Complexing of the CD-3 subunit by a monoclonal antibody activates a microtubule-associated protein 2 (MAP-2) serine kinase in Jurkat cells
dc.contributor.author | Hanekom C. | |
dc.contributor.author | Nel A. | |
dc.contributor.author | Gittinger C. | |
dc.contributor.author | Rheeder A. | |
dc.contributor.author | Landreth G. | |
dc.date.accessioned | 2011-05-15T16:03:24Z | |
dc.date.available | 2011-05-15T16:03:24Z | |
dc.date.issued | 1989 | |
dc.description.abstract | Treatment of Jurkat T-cells with anti-CD-3 monoclonal antibodies resulted in the rapid and transient activation of a serine kinase with utilized the microtubule-associated protein, MAP-2, as a substrate in vitro. The kinase was also activated on treatment of Jurkat cells with phytohaemagglutinin, but with a different time course. The activation of the MAP-2 kinase by anti-CD-3 antibodies was dose-dependent, with maximal activity observed at concentrations of > 500 ng/ml. Normal human E-rosette-positive T-cells also exhibited induction of MAP-2 kinase activity during anti-CD-3 treatment. The enzyme was optimally active in the presence of 2 mM-Mn2+; lower levels of activity were observed with Mg2+, even at concentrations up to 20 mM. The kinase was partially purified by passage over DE-52 Sephacel with the activity eluting as a single peak of 0.25 M-NaCl. The molecular mass was estimated to be 45 kDa by gel filtration. The activation of the MAP-2 kinase was probably due to phosphorylation of this enzyme as treatment with alkaline phosphatase diminished its activity. These data demonstrate that the stimulation of T-cells through the CD-3 complex results in the activation of a novel serine kinase which may be critically involved in signal transduction in these cells. | |
dc.description.version | Article | |
dc.identifier.citation | Biochemical Journal | |
dc.identifier.citation | 262 | |
dc.identifier.citation | 2 | |
dc.identifier.issn | 2646021 | |
dc.identifier.uri | http://hdl.handle.net/10019.1/12606 | |
dc.subject | cd3 antigen | |
dc.subject | microtubule associated protein 2 | |
dc.subject | monoclonal antibody | |
dc.subject | protein serine kinase | |
dc.subject | t lymphocyte receptor | |
dc.subject | cell culture | |
dc.subject | enzyme activation | |
dc.subject | leukemia cell line | |
dc.subject | priority journal | |
dc.subject | signal transduction | |
dc.subject | t lymphocyte | |
dc.subject | Antibodies, Monoclonal | |
dc.subject | Antigens, CD3 | |
dc.subject | Antigens, Differentiation, T-Lymphocyte | |
dc.subject | Ca(2+)-Calmodulin Dependent Protein Kinase | |
dc.subject | Cell Line | |
dc.subject | Dose-Response Relationship, Immunologic | |
dc.subject | Enzyme Activation | |
dc.subject | Enzyme Induction | |
dc.subject | Human | |
dc.subject | Membrane Glycoproteins | |
dc.subject | Protein Kinases | |
dc.subject | Receptors, Antigen, T-Cell | |
dc.subject | Support, Non-U.S. Gov't | |
dc.subject | Support, U.S. Gov't, Non-P.H.S. | |
dc.subject | Support, U.S. Gov't, P.H.S. | |
dc.subject | T-Lymphocytes | |
dc.title | Complexing of the CD-3 subunit by a monoclonal antibody activates a microtubule-associated protein 2 (MAP-2) serine kinase in Jurkat cells | |
dc.type | Article |