title: CD99 monoclonal antibody induce homotypic adhesion of Jurkat cells through protein tyrosine kinase and protein kinase C-dependent pathway.
abstract: CD99 is a 32 kDa cell surface glycoprotein which is involved in cell adhesion. Engagement of the CD99 molecule by CD99 monoclonal antibodies has been shown to induce homotypic aggregation of various cell types. By using a newly established CD99 monoclonal antibody, MT99/3, we show here that LFA-1/ICAM-1 independent cell adhesion pathways are activated via CD99. Engagement of the CD99 molecule by MT99/3 induced homotypic cell aggregation of Jurkat T-cells within 30 min reaching its maximal level within 4 h. The Jurkat cell aggregation was not blocked by addition of CD11a (LFA-1) and CD54 (ICAM-1) mAbs. Furthermore, MT99/3 treatment did not alter the expression of LFA-1 and ICAM-1 molecules. Induction of Jurkat homotypic aggregation by MT99/3 was, however blocked by the protein kinase C inhibitor, sphingosine, the protein tyrosine kinase inhibitor, genistein, and by actin filament polymerization blocking agent, cytochalasin B. Thus, these observations suggest that CD99 can mediate beta2-integrin independent cell adhesion that depends on activation of protein kinases and reorganization of the cytoskeleton.
authors.affiliation: Department of Clinical Immunology, Faculty of Associated Medical Sciences, Chiang Mai University, Thailand. watchar@chiangmai.ac.th
authors.forename: W
authors.initials: W
authors.lastname: Kasinrerk
authors.forename: N
authors.initials: N
authors.lastname: Tokrasinwit
authors.forename: S
authors.initials: S
authors.lastname: Moonsom
authors.forename: H
authors.initials: H
authors.lastname: Stockinger
mesh_terms: D000071443:12E7 Antigen; D000818:Animals; D000911:Antibodies, Monoclonal / Q000096:biosynthesis / Q000378:metabolism; D015703:Antigens, CD / Q000235:genetics / Q000276:immunology / Q000378:metabolism*; D019556:COS Cells; D002448:Cell Adhesion / Q000502:physiology*; D015815:Cell Adhesion Molecules / Q000235:genetics / Q000276:immunology / Q000378:metabolism*; D002449:Cell Aggregation / Q000187:drug effects; D002478:Cells, Cultured; D003001:Cloning, Molecular; D003571:Cytochalasin B / Q000494:pharmacology; D004791:Enzyme Inhibitors / Q000494:pharmacology; D005260:Female; D019833:Genistein / Q000494:pharmacology; D006801:Humans; D018799:Intercellular Adhesion Molecule-1 / Q000378:metabolism; D019169:Jurkat Cells; D020014:K562 Cells; D016169:Lymphocyte Function-Associated Antigen-1 / Q000378:metabolism; D008562:Membrane Glycoproteins / Q000235:genetics / Q000276:immunology / Q000378:metabolism*; D051379:Mice; D008807:Mice, Inbred BALB C; D011493:Protein Kinase C / Q000037:antagonists & inhibitors*; D011505:Protein-Tyrosine Kinases / Q000037:antagonists & inhibitors*; D013110:Sphingosine / Q000494:pharmacology
chemical_list: D000071443:12E7 Antigen; D000911:Antibodies, Monoclonal; D015703:Antigens, CD; C061828:CD99 protein, human; D015815:Cell Adhesion Molecules; D004791:Enzyme Inhibitors; D016169:Lymphocyte Function-Associated Antigen-1; D008562:Membrane Glycoproteins; D018799:Intercellular Adhesion Molecule-1; D003571:Cytochalasin B; D019833:Genistein; D011505:Protein-Tyrosine Kinases; D011493:Protein Kinase C; D013110:Sphingosine