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Activated human T lymphocytes express MHC class I heavy chains not associated with beta 2-microglobulin.


ABSTRACT: 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.

SUBMITTER: Schnabl E 

PROVIDER: S-EPMC2187879 | biostudies-other | 1990 May

REPOSITORIES: biostudies-other

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Activated human T lymphocytes express MHC class I heavy chains not associated with beta 2-microglobulin.

Schnabl E E   Stockinger H H   Majdic O O   Gaugitsch H H   Lindley I J IJ   Maurer D D   Hajek-Rosenmayr A A   Knapp W W  

The Journal of experimental medicine 19900501 5


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,  ...[more]

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