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. 1991 Feb 1;173(2):423–427. doi: 10.1084/jem.173.2.423

Autoantibodies against the multicatalytic proteinase in patients with systemic lupus erythematosus

PMCID: PMC2118784  PMID: 1703207

Abstract

Sera from patients with systemic lupus erythematosus contain specific autoantibodies directed against different polypeptide components of the multicatalytic proteinase (also known as proteasome or prosome). These human autoantibodies, in contrast to polyclonal antibodies obtained in rabbits against the purified enzyme, recognize highly conserved epitopes of the multicatalytic proteinase polypeptides from yeast to human.

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Selected References

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  1. Arribas J., Castaño J. G. Kinetic studies of the differential effect of detergents on the peptidase activities of the multicatalytic proteinase from rat liver. J Biol Chem. 1990 Aug 15;265(23):13969–13973. [PubMed] [Google Scholar]
  2. Arrigo A. P., Simon M., Darlix J. L., Spahr P. F. A 20S particle ubiquitous from yeast to human. J Mol Evol. 1987;25(2):141–150. doi: 10.1007/BF02101756. [DOI] [PubMed] [Google Scholar]
  3. Baumeister W., Dahlmann B., Hegerl R., Kopp F., Kuehn L., Pfeifer G. Electron microscopy and image analysis of the multicatalytic proteinase. FEBS Lett. 1988 Dec 5;241(1-2):239–245. doi: 10.1016/0014-5793(88)81069-x. [DOI] [PubMed] [Google Scholar]
  4. Dahlmann B., Kopp F., Kuehn L., Niedel B., Pfeifer G., Hegerl R., Baumeister W. The multicatalytic proteinase (prosome) is ubiquitous from eukaryotes to archaebacteria. FEBS Lett. 1989 Jul 17;251(1-2):125–131. doi: 10.1016/0014-5793(89)81441-3. [DOI] [PubMed] [Google Scholar]
  5. Domae N., Harmon F. R., Busch R. K., Spohn W., Subrahmanyam C. S., Busch H. Donut-shaped "miniparticles" in nuclei of human and rat cells. Life Sci. 1982 Feb 1;30(5):469–477. doi: 10.1016/0024-3205(82)90464-7. [DOI] [PubMed] [Google Scholar]
  6. Falkenburg P. E., Haass C., Kloetzel P. M., Niedel B., Kopp F., Kuehn L., Dahlmann B. Drosophila small cytoplasmic 19S ribonucleoprotein is homologous to the rat multicatalytic proteinase. Nature. 1988 Jan 14;331(6152):190–192. doi: 10.1038/331190a0. [DOI] [PubMed] [Google Scholar]
  7. Gautier J., Pal J. K., Grossi de Sa M. F., Beetschen J. C., Scherrer K. Differential cytolocalization of prosomes in axolotl during oogenesis and meiotic maturation. J Cell Sci. 1988 Aug;90(Pt 4):543–553. doi: 10.1242/jcs.90.4.543. [DOI] [PubMed] [Google Scholar]
  8. Grossi de Sa M. F., Martins de Sa C., Harper F., Coux O., Akhayat O., Pal J. K., Florentin Y., Scherrer K. Cytolocalization of prosomes as a function of differentiation. J Cell Sci. 1988 Feb;89(Pt 2):151–165. doi: 10.1242/jcs.89.2.151. [DOI] [PubMed] [Google Scholar]
  9. Hügle B., Kleinschmidt J. A., Franke W. W. The 22 S cylinder particles of Xenopus laevis. II. Immunological characterization and localization of their proteins in tissues and cultured cells. Eur J Cell Biol. 1983 Nov;32(1):157–163. [PubMed] [Google Scholar]
  10. Kurata N., Tan E. M. Identification of antibodies to nuclear acidic antigens by counterimmunoelectrophoresis. Arthritis Rheum. 1976 May-Jun;19(3):574–580. doi: 10.1002/art.1780190309. [DOI] [PubMed] [Google Scholar]
  11. 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]
  12. Maurizi M. R., Clark W. P., Katayama Y., Rudikoff S., Pumphrey J., Bowers B., Gottesman S. Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli. J Biol Chem. 1990 Jul 25;265(21):12536–12545. [PubMed] [Google Scholar]
  13. Maurizi M. R., Clark W. P., Kim S. H., Gottesman S. Clp P represents a unique family of serine proteases. J Biol Chem. 1990 Jul 25;265(21):12546–12552. [PubMed] [Google Scholar]
  14. Narayan K. S., Rounds D. E. Minute ring-shaped particles in cultured cells of malignant origin. Nat New Biol. 1973 May 30;243(126):146–150. doi: 10.1038/newbio243146a0. [DOI] [PubMed] [Google Scholar]
  15. Nieto A., Mira E., Castaño J. G. Transcriptional regulation of rat liver protein disulphide-isomerase gene by insulin and in diabetes. Biochem J. 1990 Apr 15;267(2):317–323. doi: 10.1042/bj2670317. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Olmsted J. B. Affinity purification of antibodies from diazotized paper blots of heterogeneous protein samples. J Biol Chem. 1981 Dec 10;256(23):11955–11957. [PubMed] [Google Scholar]
  17. Sato Y., Nagase K. I. Isolation of protective antigen from Bordetella pertussis. Biochem Biophys Res Commun. 1967 Apr 20;27(2):195–201. doi: 10.1016/s0006-291x(67)80061-5. [DOI] [PubMed] [Google Scholar]
  18. Tan E. M. Antinuclear antibodies: diagnostic markers for autoimmune diseases and probes for cell biology. Adv Immunol. 1989;44:93–151. doi: 10.1016/s0065-2776(08)60641-0. [DOI] [PubMed] [Google Scholar]
  19. Tanaka K., Ii K., Ichihara A., Waxman L., Goldberg A. L. A high molecular weight protease in the cytosol of rat liver. I. Purification, enzymological properties, and tissue distribution. J Biol Chem. 1986 Nov 15;261(32):15197–15203. [PubMed] [Google Scholar]
  20. Tanaka K., Tamura T., Kumatori A., Kwak T. H., Chung C. H., Ichihara A. Separation of yeast proteasome subunits. Immunoreactivity with antibodies against ATP-dependent protease Ti from Escherichia coli. Biochem Biophys Res Commun. 1989 Nov 15;164(3):1253–1261. doi: 10.1016/0006-291x(89)91804-4. [DOI] [PubMed] [Google Scholar]
  21. Tanaka K., Yoshimura T., Kumatori A., Ichihara A., Ikai A., Nishigai M., Kameyama K., Takagi T. Proteasomes (multi-protease complexes) as 20 S ring-shaped particles in a variety of eukaryotic cells. J Biol Chem. 1988 Nov 5;263(31):16209–16217. [PubMed] [Google Scholar]
  22. Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350–4354. doi: 10.1073/pnas.76.9.4350. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Wagner B. J., Margolis J. W. Common epitopes of bovine lens multicatalytic-proteinase-complex subunits. Biochem J. 1989 Jan 1;257(1):265–269. doi: 10.1042/bj2570265. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Young R. A., Elliott T. J. Stress proteins, infection, and immune surveillance. Cell. 1989 Oct 6;59(1):5–8. doi: 10.1016/0092-8674(89)90861-1. [DOI] [PubMed] [Google Scholar]

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