Honibald EN, Mathew S, Padmanaban J, Sundaram E RR. Perioceutics: matrix metalloproteinase inhibitors as an adjunctive therapy for inflammatory periodontal disease. J Pharm &bioallied Sci. 2012;Suppl 2(S417).

De Souza AP, Da Silva R, Cantazaro-Guimarães S. Matrix metalloproteinases: the most important pathway involved with periodontal destruction. Brazilian J Oral Sci Published online. 2005. https://doi.org/10.20396/bjos.v4i15.8641850.

Article  Google Scholar 

Yamamoto K, Murphy G, Troeberg L. Extracellular regulation of metalloproteinases. Matrix Biol Published online. 2015. https://doi.org/10.1016/j.matbio.2015.02.007.

Article  Google Scholar 

Bonnans C, Chou J, Werb Z. Remodelling the extracellular matrix in development and disease. Nat Rev Mol Cell Biol. Published online 2014. https://doi.org/10.1038/nrm3904

Hernández-Ríos P, Hernández M, Garrido M, Tervahartiala T, Leppilahti JM, Kuula H, Heikkinen AM, Mäntylä P, Rathnayake N, Nwhator SST. Oral fluid matrix metalloproteinase (MMP)-8 as a diagnostic tool in chronic periodontitis. Met Med. 2011;38(9):817–9.

Google Scholar 

Parmar NK, Nisha KJ, Guru S PS. Role of matrixmetalloproteinases in periodontal disease—a review. Biomed J Sci Tech Res. 2018;2(1.):2099–2104.

Ozmeric NGC. Chemical inhibition of matrix metalloproteinases for periodontal treatment. Clin Anti-inflamm Anti-Allergy Drugs. 2015;2(1):21–6.

CAS  Article  Google Scholar 

Sorsa T, Tjäderhane L, Konttinen YT, et al. Matrix metalloproteinases: contribution to pathogenesis, diagnosis and treatment of periodontal inflammation. Ann Med Published online. 2006. https://doi.org/10.1080/07853890600800103.

Article  Google Scholar 

Shin DS, Park JW, Suh JY, Lee JM. The expressions of inflammatory factors and tissue inhibitor of matrix metalloproteinase-2 in human chronic periodontitis with type 2 diabetes mellitus. J Periodontal Implant Sci Published online. 2010. https://doi.org/10.5051/jpis.2010.40.1.33.

Article  Google Scholar 

Barreiros D, Nelson-Filho P, Paula-Silva FWG, et al. MMP2 and MMP9 are associated with apical periodontitis progression and might be modulated by TLR2 and MyD88. Braz Dent J Published online. 2018. https://doi.org/10.1590/0103-6440201801731.

Article  Google Scholar 

Carneiro E, Menezes R, Garlet GP, et al. Expression analysis of matrix metalloproteinase-9 in epithelialized and nonepithelialized apical periodontitis lesions. Oral Surgery, Oral Med Oral Pathol Oral Radiol Endodontology. Published online 2009. https://doi.org/10.1016/j.tripleo.2008.07.030

Song J, Wu C, Zhang X, Sorokin LM. In vivo processing of CXCL5 (LIX) by matrix metalloproteinase (MMP)-2 and MMP-9 promotes early neutrophil recruitment in IL-1β–induced peritonitis. J Immunol Published online. 2013. https://doi.org/10.4049/jimmunol.1202286.

Article  Google Scholar 

Franco C, Patricia HR, Timo S, Claudia B, Marcela H. Matrix metalloproteinases as regulators of periodontal inflammation. Int J Mol Sci Published online. 2017. https://doi.org/10.3390/ijms18020440.

Article  Google Scholar 

Kawashima N, Suzuki N, Yang G, et al. Kinetics of RANKL, RANK and OPG expressions in experimentally induced rat periapical lesions. Oral Surgery, Oral Med Oral Pathol Oral Radiol Endodontology. Published online 2007. https://doi.org/10.1016/j.tripleo.2006.11.036

Menezes R, Garlet TP, Letra A, Bramante CM, Campanelli AP, de CássiaFigueira R, Sogayar MC, Granjeiro JM, Garlet GP. Differential patterns of receptor activator of nuclear factor kappa B ligand/osteoprotegerin expression in human periapical granulomas: possible association with progressive or stable nature of the lesions. J Endod. 2008;34(8):932–8.

Article  Google Scholar 

Golub LM, Lee HM, Stoner JA, et al. Subantimicrobial-dose doxycycline modulates gingival crevicular fluid biomarkers of periodontitis in postmenopausal osteopenic women. J Periodontol Published online. 2008. https://doi.org/10.1902/jop.2008.070623.

Article  Google Scholar 

Hwang BM, Chae HS, Jeong YJ, et al. Protein tyrosine phosphatase controls breast cancer invasion through the expression of matrix metalloproteinase-9. BMB Rep Published online. 2013. https://doi.org/10.5483/BMBRep.2013.46.11.053.

Article  Google Scholar 

Dayton TL, Gocheva V, Miller KM, et al. Isoform-specific deletion of PKM2 constrains tumor initiation in a mouse model of soft tissue sarcoma. Cancer Metab Published online. 2018. https://doi.org/10.1186/s40170-018-0179-2.

Article  Google Scholar 

Mueller S, Michaelis M, Lindemann S, Gigout A. Effects of three potential anabolic disease-modifying osteoarthritis drugs – sprifermin, IGF1 and BMP7 – on matrix production and the phenotype of articular chondrocytes. Osteoarthr Cartil Published online. 2019. https://doi.org/10.1016/j.joca.2019.02.227.

Article  Google Scholar 

Staines KA, Prideaux M, Hohenstein P, Buttle DJ, Pitsillides AA, Farquharson C. E11 protein stabilisation by proteasome inhibition promotes osteocyte differentiation and may protect against osteoarthritis bone pathology. Osteoarthr Cartil. 2015;23:A57.

Michigami T. Regulatory mechanisms for the development of growth plate cartilage. Cell Mol Life Sci Published online. 2013. https://doi.org/10.1007/s00018-013-1346-9.

Article  Google Scholar 

Ogura Y, Tajrishi MM, Sato S, Hindi SM, Kumar A. Therapeutic potential of matrix metalloproteinases in Duchenne muscular dystrophy. Front Cell Dev Biol Published online. 2014. https://doi.org/10.3389/fcell.2014.00011.

Article  Google Scholar 

Kiili M, Cox SW, Chen HW, et al. Collagenase-2 (MMP-8) and collagenase-3 (MMP-13) in adult periodontitis: molecular forms and levels in gingival crevicular fluid and immunolocalisation in gingival tissue. J Clin Periodontol Published online. 2002. https://doi.org/10.1034/j.1600-051x.2002.290308.x.

Article  Google Scholar 

Kudo Y, Iizuka S, Yoshida M, et al. Matrix metalloproteinase-13 (MMP-13) directly and indirectly promotes tumor angiogenesis. J Biol Chem Published online. 2012. https://doi.org/10.1074/jbc.M112.373159.

Article  Google Scholar 

Baeza M, Garrido M, Hernández-Ríos P, et al. Diagnostic accuracy for apical and chronic periodontitis biomarkers in gingival crevicular fluid: an exploratory study. J Clin Periodontol Published online. 2016. https://doi.org/10.1111/jcpe.12479.

Article  Google Scholar 

Burrage PS, Mix KS, Brinckerhoff CE. Matrix metalloproteinases: role in arthritis. Front Biosci Published online. 2006. https://doi.org/10.2741/1817.

Article  Google Scholar 

Brighton CT, Wang W, Clark CC. The effect of electrical fields on gene and protein expression in human osteoarthritic cartilage explants. J Bone Jt Surg - Ser A. Published online 2008. https://doi.org/10.2106/JBJS.F.01437

Murphy G. Riding the metalloproteinase roller coaster. J Biol Chem Published online. 2017. https://doi.org/10.1074/jbc.X117.785295.

Article  Google Scholar 

Sayed G, Omar G, Ghanem A, Mohamed N, El-Kholy M. Association of matrix metalloproteinase-9 and tissue inhibitor of metalloproteinase-1 levels with diabetic foot ulcer in Egyptians with type 2 diabetes mellitus. J Med Sci Res Published online. 2018. https://doi.org/10.4103/jmisr.jmisr_80_18.

Article  Google Scholar 

Jacobsen JA, Major Jourden JL, Miller MT, Cohen SM. To bind zinc or not to bind zinc: an examination of innovative approaches to improved metalloproteinase inhibition. Biochim Biophys Acta - Mol Cell Res. Published online 2010. https://doi.org/10.1016/j.bbamcr.2009.08.006

Leco KJ, Martin EL, Barcroft LC, Gill SE. Matrix metalloproteinase inhibitors. In: Encyclopedia of respiratory medicine, four-volume set. 2006. https://doi.org/10.1016/B0-12-370879-6/00243-X

Egawa N, Koshikawa N, Tomari T, Nabeshima K, Isobe T, Seiki M. Membrane type 1 matrix metalloproteinase (MT1-MMP/MMP-14) cleaves and releases a 22-kDa extracellular matrix metalloproteinase inducer (EMMPRIN) fragment from tumor cells. J Biol Chem Published online. 2006. https://doi.org/10.1074/jbc.M606993200.

Article  Google Scholar 

Ramer R, Hinz B. Inhibition of cancer cell invasion by cannabinoids via increased expression of tissue inhibitor of matrix metalloproteinases-1. J Natl Cancer Inst Published online. 2008. https://doi.org/10.1093/jnci/djm268.

Article  Google Scholar 

Cheng G, Fan X, Hao M, Wang J, Zhou X, Sun X. Higher levels of TIMP-1 expression are associated with a poor prognosis in triplenegative breast cancer. Mol Cancer Published online. 2016. https://doi.org/10.1186/s12943-016-0515-5.

Article  Google Scholar 

Ritter LM, Garfield SH, Thorgeirsson UP. Tissue inhibitor of metalloproteinases-1 (TIMP-1) binds to the cell surface and translocates to the nucleus of human MCF-7 breast carcinoma cells. Biochem Biophys Res Commun Published online. 1999. https://doi.org/10.1006/bbrc.1999.0408.

Article  Google Scholar 

Johanson M, Zhao XR, Huynh-Ba G, Villar CC. Matrix metalloproteinases, tissue inhibitors of matrix metalloproteinases, and inflammation in cyclosporine A–induced gingival enlargement: a pilot in vitro study using a three-dimensional model of the human oral mucosa. J Periodontol Published online. 2013. https://doi.org/10.1902/jop.2012.120224.

Article  Google Scholar 

Murphy G. Tissue inhibitors of metalloproteinases. Genome Biol Published online. 2011. https://doi.org/10.1186/gb-2011-12-11-233.

Article  Google Scholar 

Brew K, Nagase H. The tissue inhibitors of metalloproteinases (TIMPs): an ancient family with structural and functional diversity. Biochim Biophys Acta - Mol Cell Res. Published online 2010. https://doi.org/10.1016/j.bbamcr.2010.01.003

Ries C, Egea V, Karow M, Kolb H, Jochum M, Neth P. MMP-2, MT1-MMP, and TIMP-2 are essential for the invasive capacity of human mesenchymal stem cells: differential regulation by inflammatory cytokines. Blood Published online. 2007. https://doi.org/10.1182/blood-2006-10-051060.

Article  Google Scholar 

Stetler-Stevenson WG. The tumor microenvironment: regulation by MMP-independent effects of tissue inhibitor of metalloproteinases-2. Cancer Metastasis Rev Published online. 2008. https://doi.org/10.1007/s10555-007-9105-8.

Article  Google Scholar 

Peng X, Chen Z, Farshidfar F, et al. Molecular characterization and clinical relevance of metabolic expression subtypes in human cancers. Cell Rep Published online. 2018. https://doi.org/10.1016/j.celrep.2018.03.077.

Article  Google Scholar 

Higashi S, Hirose T, Takeuchi T, Miyazaki K. Molecular design of a highly selective and strong protein inhibitor against matrix metalloproteinase-2 (MMP-2). J Biol Chem Published online. 2013. https://doi.org/10.1074/jbc.M112.441758.

Article  Google Scholar 

R. R, S. F, M. H, B. H. Cannabinoids inhibit angiogenic properties of endothelial cells via increasing TIMP-1 release from lung cancer cells. Naunyn Schmiedebergs Arch Pharmacol. Published online 2014.

D’Alessio S, Ferrari G, Cinnante K, et al. Tissue inhibitor of metalloproteinases-2 binding to membrane-type 1 matrix metalloproteinase induces MAPK activation and cell growth by a non-proteolytic mechanism. J Biol Chem Published online. 2008. https://doi.org/10.1074/jbc.M705492200.

Article  Google Scholar 

Wu ZS, Wu Q, Yang JH, et al. Prognostic significance of MMP-9 and TIMP-1 serum and tissue expression in breast cancer. Int J Cancer Published online. 2008. https://doi.org/10.1002/ijc.23337.

Article  Google Scholar 

Li Z, Clarke MP, Barker MD, McKie N. TIMP3 mutation in Sorsby’s fundus dystrophy: molecular insights. Expert Rev Mol Med Published online. 2005. https://doi.org/10.1017/S1462399405010045.

Article  Google Scholar 

Warwick A, Gibson J, Sood R, Lotery A. A rare penetrant TIMP3 mutation confers relatively late onset choroidal neovascularisation which can mimic age-related macular degeneration. Eye Published online. 2016. https://doi.org/10.1038/eye.2015.204.

Article  Google Scholar 

Vargova V, Pytliak M, Mechirova V. Matrix metalloproteinases and their tissue inhibitors in diabetes, atherosclerosis and prediction of the cardiovascular risk. Curr Enzym Inhib Published online. 2011. https://doi.org/10.2174/157340810794578524.

Article  Google Scholar 

E Sharma,A Lakhani ST and SK. Role of MMPs in connective tissue breakdown and periodontal disease: a review. Austin Dent Sci. 2019;4(1).

Ingman T, Tervahartiala T, Ding Y, Tschesche H, Haerian A, Kinane DF, Konttinen YTST. Matrix metalloproteinases and their inhibitors in gingival crevicular fluid and saliva of periodontitis patients. J Clin Periodontol. 1996;23(12):1127–32.

CAS  Article  Google Scholar 

Tüter G, Kurtiş BSM. Effects of phase I periodontal treatment on gingival crevicular fluid levels of matrix metalloproteinase-1 and tissue inhibitor of metalloproteinase-1. J Periodontol. 2002;73(5):487–93.

Article  Google Scholar 

Gursoy UK, Könönen E, Pradhan-Palikhe P, et al. Salivary MMP-8, TIMP-1, and ICTP as markers of advanced periodontitis. J Clin Periodontol Published online. 2010. https://doi.org/10.1111/j.1600-051X.2010.01563.x.

Article  Google Scholar 

Sorsa T, Mäntylä P, Tervahartiala T, Pussinen PJ, Gamonal J, Hernandez M. MMP activation in diagnostics of periodontitis and systemic inflammation. J Clin Periodontol Published online. 2011. https://doi.org/10.1111/j.1600-051X.2011.01753.x.

Article  Google Scholar 

Khokha R, Murthy A, Weiss A. Metalloproteinases and their natural inhibitors in inflammation and immunity. Nat Rev Immunol Published online. 2013. https://doi.org/10.1038/nri3499.

Article  Google Scholar 

Amǎlinei C, Cǎruntu ID, Giu̧cǎ SE, Bǎlan RA. Matrix metalloproteinases involvement in pathologic conditions. Rom J Morphol Embryol. Published online. 2010.

Torok S, Rezeli M, Kelemen O, et al. Limited tumor tissue drug penetration contributes to primary resistance against angiogenesis inhibitors. Theranostics Published online. 2017. https://doi.org/10.7150/thno.16767.

Article  Google Scholar 

Kasaoka T, Nishiyama H, Okada M, Nakajima M. Matrix metalloproteinase inhibitor, MMI270 (CGS27023A) inhibited hematogenic metastasis of B16 melanoma cells in both experimental and spontaneous metastasis models. Clin Exp Metastasis Published online. 2008. https://doi.org/10.1007/s10585-008-9198-7.

Article  Google Scholar 

Fisher JF, Mobashery S. Recent advances in MMP inhibitor design. Cancer Metastasis Rev Published online. 2006. https://doi.org/10.1007/s10555-006-7894-9.

Article