| Exercise-induced immunosuppression: roles of reactive oxygen species and 5'-AMP-activated protein kinase dephosphorylation within immune cells. | |
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MedLine Citation:
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PMID: 20167678 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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We previously proposed 5'-AMP-activated protein kinase (AMPK) dephosphorylation within immune cells as an intracellular mechanism linking exercise and immunosuppression. In this study, AMPK phosphorylation underwent transient (<1 h) decreases (53.8+/-7.2% basal) immediately after exercise (45 min of cycling at 70% VO2max) in a cohort of 16 adult male participants. Similar effects were seen with running. However, because exercise-induced inactivation of AMPK was previously shown to occur in an AMP-independent manner, the means by which AMPK is inactivated in this context is not yet clear. To investigate the hypothesis that exercise-induced inactivation of AMPK is mediated via signaling mechanisms distinct from changes in cellular AMP-to-ATP ratios, reactive oxygen species (ROS) and intracellular Ca2+ signaling were investigated in mononuclear cells before and after exercise and in cultured monocytic MM6 cells. In in vitro studies, treatment with an antioxidant (ascorbic acid, 4 h, 50 microM) decreased MM6 cell intracellular ROS levels (88.0+/-5.2% basal) and induced dephosphorylation of AMPK (44.7+/-17.6% basal). By analogy, the fact that exercise decreased mononuclear cell ROS content (32.8+/-16.6% basal), possibly due to downregulation (43.4+/-8.0% basal) of mRNA for NOX2, the catalytic subunit of the cytoplasmic ROS-generating enzyme NADPH oxidase, may provide an explanation for the AMPK-dephosphorylating effect of exercise. In contrast, exercise-induced Ca2+ signaling events did not seem to be coupled to changes in AMPK activity. Thus we propose that the exercise-induced decreases in both intracellular ROS and AMPK phosphorylation seen in this study constitute evidence supporting a role for ROS in controlling AMPK, and hence immune function, in the context of exercise-induced immunosuppression. |
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Authors:
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Hannah Moir; Michael G Hughes; Stephen Potter; Craig Sims; Lee R Butcher; Nia A Davies; Kenneth Verheggen; Kenneth P Jones; Andrew W Thomas; Richard Webb |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2010-02-18 |
Journal Detail:
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Title: Journal of applied physiology (Bethesda, Md. : 1985) Volume: 108 ISSN: 1522-1601 ISO Abbreviation: J. Appl. Physiol. Publication Date: 2010 May |
Date Detail:
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Created Date: 2010-05-05 Completed Date: 2010-08-12 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 8502536 Medline TA: J Appl Physiol Country: United States |
Other Details:
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Languages: eng Pagination: 1284-92 Citation Subset: IM |
Affiliation:
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Cardiff School of Health Sciences, University of Wales Institute, Cardiff CF5 2YB, UK. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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AMP-Activated Protein Kinases
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metabolism* Antioxidants / pharmacology Ascorbic Acid / pharmacology Bicycling Calcium Signaling Cells, Cultured E-Selectin / blood Exercise* Humans Immune Tolerance* / drug effects Immunoglobulin A / metabolism Male Membrane Glycoproteins / genetics, metabolism Monocytes / drug effects, enzymology*, immunology* NADPH Oxidase / genetics, metabolism Oxidative Stress* / drug effects Phosphorylation RNA, Messenger / metabolism Reactive Oxygen Species / metabolism* Running Saliva / immunology Time Factors Young Adult |
| Chemical | |
Reg. No./Substance:
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0/Antioxidants; 0/CYBB protein, human; 0/E-Selectin; 0/Immunoglobulin A; 0/Membrane Glycoproteins; 0/RNA, Messenger; 0/Reactive Oxygen Species; 50-81-7/Ascorbic Acid; EC 1.6.3.1/NADPH Oxidase; EC 2.7.11.1/AMP-Activated Protein Kinases; EC 2.7.11.1/PRKAA1 protein, human |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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