Coordinated collagen and muscle protein synthesis in human patella tendon and quadriceps muscle after exercise
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Coordinated collagen and muscle protein synthesis in human patella tendon and quadriceps muscle after exercise. / Miller, Benjamin F; Olesen, Jens L; Hansen, Mette; Døssing, Simon; Crameri, Regina M; Welling, Rasmus J; Langberg, Henning; Flyvbjerg, Allan; Kjaer, Michael; Babraj, John A; Smith, Kenneth; Rennie, Michael J.
I: Journal of Physiology, Bind 567, Nr. Pt 3, 2005, s. 1021-33.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - Coordinated collagen and muscle protein synthesis in human patella tendon and quadriceps muscle after exercise
AU - Miller, Benjamin F
AU - Olesen, Jens L
AU - Hansen, Mette
AU - Døssing, Simon
AU - Crameri, Regina M
AU - Welling, Rasmus J
AU - Langberg, Henning
AU - Flyvbjerg, Allan
AU - Kjaer, Michael
AU - Babraj, John A
AU - Smith, Kenneth
AU - Rennie, Michael J
PY - 2005
Y1 - 2005
N2 - We hypothesized that an acute bout of strenuous, non-damaging exercise would increase rates of protein synthesis of collagen in tendon and skeletal muscle but these would be less than those of muscle myofibrillar and sarcoplasmic proteins. Two groups (n = 8 and 6) of healthy young men were studied over 72 h after 1 h of one-legged kicking exercise at 67% of maximum workload (W(max)). To label tissue proteins in muscle and tendon primed, constant infusions of [1-(13)C]leucine or [1-(13)C]valine and flooding doses of [(15)N] or [(13)C]proline were given intravenously, with estimation of labelling in target proteins by gas chromatography-mass spectrometry. Patellar tendon and quadriceps biopsies were taken in exercised and rested legs at 6, 24, 42 or 48 and 72 h after exercise. The fractional synthetic rates of all proteins were elevated at 6 h and rose rapidly to peak at 24 h post exercise (tendon collagen (0.077% h(-1)), muscle collagen (0.054% h(-1)), myofibrillar protein (0.121% h(-1)), and sarcoplasmic protein (0.134% h(-1))). The rates decreased toward basal values by 72 h although rates of tendon collagen and myofibrillar protein synthesis remained elevated. There was no tissue damage of muscle visible on histological evaluation. Neither tissue microdialysate nor serum concentrations of IGF-I and IGF binding proteins (IGFBP-3 and IGFBP-4) or procollagen type I N-terminal propeptide changed from resting values. Thus, there is a rapid increase in collagen synthesis after strenuous exercise in human tendon and muscle. The similar time course of changes of protein synthetic rates in different cell types supports the idea of coordinated musculotendinous adaptation.
AB - We hypothesized that an acute bout of strenuous, non-damaging exercise would increase rates of protein synthesis of collagen in tendon and skeletal muscle but these would be less than those of muscle myofibrillar and sarcoplasmic proteins. Two groups (n = 8 and 6) of healthy young men were studied over 72 h after 1 h of one-legged kicking exercise at 67% of maximum workload (W(max)). To label tissue proteins in muscle and tendon primed, constant infusions of [1-(13)C]leucine or [1-(13)C]valine and flooding doses of [(15)N] or [(13)C]proline were given intravenously, with estimation of labelling in target proteins by gas chromatography-mass spectrometry. Patellar tendon and quadriceps biopsies were taken in exercised and rested legs at 6, 24, 42 or 48 and 72 h after exercise. The fractional synthetic rates of all proteins were elevated at 6 h and rose rapidly to peak at 24 h post exercise (tendon collagen (0.077% h(-1)), muscle collagen (0.054% h(-1)), myofibrillar protein (0.121% h(-1)), and sarcoplasmic protein (0.134% h(-1))). The rates decreased toward basal values by 72 h although rates of tendon collagen and myofibrillar protein synthesis remained elevated. There was no tissue damage of muscle visible on histological evaluation. Neither tissue microdialysate nor serum concentrations of IGF-I and IGF binding proteins (IGFBP-3 and IGFBP-4) or procollagen type I N-terminal propeptide changed from resting values. Thus, there is a rapid increase in collagen synthesis after strenuous exercise in human tendon and muscle. The similar time course of changes of protein synthetic rates in different cell types supports the idea of coordinated musculotendinous adaptation.
KW - Adult
KW - Carbon Radioisotopes
KW - Collagen
KW - Exercise
KW - Humans
KW - Keto Acids
KW - Leucine
KW - Male
KW - Muscle Proteins
KW - Muscle, Skeletal
KW - Myofibrils
KW - Nitrogen Radioisotopes
KW - Patella
KW - Proline
KW - Sarcoplasmic Reticulum
KW - Tendons
KW - Thigh
KW - Valine
U2 - 10.1113/jphysiol.2005.093690
DO - 10.1113/jphysiol.2005.093690
M3 - Journal article
C2 - 16002437
VL - 567
SP - 1021
EP - 1033
JO - The Journal of Physiology
JF - The Journal of Physiology
SN - 0022-3751
IS - Pt 3
ER -
ID: 38366742