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Regulation of T cell proliferation by anti‐CD49d and anti‐CD29 monoclonal antibodies
Author(s) -
Bednarczyk John L.,
Teague T. Kent,
Wygant James N.,
Davis Laurie S.,
Lipsky Peter E.,
McLntyre Bradley W.
Publication year - 1992
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.52.4.456
Subject(s) - monoclonal antibody , fibronectin , biology , microbiology and biotechnology , integrin , cell adhesion , cell growth , extracellular matrix , antibody , cell , biochemistry , immunology
The ß 1 integrin VLA‐4 (α 4 ß 1 CD49d/CD29), which is expressed on a large subpopulation of peripheral blood T lymphocytes, functions as a receptor for the endothelial adhesion protein VCAM‐1 and the extracellular matrix protein fibronectin. Previous studies showed that immobilized fibronectin enhanced anti‐CD3 monoclonal antibody (mAb)‐induced T cell proliferation through binding to the integrins VLA‐4 and VLA‐5 (α 5 β 1 , CD49e/CD29). We studied the ability of the anti‐CD49d mAb L25 to potentiate proliferation. T cell proliferation was induced by subthreshold concentrations of anti‐CD3 mAb (mAb OKT3) coimmobilized with mAb L25 but not with coimmobilized anti‐CD29 (ß 1 ) mAb. Soluble anti‐ CD29 mAb inhibited the proliferation induced by coimmobilized mAb OKT3 and L25 but not proliferation induced by mAb OKT3 with PMA or coimmobilized anti‐ GD26 mAb.