Matrix metabolism rate differs in functionally distinct tendons.
Tendon matrix integrity is vital to ensure adequate mechanical properties for efficient function. Although historically tendon was considered to be relatively inert, recent studies have shown that tendon matrix turnover is active. During normal physiological activities some tendons are subjected to stress and strains much closer to their failure properties than others. Tendons with low safety margins are those which function as energy stores such as the equine superficial digital flexor tendon (SDFT) and human Achilles tendon (AT). We postulate therefore that energy storing tendons suffer a higher degree of micro-damage and thus have a higher rate of matrix turnover than positional tendons. The hypothesis was tested using tissue from the equine SDFT and common digital extensor tendon (CDET). Matrix turnover was assessed indirectly by a combination of measurements for matrix age, markers of degradation, potential for degradation and protein expression. Results show that despite higher cellularity, the SDFT has lower relative levels of mRNA for collagen types I and III. Non-collagenous proteins, although expressed at different levels per cell, do not appear to differ between tendon types. Relative levels of mRNA for MMP1, MMP13 and both pro-MMP3 and MMP13 protein activity were significantly higher in the CDET. Correspondingly levels of cross-linked carboxyterminal telopeptide of type I collagen (ICTP) were higher in the CDET and tissue fluorescence lower suggesting more rapid turnover of the collagenous component. Reduced or inhibited collagen turnover in the SDFT may account for the high level of degeneration and subsequent injury compared to the CDET.
Birch
Helen L
HL
Institute of Orthopaedics and Musculoskeletal Science, University College London, Stanmore Campus, Royal National Orthopaedic Hospital, Brockley Hill, Stanmore, HA7 4LP, UK. h.birch@ucl.ac.uk
Worboys
Sarah
S
Eissa
Sabry
S
Jackson
Brendan
B
Strassburg
Sandra
S
Clegg
Peter D
PD
D000125:Achilles Tendon / Q000473:pathology*; D000818:Animals; D003094:Collagen / Q000737:chemistry; D024042:Collagen Type I / Q000737:chemistry*; D003432:Cross-Linking Reagents / Q000494:pharmacology; D004247:DNA / Q000378:metabolism; D005109:Extracellular Matrix / Q000378:metabolism*; D015971:Gene Expression Regulation, Enzymologic; D006736:Horses; D006801:Humans; D020782:Matrix Metalloproteinases / Q000378:metabolism*; D008954:Models, Biological; D012333:RNA, Messenger / Q000378:metabolism; D013710:Tendons / Q000473:pathology*
D024042:Collagen Type I; D003432:Cross-Linking Reagents; D012333:RNA, Messenger; D003094:Collagen; D004247:DNA; D020782:Matrix Metalloproteinases