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In tendons, differing physiological requirements lead to distinct patterns of MMP-1 degradation.
Kelsey Y Gsell1, Laurent Kreplak1,2, Samuel P Veres3,4
1School of Biomedical Engineering, Dalhousie University, Halifax, NS, Canada.
Scientific Reports
|December 23, 2025
Summary
Energy-storing tendons have collagen fibrils more resistant to degradation by MMP-1, unlike positional tendons. This resistance, linked to fibril size and crosslinking, impacts tendon remodeling and injury risk.
Area of Science:
- Biomaterials Science
- Connective Tissue Biology
- Musculoskeletal Biomechanics
Background:
- Tendon collagen fibril diameter and crosslinking vary between high-stress (energy-storing) and low-stress (positional) tendons.
- Energy-storing tendons exhibit reduced remodeling and higher injury rates, potentially due to lower collagen turnover.
- Matrix metalloproteinase-1 (MMP-1) resistance has been proposed as a factor in reduced collagen turnover in energy-storing tendons.
Purpose of the Study:
- To validate and expand upon previous findings regarding MMP-1 resistance in single collagen fibrils.
- To conduct a population-level assessment of MMP-1 degradation across different tendon types.
- To develop predictive models for fibril diameter changes during degradation.
Main Methods:
- Incubation of positional and energy-storing tendon sections with buffer or MMP-1 for 24 hours.
- Scanning electron microscopy (SEM) for imaging fibril morphology.
- Custom image analysis pipeline for quantitative measurement of fibril diameter, alignment, curvature, and D-band length.
Main Results:
- MMP-1 treatment led to reduced fibril diameter, alignment, D-band length, and increased curvature in both tendon types.
- Energy-storing tendon fibrils showed significantly greater resistance to MMP-1 degradation (15% diameter reduction) compared to positional tendon fibrils (41% diameter reduction).
- Degradation exhibited a linear relationship with fibril size, with larger fibrils experiencing more pronounced diameter reduction and variation, suggesting higher core crosslinking.
Conclusions:
- Collagen fibrils in energy-storing tendons are inherently more resistant to MMP-1-mediated degradation than those in positional tendons.
- Fibril size and increased crosslinking density, particularly in the core, contribute to this resistance and influence degradation patterns.
- These findings provide insights into the distinct mechanical properties, remodeling capacities, and injury susceptibility of different tendon types.
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