| Plasma protein carbonylation and physical exercise. | |
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MedLine Citation:
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PMID: 21103510 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Regular physical activity is associated with a reduced risk of coronary heart disease, as it probably modifies the balance between free-radical generation and antioxidant activity. On the other hand, however, acute physical activity increases oxygen uptake and leads to a temporary imbalance between the production of reactive oxygen and nitrogen species (RONS) and their disposal: this phenomenon is called oxidative stress. Proteins are one of the most important oxidation targets during physical exercise and carbonylation is one of the most common oxidative protein modifications. In cells there is a physiological level of oxidized proteins that doesn't interfere with cell function; however, an increase in oxidized protein levels may cause a series of cellular malfunctions that could lead to a disease state. For this reason the quantification of protein oxidation is important to distinguish a healthy state from a disease state. Several studies have demonstrated an increase of carbonylated plasma proteins in athletes after exercise, but none have identified targets of this oxidation. Recently a process of protein decarbonylation has been discovered, this may indicate that carbonylation could be involved in signal transduction. The aim of our research was to characterize plasma protein carbonylation in response to physical exercise in trained male endurance athletes. We analyzed by proteomic approach their plasma proteins at resting condition and after two different kinds of physical exercise (PE). We used 2D-GE followed by western blot with specific antibodies against carbonylated proteins. The 2D analysis identified Haptoglobin as potential protein target of carbonylation after PE. We also identified Serotransferrin and Fibrinogen whose carbonylation is reduced after exercise. These methods have allowed us to obtain an overview of plasma protein oxidation after physical exercise. |
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Authors:
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Francesca Guidi; Francesca Magherini; Tania Gamberi; Luca Bini; Michele Puglia; Riccardo Marzocchini; Francesco Ranaldi; Pietro Amedeo Modesti; Massimo Gulisano; Alessandra Modesti |
Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2010-11-22 |
Journal Detail:
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Title: Molecular bioSystems Volume: 7 ISSN: 1742-2051 ISO Abbreviation: Mol Biosyst Publication Date: 2011 Mar |
Date Detail:
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Created Date: 2011-02-15 Completed Date: 2011-08-01 Revised Date: 2011-11-08 |
Medline Journal Info:
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Nlm Unique ID: 101251620 Medline TA: Mol Biosyst Country: England |
Other Details:
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Languages: eng Pagination: 640-50 Citation Subset: IM |
Affiliation:
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Department of Biochemical Sciences, University of Florence, Viale Morgagni, 50, 50134, Italy. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Athletes Electrophoresis, Gel, Two-Dimensional Exercise* Exercise Test Fibrinogen / chemistry, metabolism* Haptoglobins / chemistry, metabolism* Humans Male Middle Aged Physical Fitness Protein Carbonylation* Proteomics Transferrin / chemistry, metabolism* |
| Chemical | |
Reg. No./Substance:
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0/Haptoglobins; 11096-37-0/Transferrin; 9001-32-5/Fibrinogen |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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