESULTS. The peptide facilitated the adhesion of conjunctival epithelium, although not as efficiently as laminin-10. Heparinase had no effect on adhesion to the peptide. In contrast, adhesion to the peptide decreased in glycosaminoglycan-deficient cells, heparatinase-treated cells, cells blocked with exogenous heparan sulfate proteoglycan, and cells treated with antibodies to the ectodomain of syndecan-4. Cell adhesion to the peptide for 90 or 120 minutes resulted in a significant increase in focal adhesion kinase (FAK) tyrosine phosphorylation, compared with the nonadherent control.

CONCLUSIONS. Human conjunctival epithelial cells use a heparin- and cell-binding peptide of the LG4 module of laminin {alpha}5 chain in adhesion to laminin-10. Syndecan-4 is one mechanism by which the peptide facilitates adhesion. In addition to adhesion, the peptide may function in cell-signaling events.







HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2002 by the Association for Research in Vision and Ophthalmology