The DOI matches its Crossref record; 161 of the 161 references it cites were found in a registry or an index.
Metalloproteinases and their natural inhibitors in inflammation and immunity
Abstract
Over the past 50 years, steady growth in the field of metalloproteinase biology has shown that the degradation of extracellular matrix components represents only a fraction of the functions performed by these enzymes and has highlighted their fundamental roles in immunity. Metalloproteinases regulate aspects of immune cell development, effector function, migration and ligand-receptor interactions. They carry out ectodomain shedding of cytokines and their cognate receptors. Together with their endogenous inhibitors TIMPs (tissue inhibitor of metalloproteinases), these enzymes regulate signalling downstream of the tumour necrosis factor receptor and the interleukin-6 receptor, as well as that downstream of the epidermal growth factor receptor and Notch, which are all pertinent for inflammatory responses. This Review discusses the metalloproteinase family as a crucial component in immune cell development and function.
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“We did not detect corresponding increases in the soluble IL6 receptor (Figure S1A) (Khokha et al., 2013).”
From Origin and function of stress-induced IL-6 in murine models (2020) · cites this paper as Khokha et al., 2013
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Visse, R., & Nagase, H. (2003) · Circulation Research · doi:10.1161/01.res.0000070112.80711.3d · Cited by 4,575
Structure and function of matrix metalloproteinases and TIMPs
Nagase, H., Visse, R., & MURPHY, G. (2006) · Cardiovascular Research · doi:10.1016/j.cardiores.2005.12.002 · Cited by 3,507
A metalloproteinase disintegrin that releases tumour-necrosis factor-α from cells
Black, R. A., Rauch, C. T., Kozlosky, C. J., Peschon, J. J., Slack, J. L., Wolfson, M. F., Castner, B. J., Stocking, K. L., Reddy, P., Srinivasan, S., et al. (1997) · Nature · doi:10.1038/385729a0 · Cited by 3,149
Defensins: antimicrobial peptides of innate immunity
Ganz, T. (2003) · Nature Reviews Immunology · doi:10.1038/nri1180 · Cited by 3,066
Inflammasomes in health and disease
Strowig, T., Henao-Mejia, J., Elinav, E., & Flavell, R. (2012) · Nature · doi:10.1038/nature10759 · Cited by 2,230
Tumour-derived soluble MIC ligands impair expression of NKG2D and T-cell activation
Groh, V., Wu, J. D., Yee, C., & Spies, T. (2002) · Nature · doi:10.1038/nature01112 · Cited by 1,674
An Essential Role for Ectodomain Shedding in Mammalian Development
Peschon, J. J., Slack, J. L., Reddy, P., Stocking, K. L., Sunnarborg, S. W., Lee, D. C., Russell, W. E., Castner, B. J., Johnson, R. S., Fitzner, J. N., et al. (1998) · Science · doi:10.1126/science.282.5392.1281 · Cited by 1,622
Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-α
Moss, M. L., Jin, S.-L. C., Milla, M. E., Burkhart, W., Carter, H. L., Chen, W.-J., Clay, W. C., Didsbury, J. R., Hassler, D., Hoffman, C. R., et al. (1997) · Nature · doi:10.1038/385733a0 · Cited by 1,378
Grell, M., Douni, E. K., Wajant, H., Löhden, M., Clauss, M. A., Maxeiner, B., Georgopoulos, S., Lesslauer, W., Kollias, G. A., Pfizenmaier, K., et al. (1995) · Cell · doi:10.1016/0092-8674(95)90192-2 · Cited by 1,328
Innate lymphoid cells promote lung-tissue homeostasis after infection with influenza virus
Monticelli, L. A., Sonnenberg, G. F., Abt, M. C., Alenghat, T., Ziegler, C. G. K., Doering, T. A., Angelosanto, J., Laidlaw, B. J., Yang, C. Y., Sathaliyawala, T., et al. (2011) · Nature Immunology · doi:10.1038/ni.2131 · Cited by 1,327
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Resveratrol regulates neuro-inflammation and induces adaptive immunity in Alzheimer’s disease
Moussa, C., Hebron, M. L., Huang, X., Ahn, J., Rissman, R. A., Aisen, P. S. S., & Turner, R. S. (2017) · Journal of Neuroinflammation · doi:10.1186/s12974-016-0779-0 · Cited by 712
Metadata
- Authors
- Khokha, R., Murthy, A., & Weiss, A.
- Affiliations
- Princess Margaret Cancer Centre (CA)
- Corresponding author
- Khokha, Rama
- Venue
- Nature reviews. Immunology
- Published
- 2013-08-23
- Volume
- 13
- Issue
- 9
- Pages
- 649-665
- ISSN
- 1474-1733 (ISSN-L)
- 1474-1741
- OpenAlex
- W2171476567
- Cited by
- 552
- References
- 161
- Citations by year
- 2026: 21 · 2025: 31 · 2024: 29 · 2023: 40 · 2022: 31 · 2021: 41 · 2020: 34 · 2019: 35 · 2018: 50 · 2017: 64 · 2016: 56 · 2015: 61 · 2014: 54 · 2013: 5
- FWCI
- 4.87
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature reviews. Immunology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Canadian Institutes of Health Research
- 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 › Molecular Biology › TGF-β signaling in diseases
- Keywords
- metalloproteinases, metalloproteinase inhibitors, tissue inhibitors of metalloproteinases, inflammation, immunity, immune cell development, leukocyte migration, ectodomain shedding, cytokine receptors, Notch signaling, extracellular matrix degradation, innate immunity, adaptive immunity
- MeSH terms
- Animals, Humans, Immunity, Innate, Inflammation, Tissue Inhibitor of Metalloproteinases, Matrix Metalloproteinases, Adaptive Immunity
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