Cited by 1,475Protease and Inhibitor MechanismsBlood Coagulation and Thrombosis MechanismsPeptidase Inhibition and Analysis

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The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family.

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Van Wart, H E, Birkedal-Hansen, H·1990·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.87.14.5578PMC PMC54368

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Abstract

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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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
DOI: 10.1073/pnas.87.14.5578
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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The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family.

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