ALLELE AND LOCUS-SPECIFIC DIFFERENCES IN CELL-SURFACE EXPRESSION AND THE ASSOCIATION OF HLA CLASS-I HEAVY-CHAIN WITH BETA-2-MICROGLOBULIN - DIFFERENTIAL-EFFECTS OF INHIBITION OF GLYCOSYLATION ON CLASS-I SUBUNIT ASSOCIATION
ALLELE AND LOCUS-SPECIFIC DIFFERENCES IN CELL-SURFACE EXPRESSION AND THE ASSOCIATION OF HLA CLASS-I HEAVY-CHAIN WITH BETA-2-MICROGLOBULIN - DIFFERENTIAL-EFFECTS OF INHIBITION OF GLYCOSYLATION ON CLASS-I SUBUNIT ASSOCIATION
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DOI:
10.1002/eji.1830180522
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发表时间:
1988-05-01
影响因子:
5.4
通讯作者:
PLOEGH, HL
中科院分区:
文献类型:
--
作者:
NEEFJES, JJ;PLOEGH, HL
The assembly of HLA class I antigens, and the contribution of the single N-linked glycan to this process were examined. We observed a requirement for N-linked glycosylation in the proper assembly and surface expression of HLA-b locus products in particular, although considerable variation was seen within the allelic series of the HLA-A and B loci. We conclude that the single N-linked glycan can contribute in a major way to that conformation of the heavy (H) chain which is competent to associated with the light chain .beta.2-microglobulin, and that the presence, rather than the type, of carbohydrate chain is important in this respect. The association of human class I H chains with .beta.2-microglobulin shows biphasic kinetics, where an initially rapid phase is followed by a prolonged period during which no further association can be measured. It appears that HLA-C H chains are initially synthesized in amounts similar to HLA-A and B H chains, but associate inefficiently with .beta.2-microglobulin, resulting in low expression of HLA-C at the cell surface. The individual stages of assembly and maturation of class I antigens including the transfer from Golgi to cell surface were found to display characteristic allelic variation.