A mini review on the associations of matrix metalloproteinases (MMPs) -1, -8, -13 with periodontal disease

Fazle Khuda; Nur Najmi Mohamad Anuar; Badiah Baharin; Nurrul Shaqinah Nasruddin; Fazle Khuda; Nur Najmi Mohamad Anuar; Badiah Baharin; Nurrul Shaqinah Nasruddin

doi:10.3934/molsci.2021002

AIMS Molecular Science

2021, Volume 8, Issue 1: 13-31. doi: 10.3934/molsci.2021002

Previous Article Next Article

Review

A mini review on the associations of matrix metalloproteinases (MMPs) -1, -8, -13 with periodontal disease

1.
Department of Craniofacial Diagnostics and Biosciences, Faculty of Dentistry, Universiti Kebangsaan Malaysia, Jalan Raja Muda Abdul Aziz, 50300 Kuala Lumpur, Malaysia
2.
Programme of Biomedical Science, Centre for Toxicology and Health Risk Studies, Faculty of Health Sciences, Universiti Kebangsaan Malaysia, Jalan Raja Muda Abdul Aziz, 50300 Kuala Lumpur, Malaysia
3.
Department of Restorative Dentistry, Faculty of Dentistry, Universiti Kebangsaan Malaysia, Jalan Raja Muda Abdul Aziz, 50300 Kuala Lumpur, Malaysia

Received: 16 October 2020 Accepted: 06 January 2021 Published: 07 January 2021

Matrix metalloproteinases (MMPs) are one of the most important endopeptidases in periodontal disease that generally degrade extracellular matrix (ECM) components of periodontal supporting tissues, leading to tooth loss. Among the MMP family, MMP-1, -8 and -13, which are also known as the collagenase group, play a vital role in the degradation of ECM collagen and non-collagen substances. Elevated levels of MMP -1, -8 and -13 are markedly significant within tissue, gingival crevicular fluid (GCF), and saliva of patients with periodontitis, which help to explain the progression pattern of the disease. This review provides an overview of MMP -1, -8, and -13 on their structures, functions and their critical role in periodontitis.
- collagenase,
- matrix metalloproteinase,
- MMPs,
- periodontitis,
- periodontal disease
Citation: Fazle Khuda, Nur Najmi Mohamad Anuar, Badiah Baharin, Nurrul Shaqinah Nasruddin. A mini review on the associations of matrix metalloproteinases (MMPs) -1, -8, -13 with periodontal disease[J]. AIMS Molecular Science, 2021, 8(1): 13-31. doi: 10.3934/molsci.2021002

Related Papers:

Abstract

Matrix metalloproteinases (MMPs) are one of the most important endopeptidases in periodontal disease that generally degrade extracellular matrix (ECM) components of periodontal supporting tissues, leading to tooth loss. Among the MMP family, MMP-1, -8 and -13, which are also known as the collagenase group, play a vital role in the degradation of ECM collagen and non-collagen substances. Elevated levels of MMP -1, -8 and -13 are markedly significant within tissue, gingival crevicular fluid (GCF), and saliva of patients with periodontitis, which help to explain the progression pattern of the disease. This review provides an overview of MMP -1, -8, and -13 on their structures, functions and their critical role in periodontitis.

Acknowledgments

This research was financially supported by the Young Researcher’s Incentive Grants GGPM-2017-051, Universiti Kebangsaan Malaysia.

Conflict of interest

All authors declare no conflict of interest in this paper.

References

[1]	Beck JD, Philips K, Moss K, et al. (2020) Periodontal disease classifications and incident coronary heart disease in the atherosclerosis risk in communities study. J Periodontol 91: 1409-1408. doi: 10.1002/JPER.19-0723
[2]	Preethanath RS, Ibraheem WI, Anil A (2020) Pathogenesis of gingivitis. Oral Diseases 1-19.
[3]	Yakob M, Meurman J, Sorsa T, et al. (2013) Treponema denticola associates with increased levels of MMP-8 and MMP-9 in gingival crevicular fluid. Oral Dis 19: 694-701. doi: 10.1111/odi.12057
[4]	Sorsa T, Ding YL, Ingman T, et al. (2016) Cellular source, activation and inhibition of dental plaque collagenase. J Clin Periodontol 22: 709-717. doi: 10.1111/j.1600-051X.1995.tb00831.x
[5]	Dom TNM, Ayob R, Abd Muttalib K, et al. (2016) National economic burden sssociated with management of periodontitis in Malaysia. Int J Dent Article ID 1891074.
[6]	Nazir M, Al-Ansari A, Al-Khalifa K, et al. (2020) Global prevalence of periodontal disease and lack of its surveillance. Sci World J Article ID 2146160.
[7]	Dyke TEV, Dave S (2006) Risk factors for periodontitis. J Int Acad Periodontol 7: 3-7.
[8]	Charles K, Honibald E, Palani A, et al. (2014) Role of matrix metalloproteinases (MMPs) in periodontitis and its management. J Indian Acad Dent Spec Res 1: 65-69. doi: 10.4103/2229-3019.148262
[9]	Ye S (2015) Putative targeting of matrix metalloproteinase-8 in atherosclerosis. Pharmacol Ther 147: 111-122. doi: 10.1016/j.pharmthera.2014.11.007
[10]	Zhang Z, Yang X, Zhang H, et al. (2018) The role of ECM metalloproteinase inducer glycosylation in regulating matrix metalloproteinases in periodontitis. J Periodontal Res 53: 391-402. doi: 10.1111/jre.12524
[11]	Rangasamy L, Di Geronimo B, Ortín I, et al. (2019) Molecular imaging probes based on matrix metalloproteinase inhibitors (MMPIs). Molecules 24: 2982. doi: 10.3390/molecules24162982
[12]	Anuar NNM, Zulkafali NIN, Ugusman A (2020) Modulation of matrix metalloproteinases by plant-derived products. Curr Cancer Drug Targets PMID 33222671.
[13]	Letra A, Silva RM, Rylands RJ, et al. (2012) MMP-3 and TIMP-1 variants contribute to chronic periodontitis and may be implicated in disease progression. J Clin Periodontol 39: 707-716. doi: 10.1111/j.1600-051X.2012.01902.x
[14]	Caldeira J, Laronha H (2020) Structure and function of human matrix metalloproteinases. Cells 9: 1076. doi: 10.3390/cells9051076
[15]	Checchi V, Maravic T, Bellini P, et al. (2020) The role of matrix metalloproteinases in periodontal disease. Int J Environ Res Public Health 17: 1-13. doi: 10.3390/ijerph17144923
[16]	Gonzalez-Avila G, Sommer B, Mendoza-Posada DA, et al. (2019) Matrix metalloproteinases participation in the metastatic process and their diagnostic and therapeutic applications in cancer. Crit Rev Oncol Hematol 137: 57-83. doi: 10.1016/j.critrevonc.2019.02.010
[17]	Hannas AR, Pereira JC, Granjeiro JM, et al. (2007) The role of matrix metalloproteinases in the oral environment. Acta Odontol Scand 65: 1-13. doi: 10.1080/00016350600963640
[18]	Verma RP, Hansch C (2007) Matrix metalloproteinases (MMPs): chemical-biological functions and (Q)SARs. Bioorg Med Chem 15: 2223-2268. doi: 10.1016/j.bmc.2007.01.011
[19]	Klein T, Bischoff R (2011) Physiology and pathophysiology of matrix metalloproteases. Amino Acids 41: 271-290. doi: 10.1007/s00726-010-0689-x
[20]	Nagase H, Visse R, Murphy G (2006) Structure and function of matrix metalloproteinases and TIMPs. Cardiovasc Res 69: 562-573. doi: 10.1016/j.cardiores.2005.12.002
[21]	Cui N, Hu M, Khalil RA (2017) Biochemical and biological attributes of matrix metalloproteinases. Progress in Molecular Biology and Translational Science Elsevier Inc.
[22]	Pérez-García S, Carrión M, Gutiérrez-Cañas I, et al. (2019) Profile of matrix-remodeling proteinases in osteoarthritis: Impact of fibronectin. Cells 9: 40. doi: 10.3390/cells9010040
[23]	Sapna G, Gokul S (2013) Matrix metalloproteinases and periodontal diseases. Oral Dis 20: 538-550. doi: 10.1111/odi.12159
[24]	Franco C, Patricia HR, Timo S, et al. (2017) Matrix metalloproteinases as regulators of periodontal inflammation. Int J Mol Sci 18: 1-12.
[25]	Verstappen J, Hoff JWVD (2006) Critical reviews in oral biology and medicine tissue inhibitors of metalloproteinases (TIMPs). J Dent Res 85: 1074-1084. doi: 10.1177/154405910608501202
[26]	Visse R, Nagase H (2003) Matrix metalloproteinases and tissue inhibitors of metalloproteinases: Structure, function, and biochemistry. Circ Res 92: 827-839. doi: 10.1161/01.RES.0000070112.80711.3D
[27]	Lahdentausta LSJ, Paju S, Mäntylä P, et al. (2018) Saliva and serum biomarkers in periodontitis and coronary artery disease. J Clin Periodontol 45: 1045-1055. doi: 10.1111/jcpe.12976
[28]	Li W, Zhu Y, Singh P, et al. (2016) Association of common variants in MMPs with periodontitis risk. Dis Markers 2016: 1-20.
[29]	Yamamoto K, Okano H, Miyagawa W, et al. (2015) MMP-13 is constitutively produced in human chondrocytes and co-endocytosed with ADAMTS-5 and TIMP-3 by the endocytic receptor LRP1. Matrix Biol 56: 57-73. doi: 10.1016/j.matbio.2016.03.007
[30]	Chow YY, Chin KY (2020) The Role of Inflammation in the Pathogenesis of Osteoarthritis. Mediat Inflamm Article ID 8293921.
[31]	Navjot KP, Nisha KJ, Sanjeela GSP (2018) Role of matrixmetalloproteinases in periodontal disease - A Review. Biomed J Sci Tech Res 2: 2099.
[32]	Pardo A, Selman M (2005) MMP-1: The elder of the family. Int J Biochem Cell Biol 37: 283-288. doi: 10.1016/j.biocel.2004.06.017
[33]	Chang YT, Chu LJ, Liu YC, et al. (2020) Verification of saliva matrix metalloproteinase-1 as a strong diagnostic marker of oral cavity cancer. Cancers (Basel) 12: 1-18.
[34]	Balli U, Cetinkaya BO, Keles GC, et al. (2016) Assessment of MMP-1, MMP-8 and TIMP-2 in experimental periodontitis treated with kaempferol. JPIS 46: 84-95.
[35]	Wang J, Yang D, Li C, et al. (2014) Expression of ECM metalloproteinase inducer glycosylation and caveolin-1 in healthy and inflamed human gingiva. J Periodontal Res 49: 197-204. doi: 10.1111/jre.12095
[36]	Hazzaa H, Abo Hager E (2017) Expression of MMP-1 and MMP-9 in localized aggressive periodontitis patients before and after treatment: A clinical and immunohistochemical study. Egypt Dent J 63: 667-684. doi: 10.21608/edj.2017.75015
[37]	Popat RP, Bhavsar NV, Popat PR (2014) Gingival crevicular fluid levels of matrix metalloproteinase-1 (MMP-1) and tissue inhibitor of metalloproteinase-1 (TIMP-1) in periodontal health and disease. Singapore Dent J 35: 59-64. doi: 10.1016/j.sdj.2014.07.003
[38]	Ghodpage PS, Kolte RA, Kolte AP, et al. (2014) Influence of phase I periodontal therapy on levels of matrix metalloproteinase 1 and tissue inhibitor of metalloproteinase 1. Saudi Dent J 26: 171-175. doi: 10.1016/j.sdentj.2014.05.003
[39]	Beklen A (2017) Effects of IL-13 on TGF-β and MMP-1 in periodontitis. Biotech Histochem 92: 374-380. doi: 10.1080/10520295.2017.1312526
[40]	Nokhbehsaim M, Nogueira AVB, Damanaki A, et al. (2020) Regulation of matrix metalloproteinase-1 by filifactor alocis in human gingival and monocytic cells. Clin Oral Investig 24: 1987-1995. doi: 10.1007/s00784-019-03062-0
[41]	Sorsa T, Gursoy UK, Nwhator S, et al. (2016) Analysis of matrix metalloproteinases, especially MMP-8, in gingival creviclular fluid, mouthrinse and saliva for monitoring periodontal diseases. Periodontology 2000 70: 142-163. doi: 10.1111/prd.12101
[42]	Kraft-Neumärker M, Lorenz K, Koch R, et al. (2012) Full-mouth profile of active MMP-8 in periodontitis patients. J Periodontal Res 47: 121-128. doi: 10.1111/j.1600-0765.2011.01416.x
[43]	Sorsa T, Alassiri S, Grigoriadis A, et al. (2020) Active MMP-8 (AMMP-8) as a grading and staging biomarker in the periodontitis classification. Diagnostics (Basel) 10: 1-10.
[44]	Juurikka K, Butler GS, Salo T, et al. (2019) The role of MMP-8 in cancer: A systematic review. Int J Mol Sci 20: 1-27. doi: 10.3390/ijms20184506
[45]	Lenglet S, Mach F, Montecucco F (2013) Role of matrix metalloproteinase-8 in atherosclerosis. Mediat Inflamm 2013: 659282. doi: 10.1155/2013/659282
[46]	Yakob M, Kari K, Tervahartiala T, et al. (2012) Associations of periodontal microorganisms with salivary proteins and MMP-8 in gingival crevicular fluid. J Clin Periodontol 39: 256-263. doi: 10.1111/j.1600-051X.2011.01813.x
[47]	Honibald E, Mathew S, Padmanaban J, et al. (2012) Perioceutics: Matrix metalloproteinase inhibitors as an adjunctive therapy for inflammatory periodontal disease. J Pharm Bioallied Sci 4: 417-421. doi: 10.4103/0975-7406.100315
[48]	Leppilahti JM, Ahonen MM, Hernández M, et al. (2011) Oral rinse MMP-8 point-of-care immuno test identifies patients with strong periodontal inflammatory burden. Oral Dis 17: 115-122. doi: 10.1111/j.1601-0825.2010.01716.x
[49]	Rathnayake N, Gieselmann DR, Heikkinen A, et al. (2017) Salivary diagnostics point-of-care diagnostics of MMP-8 in dentistry and medicine. Diagnostics (Basel) 7: 7. doi: 10.3390/diagnostics7010007
[50]	Munhoz F, Branco F, Souza R, et al. (2019) MMP-13 polymorphism as a risk factor in implant loss. Int J Oral Maxillofac Implant 34: 768-771. doi: 10.11607/jomi.7057
[51]	Virtanen E, Yakob M, Tervahartiala T, et al. (2017) Salivary MMP-13 gender differences in periodontitis: A cross-sectional study from Sweden. Clin Exp Dent Res 3: 165-170. doi: 10.1002/cre2.76
[52]	Choi JY, Fuerst R, Knapinska AM, et al. (2017) Structure-based design and synthesis of potent and selective matrix metalloproteinase-13 inhibitors. J Med Chem 60: 5816-5825. doi: 10.1021/acs.jmedchem.7b00514
[53]	Stura EA, Visse R, Cuniasse P, et al. (2013) Crystal structure of full-length human collagenase 3 (MMP-13) with peptides in the active site defines exosites in the catalytic domain. FASEB J 27: 4395-4405. doi: 10.1096/fj.13-233601
[54]	Leppilahti JM, Hernández-Ríos PA, Gamonal JA, et al. (2014) Matrix metalloproteinases and myeloperoxidase in gingival crevicular fluid provide site-specific diagnostic value for chronic periodontitis. J Clin Periodontol 41: 348-356. doi: 10.1111/jcpe.12223
[55]	Gursoy UK, Könönen E, Huumonen S, et al. (2013) Salivary type i collagen degradation end-products and related matrix metalloproteinases in periodontitis. J Clin Periodontol 40: 18-25. doi: 10.1111/jcpe.12020
[56]	Aleksandrowicz P, Zelechowska P, Agier J, et al. (2017) Evaluation of metalloproteinase-8 levels in crevicular fluid of patients with healthy implants or periodontitis. Mediat Inflamm Article ID 4920847.
[57]	Pawar DD, Mehta DS (2015) Effect of phase 1 periodontal therapy on gingival crevicular fluid levels of matrix metalloproteinases-3 and -13 in chronic periodontitis patients. J Investig Clin Dent 6: 118-124. doi: 10.1111/jicd.12072
[58]	Räisänen IT, Sorsa T, Schoor G, et al. (2019) Active matrix metalloproteinase-8 Point-Of-Care (POC)/chairside mouthrinse test vs. bleeding on probing in diagnosing subclinical periodontitis in adolescents. Diagnostics 9: 6-11. doi: 10.3390/diagnostics9010034
[59]	Alassiri S, Parnanen P, Rathnayake N, et al. (2018) The ability of quantitative, specific, and sensitive point-of-care/chair-side oral fluid immunotests for aMMP-8 to detect periodontal and peri-implant diseases. Dis Markers Article ID 1306396.
[60]	Srivastava N, Nayak PA, Rana S (2017) Point of care- A novel approach to periodontal diagnosis-A review. J Clin Diagnostic Res 11: 1-6. doi: 10.1111/crj.12541
[61]	Räisänen I, Heikkinen A, Siren E, et al. (2018) Point-of-care/chairside aMMP-8 analytics of periodontal diseases' Activity and Episodic Progression. Diagnostics 8: 74. doi: 10.3390/diagnostics8040074
[62]	Heikkinen AM, Nwhator SO, Rathnayake N, et al. (2015) Pilot study on oral health status as assessed by an active matrix metalloproteinase-8 chairside mouthrinse test in adolescents. J Periodontol 87: 36-40. doi: 10.1902/jop.2015.150377
[63]	Raivisto T, Sorsa T, Räisänen I, et al. (2020) Active matrix metalloproteinase-8 chair side mouth rinse test, health behaviour and oral Health in finnish adolescent cohort. J Clin Diagnostic Res 35-39.
[64]	Rautava J, Gursoy U, Kullstrom A, et al. (2020) An oral rinse active matrix metalloproteinase-8 point-of-care immunotest may be less accurate in patients with crohn's disease. Biomolecules 10: 395. doi: 10.3390/biom10030395
[65]	Pajnigara NG, Kolte AP, Kolte RA, et al. (2016) Chair side diagnostic kits in periodontics. IDJSR 4: 25-31.
[66]	Hamodat HF, Taha MYM (2020) Estimation of salivary MMP-8, MMP-9, MMP-13 and TIMP-1 in chronic periodontitis in Mosul. IJDSR 8: 22-26.
[67]	Özcan E, Işıl Saygun N, Serdar MA, et al. (2016) Non-surgical periodontal therapy reduces saliva adipokine and matrix metalloproteinase levels in periodontitis. J Periodontol 87: 934-943. doi: 10.1902/jop.2016.160046
[68]	Keles Yucel ZP, Afacan B, Emingil G, et al. (2020) Local and systemic levels of aMMP-8 in gingivitis and stage 3 grade C periodontitis. J Periodontal Res 1-8.
[69]	Sorsa T, Hernández M, Leppilahti J, et al. (2010) Detection of gingival crevicular fluid MMP-8 levels with different laboratory and chair-side methods. Oral Dis 16: 39-45. doi: 10.1111/j.1601-0825.2009.01603.x
[70]	Gonçalves PF, Huang H, McAninley S, et al. (2013) Periodontal treatment reduces matrix metalloproteinase levels in localized aggressive periodontitis. J Periodontol 84: 1801-1808. doi: 10.1902/jop.2013.130002
[71]	Leppilahti JM, Kallio MA, Tervahartiala T, et al. (2014) Gingival crevicular fluid matrix metalloproteinase-8 levels predict treatment outcome among smokers with chronic periodontitis. J Periodontol 85: 250-260. doi: 10.1902/jop.2013.130156

Reader Comments

Your name:*

Email:*
© 2021 the Author(s), licensee AIMS Press. This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0)