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CD1 1b/CD18‐Dependent Polymorphonuclear Leucocyte Interaction with Matrix Proteins in Adhesion and Migration
Author(s) -
LUNDGRENÅKERLUND E.,
OLOFSSON A. M.,
BERGER E.,
ARFORS K.E.
Publication year - 1993
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.1365-3083.1993.tb02573.x
Subject(s) - cd18 , adhesion , integrin alpha m , laminin , monoclonal antibody , chemistry , cell adhesion , microbiology and biotechnology , granulocyte , matrix (chemical analysis) , antibody , receptor , immunology , biochemistry , biology , extracellular matrix , organic chemistry , chromatography
Adhesion of human polymorphonuclear leucocytes (PMN) stimulated with phorbol myristate acetate (PMA) to plastic dishes coated with the matrix proteins laminin (LM), libronectin (FN), collagen type I (CI) or collagen type IV (CIV) was inhibited by the monoclonal antibody 60.3 (MoAb 60.3; anti‐CD18). The highest inhibitory effect was seen on adhesion to CI. PMN adhesion to CI was also effectively inhibited by Mol (anti‐CD11b) but this antibody had only a minor effect on attachment of PMN to the other matrix proteins. In other experiments MoAb 60.3 inhibited LTB 4 ‐induccd migration of PMN through polycarbonate filters (3 μm pores) coated with LM, FN, CI or CIV, with the most pronounced effect on migration through those filters coated with CI. By contrast, the antibody Mol had no effect on migration through any of the protein‐coated filters tested. The results in this study suggest that the CD18 epitope, recognized by 60.3, mediates both adhesion and migration of PMN while theepitopeonCDl 1b recognized by the antibody Mol is restricted to adhesion. The results also indicate that CD11b/CD18 is the major receptor on human PMN for CI while interaction with LM, FN and CIV may in addition involve other mechanisms.