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J Physiol Volume 567, Number 3, 1021-1033, September 15, 2005 DOI: 10.1113/jphysiol.2005.093690
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Coordinated collagen and muscle protein synthesis in human patella tendon and quadriceps muscle after exercise

Benjamin F Miller1, Jens L Olesen1, Mette Hansen1, Simon Døssing1, Regina M Crameri1, Rasmus J Welling1, Henning Langberg1, Allan Flyvbjerg2, Michael Kjaer1, John A Babraj3, Kenneth Smith3,4 and Michael J Rennie3,4

1 Institute of Sports Medicine, Copenhagen, Bispebjerg Hospital, 2400 Copenhagen NV, Denmark
2 Department of Diabetes and Endocrinology and the Medical Research Laboratories, Aarhus University Hospital, 8000 Aarhus, Denmark
3 Division of Molecular Physiology, Faculty of Life Sciences, University of Dundee, Dundee DD1 4HN, Scotland, UK
4 University of Nottingham, Graduate Medical School, Derby City General Hospital, Derby, DE22 3DT, UK

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 (Wmax). To label tissue proteins in muscle and tendon primed, constant infusions of [1-13C]leucine or [1-13C]valine and flooding doses of [15N] or [13C]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.

(Received 27 June 2005; accepted after revision 5 July 2005; first published online 7 July 2005)
Corresponding author M. Kjaer: Institute of Sports Medicine, Copenhagen, Bispebjerg Hospital, 2400 Copenhagen NV, Denmark. Email: m.kjaer{at}mfi.ku.dk




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