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Journal of Cell Science, Vol 112, Issue 1 1-10, Copyright © 1999 by Company of Biologists

JOURNAL ARTICLES

Identification of laminin-10/11 as a strong cell adhesive complex for a normal and a malignant human epithelial cell line

M Ferletta and P Ekblom
Department of Animal Physiology, Uppsala University Biomedical Center, BOX 596, SE-75124 Uppsala, Sweden.

Laminins are heterotrimeric proteins of basement membranes. More than 50 different trimers may exist. Laminin-10 (alpha5beta1gamma1 rather than laminin-1 (alpha1beta1gamma1) 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 (alpha5beta1gamma1), some laminin-11 (alpha5beta2gamma1), 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 beta1, alpha6 or alpha3 (at 50 microgram/ml) or dystroglycan did not inhibit cell attachment to laminin-10/11, although lower concentrations of anti-dystroglycan and integrin alpha6 antibodies inhibited cell binding to laminin-1.


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