Resumen
The mechanical properties of tendon are due to the properties and arrangement of its collagen fibril content. Collagen fibrils are highly-organized supermolecular structures with a periodic banding pattern (D-band) indicative of the geometry of molecular organization. Following mechanical overload of whole tendon, collagen fibrils may plastically deform at discrete sites along their length, forming kinks, and acquiring a fuzzy, non-D-banded, outer layer (shell). Termed discrete plasticity, such non-uniform damage to collagen fibrils suggests localized cellular response at the fibril level during subsequent repair/replacement. Matrix metallo-proteinases (MMPs) are enzymes which act upon the extracellular matrix, facilitating cell mobility and playing important roles in wound healing. A sub-group within this family are the gelatinases, MMP-2 and MMP-9, which selectively cleave denatured collagen molecules. Of these two, MMP-9 is specifically upregulated during the initial stages of tendon repair. This suggests a singular function in damage debridement. Using atomic force microscopy (AFM), a novel fibril-level enzymatic assay was employed to assess enzymatic removal of material by trypsin and MMP-9 from individual fibrils which were: (i) untreated, (ii) partially heat denatured, (iii) or displaying discrete plasticity damaged after repeated mechanical overload. Both enzymes removed material from heat denatured and discrete plasticity-damaged fibrils; however, only MMP-9 demonstrated the selective removal of non-D-banded material, with greater removal from more damaged fibrils. The selectivity of MMP-9, coupled with documented upregulation, suggests a likely mechanism for the in vivo debridement of individual collagen fibrils, following tendon overload injury, and prior to deposition of new collagen.
Idioma original | English |
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Páginas (desde-hasta) | 67-75 |
Número de páginas | 9 |
Publicación | Journal of the Mechanical Behavior of Biomedical Materials |
Volumen | 95 |
DOI | |
Estado | Published - jul. 2019 |
Nota bibliográfica
Funding Information:A Canadian Institutes of Health Research grant awarded to LK and JML (grant MOP-133453 ) and a Discovery Grant awarded to LK (grant RGPIN03781 ) from the Natural Sciences and Engineering Research Council of Canada supported this work. SB is a recipient of the PhD scholarship Collaborative Research and Training Experience (CREATE) in Applied Science in Photonics and Innovative Research in Engineering ( ASPIRE ).
Funding Information:
A Canadian Institutes of Health Research grant awarded to LK and JML (grant MOP-133453) and a Discovery Grant awarded to LK (grant RGPIN03781) from the Natural Sciences and Engineering Research Council of Canada supported this work. SB is a recipient of the PhD scholarship Collaborative Research and Training Experience (CREATE) in Applied Science in Photonics and Innovative Research in Engineering (ASPIRE). The authors would like to thank Reid's Meats (Wolfville, Nova Scotia), the abattoir which provided bovine tendon samples.
Publisher Copyright:
© 2019 Elsevier Ltd
ASJC Scopus Subject Areas
- Biomaterials
- Biomedical Engineering
- Mechanics of Materials
PubMed: MeSH publication types
- Journal Article
- Research Support, Non-U.S. Gov't