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Volume 271, Number 49, Issue of December 6, 1996 pp. 31179-31184
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Peptide G, Containing the Binding Site of the 67-kDa Laminin Receptor, Increases and Stabilizes Laminin Binding to Cancer Cells

(Received for publication, February 15, 1996, and in revised form, July 31, 1996)

Alessandra Magnifico , Elda Tagliabue , Simona Butó , Elena Ardini , Vincent Castronovo ^§ , Maria I. Colnaghi and Sylvie Ménard

From the  Division of Experimental Oncology E, Istituto Nazionale Tumori, Via Venezian 1, 20133 Milan, Italy and the ^§ Metastasis Research Laboratory, University of Liege, B-4000 Liege 1, Belgium

We investigated the effect of peptide G, a synthetic peptide derived from the sequence of the 37-kDa laminin receptor precursor, on the interaction of laminin in two tumor cell lines one of which produces laminin and one of which does not. Addition of peptide G to the culture medium induced a significant increase in the amount of endogenous laminin detectable on the cell membrane of both cell lines. Moreover, pretreatment of exogenous laminin with peptide G dramatically increased laminin binding on both cell lines. Kinetics analysis of membrane-bound labeled laminin revealed a 3-fold decrease in the k_d of peptide G-treated laminin compared with untreated or unrelated or scrambled peptide-treated laminin. Moreover, the affinity constant of peptide G-treated laminin increased 2-fold, with a doubling of the number of laminin binding sites, as determined by Scatchard analysis. Expression of the VLA6 integrin receptor on the cell membrane increased after incubation with peptide G-treated laminin. However, the lower binding inhibition of peptide G-treated laminin after anti-VLA6 antibody or cation chelation treatment indicates that membrane molecules in addition to integrin receptors are involved in the recognition of peptide G-modified laminin. These "new" laminin-binding proteins also mediated cell adhesion to laminin, the first step in tumor invasion. Together, the data suggest that peptide G increases and stabilizes laminin binding on tumor cells, involving surface receptors that normally do not take part in this interaction. This might explain the abundant clinical and experimental data suggesting a key role for the 67-kDa laminin receptor in the interaction between cancer cells and the basement membrane glycoprotein laminin during tumor invasion and metastasis.

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