Identification of Motifs for Cell Adhesion within the Repeated Domains of Transforming Growth Factor-β-induced Gene,βig-h3 *

作者: Jung-Eun Kim , Song-Ja Kim , Byung-Heon Lee , Rang-Woon Park , Ki-San Kim

DOI: 10.1074/JBC.M002752200

关键词:

摘要: betaig-h3 is a transforming growth factor-beta-inducible cell adhesion molecule that has four characteristic homologous repeated domains. We made recombinant proteins, which were highly active in mediating human corneal epithelial (HCE) and spreading. The 2nd the 4th domains sufficient to mediate HCE adhesion. A sequence analysis showed aspartic acid (Asp) isoleucine (Ile) of are conserved many fasciclin 1 (fas-1) Substitution mutational study identified these two amino acids essential for Synthetic peptides containing Asp Ile, NKDIL EPDIM derived from domains, respectively, almost completely blocked mediated by not only wild type but also each These alone fully In addition, we demonstrated functional receptor alpha(3)beta(1) integrin. results, therefore, establish motifs within betaig-h3, interact with integrin suggest other proteins Asp-Ile their fas-1 could possibly function as molecules.

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