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The cytoplasmic domain of the H-2Ld class I major histocompatibility complex molecule is differentially accessible to immunological and biochemical probes during transport to the cell surface.
- Source :
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The Journal of biological chemistry [J Biol Chem] 1993 Oct 05; Vol. 268 (28), pp. 21263-70. - Publication Year :
- 1993
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Abstract
- An antiserum was generated against a synthetic peptide corresponding to a portion of the cytoplasmic domains of the H-2Ld and H-2Db class I major histocompatibility complex molecules of the mouse. This antibody preparation, R4, binds exclusively to endoglycosidase H-resistant H-2Ld/Db molecules which are not associated with beta 2-microglobulin. Interestingly, acquisition of resistance to endoglycosidase H precedes acquisition of R4 reactivity by 30 min. R4-reactive H-2Ld and H-2Db molecules occur on the cell surface and are phosphorylated in vivo. Other studies show that the tyrosine in the cytoplasmic domain is accessible to radioiodination on only a subset of H-2Ld molecules, and that the two-dimensional electrophoretic profiles of phosphorylated H-2L/Db molecules, of R4-reactive molecules, and of H-2Ld molecules radiolabeled on this cytoplasmic domain tyrosine are virtually identical. R4-reactive H-2Ld molecules do not undergo the peptide- and beta 2-microglobulin-induced conformational changes characteristic of free class I major histocompatibility complex heavy chains. The accessibility of the H-2Ld cytoplasmic domain to R4 and to radioiodination late in biosynthesis and its biological significance are discussed.
Details
- Language :
- English
- ISSN :
- 0021-9258
- Volume :
- 268
- Issue :
- 28
- Database :
- MEDLINE
- Journal :
- The Journal of biological chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 8407964