Abstract
Mol is a heterodimeric glycoprotein (gp 155,95) expressed on the plasma membrane of neutrophils (PMN), monocytes and certain macrophages, and a subset of large granular lymphoid cells (reviewed in 1). The identification and characterization of Mol was made possible by the generation of monoclonal antibodies specific for epitopes expressed on the higher molecular weight α-subunit or the lower molecular weight β-subunit. According to World Health Organization (WHO) nomenclature, antibodies recognizing the α-subunit of Mol are designated anti-CD11b while antibodies specific for the β-subunit are termed anti-CD 18 (2). Mol (CD11b/CD18) is a member of a family of three structurally related glycoproteins that include LFA-1 (CD11a/CD18) and p150,95 (CD11c/CD18) (3). Each member of this family has a unique higher molecular weight α-subunit that is noncovalently linked with a structurally identical β-subunit (CD18) (Fig. 9.1). Considerable progress has been made in the biochemical characterization of Mol, LFA-1, and p150,95 (3), and the genes encoding the CD11b and CD18 subunits of Mol have been cloned (4,5). Similarly, the functional significance of the CD11/CD18 glycoproteins has been deduced from the results of antibody blocking experiments in which selective functional defects are exhibited by normal cells pre-treated with monoclonal antibodies specific for CD11 or CD18 epitopes.
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References
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Todd, R.F., Simpson, P.J., Lucchesi, B.R. (1990). Anti-Inflammatory Properties of Monoclonal Anti-Mo1 (CD11b/CD18) Antibodies In Vitro and In Vivo. In: Springer, T.A., Anderson, D.C., Rothlein, R., Rosenthal, A.S. (eds) Leukocyte Adhesion Molecules. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-3234-6_10
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DOI: https://doi.org/10.1007/978-1-4612-3234-6_10
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