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The Nonintegrin Laminin Binding Protein (p67 LBP) Is Expressed on a Subset of Activated Human T Lymphocytes and, Together with the Integrin Very Late Activation Antigen-6, Mediates Avid Cellular Adherence to Laminin¹

Laboratory of Molecular Immunology, Department of Medicine, Columbia University, New York, NY 10032

A search for genes expressed in activated T cells revealed that the nonintegrin, 67-kDa laminin binding protein (p67 LBP) is expressed on the surface of a subset (10–15%) of activated peripheral blood T cells. Surface p67 LBP expression is detectable by FACS using the anti-p67 LBP mAb, MLuC5, within 6 h of T cell activation with phorbol dibutyrate and ionomycin, peaks 18–36 h postactivation, and persists for 7–10 days. The subset of T cells expressing p67 LBP is composed of mature, single-positive cells (85% CD4⁺8^-, 15% CD4^-8⁺) of memory cell phenotype (100% CD45 RO⁺/CD45 RA^-). The p67 LBP⁺ T cells also express the integrin ₆ chain (CD49f), which is known to associate with p67 LBP on tumor cells. In addition, the p67 LBP⁺ T cells express the integrin ß₁, which associates with ₆ in the laminin-specific integrin receptor very late activation Ag (VLA)-6 (₆ß₁). Expression of an exogenous cDNA encoding the 37-kDa LBP precursor (p37 LBPP) confers p67 LBP surface expression on a p67 LBP-negative Jurkat T cell line (B2.7). Expression of p67 LBP induces B2.7 transfectants to adhere to laminin, but avid laminin binding depends on coexpression of VLA-6. Taken together, these data indicate that p67 LBP is an activation-induced surface structure on memory T cells that, together with VLA-6, mediates cellular adherence to laminin.

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