The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Matrix metalloproteinases, a disintegrin and metalloproteinases, and a disintegrin and metalloproteinases with thrombospondin motifs in non-neoplastic diseases: MMP, ADAM and ADAMTS in pathology
Open accessAbstract
Cellular functions within tissues are strictly regulated by the tissue microenvironment which comprises extracellular matrix and extracellular matrix-deposited factors such as growth factors, cytokines and chemokines. These molecules are metabolized by matrix metalloproteinases (MMP), a disintegrin and metalloproteinases (ADAM) and ADAM with thrombospondin motifs (ADAMTS), which are members of the metzincin superfamily. They function in various pathological conditions of both neoplastic and non-neoplastic diseases by digesting different substrates under the control of tissue inhibitors of metalloproteinases (TIMP) and reversion-inducing, cysteine-rich protein with Kazal motifs (RECK). In neoplastic diseases MMP play a central role in cancer cell invasion and metastases, and ADAM are also important to cancer cell proliferation and progression through the metabolism of growth factors and their receptors. Numerous papers have described the involvement of these metalloproteinases in non-neoplastic diseases in nearly every organ. In contrast to the numerous review articles on their roles in cancer cell proliferation and progression, there are very few articles discussing non-neoplastic diseases. This review therefore will focus on the properties of MMP, ADAM and ADAMTS and their implications for non-neoplastic diseases of the cardiovascular system, respiratory system, central nervous system, digestive system, renal system, wound healing and infection, and joints and muscular system.
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Citations
Cites
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Cited by
Extracellular Matrix Degradation and Remodeling in Development and Disease
Lu, P., Takai, K., Weaver, V. M., & Werb, Z. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a005058 · Cited by 2,265
Mechanisms and therapeutic implications of cellular senescence in osteoarthritis
Coryell, P. R., Diekman, B. O., & Loeser, R. F. (2021) · Nature Reviews Rheumatology · doi:10.1038/s41584-020-00533-7 · Cited by 761
Fluorogenic probes for disease-relevant enzymes
Zhang, J., Chai, X., He, X.-P., Kim, H.-J., Yoon, J., & Tian, H. (2019) · Chemical Society Reviews · doi:10.1039/c7cs00907k · Cited by 606
Osteoarthritis Pathogenesis: A Review of Molecular Mechanisms
Xia, B., Chen, D., Zhang, J., Hu, S., Jin, H., & Tong, P. (2014) · Calcified Tissue International · doi:10.1007/s00223-014-9917-9 · Cited by 543
MMP13 is a critical target gene during the progression of osteoarthritis
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Metadata
- Authors
- Shiomi, T., Lemaître, V., D'Armiento, J., & Okada, Y.
- Venue
- Pathology International
- Publisher
- Wiley
- Published
- 2010-05-30
- Volume
- 60
- Issue
- 7
- Pages
- 477-496
- ISSN
- 1320-5463 (ISSN-L)
- 1440-1827
- OpenAlex
- W2099673732
- Cited by
- 274
- References
- 9
- FWCI
- 3.70
- Type
- journal article
- Language
- en
- Open access
- green
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- Shiomi, T., Lemaître, V., D'Armiento, J., & Okada, Y. (2010). Matrix metalloproteinases, a disintegrin and metalloproteinases, and a disintegrin and metalloproteinases with thrombospondin motifs in non-neoplastic diseases: MMP, ADAM and ADAMTS in pathology. Pathology International. https://doi.org/10.1111/j.1440-1827.2010.02547.x
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