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1 Sports Medicine Research Unit, Bispebjerg Hospital, Copenhagen, Denmark
* To whom correspondence should be addressed. E-mail: sk04{at}bbh.hosp.dk.
Microdialysis studies indicate that mechanical loading of human tendon tissue during exercise/training can affect local synthesis and degradation of type I collagen. Degradation of collagen and other extracellular matrix proteins is controlled by an interplay between matrix metalloproteinases (MMPs) and their inhibitors (TIMPs). However, it is unknown whether local levels of MMPs and TIMPs are affected by tendon loading in humans in vivo. In the present experiment, six healthy young males performed 1 hour of uphill (3%) treadmill running. Dialysate was collected from microdialysis probes (placed in the peritendinous tissue immediately anterior to the Achilles tendon) before, immediately after, 1 day and 3 days after the exercise bout. MMP-2 and MMP-9 were measured in dialysate by gelatin zymography and amounts were quantified by densitometry in relation to total protein content in the dialysate. TIMP-1 and TIMP-2 were analyzed by reverse gelatine zymography and semi-quantitated visually. ProMMP-9 increased markedly after exercise and remained high for 3 days post exercise. ProMMP-2 dropped from the basal level immediately after exercise and remained low on day 1, but was slightly elevated at day 3. The MMP-2 inhibitory activity of TIMP-1 was clearly elevated 1 and 3 days post exercise and the MMP-2 inhibitory activity of TIMP-2 rose on day 1 after loading. The present findings demonstrate enhanced interstitial amounts of MMPs and TIMPs after exercise in the human peritendinous tissue in vivo, and the magnitude and time pattern of these changes may well indicate that matrix metalloproteinases and their inhibitors are playing a role in extracellular matrix adaptation to exercise in tendon tissue.
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