Cited by 205Protease and Inhibitor MechanismsCollagen: Extraction and CharacterizationTGF-β signaling in diseases

Interstitial Collagen Catabolism

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Fields, Gregg B.·2013·Journal of Biological Chemistry

Abstract

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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Crossref · 10.1074/jbc.r113.451211

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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”

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  1. [10]10. Amar, S., Fields, G. B., (2012) Production and characterization of matrix metalloproteinases implicated in multiple sclerosis. in Peptides 2012: Proceedings of the Thirty-Second European Peptide Symposium (Kokotos, G., Constantinou-Kokotou, V., Matsoukas, J., eds) pp. 102–103, European Peptide Society, Athens, Greece Google Scholar

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Authors
Fields, G. B.
Affiliations
Torrey Pines Institute For Molecular Studies (US)
Corresponding author
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)
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
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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