Physical exercise can influence local levels of matrix metalloproteinases and their inhibitors in tendon-related connective tissue

Research output: Contribution to journalJournal articleResearchpeer-review

Standard

Physical exercise can influence local levels of matrix metalloproteinases and their inhibitors in tendon-related connective tissue. / Koskinen, S O A; Heinemeier, K M; Olesen, J L; Langberg, Henning; Kjaer, M.

In: Journal of Applied Physiology, Vol. 96, No. 3, 2004, p. 861-4.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Koskinen, SOA, Heinemeier, KM, Olesen, JL, Langberg, H & Kjaer, M 2004, 'Physical exercise can influence local levels of matrix metalloproteinases and their inhibitors in tendon-related connective tissue', Journal of Applied Physiology, vol. 96, no. 3, pp. 861-4. https://doi.org/10.1152/japplphysiol.00489.2003

APA

Koskinen, S. O. A., Heinemeier, K. M., Olesen, J. L., Langberg, H., & Kjaer, M. (2004). Physical exercise can influence local levels of matrix metalloproteinases and their inhibitors in tendon-related connective tissue. Journal of Applied Physiology, 96(3), 861-4. https://doi.org/10.1152/japplphysiol.00489.2003

Vancouver

Koskinen SOA, Heinemeier KM, Olesen JL, Langberg H, Kjaer M. Physical exercise can influence local levels of matrix metalloproteinases and their inhibitors in tendon-related connective tissue. Journal of Applied Physiology. 2004;96(3):861-4. https://doi.org/10.1152/japplphysiol.00489.2003

Author

Koskinen, S O A ; Heinemeier, K M ; Olesen, J L ; Langberg, Henning ; Kjaer, M. / Physical exercise can influence local levels of matrix metalloproteinases and their inhibitors in tendon-related connective tissue. In: Journal of Applied Physiology. 2004 ; Vol. 96, No. 3. pp. 861-4.

Bibtex

@article{f2bd95724502463e99360bc1398f4601,
title = "Physical exercise can influence local levels of matrix metalloproteinases and their inhibitors in tendon-related connective tissue",
abstract = "Microdialysis studies indicate that mechanical loading of human tendon tissue during exercise or 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 tissue 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 men performed 1 h 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 after, and 3 days after an 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 in the dialysate. TIMP-1 and TIMP-2 were analyzed by reverse gelatin zymography and semiquantitated visually. Pro-MMP-9 increased markedly after exercise and remained high for 3 days after exercise. Pro-MMP-2 dropped from the basal level immediately after exercise and remained low 1 day after exercise but was slightly elevated 3 days after exercise. The MMP-2 inhibitory activity of TIMP-1 was clearly elevated 1 and 3 days after exercise, and the MMP-2 inhibitory activity of TIMP-2 rose 1 day 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 MMPs and TIMPs are playing a role in extracellular matrix adaptation to exercise in tendon tissue.",
keywords = "Achilles Tendon, Adult, Exercise Test, Humans, Male, Matrix Metalloproteinases, Physical Exertion, Statistics, Nonparametric, Tissue Inhibitor of Metalloproteinases",
author = "Koskinen, {S O A} and Heinemeier, {K M} and Olesen, {J L} and Henning Langberg and M Kjaer",
year = "2004",
doi = "10.1152/japplphysiol.00489.2003",
language = "English",
volume = "96",
pages = "861--4",
journal = "Journal of Applied Physiology",
issn = "8750-7587",
publisher = "American Physiological Society",
number = "3",

}

RIS

TY - JOUR

T1 - Physical exercise can influence local levels of matrix metalloproteinases and their inhibitors in tendon-related connective tissue

AU - Koskinen, S O A

AU - Heinemeier, K M

AU - Olesen, J L

AU - Langberg, Henning

AU - Kjaer, M

PY - 2004

Y1 - 2004

N2 - Microdialysis studies indicate that mechanical loading of human tendon tissue during exercise or 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 tissue 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 men performed 1 h 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 after, and 3 days after an 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 in the dialysate. TIMP-1 and TIMP-2 were analyzed by reverse gelatin zymography and semiquantitated visually. Pro-MMP-9 increased markedly after exercise and remained high for 3 days after exercise. Pro-MMP-2 dropped from the basal level immediately after exercise and remained low 1 day after exercise but was slightly elevated 3 days after exercise. The MMP-2 inhibitory activity of TIMP-1 was clearly elevated 1 and 3 days after exercise, and the MMP-2 inhibitory activity of TIMP-2 rose 1 day 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 MMPs and TIMPs are playing a role in extracellular matrix adaptation to exercise in tendon tissue.

AB - Microdialysis studies indicate that mechanical loading of human tendon tissue during exercise or 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 tissue 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 men performed 1 h 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 after, and 3 days after an 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 in the dialysate. TIMP-1 and TIMP-2 were analyzed by reverse gelatin zymography and semiquantitated visually. Pro-MMP-9 increased markedly after exercise and remained high for 3 days after exercise. Pro-MMP-2 dropped from the basal level immediately after exercise and remained low 1 day after exercise but was slightly elevated 3 days after exercise. The MMP-2 inhibitory activity of TIMP-1 was clearly elevated 1 and 3 days after exercise, and the MMP-2 inhibitory activity of TIMP-2 rose 1 day 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 MMPs and TIMPs are playing a role in extracellular matrix adaptation to exercise in tendon tissue.

KW - Achilles Tendon

KW - Adult

KW - Exercise Test

KW - Humans

KW - Male

KW - Matrix Metalloproteinases

KW - Physical Exertion

KW - Statistics, Nonparametric

KW - Tissue Inhibitor of Metalloproteinases

U2 - 10.1152/japplphysiol.00489.2003

DO - 10.1152/japplphysiol.00489.2003

M3 - Journal article

C2 - 14506093

VL - 96

SP - 861

EP - 864

JO - Journal of Applied Physiology

JF - Journal of Applied Physiology

SN - 8750-7587

IS - 3

ER -

ID: 38367371