Assembly and intracellular transport of HLA-DM and correction of the class II antigen-processing defect in T2 cells.

Autor: Denzin LK; Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, Connecticut 06520-8011, USA., Robbins NF, Carboy-Newcomb C, Cresswell P
Jazyk: angličtina
Zdroj: Immunity [Immunity] 1994 Oct; Vol. 1 (7), pp. 595-606.
DOI: 10.1016/1074-7613(94)90049-3
Abstrakt: MHC class II molecules expressed in T2 cells fail to acquire a normal complement of endocytically generated peptides. The defect is repaired by introducing HLA-DMA and HLA-DMB cDNA expression vectors, determined by the restoration of SDS stability of class II alpha beta dimers, restoration of a normal conformation for HLA-DR3 as detected by a monoclonal antibody, and by a reduction in class II-associated invariant chain peptides. The intracellular distribution of class II and invariant chain molecules is also restored to that of wild-type cells. The HLA-DMA and HLA-DMB products appear to form a heterodimer that, although transported at least to the medial Golgi, is not expressed at the cell surface. These findings are consistent with HLA-DM functioning intracellularly to facilitate class II-restricted antigen processing.
Databáze: MEDLINE