Research article summary (published 26 May 2008):

Role of copper,zinc-superoxide dismutase in catalyzing nitrotyrosine formation in murine liver.

Full Abstract

The only known function of Cu,Zn-superoxide dismutase (SOD1) is to catalyze the dismutation of superoxide anion into hydrogen peroxide. Our objective was to determine if SOD1 catalyzes murine liver protein nitration induced by acetaminophen (APAP) and lipopolysaccharide (LPS). Liver and plasma samples were collected from young adult SOD1 knockout mice (SOD1-/-) and wild-type (WT) mice at 5 or 6 h after an ip injection of saline, APAP, or LPS. Hepatic nitrotyrosine formation was induced by APAP and LPS only in the WT mice. The diminished hepatic protein nitration in the SOD1-/- mice was not directly related to plasma nitrite and nitrate concentrations. Similar genotype differences were seen in liver homogenates treated with a bolus of peroxynitrite. Adding only the holo-, and not the apo-, SOD1 enzyme into the liver homogenates enhanced the reaction in an activity-dependent fashion and nearly eliminated the genotype difference at the high doses. Mass spectrometry showed four more nitrotyrosine residues in bovine serum albumin and 10 more nitrated protein candidates in the SOD1-/- liver homogenates by peroxynitrite with added SOD1. In conclusion, the diminished hepatic protein nitration mediated by APAP or LPS in the SOD1-/- mice is due to the lack of SOD1 activity per se.

Author information

Author/s: Zhu, Jian-Hong (JH); Zhang, Xiaomei (X); Roneker, Carol A (CA); McClung, James P (JP); Zhang, Sheng (S); Thannhauser, Theodore W (TW); Ripoll, Daniel R (DR); Sun, Qi (Q); Lei, Xin Gen (XG);

Affiliation: Department of Animal Science, Cornell University, Ithaca, NY 14853, USA.

Grants: DK53108 (Agency:NIDDK NIH HHS)

Journal and publication information

Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't

Journal: Free radical biology & medicine (Free Radic Biol Med), published in United States. (Language: eng)

Reference: 2008-Sep; vol 45 (issue 5) : pp 611-8

Dates: Created 2008/08/11; Completed 2008/10/03; Revised 2009/09/15;

PMID: 18573333, status: MEDLINE (last retrieval date: 9/16/2009, IMS Date: )

Sourced from the National Library of Medicine. Abstract text and other information may be subject to copyright.

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MeSH headings (categories)

This article was linked to the MESH Headings shown below.

Acetaminophen - pharmacology Animals Catalysis Cattle Genotype Lipopolysaccharides - pharmacology Liver - drug effects; enzymology

Mice Mice, Knockout Nitrogen - metabolism Nitrogen Oxides - blood Substrate Specificity Superoxide Dismutase - deficiency; genetics; metabolism Tyrosine - analogs & derivatives; biosynthesis

Associated Chemicals: Lipopolysaccharides (0) ; Nitrogen Oxides (0) ; Acetaminophen (103-90-2) ; 3-nitrotyrosine (3604-79-3) ; Tyrosine (55520-40-6) ; Nitrogen (7727-37-9) ; Superoxide Dismutase (EC 1.15.1.1)

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