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Molecular profiles of the cell membrane bound and cytoplasmic forms of the human MHC Class‐II associated invariant polypeptides
Author(s) -
Fernandez Nelson,
Klidis Aristea
Publication year - 1991
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150120711
Subject(s) - cd74 , cytoplasm , major histocompatibility complex , mhc class ii , biology , protein subunit , flow cytometry , mhc class i , invariant (physics) , microbiology and biotechnology , antigen , biochemistry , genetics , physics , gene , mathematical physics
Several sub‐types of histocompatibility class‐II molecules are known to exist, including DR, DQ and DP, each subset organized in alpha and beta heterodimers. These molecules play a central role in immunorecognition via direct noncovalent binding of degraded nonself immunogenic peptides followed by ligand‐interaction with T cells. In the cytoplasm the class‐II alpha and beta chains associate, in addition with a third backbone molecule known as the invariant chain. In this study we show that all class‐II subsets associate with the invariant chain probably from the same pool and that a subset of invariant chain is expressed as a cell surface subunit. This sub‐unit, whose function is still unknown, was detected by flowcytometry and by two‐dimensional gel analysis followed by antibody‐mediated immunoprecipitations.