Cited by 185Protease and Inhibitor MechanismsCell death mechanisms and regulationTGF-β signaling in diseases

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Tissue inhibitors of metalloproteinases and programmed cell death: Conundrums, controversies and potential implications

Mannello, F., Gazzanelli, G.·2001·Apoptosis

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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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Matrix Metalloproteinases
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
Proteases to die for
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
Divergent effects of tissue inhibitor of metalloproteinase-1, -2, or -3 overexpression on rat vascular smooth muscle cell invasion, proliferation, and death in vitro. TIMP-3 promotes apoptosis.
Baker, A. H., Zaltsman, A. B., George, S. J., & Newby, A. C. (1998) · Journal of Clinical Investigation · doi:10.1172/jci1584 · Cited by 464
In vitro suppression of programmed cell death of B cells by tissue inhibitor of metalloproteinases-1.
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

Show all 31 references

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Anticarcinogenic Effects of Isothiocyanates on Hepatocellular Carcinoma
Zhang, Y., Huang, H., Jin, L., & Lin, S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232213834 · Cited by 24
The Matrix Metalloproteinase Inhibitor Marimastat Promotes Neural Progenitor Cell Differentiation into Neurons by Gelatinase-Independent TIMP-2-Dependent Mechanisms
Sinno, M., Biagioni, S., Ajmone‐Cat, M. A., Pafumi, I., Caramanica, P., Medda, V., Tonti, G. A., Minghetti, L., Mannello, F., & Cacci, E. (2012) · Stem Cells and Development · doi:10.1089/scd.2012.0299 · Cited by 24
Self-citation
Matrix metalloproteinases and their inhibitors as biomarkers for metal toxicity in vitro
Cammarota, M., Lamberti, M., Masella, L., Galletti, P., ROSA, M. D., Sannolo, N., & Giuliano, M. (2006) · Toxicology in Vitro · doi:10.1016/j.tiv.2006.02.004 · Cited by 24
What does matrix metalloproteinase-1 expression in patients with breast cancer really tell us?
Mannello, F. (2011) · BMC Medicine · doi:10.1186/1741-7015-9-95 · Cited by 23
Self-citation
Changes in Gene and Protein Expression of Metalloproteinase-2 and -9 and Their Inhibitors TIMP2 and TIMP3 in Different Parts of Fluoride-Exposed Rat Brain
Łukomska, A., Baranowska‐Bosiacka, I., Dec, K., Pilutin, A., Tarnowski, M., Jakubczyk, K., Żwierełło, W., Skórka-Majewicz, M., Chlubek, D., & Gutowska, I. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms22010391 · Cited by 23
Docosahexaenoic acid reduces in vitro invasion of renal cell carcinoma by elevated levels of tissue inhibitor of metalloproteinase-1
McCabe, A., Wallace, J. M. W., Gilmore, W., McGlynn, H., & Strain, J. (2005) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2004.07.006 · Cited by 22
Genes and Molecules That Can Potentiate or Attenuate Psychostimulant Dependence: Relevance of Data from Animal Models to Human Addiction
Niwa, M., Yan, Y., & Nabeshima, T. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1441.024 · Cited by 21
The effect of antihypertensive treatment on arterial stiffness and serum concentration of selected matrix metalloproteinases
Rajzer, M., Wojciechowska, W., Kameczura, T., Olszanecka, A., Fedak, D., Terlecki, M., Kawecka−Jaszcz, K., & Czarnecka, D. (2016) · Archives of Medical Science · doi:10.5114/aoms.2016.58825 · Cited by 21
Antifibrotic effect of meloxicam in rat liver: role of nuclear factor kappa B, proinflammatory cytokines, and oxidative stress
Hassan, M. H., & Ghobara, M. (2016) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-016-1263-1 · Cited by 21
Enhanced migration of tissue inhibitor of metalloproteinase overexpressing hepatoma cells is attributed to gelatinases: Relevance to intracellular signaling pathways
Roeb, E. (2005) · World Journal of Gastroenterology · doi:10.3748/wjg.v11.i8.1096 · Cited by 21
The role of matrix metalloproteinase-2 in the metastatic cascade: a review
Murray, N. P. (2024) · ONCOLOGIE · doi:10.1515/oncologie-2023-0368 · Cited by 20
Tissue Inhibitor of Metalloproteinase-3 Deficiency Inhibits Blood Pressure Elevation and Myocardial Microvascular Remodeling Induced by Chronic Administration of N.OMEGA.-Nitro-L-Arginine Methyl Ester in Mice
Higuchi, M., Yasuda, O., Kawamoto, H., Yotsui, T., Yoshichika, B. A. B. A., OZAKI, T., Maeda, N., Fukuo, K., Rakugi, H., & Ogihara, T. (2007) · Hypertension Research · doi:10.1291/hypres.30.563 · Cited by 20
Multiple effects of α1-antitrypsin on breast carcinoma MDA-MB 468 cell growth and invasiveness
Zelvyté, I., Lindgren, S. C., & Janciauskiene, S. M. (2003) · European Journal of Cancer Prevention · doi:10.1097/00008469-200304000-00005 · Cited by 20
Effective Treatment of Advanced Colorectal Cancer by Rapamycin and 5-FU/Oxaliplatin Monitored by TIMP-1
Wagner, M., Roh, V., Strehlen, M., Laemmle, A., Stroka, D., Egger, B., Trochsler, M., Hunt, K. K., Candinas, D., & Vorburger, S. A. (2009) · Journal of Gastrointestinal Surgery · doi:10.1007/s11605-009-0948-x · Cited by 20
Age and Diet Affect Gene Expression Profile in Canine Skeletal Muscle
Middelbos, I. S., Vester, B. M., Karr‐Lilienthal, L. K., Schook, L. B., & Swanson, K. S. (2009) · PLoS ONE · doi:10.1371/journal.pone.0004481 · Cited by 18
Tissue inhibitor of metalloproteinases-4 is expressed in cervical cancer patients.
Lizárraga, F., Espinosa, M., Maldonado, V., & Meléndez-Zajgla, J. (2005) · PubMed · Cited by 18
Hyperphagia and Leptin Resistance in Tissue Inhibitor of Metalloproteinase-2 Deficient Mice
Stradecki, H. M., & Jaworski, D. M. (2010) · Journal of Neuroendocrinology · doi:10.1111/j.1365-2826.2010.02105.x · Cited by 17
Matrix metalloproteinase‐26 is present more frequently in squamous cell carcinomas of immunosuppressed compared with immunocompetent patients
Kuivanen, T., Jeskanen, L., Kyllönen, L., Isaka, K., & Saarialho‐Kere, U. (2009) · Journal of Cutaneous Pathology · doi:10.1111/j.1600-0560.2009.01188.x · Cited by 16
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Raji, E., Vahedian, V., Golshanrad, P., Nahavandi, R., Behshood, P., Soltani, N., Gharibi, M., Rashidi, M., & Maroufi, N. F. (2023) · Pathology - Research and Practice · doi:10.1016/j.prp.2023.154686 · Cited by 15
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Porter, J. F., Sharma, S. B., Wilson, D. L., Deyssenroth, M. A., Hart, R. P., & Denhardt, D. T. (2005) · Breast Cancer Research and Treatment · doi:10.1007/s10549-005-7728-4 · Cited by 15
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Engers, R., Springer, E., Kehren, V., Simic, T. P., Young, D. A., Beier, J. I., Klotz, L., Clark, I. M., Sies, H., & Gabbert, H. E. (2006) · FEBS Journal · doi:10.1111/j.1742-4658.2006.05476.x · Cited by 15
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Neuhaus, J., Schiffer, E., Mannello, F., Horn, L., Ganzer, R., & Stolzenburg, J. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18050976 · Cited by 14
Self-citation
Tear and serum MMP-9 and serum TIMPs levels in the severe sulfur mustard eye injured exposed patients
Ghasemi, H., Yaraee, R., Faghihzadeh, S., Ghassemi‐Broumand, M., Mahmoudi, M., Babaei, M., Naderi, M., Safavi, M., Ghazanfari, Z., Rastin, M., et al. (2019) · International Immunopharmacology · doi:10.1016/j.intimp.2019.105812 · Cited by 14
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Michalak, S., Wender, M., Michałowska-Wender, G., & Kozubski, W. P. (2010) · PubMed · Cited by 13
Expression and functional properties of antibodies to tissue inhibitors of metalloproteinases (TIMPs) in rheumatoid arthritis.
Bokarewa, M. I., Dahlberg, L., & Tarkowski, A. (2005) · Arthritis Research & Therapy · doi:10.1186/ar1771 · Cited by 12
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Reynolds, J. L., Mahajan, S. D., Aalinkeel, R., Nair, B. B., Sykes, D. E., & Schwartz, S. A. (2011) · Immunological Investigations · doi:10.3109/08820139.2011.559499 · Cited by 12
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Magueresse‐Battistoni, B. L. (2009) · Advances in experimental medicine and biology · doi:10.1007/978-0-387-09597-4_8 · Cited by 12
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Zhang, Y., Qin, L., Ma, X., Wang, Y., Wu, Y., & Jiang, J. (2020) · Disease Markers · doi:10.1155/2020/8831466 · Cited by 12
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Brandhorst, H., Brandhorst, D., Abraham, A., Acreman, S., Schive, S. W., Scholz, H., & Johnson, P. (2020) · Cell Transplantation · doi:10.1177/0963689720952332 · Cited by 9
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Krol, J., Sato, S., Rettenberger, P. M., Assfalg‐Machleidt, I., Schmitt, M., Magdolen, V., & Magdolen, U. (2003) · Biological Chemistry · doi:10.1515/bc.2003.121 · Cited by 9
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Curry, T. E., & Wheeler, S. E. (2002) · Biology of Reproduction · doi:10.1095/biolreprod.102.003681 · Cited by 8
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Shao, X., Lu, W. Q., & Liu, C. (2008) · PubMed · Cited by 6
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Kang, J., Yoon, S., Sung, Y.-K., & Lee, S. (2011) · Experimental Biology and Medicine · doi:10.1258/ebm.2011.011219 · Cited by 6
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Chen, X., Gao, H., Gao, F., Wei, P., Hu, Z., & Liu, Y. (2006) · Science in China Series C Life Sciences · doi:10.1007/s11427-004-0120-5 · Cited by 6
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Self-citation
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de Almeida, S. M., Rotta, I., Liao, A., Tang, B., Vaida, F., de Pereira, A. P., Letendre, S. L., & Ellis, R. J. (2026) · Research Square · doi:10.21203/rs.3.rs-10474891/v1
BindingDB Entry 50001425: A pentanoic acid derivative targeting matrix metalloproteinase-2 (MMP-2) induces apoptosis in a chronic myeloid leukemia cell line.
BindingDB (2020) · UC San Diego · doi:10.7270/q29s1tjt

Authors: Mannello, F., & Gazzanelli, G.
Affiliations: University of Urbino (IT)
Corresponding author: Mannello, F.
ORCID: Mannello, F.
Venue: Apoptosis
Publisher: Springer Science and Business Media LLC
Published: 2001-12
Volume: 6
Issue: 6
Pages: 479-482
ISSN: 1360-8185 (ISSN-L)
1573-675X
DOI: 10.1023/a:1012493808790
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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Tissue inhibitors of metalloproteinases and programmed cell death: Conundrums, controversies and potential implications

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