Invariant chain is the core protein of the Ia-associated chondroitin sulfate proteoglycan

The murine Ia-associated chondroitin sulfate proteoglycan (CSPG) was studied both biochemically and immunochemically to determine the nature of its core protein. Chondroitinase ABC or chondroitinase AC treatment of the CSPG digested the chondroitin sulfate glycosaminoglycan, yielding a core protein...

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Bibliographic Details
Published in:The Journal of experimental medicine 1985-12, Vol.162 (6), p.1916-1934
Main Authors: SANT, A. J, CULLEN, S. E, GIACOLETTO, K. S, SCHWARTZ, B. D
Format: Article
Language:English
Subjects:
Animals
Antibodies, Monoclonal
Antibody Specificity
Antigens
Autoradiography
Biological and medical sciences
Chondroitin Sulfate Proteoglycans - analysis
Chondroitin Sulfate Proteoglycans - genetics
Chondroitin Sulfate Proteoglycans - immunology
Electrophoresis, Polyacrylamide Gel
Fundamental and applied biological sciences. Psychology
Fundamental immunology
Histocompatibility antigens (hla, h-2 and other systems)
Histocompatibility Antigens Class II - analysis
Histocompatibility Antigens Class II - genetics
Histocompatibility Antigens Class II - immunology
Mice
Mice, Inbred Strains
Molecular immunology
Molecular Weight
Peptides - analysis
Precipitin Tests
Proteoglycans - analysis
Spleen - cytology
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Summary:The murine Ia-associated chondroitin sulfate proteoglycan (CSPG) was studied both biochemically and immunochemically to determine the nature of its core protein. Chondroitinase ABC or chondroitinase AC treatment of the CSPG digested the chondroitin sulfate glycosaminoglycan, yielding a core protein that migrated with an apparent molecular weight of 38,000. Comparative V8 protease digestion of the CSPG core protein and conventional invariant glycoproteins yielded homologous peptides, indicating that the core protein and invariant chain were structurally similar. The purified CSPG and its core protein were both shown to react directly with the monoclonal anti-invariant chain antibody, In-1. Comparative tryptic peptide analysis by high performance liquid chromatography demonstrated coelution of the majority of the peptides from the invariant chain and the CSPG core protein. Collectively, these results indicate that the CSPG is an alternatively processed form of invariant chain.
ISSN:0022-1007
1540-9538
DOI:10.1084/jem.162.6.1916