Serologically detectable polymorphism of the HLA-DC alpha-subunit.
Open Access
- 1 January 1984
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Immunology
- Vol. 132 (1) , 277-282
- https://doi.org/10.4049/jimmunol.132.1.277
Abstract
Two 8th Workshop alloantisera, 8W1062 and 8W614, which were classified respectively as anti-DR5 and anti-DR3, were found to react with an Ia preparation from LG38 cells (DR5,5) that was depleted of DR and BR molecules and enriched in DC molecules by pretreatment with a monoclonal antibody and an antiserum against alpha-subunits of DR and BR molecules. The reaction of both alloantisera was inhibited by DR3-positive, DR5-positive, and DRW13-positive individuals. This pattern does not correspond to any of the hitherto reported supertypic specificities. Both antisera were shown to bind to the alpha-subunit isolated from the DC-enriched preparation but not to the beta-subunit. The specificity has been named DC alpha 3. Family studies show the segregation according to the HLA haplotype patterns. This demonstrates by formal genetics criteria the HLA linkage of the locus controlling the DC alpha-subunit.This publication has 3 references indexed in Scilit:
- Sequences related to HLA-DR alpha chain on human chromosome 6: restriction enzyme polymorphism detected with DC alpha chain probes.Proceedings of the National Academy of Sciences, 1983
- Microfingerprinting analysis of human Ia molecules favours a three loci modelMolecular Immunology, 1983
- Immunological dissection of human Ia molecules.The Journal of Experimental Medicine, 1978