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. 1985 Dec 1;162(6):1916–1934. doi: 10.1084/jem.162.6.1916

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

PMCID: PMC2187998  PMID: 3864916

Abstract

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.

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Selected References

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  1. Abruzzini L. N., Schwartz B. D. Tentative assignment of alleles for guinea pig Ia antigens. I. Ia.3,5 and Ia.4,5 share structural homology expected for alleles. J Immunol. 1982 Jun;128(6):2682–2690. [PubMed] [Google Scholar]
  2. Accolla R. S., Carra G., Buchegger F., Carrel S., Mach J. P. The human Ia-associated invariant chain is synthesized in Ia-negative B cell variants and is not expressed on the cell surface of both Ia-negative and Ia-positive parental cells. J Immunol. 1985 May;134(5):3265–3271. [PubMed] [Google Scholar]
  3. Charron D. J., McDevitt H. O. Analysis of HLA-D region-associated molecules with monoclonal antibody. Proc Natl Acad Sci U S A. 1979 Dec;76(12):6567–6571. doi: 10.1073/pnas.76.12.6567. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Claesson L., Larhammar D., Rask L., Peterson P. A. cDNA clone for the human invariant gamma chain of class II histocompatibility antigens and its implications for the protein structure. Proc Natl Acad Sci U S A. 1983 Dec;80(24):7395–7399. doi: 10.1073/pnas.80.24.7395. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Cleveland D. W., Fischer S. G., Kirschner M. W., Laemmli U. K. Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis. J Biol Chem. 1977 Feb 10;252(3):1102–1106. [PubMed] [Google Scholar]
  6. Fransson L. A., Carlstedt I., Cöster L., Malmström A. Binding of transferrin to the core protein of fibroblast proteoheparan sulfate. Proc Natl Acad Sci U S A. 1984 Sep;81(18):5657–5661. doi: 10.1073/pnas.81.18.5657. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Frelinger J. G., Hood L., Wettstein P. Analyses of RT1 products using two-dimensional polyacrylamide gels. Transplant Proc. 1981 Jun;13(2):1360–1363. [PubMed] [Google Scholar]
  8. Holt G. D., Swiedler S. J., Freed J. H., Hart G. W. Murine Ia-associated invariant chain's processing to complex oligosaccharide forms and its dissociation from the I-Ak complex. J Immunol. 1985 Jul;135(1):399–407. [PubMed] [Google Scholar]
  9. Kimata K., Okayama M., Ooira A., Suzuki S. Heterogeneity of proteochondroitin sulfates produced by chondrocytes at different stages of cytodifferentiation. J Biol Chem. 1974 Mar 10;249(5):1646–1653. [PubMed] [Google Scholar]
  10. Kranz D. M., Voss E. W., Jr Partial elucidation of an anti-hapten repertoire in BALB/c mice: comparative characterization of several monoclonal anti-fluorescyl antibodies. Mol Immunol. 1981 Oct;18(10):889–898. doi: 10.1016/0161-5890(81)90012-2. [DOI] [PubMed] [Google Scholar]
  11. Kupinski J. M., Plunkett M. L., Freed J. H. Assignment of antigenic determinants to separated I-A kappa chains. J Immunol. 1983 May;130(5):2277–2281. [PubMed] [Google Scholar]
  12. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  13. Machamer C. E., Cresswell P. Biosynthesis and glycosylation of the invariant chain associated with HLA-DR antigens. J Immunol. 1982 Dec;129(6):2564–2569. [PubMed] [Google Scholar]
  14. Moosic J. P., Sung E., Nilson A., Jones P. P., McKean D. J. The selective solubilization of different murine splenocyte membrane fractions with lubrol WX and triton X-100 distinguishes two forms of Ia antigens. A cell surface (alpha, beta) and an intracellular (alpha, Ii, beta). J Biol Chem. 1982 Aug 25;257(16):9684–9691. [PubMed] [Google Scholar]
  15. Omary M. B., Trowbridge I. S. Covalent binding of fatty acid to the transferrin receptor in cultured human cells. J Biol Chem. 1981 May 25;256(10):4715–4718. [PubMed] [Google Scholar]
  16. Owen M. J., Kissonerghis A. M., Lodish H. F., Crumpton M. J. Biosynthesis and maturation of HLA-DR antigens in vivo. J Biol Chem. 1981 Sep 10;256(17):8987–8993. [PubMed] [Google Scholar]
  17. Pugsley A. P., Schnaitman C. A. Factors affecting the electrophoretic mobility of the major outer membrane proteins of Escherichia coli in polyacrylamide gels. Biochim Biophys Acta. 1979 Nov 23;581(1):163–178. doi: 10.1016/0005-2795(79)90233-2. [DOI] [PubMed] [Google Scholar]
  18. Sant A. J., Cullen S. E., Schwartz B. D. Biosynthetic relationships of the chondroitin sulfate proteoglycan with Ia and invariant chain glycoproteins. J Immunol. 1985 Jul;135(1):416–422. [PubMed] [Google Scholar]
  19. Sant A. J., Cullen S. E., Schwartz B. D. Identification of a sulfate-bearing molecule associated with HLA class II antigens. Proc Natl Acad Sci U S A. 1984 Mar;81(5):1534–1538. doi: 10.1073/pnas.81.5.1534. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Sant A. J., Schwartz B. D., Cullen S. E. Cellular distribution of the Ia-associated chondroitin sulfate proteoglycan. J Immunol. 1985 Jul;135(1):408–415. [PubMed] [Google Scholar]
  21. Sant A. J., Schwartz B. D., Cullen S. E. Identification of a new component in the murine Ia molecular complex. J Exp Med. 1983 Dec 1;158(6):1979–1992. doi: 10.1084/jem.158.6.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Schneider C., Owen M. J., Banville D., Williams J. G. Primary structure of human transferrin receptor deduced from the mRNA sequence. Nature. 1984 Oct 18;311(5987):675–678. doi: 10.1038/311675b0. [DOI] [PubMed] [Google Scholar]
  23. Shackelford D. A., Strominger J. L. Demonstration of structural polymorphism among HLA-DR light chains by two-dimensional gel electrophoresis. J Exp Med. 1980 Jan 1;151(1):144–165. doi: 10.1084/jem.151.1.144. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Singer P. A., Lauer W., Dembić Z., Mayer W. E., Lipp J., Koch N., Hämmerling G., Klein J., Dobberstein B. Structure of the murine Ia-associated invariant (Ii) chain as deduced from a cDNA clone. EMBO J. 1984 Apr;3(4):873–877. doi: 10.1002/j.1460-2075.1984.tb01899.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Stearne P. A., Pietersz G. A., Goding J. W. cDNA cloning of the murine transferrin receptor: sequence of trans-membrane and adjacent regions. J Immunol. 1985 May;134(5):3474–3479. [PubMed] [Google Scholar]
  26. Strubin M., Mach B., Long E. O. The complete sequence of the mRNA for the HLA-DR-associated invariant chain reveals a polypeptide with an unusual transmembrane polarity. EMBO J. 1984 Apr;3(4):869–872. doi: 10.1002/j.1460-2075.1984.tb01898.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Yamamoto K., Koch N., Steinmetz M., Hämmerling G. J. One gene encodes two distinct Ia-associated invariant chains. J Immunol. 1985 May;134(5):3461–3467. [PubMed] [Google Scholar]
  28. Zecher R., Ballhausen W., Reske K., Linder D., Schlüter M., Stirm S. The invariant chains of mouse class II antigens: biochemical properties and molecular relationship. Eur J Immunol. 1984 Jun;14(6):511–517. doi: 10.1002/eji.1830140606. [DOI] [PubMed] [Google Scholar]

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