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. 1992 Aug 14;186(3):1674-80.
doi: 10.1016/s0006-291x(05)81601-8.

Dichotomy in the laminin-binding properties of soluble and membrane-bound human galactoside-binding protein

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Dichotomy in the laminin-binding properties of soluble and membrane-bound human galactoside-binding protein

J Ochieng et al. Biochem Biophys Res Commun. .

Abstract

Recent studies indicate that galactoside-binding proteins may bind the poly-N-acetyllactosamine sequences of laminin. We questioned whether human galactoside-binding protein (hL-31) binds to laminin and whether cells that express hL-31 on their surface use it as a laminin receptor to promote cellular attachment. The data show that both lectin and cells bind to immobilized laminin. The binding of soluble lectin to laminin is inhibited by lactose, while cell adhesion to it is not. The results indicate that laminin may be a ligand for soluble galactoside-binding proteins.

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