Abstract
Laminins are heterotrimeric proteins of basement membranes. More than 50 different trimers may exist. Laminin-10 (α5β1γ1) rather than laminin-1 (α1β1γ1) could be the most abundant isoform in the adult stage, and laminin-10 is made by several developing epithelial sheets. We show here that a much used commercial human preparation contains laminin-10 (α5β1γ1), some laminin-11 (α5β2γ1), but no laminin-1. Moreover, the laminin-10/11 mixture was found to be a strong adhesive for two human cell lines derived from epithelia. Antibodies against integrin β1, α6 or α3 (at 50 µg/ml) or dystroglycan did not inhibit cell attachment to laminin-10/11, although lower concentrations of anti-dystroglycan and integrin α6 antibodies inhibited cell binding to laminin-1.

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