Interstitial Collagen Catabolism
Open accessAbstract
Interstitial collagen mechanical and biological properties are altered by proteases that catalyze the hydrolysis of the collagen triple-helical structure. Collagenolysis is critical in development and homeostasis but also contributes to numerous pathologies. Mammalian collagenolytic enzymes include matrix metalloproteinases, cathepsin K, and neutrophil elastase, and a variety of invertebrates and pathogens possess collagenolytic enzymes. Components of the mechanism of action for the collagenolytic enzyme MMP-1 have been defined experimentally, and insights into other collagenolytic mechanisms have been provided. Ancillary biomolecules may modulate the action of collagenolytic enzymes.
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At the bone remodeling site, BLCs disconnect from the underlying osteocytes through gap junction disruption, and digest fibrillary collagen, the most abundant component in the bone extracellular matrix (ECM), which is tightly packed in a helical structure to provide mechanical stability and confer resistance against proteolysis.
“At the bone remodeling site, BLCs disconnect from the underlying osteocytes through gap junction disruption, and digest fibrillary collagen, the most abundant component in the bone extracellular matrix (ECM), which is tightly packed in a helical structure to provide mechanical stability and confer resistance against proteolysis.118”
From Bone remodeling: an operational process ensuring survival and bone mechanical competence (2022) · cites this paper as [118]
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Remodeling of imbalanced extracellular matrix homeostasis for reversal of pancreatic fibrosis
Qi, L., Han, H., Han, M.-M., Sun, Y., Xing, L., Jiang, H.-L., Pandol, S. J., & Li, L. (2023) · Biomaterials · doi:10.1016/j.biomaterials.2022.121945 · Cited by 36 · see citing works
- Authors
- Fields, G. B.
- Affiliations
- Torrey Pines Institute For Molecular Studies (US)
- Corresponding author
- Fields, Gregg B.
- ORCID
- Fields, Gregg B.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2013-03
- Volume
- 288
- Issue
- 13
- Pages
- 8785-8793
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC3610953
- OpenAlex
- W2037060384
- Cited by
- 205
- References
- 100
- Citations by year
- 2026: 9 · 2025: 11 · 2024: 17 · 2023: 12 · 2022: 19 · 2021: 20 · 2020: 12 · 2019: 20 · 2018: 15 · 2017: 14 · 2016: 17 · 2015: 18 · 2014: 16 · 2013: 5
- FWCI
- 1.55
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- U.S. Public Health Service (268201000036C)
- National Institute of Mental Health (MH78948)
- National Cancer Institute (CA 98799, R01CA098799)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Physical Sciences › Materials Science › Biomaterials › Collagen: Extraction and Characterization
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › TGF-β signaling in diseases
- Keywords
- interstitial collagen, collagen catabolism, collagen degradation, collagenolytic enzymes, matrix metalloproteinases, MMP-1, cathepsin K, neutrophil elastase, collagen triple helix, enzyme mechanism of action, extracellular matrix homeostasis
- MeSH terms
- Animals, Arthritis, Binding Sites, Catalysis, Collagen, Humans, Metabolism, Molecular Conformation, Neoplasms, Protein Binding, Serine, Substrate Specificity, Gene Expression Regulation, Enzymologic, Protein Structure, Tertiary, Leukocyte Elastase, Matrix Metalloproteinase 1, Matrix Metalloproteinases, Cathepsin K
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