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Publication : Characterization of a cell surface-expressed disulfide-linked dimer involved in murine T cell activation.

First Author  Yokoyama WM Year  1988
Journal  J Immunol Volume  141
Issue  2 Pages  369-76
PubMed ID  2838547 Mgi Jnum  J:9232
Mgi Id  MGI:57695 Doi  10.4049/jimmunol.141.2.369
Citation  Yokoyama WM, et al. (1988) Characterization of a cell surface-expressed disulfide-linked dimer involved in murine T cell activation. J Immunol 141(2):369-76
abstractText  We have produced a hamster mAb, H1.2F3, which was derived by immunization with a murine TCR-gamma delta + epidermal T cell line. H1.2F3 immunoprecipitates a cell surface-expressed disulfide-linked dimer that has a m.w. of 85,000 under non-reducing conditions and consists of subunits of 35,000 to 39,000 m.w. This dimer is distinct from the CD3-associated TCR-gamma delta complex (CD3/TCR), inasmuch as H1.2F3 does not co-precipitate or co-modulate with the CD3/TCR complex and recognizes an Ag with a single-peptide backbone of 22,000 m.w. after N-Glycanase treatment. H1.2F3 is weakly reactive with a small percentage of cells from unfractionated thymus, spleen, or lymph node, but reactivity with both T and B lymphocytes is markedly enhanced by a brief period of stimulation with Con A or PMA in vitro. This enhancement requires de novo protein synthesis. Enhanced expression of the H1.2F3 Ag can also be induced in vivo by injection of Con A or anti-CD3. H1.2F3 is a potent stimulator of T, but not B, cell proliferation in the presence of PMA and FcR-bearing accessory cells. These functional and biochemical studies strongly suggest that the Ag recognized by H1.2F3 is the murine homologue of the human CD28 Ag recognized by mAb 9.3.
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