The DOI matches its Crossref record; 51 of the 51 references it cites were found in a registry or an index.
The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family.
Open accessAbstract
The general applicability of the "cysteine-switch" activation mechanism to the members of the matrix metalloproteinase (MMP) gene family is examined here. All currently known members of the MMP gene family share the characteristic that they are synthesized in a latent, inactive, form. Recent evidence suggests that this latency in human fibroblast collagenase (HFC) is the result of formation of an intramolecular complex between the single cysteine residue in its propeptide domain and the essential zinc atom in the catalytic domain, a complex that blocks the active site. Latent HFC can be activated by multiple means, all of which effect the dissociation of the cysteine residue from the complex. This is referred to as the "cysteine-switch" mechanism of activation. The propeptide domain that contains the critical cysteine residue and the catalytic domain that contains the zinc-binding site are the only two domains common to all of the MMPs. The amino acid sequences surrounding both the critical cysteine residue and a region of the protein chains containing two of the putative histidine zinc-binding ligands are highly conserved in all of the MMPs. A survey of the literature shows that many of the individual MMPs can be activated by the multiple means observed for latent HFC. These observations support the view that the cysteine-switch mechanism is applicable to all members of this gene family. This mechanism is unprecedented in enzymology as far as we know and offers the opportunity for multiple modes of physiological activation of these important enzymes. Since conditions in different cells and tissues may match those necessary to effect one of these activation modes for a given MMP, this may offer metabolic flexibility in the control of MMP activation.
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“The ADAM (A Disintegrin And Metalloprotease) and ADAMTS families of metalloproteases are encoded by over 40 human genes, mediate cell-cell and cell-matrix interactions (20, 21) and are involved in a range of human diseases, including cancer metastasis, inflammatory disorders, neurological diseases and asthma (21, 22).”
From Accurate prediction of protein structures and interactions using a 3-track network (2021) · cites this paper as [21]
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Identification of nitroglycerin-induced cysteine modifications of pro-matrix metalloproteinase-9
Krishnatry, A. S., Kamei, T., Wang, H., Qu, J., & Fung, H. (2011) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.5118 · Cited by 9
Metadata
- Authors
- Van Wart, H. E., & Birkedal-Hansen, H.
- Affiliations
- Department of Chemistry, Florida State University, Tallahassee 32306-3015.
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1990-07
- Volume
- 87
- Issue
- 14
- Pages
- 5578-5582
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC54368
- OpenAlex
- W2167709602
- Cited by
- 1,475
- References
- 51
- Citations by year
- 2026: 23 · 2025: 28 · 2024: 38 · 2023: 28 · 2022: 34 · 2021: 31 · 2020: 30 · 2019: 28 · 2018: 40 · 2017: 48 · 2016: 33 · 2015: 47 · 2014: 60 · 2013: 45 · 2012: 61
- FWCI
- 14.57
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01de006028-07, 5r01de009122-05, 5r01gm027939-15)
- National Institute of General Medical Sciences (GM-27939)
- National Institute of Dental and Craniofacial Research (DE06028, DE09122)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Health Sciences › Medicine › Hematology › Blood Coagulation and Thrombosis Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Peptidase Inhibition and Analysis
- Keywords
- matrix metalloproteinases, enzyme activation, latent collagenase, zinc binding site, conserved amino acid sequence
- MeSH terms
- Amino Acid Sequence, Animals, Microbial Collagenase, Cysteine, Multigene Family, Humans, Metalloendopeptidases, Molecular Sequence Data, Protein Binding, Rabbits, Sequence Homology, Nucleic Acid, Species Specificity, Zinc, Rats
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