The DOI matches its Crossref record; 34 of the 34 references it cites were found in a registry or an index.
Tissue inhibitors of metalloproteinases and programmed cell death: Conundrums, controversies and potential implications
Abstract
Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases, which can synergistically degrade the major components of extracellular matrix (ECM). A key role in maintaining the balance between ECM deposition and degradation in several physio-pathological processes is carried out, through multiple biological functions, by four members of the tissue inhibitors of metalloproteinases (TIMPs) family. TIMP-1 and TIMP-2 are capable of inhibiting the activities of MMPs, can inhibit tumour growth, invasion and metastasis, exhibit growth factor-like activity, can inhibit angiogenesis and suppress programmed cell death (PCD) independently of the MMP-inhibitory activity. TIMP-3 is the only member which is tightly bound to ECM, inhibits TNF-alpha converting enzyme and induces PCD through the stabilization of TNF-alpha receptors on the cell surface. TIMP-4 plays a role in ECM homeostasis in a tissue-specific fashion and its overexpression induces PCD. The aim of this article is to review the exciting and intriguing literature on TIMPs, with special emphasis on their conflicting-paradoxical roles in PCD and their potential clinical usefulness.
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“Importantly, it inhibits tumor necrosis factor alpha-converting enzyme and induces apoptosis through the stabilization of tumor necrosis factor alpha receptors on the cell surface (42).”
From MicroRNA 21 Promotes Glioma Invasion by Targeting Matrix Metalloproteinase Regulators (2008) · cites this paper as [42]
Citations
Cites
Nagase, H., & Woessner, J. F. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.31.21491 · Cited by 3,912
Tissue inhibitors of metalloproteinases: evolution, structure and function
Brew, K., Dinakarpandian, D., & Nagase, H. (2000) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(99)00279-4 · Cited by 1,908
Tissue inhibitors of metalloproteinases: structure, regulation and biological functions.
Gomez, D. E., Alonso, D. F., Yoshiji, H., & Thorgeirsson, U. P. (1997) · PubMed · Cited by 1,508
Cryns, V., & Yuan, J. (1998) · Genes & Development · doi:10.1101/gad.12.11.1551 · Cited by 1,228
Cancer risk in patients with inflammatory bowel disease: A population-based study
Bernstein, C. N., Blanchard, J., Kliewer, E. V., & Wajda, A. (2001) · Cancer · doi:10.1002/1097-0142(20010215)91:4<785::aid-cncr1065>3.0.co;2-r · Cited by 1,179
Suppression of ICE and Apoptosis in Mammary Epithelial Cells by Extracellular Matrix
Boudreau, N., Sympson, C. J., Werb, Z., & Bissell, M. J. (1995) · Science · doi:10.1126/science.7531366 · Cited by 1,175
Proteolytic remodeling of extracellular matrix
Birkedal-Hansen, H. (1995) · Current Opinion in Cell Biology · doi:10.1016/0955-0674(95)80116-2 · Cited by 1,074
TNF‐α converting enzyme (TACE) is inhibited by TIMP‐3
Amour, A., Slocombe, P. M., Webster, A., Butler, M., Knight, C. G., Smith, B. J., Stephens, P. E., Shelley, C., Hutton, M., Knäuper, V., et al. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)01031-x · Cited by 609
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Guedez, L., Stetler-Stevenson, W. G., Wolff, L., Wang, J., Fukushima, P., Mansoor, A., & Stetler-Stevenson, M. (1998) · Journal of Clinical Investigation · doi:10.1172/jci2881 · Cited by 397
Cited by
Matrix Metalloproteinases: Role In Arthritis
Burrage, P. (2006) · Frontiers in Bioscience · doi:10.2741/1817 · Cited by 1,292
MicroRNA 21 Promotes Glioma Invasion by Targeting Matrix Metalloproteinase Regulators
Gabriely, G., Wurdinger, T., Kesari, S., Esau, C. C., Burchard, J., Linsley, P. S., & Krichevsky, A. M. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00479-08 · Cited by 888
Is there new hope for therapeutic matrix metalloproteinase inhibition?
Vandenbroucke, R. E., & Libert, C. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4390 · Cited by 832
Multiple roles for MMPs and TIMPs in cerebral ischemia
Cunningham, L. A., Wetzel, M., & Rosenberg, G. A. (2005) · Glia · doi:10.1002/glia.20169 · Cited by 411
Role of muscle endopeptidases and their inhibitors in meat tenderness
Sentandreu, M. A., Coulis, G., & Ouali, A. (2002) · Trends in Food Science & Technology · doi:10.1016/s0924-2244(02)00188-7 · Cited by 366
Metadata
- Authors
- Mannello, F., & Gazzanelli, G.
- Affiliations
- University of Urbino (IT)
- Corresponding author
- Mannello, F.
- ORCID
- Mannello, F.
- Venue
- Apoptosis
- Published
- 2001-12
- Volume
- 6
- Issue
- 6
- Pages
- 479-482
- ISSN
- 1360-8185 (ISSN-L)
- 1573-675X
- OpenAlex
- W309980051
- Cited by
- 185
- References
- 31
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 4 · 2023: 4 · 2022: 2 · 2021: 2 · 2020: 4 · 2019: 6 · 2018: 4 · 2017: 6 · 2016: 3 · 2015: 3 · 2014: 5 · 2013: 7 · 2012: 8
- FWCI
- 4.28
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springernature.com/gp/researchers/text-and-data-mining (tdm)
- www.springernature.com/gp/researchers/text-and-data-mining (vor)
- Locations
- APOPTOSIS (publishedVersion)
- PubMed (publishedVersion)
- CINECA IRIS Institutional Research information system (University of Urbino) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › TGF-β signaling in diseases
- Keywords
- tissue inhibitors of metalloproteinases, matrix metalloproteinases, programmed cell death, extracellular matrix degradation, TIMP-1, TIMP-2, TIMP-3, TIMP-4, TNF-alpha converting enzyme, angiogenesis inhibition, tumor invasion and metastasis
- MeSH terms
- Animals, Humans, Neoplasms, Tumor Necrosis Factor-alpha, Apoptosis, Tissue Inhibitor of Metalloproteinases
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
