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Immunological Mapping of the Human Leucocyte Adhesion Glycoprotein gp90 (CD 18) by Monoclonal Antibodies
Author(s) -
NORTAMO P.,
PATARROYO M.,
KANTOR C.,
SUOPANKI J.,
GAHMBERG C. G.
Publication year - 1988
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1988.tb01485.x
Subject(s) - monoclonal antibody , antigen , epitope , glycoprotein , cd11a , cd18 , antibody , biology , microbiology and biotechnology , adhesion , macrophage 1 antigen , immunology , chemistry , organic chemistry
The leucocyte surface glycoproteins CD11a (gp160, LFA‐1 antigen, TA‐1 antigen), CD11b (gp155, Mac‐1 antigen, Mo‐1 antigen), CD11c (gp 130, Leu‐M5 antigen), and CD18 (gp90) constitute three heterodimers with different α chain and a common β chain Monoclonal antibodies to CD11a, b, or c block adhesion of certain types of leucocytes only, while several antibodies to CD 18 inhibit adhesion in all of them. The functionally important site or sites on CD 18 are not known. We have now isolated the CD11a,b,c‐CD18 leucocyte antigen complex in large amounts from human leucocytes, and produced several new monoclonal antibodies reacting with CD18. One of these antibodies, like those described earlier, inhibits leucocyte adhesion, whereas the others do not. By means of competition experiments, at least four epitope regions were found. These antibodies should be valuable in elucidating the regions essential in CD18‐mediated leucocyte functions.