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Orthopaedic Proceedings
Vol. 91-B, Issue SUPP_III | Pages 450 - 450
1 Sep 2009
Pasternak B Schepull T Aspenberg P
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Local dysregulation of the proteolytic matrix metalloproteinases (MMPs) and their tissue inhibitors of metalloproteinases (TIMPs) is a feature of tendon degeneration and rupture.1,2 To assess the role of systemic MMPs and TIMPs in tendon rupture we compared serum MMPs and TIMPs between patients who have previously suffered Achilles tendon rupture and healthy controls. We also followed serum MMPs and TIMPs prospectively in patients with acute tendon rupture.

At three years after injury, we measured serum MMP-1, -2, -3, -7, -8, -9 and -13 and TIMP-1 and -2 in eight patients who had suffered Achilles tendon rupture. Serum was also obtained from 12 blood donors with similar age and sex distribution. In another eight patients, MMPs and TIMPs were followed over time, with samples taken at the time of Achilles tendon injury, and after 4, 8 and 24 weeks. MMPs were determined using Fluorokine Multi Analyte Profiling kits while TIMPs were analysed using ELISA (R& D systems). The study was approved by the ethics committee and written informed consent was obtained from all patients.

Patients who had previously suffered tendon rupture had increased levels of MMP-2 (median difference (m.d.) 10 %; p = 0.01), MMP-7 (m.d. 15 %; p = 0.02) and TIMP-2 (m.d. 36%; p = 0.02), as compared to controls. In patients with acute tendon rupture, MMP-2 was the only MMP or TIMP to change significantly over time (p = 0.009). MMP-7 appeared to be higher than control values already at the time of rupture. MMP-13 could not be detected in any sample.

In conclusion, patients with a history of tendon rupture had elevated serum levels of MMP-2, MMP-7 and TIMP-2. Changes in MMP-7 might be present already at the time of rupture. This suggests that disturbances in proteolytic control might render tendons prone to rupture.