Effects of long-term immobilization and recovery on human triceps surae and collagen turnover in the Achilles tendon in patients with healing ankle fracture

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Britt Christensen, Eva Dyrberg, Per Aagaard, Susanne Enehjelm, Michael Krogsgaard, Michael Kjaer, Henning Langberg

The aim of the present study was to analyze how human tendon connective tissue responds to an approximately 7-wk period of immobilization and a remobilization period of a similar length, in patients with unilateral ankle fracture, which is currently unknown. Calf muscle cross-sectional area (CSA) decreased by 15% (5,316 to 4,517 mm2) and strength by 54% (239 to 110 N.m) in the immobilized leg after 7 wk. During the 7-wk remobilization, the CSA increased by 9% (to 4,943 mm2) and strength by 37% (to 176 Nm). Achilles tendon CSA did not change significantly during either immobilization or remobilization. Local collagen turnover was measured as the peritendinous concentrations of NH2-terminal propeptide of type I collagen (PINP) and COOH-terminal telopeptide region of type I collagen (ICTP), markers thought to be indexes of type I collagen synthesis and degradation, respectively. Both markers were increased (PINP: 257 vs. 56 ng/ml; ICTP: 9.8 vs. 2.1 microg/l) in the immobilized leg compared with the control leg after the 7 wk of immobilization, and levels decreased again in the immobilized leg during the recovery period (PINP: 103 vs. 44 ng/ml; ICTP: 4.2 vs. 1.9 microg/l). A significant reduction in calf muscle CSA and strength was found in relation to 7 wk of immobilization. Immobilization increased both collagen synthesis and degradation in tendon near tissue. However, it cannot be excluded that the facture of the ankle in close proximity could have affected these data. Remobilization increased muscle size and strength and tendon synthesis and degradation decreased to baseline levels. These dynamic changes in tendon connective tissue turnover were not associated with macroscopic changes in tendon size.
OriginalsprogEngelsk
TidsskriftJournal of Applied Physiology
Vol/bind105
Udgave nummer2
Sider (fra-til)420-426
Antal sider7
ISSN8750-7587
DOI
StatusUdgivet - 2008

Bibliografisk note

IS - 8750-7587 (Print)LA - engPT - Journal ArticleRN - 0 (Biological Markers)RN - 0 (Collagen Type I)RN - 0 (Peptide Fragments)RN - 0 (Procollagen)RN - 0 (procollagen Type I N-terminal peptide)SB - IM

ID: 10454728