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Redox balance and carbonylated proteins in limb and heart muscles of cachectic rats

Marin-Corral, Judith; Fontes , Cibely LU ; Pascual-Guardia, Sergi; Sanchez, Francisco; Olivan, Mireia; Argilés, Josep M; Busquets, Sílvia; López-Soriano, Francisco J and Barreiro, Esther (2010) In Antioxidants and Redox Signaling 12(3). p.80-365
Abstract

In fast- and slow-twitch limb and heart muscles of cachectic rats, redox balance and muscle structure were explored. The nature of the oxidatively modified proteins also was identified in these muscles. Reactive carbonyls, hydroxynonenal (HNE)- and malondialdehyde (MDA)-protein adducts, and antioxidant enzyme levels were determined in limb and heart muscles of cachectic (7 days after inoculation of Yoshida AH-130 ascites hepatoma) and control rats. Moreover, carbonylated proteins were identified (proteomics), and fiber-type composition evaluated (morphometry) in these muscles. In cachectic rats, compared with the controls: (a) HNE- and MDA-protein adducts levels were greater in gastrocnemius, tibialis anterior, soleus, and heart; (b) in... (More)

In fast- and slow-twitch limb and heart muscles of cachectic rats, redox balance and muscle structure were explored. The nature of the oxidatively modified proteins also was identified in these muscles. Reactive carbonyls, hydroxynonenal (HNE)- and malondialdehyde (MDA)-protein adducts, and antioxidant enzyme levels were determined in limb and heart muscles of cachectic (7 days after inoculation of Yoshida AH-130 ascites hepatoma) and control rats. Moreover, carbonylated proteins were identified (proteomics), and fiber-type composition evaluated (morphometry) in these muscles. In cachectic rats, compared with the controls: (a) HNE- and MDA-protein adducts levels were greater in gastrocnemius, tibialis anterior, soleus, and heart; (b) in the gastrocnemius, type II fiber size was reduced, and the intensity of carbonylated protein immunostaining was significantly greater in these fibers; and (c) proteins involved in glycolysis, ATP production and distribution, carbon dioxide hydration, muscle contraction, and mitochondrial metabolism were significantly more carbonylated in limb and heart muscles. Cancer cachexia alters redox balance in fast- and slow-twitch limb and heart muscles of rats, inducing increased oxidative modifications of key proteins involved in muscle structure and function. Additionally, it induces a reduction in type II fiber size in the gastrocnemius, which is associated with increased protein oxidation.

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published
keywords
Animals, Cachexia, Electrophoresis, Electrophoresis, Gel, Two-Dimensional, Immunoblotting, Immunohistochemistry, Male, Malondialdehyde, Muscle, Skeletal, Myocardium, Oxidation-Reduction, Protein Carbonylation, Rats, Rats, Wistar, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Journal Article, Research Support, Non-U.S. Gov't
in
Antioxidants and Redox Signaling
volume
12
issue
3
pages
16 pages
publisher
Mary Ann Liebert, Inc.
external identifiers
  • scopus:75149151430
ISSN
1557-7716
DOI
10.1089/ars.2009.2818
language
English
LU publication?
no
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cc3371b1-6e67-40d1-a822-e8a9a0976ace
date added to LUP
2017-02-28 16:15:45
date last changed
2018-05-29 10:11:45
@article{cc3371b1-6e67-40d1-a822-e8a9a0976ace,
  abstract     = {<p>In fast- and slow-twitch limb and heart muscles of cachectic rats, redox balance and muscle structure were explored. The nature of the oxidatively modified proteins also was identified in these muscles. Reactive carbonyls, hydroxynonenal (HNE)- and malondialdehyde (MDA)-protein adducts, and antioxidant enzyme levels were determined in limb and heart muscles of cachectic (7 days after inoculation of Yoshida AH-130 ascites hepatoma) and control rats. Moreover, carbonylated proteins were identified (proteomics), and fiber-type composition evaluated (morphometry) in these muscles. In cachectic rats, compared with the controls: (a) HNE- and MDA-protein adducts levels were greater in gastrocnemius, tibialis anterior, soleus, and heart; (b) in the gastrocnemius, type II fiber size was reduced, and the intensity of carbonylated protein immunostaining was significantly greater in these fibers; and (c) proteins involved in glycolysis, ATP production and distribution, carbon dioxide hydration, muscle contraction, and mitochondrial metabolism were significantly more carbonylated in limb and heart muscles. Cancer cachexia alters redox balance in fast- and slow-twitch limb and heart muscles of rats, inducing increased oxidative modifications of key proteins involved in muscle structure and function. Additionally, it induces a reduction in type II fiber size in the gastrocnemius, which is associated with increased protein oxidation.</p>},
  author       = {Marin-Corral, Judith and Fontes , Cibely and Pascual-Guardia, Sergi and Sanchez, Francisco and Olivan, Mireia and Argilés, Josep M and Busquets, Sílvia and López-Soriano, Francisco J and Barreiro, Esther},
  issn         = {1557-7716},
  keyword      = {Animals,Cachexia,Electrophoresis,Electrophoresis, Gel, Two-Dimensional,Immunoblotting,Immunohistochemistry,Male,Malondialdehyde,Muscle, Skeletal,Myocardium,Oxidation-Reduction,Protein Carbonylation,Rats,Rats, Wistar,Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization,Journal Article,Research Support, Non-U.S. Gov't},
  language     = {eng},
  number       = {3},
  pages        = {80--365},
  publisher    = {Mary Ann Liebert, Inc.},
  series       = {Antioxidants and Redox Signaling},
  title        = {Redox balance and carbonylated proteins in limb and heart muscles of cachectic rats},
  url          = {http://dx.doi.org/10.1089/ars.2009.2818},
  volume       = {12},
  year         = {2010},
}