Molecular profiles of the cell membrane bound and cytoplasmic forms of the human MHC class-II associated invariant polypeptides.

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 flow-cytometry and by two-dimensional gel analysis followed by antibody-mediated immunoprecipitations.