Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/195297
Type: Artigo de periódico
Title: Induction Of Protein Catabolism And The Ubiquitin-proteasome Pathway By Mild Oxidative Stress.
Author: Gomes-Marcondes, Maria Cristina C
Tisdale, Michael J
Abstract: Muscle wasting in cancer cachexia is associated with increased levels of malondialdehyde (MDA) in gastrocnemius muscles, suggesting an increased oxidative stress. To determine whether oxidative stress contributes to muscle protein catabolism, an in vitro model system, consisting of C2C12 myotubes, was treated with either 0.2 mM FeSO4, 0.1 mM H2O2, or both, to replicate the rise in MDA content in cachexia. All treatments caused an increased protein catabolism and a decreased myosin expression. There was an increase in the proteasome chymotrypsin-like enzyme activity, while immunoblotting showed an increased expression of the 20S proteasome alpha-subunits, p42, and the ubiquitin-conjugating enzyme, E214k. These results show that mild oxidative stress increases protein degradation in skeletal muscle by causing an increased expression of the major components of the ubiquitin-proteasome pathway.
Subject: Animals
Blotting, Western
Cachexia
Cells, Cultured
Cysteine Endopeptidases
Egg Proteins
Malondialdehyde
Membrane Glycoproteins
Mice
Multienzyme Complexes
Muscle, Skeletal
Myosins
Oxidative Stress
Proteasome Endopeptidase Complex
Proteins
Receptors, Cell Surface
Time Factors
Ubiquitin
Rights: fechado
Identifier DOI: 
Address: http://www.ncbi.nlm.nih.gov/pubmed/11911972
Date Issue: 2002
Appears in Collections:Unicamp - Artigos e Outros Documentos

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