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Journal of Experimental Medicine, Vol 171, 1431-1442, Copyright © 1990 by Rockefeller University Press
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E Schnabl, H Stockinger, O Majdic, H Gaugitsch, IJ Lindley, D Maurer, A Hajek- Rosenmayr and W Knapp
Institute of Immunology, Vienna, Austria.
We present here the molecular characterization of a new activation- induced surface structure on human T lymphocytes, termed LA45, with high homology (93% at protein level) to MHC class I molecules. Antigen modulation and sequential immunoprecipitation experiments revealed that LA45 and HLA class I proteins do not crossreact with the corresponding antibodies. Furthermore, LA45 is not associated with beta 2-m. On the other hand, we could show that the separation of HLA-A,B,C and beta 2m molecules, induced by SDS-denaturation, leads to a conformational change in the heavy chain in such a way that it becomes reactive with LA45. The 90/45 kD LA45 proteins thus appear to be non-beta 2m- associated MHC class I alpha chains that are selectively expressed by activated but not by resting human T lymphocytes.
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