Skip to main content
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1986 May;83(10):3437–3438. doi: 10.1073/pnas.83.10.3437

Self and non-self discrimination by "restriction proteases".

I Lefkovits
PMCID: PMC323529  PMID: 2422649

Abstract

I propose that an organism possesses a set of specific enzymes ("restriction proteases") that cleave self proteins at defined amino acid sequences unless these sequences are rendered inaccessible by glycosylation. Intracellular proteins are degraded by restriction proteases when cells die. In this way, intracellular proteins remain undetected by the immune system. I propose that some autoimmune diseases are caused by the absence of a specific restriction protease.

Full text

PDF
3437

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Anderson N. G., Anderson L. The Human Protein Index. Clin Chem. 1982 Apr;28(4 Pt 2):739–748. [PubMed] [Google Scholar]
  2. Anderson N. L., Anderson N. G. Analytical techniques for cell fractions. XXII. Two-dimensional analysis of serum and tissue proteins: multiple gradient-slab gel electrophoresis. Anal Biochem. 1978 Apr;85(2):341–354. doi: 10.1016/0003-2697(78)90230-0. [DOI] [PubMed] [Google Scholar]
  3. Briles E. B. Lectin-resistant cell surface variants of eukaryotic cells. Int Rev Cytol. 1982;75:101–165. doi: 10.1016/s0074-7696(08)61003-7. [DOI] [PubMed] [Google Scholar]
  4. Grabar P. "Self"and "not-self" in immunology. Lancet. 1974 Jun 29;1(7870):1320–1322. doi: 10.1016/s0140-6736(74)90685-0. [DOI] [PubMed] [Google Scholar]
  5. LIND P. E., BURNET F. M. Recombination between virulent and non-virulent strains of influenza virus. II. The behaviour of virulence markers on recombination. Aust J Exp Biol Med Sci. 1957 Feb;35(1):67–78. doi: 10.1038/icb.1957.8. [DOI] [PubMed] [Google Scholar]
  6. Nossal G. J., Pike B. L. Clonal anergy: persistence in tolerant mice of antigen-binding B lymphocytes incapable of responding to antigen or mitogen. Proc Natl Acad Sci U S A. 1980 Mar;77(3):1602–1606. doi: 10.1073/pnas.77.3.1602. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. O'Brien S. J. On estimating functional gene number in eukaryotes. Nat New Biol. 1973 Mar 14;242(115):52–54. doi: 10.1038/newbio242052a0. [DOI] [PubMed] [Google Scholar]
  8. Pink J. R. Changes in T-lymphocyte glycoprotein structures associated with differentiation. Contemp Top Mol Immunol. 1983;9:89–113. doi: 10.1007/978-1-4684-4517-6_3. [DOI] [PubMed] [Google Scholar]
  9. Pollack L., Atkinson P. H. Correlation of glycosylation forms with position in amino acid sequence. J Cell Biol. 1983 Aug;97(2):293–300. doi: 10.1083/jcb.97.2.293. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Schreier M. H., Tees R. Clonal induction of helper T cells: conversion of specific signals into nonspecific signals. Int Arch Allergy Appl Immunol. 1980;61(2):227–237. doi: 10.1159/000232437. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES