Autor: |
Sellares J; Muscle and Respiratory System Research Unit, Respiratory Medicine Department, IMIM-Hospital del Mar, Universitat Pompeu Fabra, C/Dr. Aiguader, 80, E-08003 Barcelona, Spain., Mas S, Melo E, Sánchez F, Marin J, Gea J, Barreiro E |
Jazyk: |
angličtina |
Zdroj: |
Respiratory physiology & neurobiology [Respir Physiol Neurobiol] 2007 Feb 15; Vol. 155 (2), pp. 156-66. Date of Electronic Publication: 2006 Jun 03. |
DOI: |
10.1016/j.resp.2006.05.008 |
Abstrakt: |
Hyperthermia was shown to induce oxidative stress by uncoupling mitochondrial respiratory chain and to reduce superoxide dismutase (SOD) activity in muscles. Reactive carbonyl groups, malondialdehyde (MDA)-protein adducts, 3-nitrotyrosine immunoreactivity, Mn-SOD, and catalase were detected using immunoblotting in rat diaphragm specimens and homogenates thawed at room temperature (after previous storage at -80 degrees C) for 5, 15, 30, and 60 min, and 3, 6, and 24h to be subsequently and immediately stored at -80 degrees C. Mn-SOD activity was also measured in all muscles. Both total protein carbonylation (reactive carbonyl groups and MDA-protein adducts) and nitration were significantly increased over time, reaching their peaks in the diaphragms of the 60- and 15-min groups, respectively. Mn-SOD expression and activity were significantly reduced over time, while catalase expression showed no significant variation. Protein oxidation was significantly increased in the rat diaphragms exposed to freezing-thawing cycles of different time lengths, while Mn-SOD was substantially reduced in all muscles. |
Databáze: |
MEDLINE |
Externí odkaz: |
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