Oxidized proteins in erythrocytes are rapidly degraded by the adenosine triphosphate-dependent proteolytic system - PubMed (original) (raw)

Oxidized proteins in erythrocytes are rapidly degraded by the adenosine triphosphate-dependent proteolytic system

A L Goldberg et al. Science. 1982.

Abstract

The rate of protein degradation in rabbit erythrocytes in normally very low. However, when cells were exposed to agents that oxidize cell proteins (nitrite or phenylhydrazine), the degradation of erythrocyte proteins to amino acids increased 7- to 33-fold. This effect was inhibited by the reducing agent methylene blue. Stimulation of proteolysis also occurred in cell extracts and resulted from the production of substrates (damaged proteins) rather than from activation of proteases. Inhibitors of glycolysis and of the soluble adenosine triphosphate-dependent proteolytic pathway decreased the protein degradation induced by nitrite, whereas inhibitors of lysosomal proteolysis had no effect. Thus, the adenosine triphosphate-dependent proteolytic system is present in mature red cells where it may help protect against the accumulation of proteins damaged by oxidation or other means.

PubMed Disclaimer

Similar articles

• Red blood cells contain a pathway for the degradation of oxidant-damaged hemoglobin that does not require ATP or ubiquitin.
  Fagan JM, Waxman L, Goldberg AL. Fagan JM, et al. J Biol Chem. 1986 May 5;261(13):5705-13. J Biol Chem. 1986. PMID: 3009430
• Increased proteolysis of oxidatively damaged hemoglobin in erythrocyte lysates in diabetes mellitus.
  Raghothama C, Rao P. Raghothama C, et al. Clin Chim Acta. 1994 Feb;225(1):65-70. doi: 10.1016/0009-8981(94)90028-0. Clin Chim Acta. 1994. PMID: 8033355 No abstract available.
• Characterization of hydrazine-stimulated proteolysis in human erythrocytes.
  Runge-Morris MA, Iacob S, Novak RF. Runge-Morris MA, et al. Toxicol Appl Pharmacol. 1988 Jul;94(3):414-26. doi: 10.1016/0041-008x(88)90282-7. Toxicol Appl Pharmacol. 1988. PMID: 2840755
• Regulation by proteolysis: energy-dependent proteases and their targets.
  Gottesman S, Maurizi MR. Gottesman S, et al. Microbiol Rev. 1992 Dec;56(4):592-621. doi: 10.1128/mr.56.4.592-621.1992. Microbiol Rev. 1992. PMID: 1480111 Free PMC article. Review.
• ATP-dependent proteases in prokaryotic and eukaryotic cells.
  Goldberg AL. Goldberg AL. Semin Cell Biol. 1990 Dec;1(6):423-32. Semin Cell Biol. 1990. PMID: 2103893 Review.

Cited by

• Polyubiquitin Chains Linked by Lysine Residue 48 (K48) Selectively Target Oxidized Proteins In Vivo.
  Manohar S, Jacob S, Wang J, Wiechecki KA, Koh HWL, Simões V, Choi H, Vogel C, Silva GM. Manohar S, et al. Antioxid Redox Signal. 2019 Nov 20;31(15):1133-1149. doi: 10.1089/ars.2019.7826. Antioxid Redox Signal. 2019. PMID: 31482721 Free PMC article.
• Age-related changes in cerebral oxidative metabolism. Implications for drug therapy.
  Hoyer S. Hoyer S. Drugs Aging. 1995 Mar;6(3):210-8. doi: 10.2165/00002512-199506030-00004. Drugs Aging. 1995. PMID: 7620233 Review.
• Determinants and Regulation of Protein Turnover in Yeast.
  Martin-Perez M, Villén J. Martin-Perez M, et al. Cell Syst. 2017 Sep 27;5(3):283-294.e5. doi: 10.1016/j.cels.2017.08.008. Epub 2017 Sep 13. Cell Syst. 2017. PMID: 28918244 Free PMC article.
• Degradation of native and modified forms of fructose-bisphosphate aldolase microinjected into HeLa cells.
  Hopgood MF, Knowles SE, Bond JS, Ballard FJ. Hopgood MF, et al. Biochem J. 1988 Nov 15;256(1):81-8. doi: 10.1042/bj2560081. Biochem J. 1988. PMID: 3223914 Free PMC article.

Publication types

MeSH terms

Substances

LinkOut - more resources

• Full Text Sources

  • Atypon