Identification of a Sulfate-Bearing Molecule Associated with HLA Class II Antigens

The human Ia antigens (DR, DS, and SB), determined by genes contained within the HLA complex on chromosome 6, are glycoprotein heterodimers consisting of a Mr≈ 34,000 α chain and a Mr≈ 28,000 β chain. As a result of studies exploring the possibility that α or β (or both) might be sulfated, a unique...

Full description

Saved in:
Bibliographic Details
Published inProceedings of the National Academy of Sciences - PNAS Vol. 81; no. 5; pp. 1534 - 1538
Main Authors Sant, Andrea J., Cullen, Susan E., Schwartz, Benjamin D.
Format Journal Article
LanguageEnglish
Published United States National Academy of Sciences of the United States of America 01.03.1984
National Acad Sciences
Subjects
Online AccessGet full text

Cover

Loading…
More Information
Summary:The human Ia antigens (DR, DS, and SB), determined by genes contained within the HLA complex on chromosome 6, are glycoprotein heterodimers consisting of a Mr≈ 34,000 α chain and a Mr≈ 28,000 β chain. As a result of studies exploring the possibility that α or β (or both) might be sulfated, a unique component of the oligomeric Ia antigen complex was discovered. When anti-Ia immunoprecipitates from Nonidet P-40 lysates of [35S]sulfate-labeled lymphoid cells were analyzed by NaDodSO4/PAGE, a molecule of considerable size heterogeneity (Mr40,000-70,000) was observed. This component was present in both anti-DR and anti-DS immunoprecipitates prepared from both human tonsil cells and lymphoblastoid B-cell lines but was not observed in control precipitates or in association with immunoglobulin or class I HLA molecules. Preliminary biochemical studies indicate that this Mr40,000-70,000 molecule is polyanionic, disperse in molecular weight, and sensitive to protease digestion. The sulfate-bearing moiety of this component was resistant to Pronase but sensitive to chondroitinase ABC, indicating that this molecule belongs to the chondroitin sulfate class of proteoglycans.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
content type line 23
ObjectType-Article-1
ObjectType-Feature-2
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.81.5.1534