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Monoclonal antibodies to the carbohydrate structure Lewis x stimulate the adhesive activity of leukocyte integrin CD11b/CD18 (CR3, Mac‐1, α m β 2 ) on human granulocytes
Author(s) -
Stockl Johannes,
Magdic Otto,
Rosenkranz Alexander,
Fiebiger Edda,
Kniep J Bernhard,
Stockinged Hannes,
Knapp Walter
Publication year - 1993
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1002/jlb.53.5.541
Subject(s) - monoclonal antibody , integrin alpha m , biology , selectin , integrin , sialyl lewis x , cd18 , glycoprotein , divalent , microbiology and biotechnology , antibody , antigen , biochemistry , immunology , receptor , chemistry , flow cytometry , cell adhesion molecule , organic chemistry
Several carbohydrate structures on human granulocytes have been discussed as potential ligands for C‐ type lectins (selectins) on endothelial cells. Among them are the lacto‐series type II chain antigens sialyl‐Lewis x (SLe x ), Lewis x (Le x ), and VIM2. We demonstrated in this study that monoclonal antibodies (mAbs) to Le x and to SLe x , but not other anticarbohydrate mAbs (VIM2, CDwl7, CD24), can stimulate granulocytes to form homotypic aggregates. This effect was particularly noticeable with three distinct anti‐Le x mAbs (3C6, 4D1, 6C7). Much less impressive effects were also seen with nine other anti‐Le x mAbs and with the anti‐SLe x mAb CSLEX1. Aggregation was shown to be an active process. It is temperature and energy dependent, requires divalent cations, and is selective in terms of mAb specificity. Anti‐ Le x ‐induced homoaggregate formation could be inhibited with CDllb mAb JML‐H11 and CD54 (ICAM1) mAb LB‐2 and thus seems to be associated with activation of the β2‐integrin cytoadhesion pathway.