Metabolic activity and collagen turnover in human tendon in response to physical activity

TY - JOUR

T1 - Metabolic activity and collagen turnover in human tendon in response to physical activity

AU - Kjaer, M

AU - Langberg, H

AU - Miller, B F

AU - Boushel, Robert Christopher

AU - Crameri, R

AU - Koskinen, S

AU - Heinemeier, K

AU - Olesen, J L

AU - Døssing, S

AU - Hansen, M

AU - Pedersen, S G

AU - Rennie, M J

AU - Magnusson, P

PY - 2005/3/1

Y1 - 2005/3/1

N2 - Connective tissue of the human tendon plays an important role in force transmission. The extracellular matrix turnover of tendon is influenced by physical activity. Blood flow, oxygen demand, and the level of collagen synthesis and matrix metalloproteinases increase with mechanical loading. Gene transcription and especially post-translational modifications of proteins of the extracellular matrix are enhanced following exercise. Conversely, inactivity markedly decreases collagen turnover. Training leads to a chronically increased collagen turnover, and dependent on the type of collagen also to some degree of net collagen synthesis. These changes modify the biomechanical properties of the tissue (for example, viscoelastic characteristics) as well as the structural properties of the in collagen (for example, cross-sectional area). Mechanical loading of human tendon does result in a marked interstitial increase in growth factors that are known potentially to stimulate synthesis of collagen and other extracellular matrix proteins. Taken together, human tendon tissue mounts a vigorous acute and chronic response to mechanical loading in terms of metabolic-circulatory changes as well as of extracellular matrix formation. These changes may contribute to training-induced adaptation of biomechanical properties consisting of altered resistance to loading and enhanced tolerance to strenuous exercise. Understanding of such changes is a pre-requisite in the development of measures aimed at prevention of overuse tendon injuries occurring during sport, work or leisure-related activities.

AB - Connective tissue of the human tendon plays an important role in force transmission. The extracellular matrix turnover of tendon is influenced by physical activity. Blood flow, oxygen demand, and the level of collagen synthesis and matrix metalloproteinases increase with mechanical loading. Gene transcription and especially post-translational modifications of proteins of the extracellular matrix are enhanced following exercise. Conversely, inactivity markedly decreases collagen turnover. Training leads to a chronically increased collagen turnover, and dependent on the type of collagen also to some degree of net collagen synthesis. These changes modify the biomechanical properties of the tissue (for example, viscoelastic characteristics) as well as the structural properties of the in collagen (for example, cross-sectional area). Mechanical loading of human tendon does result in a marked interstitial increase in growth factors that are known potentially to stimulate synthesis of collagen and other extracellular matrix proteins. Taken together, human tendon tissue mounts a vigorous acute and chronic response to mechanical loading in terms of metabolic-circulatory changes as well as of extracellular matrix formation. These changes may contribute to training-induced adaptation of biomechanical properties consisting of altered resistance to loading and enhanced tolerance to strenuous exercise. Understanding of such changes is a pre-requisite in the development of measures aimed at prevention of overuse tendon injuries occurring during sport, work or leisure-related activities.

KW - Adaptation, Physiological

KW - Collagen

KW - Energy Metabolism

KW - Extracellular Matrix Proteins

KW - Humans

KW - Movement

KW - Physical Fitness

KW - Stress, Mechanical

KW - Tendons

KW - Weight-Bearing

M3 - Journal article

C2 - 15788870

SN - 1108-7161

VL - 5

SP - 41

EP - 52

JO - Journal of Musculoskeletal and Neuronal Interactions

JF - Journal of Musculoskeletal and Neuronal Interactions

IS - 1

ER -