Journal article
Proteolytic Degradation of Tyrosine Nitrated Proteins
Archives of biochemistry and biophysics, v 380(2), pp 360-366
15 Aug 2000
PMID: 10933892
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Tyrosine nitration is a covalent posttranslational protein modification that has been detected under several pathological conditions. This study reports that nitrated proteins are degraded by chymotrypsin and that protein nitration enhances susceptibility to degradation by the proteasome. Chymotrypsin cleaved the peptide bond between nitrated-tyrosine 108 and serine 109 in bovine Cu,Zn superoxide dismutase. However, the rate of chymotryptic cleavage of nitrated peptides was considerably slower than control. In contrast, nitrated bovine Cu,Zn superoxide dismutase was degraded at a rate 1.8-fold faster than that of control by a gradient-purified 20S/26S proteasome fraction from bovine retina. Exposure of PC12 cells to a nitrating agent resulted in the nitration of tyrosine hydroxylase and a 58 ± 12.5% decline in the steady-state levels of the protein 4 h after nitration. The steady-state levels of tyrosine hydroxylase were restored by selective inhibition of the proteasome activity with lactacystin. These data indicate that nitration of tyrosine residue(s) in proteins is sufficient to induce an accelerated degradation of the modified proteins by the proteasome and that the proteasome may be critical for the removal of nitrated proteins in vivo.
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Details
- Title
- Proteolytic Degradation of Tyrosine Nitrated Proteins
- Creators
- José M. Souza - Children's Hospital of PhiladelphiaIrene Choi - Children's Hospital of PhiladelphiaQiping Chen - Children's Hospital of PhiladelphiaMarie Weisse - Children's Hospital of PhiladelphiaEvgueni Daikhin - Children's Hospital of PhiladelphiaMarc Yudkoff - Children's Hospital of PhiladelphiaMartin Obin - Jean Mayer Human Nutrition Research Center on AgingJahan Ara - Hahnemann University HospitalJoel Horwitz - Hahnemann University HospitalHarry Ischiropoulos - Children's Hospital of Philadelphia
- Publication Details
- Archives of biochemistry and biophysics, v 380(2), pp 360-366
- Publisher
- Elsevier
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Pharmacology and Physiology
- Web of Science ID
- WOS:000088948700018
- Scopus ID
- 2-s2.0-0034663360
- Other Identifier
- 991019169491804721
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- Collaboration types
- Domestic collaboration
- International collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology
- Biophysics