Synthetic pentapeptide from the B1 chain of laminin promotes B16F10 melanoma cell migration

✍ Scribed by Y. Iwamoto; J. Graf; M. Sasaki; H. K. Kleinman; D. R. Greatorex; G. R. Martin; F. A. Robey; Y. Yamada

• Publisher: John Wiley and Sons
• Year: 1988
• Tongue: English
• Weight: 511 KB
• Volume: 134
• Category: Article
• ISSN: 0021-9541
• DOI: 10.1002/jcp.1041340216

✦ Synopsis

Laminin is a basement membrane-specific glycoprotein that promotes cell adhesion, proliferation, differentiation, and tumor cell migration. Synthetic peptides from the amino arid sequence deduced from a cDNA clone of the B1 chain of laminin were tested for their ability to promote the migration of B16F10 melanoma cells. A peptide, CDPGYIGSR, that is able to mediate epithelial cell attachment to laminin was found to promote migration, and the constituent pentapeptide YIGSR was also active but to a lesser degree. This nine-amino acid peptide blocked migration of melanoma cells to laminin but had no effect on migration to fibronectin. These data suggest that the cellbinding site and migration site on laminin share a common sequence that is unique to laminin.

Laminin, a large cross-shaped glycoprotein (Mr = 800,000), is a major constituent of all basement membranes (Timpl et al., 1979;Engel et al., 1981). It is composed of A (Mr = 400,000), B1 (M, = 210,000), and