This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Wewer, U. M. Articles by Liotta, L. A. Search for Related Content PubMed PubMed Citation Articles by Wewer, U. M. Articles by Liotta, L. A.

Role of Laminin Receptor in Tumor Cell Migration¹

Laboratory of Pathology, National Cancer Institute, NIH, Bethesda, Maryland 20892 [U. M. W., G. T., M. S., L. A. L.]; and University Institute of Pathological Anatomy, Copenhagen, Denmark [R. A.]

Polyclonal antisera were made against biochemically purified laminin receptor protein as well as against synthetic peptides deduced from a complementary DNA clone corresponding to the COOH-terminal end of the laminin receptor (U. M. Wewer et al., Proc. Natl. Acad. Sci. USA, 83: 7137–7141, 1986). These antisera were used to study the potential role of laminin receptor in laminin-mediated attachment and haptotactic migration of human A2058 melanoma cells. The anti-laminin receptor antisera reacted with the surface of suspended, nonpermeabilized melanoma and carcinoma cells. The anti-laminin receptor antisera blocked the surface interaction of A2058 cells with endogenous laminin, resulting in the inhibition of laminin-mediated cell attachment. The A2058 melanoma cells migrated toward a gradient of solid phase laminin or fibronectin (haptotaxis). Anti-laminin antiserum abolished haptotaxis on laminin but not on fibronectin. Synthetic peptide GRGDS corresponding to the fibronectin cell-binding domain inhibited haptotaxis on fibronectin but not on laminin. Both types of anti-laminin receptor antisera inhibited haptotaxis on laminin but not on fibronectin. Using immunohistochemistry, invading human carcinoma cells in vivo exhibited a marked cytoplasmic immunoreactivity for the receptor antigen. Together these findings indicate a specific role for the laminin receptor in laminin-mediated migration and that the ligand binding of the laminin receptor is encompassed in the COOH-terminal end of the protein.

¹ This study was supported in part by the Danish Cancer Society.

² To whom requests for reprints should be addressed, at University Institute of Pathological Anatomy, Frederik V's Vej 11, 2100 Copenhagen, Denmark.

Received 4/22/87. Revised 7/29/87. Accepted 8/ 5/87.

This article has been cited by other articles:

				C. Selleri, P. Ragno, P. Ricci, V. Visconte, N. Scarpato, M. V. Carriero, B. Rotoli, G. Rossi, and N. Montuori The metastasis-associated 67-kDa laminin receptor is involved in G-CSF-induced hematopoietic stem cell mobilization Blood, October 1, 2006; 108(7): 2476 - 2484. [Abstract] [Full Text] [PDF]

				A N SHMAKOV and S GHOSH Prion proteins and the gut: une liaison dangereuse? Gut, April 1, 2001; 48(4): 443 - 447. [Full Text] [PDF]

				A. Magnifico, E. Tagliabue, S. Buto, E. Ardini, V. Castronovo, M. I. Colnaghi, and S. Menard Peptide G, Containing the Binding Site of the 67-kDa Laminin Receptor, Increases and Stabilizes Laminin Binding to Cancer Cells J. Biol. Chem., December 6, 1996; 271(49): 31179 - 31184. [Abstract] [Full Text] [PDF]

				J. Nelson, W. N. Scott, W. E. Allen, D. J. Wilson, P. Harriott, N. V. McFerran, and B. Walker Murine Epidermal Growth Factor Peptide (33-42) Binds to a YIGSR-specific Laminin Receptor on both Tumor and Endothelial Cells J. Biol. Chem., October 18, 1996; 271(42): 26179 - 26186. [Abstract] [Full Text] [PDF]