A novel recognition site on laminin for the alpha 3 beta 1 integrin

Experimental Cell Research
S PattaramalaiA P Skubitz

Abstract

Synthetic peptide GD-2 is a sequence of amino acids derived from the carboxy-terminal long arm of the A chain of laminin. Previous studies have shown that peptide GD-2 promotes the adhesion of human squamous cell carcinoma (SCC) cells as well as a variety of other cell lines. In this study, we attempted to identify the receptor that SCC cells use to adhere to peptide GD-2. Monoclonal antibodies (mAbs) against a human SCC cell line were generated. One of these mAbs, ASC-1, bound to the surface of SCC cells as determined by flow cytometry. This mAb inhibited SCC cell adhesion to peptide GD-2 and laminin, but not fibronectin or type IV collagen, suggesting that mAb ASC-1 binds to the SCC receptor for the peptide GD-2 sequence of laminin. MAb ASC-1 immunoprecipitated a complex composed of two components of 135 and 116 kDa. Immunoadsorption of ASC-1-binding material from the SCC cell extract by incubation with mAb ASC-1 resulted in the removal of the alpha 3 beta 1 integrin from the extract. Immunohistochemical staining of tissue from a normal human tongue and from a patient with SCC of the tongue revealed that mAb ASC-1 stained the surface of epithelial cells that were in contact with the basement membrane, as well as those cells l...Continue Reading

Citations

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