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We have generated a series of proteolytic fragments of the human basement membrane protein laminin-5 (LN5) in order to identify the region(s) responsible for binding to epithelial cells and for other possible biological activities. We show that the putative cell-binding domain, the EGF-like domain, and the calcium-binding domain of LN5 are each capable of promoting cell adhesion in vitro and in vivo. A minor cell-binding peptide is also generated by proteolysis at the link region between the two EGF-like domains. In contrast, the disintegrin-like sequence and the cysteine-rich domain are inactive in these assays. The results indicate that LN5 undergoes a proteolytic processing at the cell-binding domain to yield a major cell-binding peptide and a minor cell-binding peptide. The major cell-binding peptide is capable of promoting cell adhesion and spreading, whereas the minor peptide has no effect.
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