Abstract
Human leukocyte function-associated antigens (LFA) have been defined by their association with human T lymphocyte-mediated cytolysis (1). One of these, LFA-1, is present on lymphocyte, thymocytes, monocytes, and granulocytes. Antibodies to LFA-1 have been shown to interfere with T lymphocyte-mediated cytotoxicity, NK cell-mediated cytolysis, and T cell proliferation to soluble antigens, alloantigens, and mitogens as well as various myeloid cell functions (1–4). OKM1 is a biomolecular structure and it has been identified to be the C3bi receptor of human monocytes and macrophages (5). Recently, LFA-1 and OKM1 were found to have a common ß subunit and they belong to a human leukocyte differentiation antigen family (6).
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Hara, T., Fu, S.M. (1986). Phosphorylation of α,ß Subunits of 180/100-Kd Polypeptides (LFA-1) and Related Antigens. In: Reinherz, E.L., Nadler, L.M., Haynes, B.F., Bernstein, I.D. (eds) Leukocyte Typing II. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-4850-7_6
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DOI: https://doi.org/10.1007/978-1-4612-4850-7_6
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