Tension in fibrils suppresses their enzymatic degradation - A molecular mechanism for 'use it or lose it'
| Autor: | Sangkyun Cho, Lawrence J. Dooling, Karanvir Saini, Dennis E. Discher |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
0301 basic medicine
Strain (chemistry) Chemistry Fibrillar Collagens Substrate (chemistry) Proteomics Fibril Article Extracellular Matrix Extracellular matrix 03 medical and health sciences 030104 developmental biology 0302 clinical medicine 030220 oncology & carcinogenesis Collagenase medicine Biophysics Humans Mechanosensitive channels Collagenases Stress Mechanical Molecular Biology Tissue homeostasis medicine.drug |
| Zdroj: | Matrix Biol |
| ISSN: | 1569-1802 |
| Popis: | Tissue homeostasis depends on a balance of synthesis and degradation of constituent proteins, with turnover of a given protein potentially regulated by its use. Extracellular matrix (ECM) is predominantly composed of fibrillar collagens that exhibit tension-sensitive degradation, which we review here at different levels of hierarchy. Past experiments and recent proteomics measurements together suggest that mechanical strain stabilizes collagen against enzymatic degradation at the scale of tissues and fibrils whereas isolated collagen molecules exhibit a biphasic behavior that depends on load magnitude. Within a Michaelis-Menten framework, collagenases at constant concentration effectively exhibit a low activity on substrate fibrils when the fibrils are strained by tension. Mechanisms of such mechanosensitive regulation are surveyed together with relevant interactions of collagen fibrils with cells. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect