Journal
FREE RADICAL RESEARCH
Volume 48, Issue 1, Pages 12-29Publisher
TAYLOR & FRANCIS LTD
DOI: 10.3109/10715762.2013.830718
Keywords
mitochondrial permeability transition pore; inner membrane anion channel; TOM40; NOX2; NOX4
Categories
Funding
- Research into Ageing
- Medical Research Council [G1002120]
- United States National Institute on Aging [AG-20591]
- Medical Research Council [MR/K006312/1] Funding Source: researchfish
- NATIONAL INSTITUTE ON AGING [P01AG020591] Funding Source: NIH RePORTER
- MRC [MR/K006312/1, G1002120] Funding Source: UKRI
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The production of reactive oxygen and nitrogen species (RONS) by skeletal muscle is important as it (i) underlies oxidative damage in many degenerative muscle pathologies and (ii) plays multiple regulatory roles by fulfilling important cellular functions. Superoxide and nitric oxide (NO) are the primary radical species produced by skeletal muscle and studies in the early 1980s demonstrated that their generation is augmented during contractile activity. Over the past 30 years considerable research has been undertaken to identify the major sites that contribute to the increased rate of RONS generation in response to contractions. It is widely accepted that NO is regulated by the nitric oxide synthases, however the sites that modulate changes in superoxide during exercise remain unclear. Despite the initial indications that the mitochondrial electron transport chain was the predominant source of superoxide during activity, with the development of analytical methods a number of alternative potential sites have been identified including the NAD(P)H oxidases, xanthine oxidase, cyclooxygenases, and lipoxygenases linked to the activity of the phospholipase A 2 enzymes. In the present review we outline the subcellular sites that modulate intracellular changes in superoxide in skeletal muscle and based on the available experimental evidence in the literature we conclude that the NAD(P) H oxidases are likely to be the major superoxide generating sources in contracting skeletal muscle.
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