NDLI: Endurance exercise activates matrix metalloproteinases in human skeletal muscle.

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Endurance exercise activates matrix metalloproteinases in human skeletal muscle.

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Endurance exercise activates matrix metalloproteinases in human skeletal muscle.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Rullman, Eric Norrbom, Jessica Strömberg, Anna Wågsäter, Dick Rundqvist, Helene Haas, Tara Gustafsson, Thomas
Description	Country affiliation: Sweden Author Affiliation: Rullman E ( Department of Laboratory Medicine, Division of Clinical Physiology, Karolinska University Hospital, Karolinska Institute, Stockholm, Sweden. eric.rullman@ki.se)
Abstract	In the present study, the effect of exercise training on the expression and activity of matrix metalloproteinases (MMPs) in the human skeletal muscle was investigated. Ten subjects exercised one leg for 45 min with restricted blood flow and then exercised the other leg at the same absolute workload with unrestricted blood flow. The exercises were conducted four times per week for 5 wk. Biopsies were taken from the vastus lateralis muscles of both legs at rest before the training period, after 10 days and 5 wk of training, and 2 h after the first exercise bout for analysis of MMP and tissue inhibitor of metalloproteinase-1 (TIMP-1) mRNA, enzyme activity, and protein expression. Levels of MMP-2, MMP-14, and TIMP-1 mRNA in muscle tissue increased after 10 days of training regardless of blood flow condition. MMP-2 mRNA level in laser-dissected myofibers and MMP-2 activity in whole muscle increased with training. The level of MMP-9 mRNA and activity increased after the first bout of exercise. Although MMP-9 mRNA levels appeared to be very low, the activity of MMP-9 after a single bout of exercise was similar to that of MMP-2 after 10 days of exercise. MMP-2 and MMP-9 protein was both present throughout the extracellular matrix of the muscle, both around fibers and capillaries, but MMP-2 was also present within the skeletal muscle fibers. These results show that MMPs are activated in skeletal muscle in nonpathological conditions such as voluntary exercise. The expression and time pattern indicate differences between the MMPs in regards of production sites as well as in the regulating mechanism.
File Format	HTM / HTML
ISSN	87507587
e-ISSN	15221601
Journal	Journal of Applied Physiology
Issue Number	3
Volume Number	106
Language	English
Publisher	American Physiological Society
Publisher Date	2009-03-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Discipline Physiology Physiology Matrix Metalloproteinases Metabolism Muscle, Skeletal Enzymology Physical Endurance Gene Expression Genetics Rna, Messenger Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Physiology Physiology (medical) Sports Science

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