Lymphocyte surface antigen L25 is a member of the integrin receptor superfamily.

Monoclonal antibody (mAb) anti-L25 identifies an antigen on the surface of human lymphocytes. This mAb immunoprecipitated three distinct polypeptides of Mr 150,000, 85,000, and 75,000 from Nonidet P-40 lysates of surface radioiodinated lymphocytes. The three polypeptides were found under both nonreducing and reducing conditions. An additional polypeptide of Mr 130,000 was detected in mAb anti-L25 immuno-precipitates when cells were lysed with CHAPS (3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate). Epitope localization experiments indicated that both the Mr 150,000 and 85,000 polypeptides contained antibody reactive sites. Peptide mapping studies demonstrated structural similarities in the Mr 150,000 and 85,000 components. The analysis of L25 subunits from lysates of antigen-stimulated T lymphocytes revealed a loss of the Mr 150,000 polypeptides in mAb anti-L25 immunoprecipitates. Solid phase double determinant binding assays demonstrated that L25 is similar and probably identical to lymphocyte surface antigen very late activation-4. This relationship placed L25 as a member of the integrin receptor superfamily.