The Laminin α3 LG4 Domain Promotes Cell Adhesion through Syndecans

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概要

• 論文の詳細を見る

• Laminin-5 (α3β3γ2) is localized in the skin basement membrane and regulates various cellular functions. The α chains of laminins have been shown to have various biological activities. We found that the α3 chain LG4 module has activity for cell adhesion. Studies with synthetic peptides delineated the A3G75aR sequence (NSFMALYLSKGR, residues 1412-1423) within LG4 as a major site for both heparin and cell binding. Cell adhesion to LG4 and A3G75aR was inhibited by heparitinase I treatment of cells, suggesting that cell binding to the A3G75aR site was mediated by cell surface heparan sulfate proteoglycans. Stably transfected 293T cells with expression vectors for syndecan-2 and -4, but not glypican-1, specifically adhered to LG4 and A3G75aR. These results indicate that the A3G75aR sequence within the laminin α3 LG4 module is responsible for cell adhesion and suggest that syndecan-2 and -4 mediate this activity. This review focuses on the identification of syndecans as a receptor for cell adhesion to laminin α3L G4 module.

• 日本結合組織学会の論文
• 2003-12-25

著者

• Utani Atsushi

  The Department Of Dermatology Graduate School Of Medicine Chiba University

関連論文

• Neurite Outgrowth Promoting Sites on the Laminin Alpha 3 Chain
• Identification of Biologically Active Sequences on the Laminin Alpha Chain G Domains
• IDENTIFICATION OF HEPARIN-DEPENDENT CELL ADHESION SITE WITHIN LAMININ α4 CHAIN C-TERMINAL GLOBULAR DOMAIN
• Peptide Mapping of Biologically Active Sequences in the Laminin Alpha 4 Chain G Domain
• The Laminin α3 LG4 Domain Promotes Cell Adhesion through Syndecans

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