Abstract
Collagen is the predominant structural protein in mammals and is most abundant in stiff, solid tissues that sustain mechanical stress. Some studies have suggested tension can stabilize fibers against degradation independent of cell activity. Here, strain gradients were generated in isolated tendon fascicle using three-point bending, with patterned photo-bleaching of fluorescent tendon used to measure strain. Deformed fascicle was exposed to collagenase, and degradation was tracked using Second Harmonic Generation (SHG) signal produced by fibrillar collagen. Importantly, mechanical strains up to 5∼8% magnitude maximize collagen fibril lifetime when exposed to collagenase. Fluorescent dextran permeation of the tendon further showed relatively uniform density, while Fluorescence Recovery after Photobleaching (FRAP) revealed strain dependent increase in mobility. Applied mechanical strain preserves collagen fibrils in tissue in the presence of collagenase. Our results have the potential to deepen the understanding of collagen matrices in development, adaptation, and disease.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
