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Review
. 2022 Sep 11;23(18):10546.
doi: 10.3390/ijms231810546.

The Role of Matrix Metalloproteinase in Inflammation with a Focus on Infectious Diseases

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Review

The Role of Matrix Metalloproteinase in Inflammation with a Focus on Infectious Diseases

Han Sol Lee et al. Int J Mol Sci. .

Abstract

Matrix metalloproteinases (MMPs) are involved in extracellular matrix remodeling through the degradation of extracellular matrix components and are also involved in the inflammatory response by regulating the pro-inflammatory cytokines TNF-α and IL-1β. Dysregulation in the inflammatory response and changes in the extracellular matrix by MMPs are related to the development of various diseases including lung and cardiovascular diseases. Therefore, numerous studies have been conducted to understand the role of MMPs in disease pathogenesis. MMPs are involved in the pathogenesis of infectious diseases through a dysregulation of the activity and expression of MMPs. In this review, we discuss the role of MMPs in infectious diseases and inflammatory responses. Furthermore, we present the potential of MMPs as therapeutic targets in infectious diseases.

Keywords: SARS-CoV-2; infectious diseases; influenza A virus; matrix metalloproteinases.

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Conflict of interest statement

The authors declare no conflict of interest.

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References

    1. Kleiner D.E., Stetler-Stevenson W.G. Matrix metalloproteinases and metastasis. Cancer Chemother. Pharmacol. 1999;43:S42–S51. doi: 10.1007/s002800051097. - DOI - PubMed
    1. Das A., Monteiro M., Barai A., Kumar S., Sen S. MMP proteolytic activity regulates cancer invasiveness by modulating integrins. Sci. Rep. 2017;7:14219. doi: 10.1038/s41598-017-14340-w. - DOI - PMC - PubMed
    1. Malemud C.J. Inhibition of MMPs and ADAM/ADAMTS. Biochem. Pharmacol. 2019;165:33–40. doi: 10.1016/j.bcp.2019.02.033. - DOI - PMC - PubMed
    1. Das N., Benko C., Gill S.E., Dufour A. The Pharmacological TAILS of Matrix Metalloproteinases and Their Inhibitors. Pharmaceuticals. 2020;14:31. doi: 10.3390/ph14010031. - DOI - PMC - PubMed
    1. Fu X., Kassim S.Y., Parks W.C., Heinecke J.W. Hypochlorous acid oxygenates the cysteine switch domain of pro-matrilysin (MMP-7). A mechanism for matrix metalloproteinase activation and atherosclerotic plaque rupture by myeloperoxidase. J. Biol. Chem. 2001;276:41279–41287. doi: 10.1074/jbc.M106958200. - DOI - PubMed

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