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Structural analysis of the N-linked oligosaccharides on HLA-DR and HLA-DQ molecules from normal lymphocytes

Conference · · Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States)
OSTI ID:7024674
To determine if the glycosylation pattern of class II molecules was similar for normal cells and B-lymphoblastoid cell lines, they have used serial lectin affinity chromatography to analyze the structure of the N-linked oligosaccharides on HLA-DR and DQ molecules derived from normal tonsil cells. Tonsil cells were labeled with /sup 3/H-mannose and chased so that only mature molecules would be analyzed. Invariant chain was dissociated from ..cap alpha beta.. complexes. HLA-DQ molecules migrated as single ..cap alpha.. and ..beta.. chains; the DR molecules migrated as two ..cap alpha.. chains (..cap alpha../sub 1/ and ..cap alpha../sub 2/) and two ..beta.. chains (..beta../sub 1/ and ..beta../sub 2/). Pronase released glycopeptides were analyzed by serial lectin affinity chromatography. The DQ ..cap alpha.. chain bore one high mannose oligosaccharide and one complex tri- or tetra-antennary oligosaccharide which was fucosylated 50% of the time. The majority of the DQ ..beta.. chains bore one complex fucosylated tri- or tetra-antennary oligosaccharide. The glycosylation patterns of the DR ..cap alpha../sub 1/ and ..cap alpha../sub 2/ chains and DR ..beta../sub 1/ chains were similar to that of the DQ ..cap alpha.. and ..beta.. chains, respectively. However, the DR ..beta../sub 2/ chain bore predominantly a high-mannose oligosaccharide. These data suggest that the glycosylation patterns of DQ molecules are similar to those of DR molecules, and that the glycosylation patterns of DR molecules are similar for normal and lymphoblastoid cells.
Research Organization:
Howard Hughes Medical Institute, St. Louis, MO
OSTI ID:
7024674
Report Number(s):
CONF-8604222-
Conference Information:
Journal Name: Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States) Journal Volume: 45:4
Country of Publication:
United States
Language:
English