Subject(s)
Glycosaminoglycans/analysis , Membrane Proteins/analysis , Proteoglycans/analysis , Chondroitinases and Chondroitin Lyases , Cytological Techniques , Electrophoresis, Polyacrylamide Gel , Electrophysiology , Histocompatibility Antigens Class II/analysis , Humans , Immunologic Techniques , Isotope Labeling , Molecular Weight , Sulfates/analysisABSTRACT
The human Ia antigens (DR, DQ, and DP), determined by genes with the HLA complex, are heterodimers consisting of a 34,000-Da alpha-chain glycoprotein and a 29,000-Da beta-chain glycoprotein. During the course of studies characterizing a recently described sulfated proteoglycan that is specifically associated with Ia, we discovered that there were also nonproteoglycan sulfated components present in the Ia immunoprecipitates. One-dimensional sodium dodecyl sulfate-gel analysis of these latter sulfated components derived from both DR and DQ immunoprecipitates indicated that these components have mobilities indistinguishable from conventional Ia alpha and beta glycoproteins. Two-dimensional gel analysis confirmed these findings and revealed that Ia-associated invariant proteins are sulfated as well. The sulfate moiety was not removed by endoglycosidase F treatment, suggesting that the protein portion of the molecule was sulfated. These results indicate that Ia alpha-, beta-, and invariant chains can be sulfated and raise the possibility that sulfation may play a role in the physiology of Ia molecules.