Classification, regulation of activity, and genetic polymorphism of matrix metalloproteinases in health and disease

Cover Page


Cite item

Full Text

Abstract

Matrix metalloproteinases (MMPs) are a family of zinc-containing endopeptidases that catalyze the degradation reactions of the extracellular matrix components. In humans, 23 enzymes of this family are known, which are subdivided into 6 groups based on their structure and substrate types: collagenases, gelatinases, stromelysins, matrilizines, MMP membrane type and other MMPs. MMP functions are diverse, and an imbalance of their activity may be one of the etiological factors of various diseases. The review considers classification, regulation of activity and genetic polymorphism of matrix metalloproteinases in health and in various pathological processes in the human body. A list of the most studied polymorphic variants of MMP genes is given, their functional effects are described and the results of associative studies are presented.

About the authors

A. S. Shadrina

Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of Russian Academy of Sciences

Author for correspondence.
Email: weiner.alexserg@gmail.com

PhD (in Biology), Junior Researcher, Laboratory of Pharmacogenomics

8 Akademika Lavrent'eva prosp., Novosibirsk, 630090, Russian Federation. Tel.: +7 (383) 363 51 71

Russian Federation

Ya. Z. Plieva

Moscow State University of Medicine and Dentistry named after A.I. Evdokimov

Email: fake@neicon.ru

PhD Student, Chair of Clinical Biochemistry and Laboratory Diagnostics

20–1 Delegatskaya ul., Moscow, 127473, Russian Federation

Russian Federation

D. N. Kushlinskiy

N.N. Blokhin Russian Cancer Research Center

Email: fake@neicon.ru

MD, PhD, Surgeon/Gynecologist

24 Kashirskoe shosse, Moscow, 115478, Russian Federation

Russian Federation

A. A. Morozov

Moscow State University of Medicine and Dentistry named after A.I. Evdokimov

Email: fake@neicon.ru

PhD Student, Chair of Clinical Biochemistry and Laboratory Diagnostics

20–1 Delegatskaya ul., Moscow, 127473, Russian Federation

Russian Federation

M. L. Filipenko

Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of Russian Academy of Sciences

Email: fake@neicon.ru

PhD (in Biology), Head of Laboratory of Pharmacogenomics

8 Akademika Lavrent'eva prosp., Novosibirsk, 630090, Russian Federation

Russian Federation

V. L. Chang

Moscow State University of Medicine and Dentistry named after A.I. Evdokimov

Email: fake@neicon.ru

PhD Student, Chair of Clinical Biochemistry and Laboratory Diagnostics

20–1 Delegatskaya ul., Moscow, 127473, Russian Federation

Russian Federation

N. E. Kushlinskii

N.N. Blokhin Russian Cancer Research Center

Email: fake@neicon.ru

MD, PhD, Professor, Member-Correspondent of Russian Academy of Sciences, Head of Clinical Biochemistry Laboratory

24 Kashirskoe shosse, Moscow, 115478, Russian Federation

Russian Federation

References

  1. Verma RP, Hansch C. Matrix metalloproteinases (MMPs): chemical-biological functions and (Q) SARs. Bioorg Med Chem. 2007;15(6): 2223–68.
  2. Raffetto JD, Khalil RA. Matrix metalloproteinases and their inhibitors in vascular remodeling and vascular disease. Biochem Pharmacol. 2008;75(2): 346–59.
  3. Visse R, Nagase H. Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry. Circ Res. 2003;92(8): 827–39.
  4. Page-McCaw A, Ewald AJ, Werb Z. Matrix metalloproteinases and the regulation of tissue remodelling. Nat Rev Mol Cell Biol. 2007;8(3): 221–33.
  5. Nagase H, Visse R, Murphy G. Structure and function of matrix metalloproteinases and TIMPs. Cardiovasc Res. 2006;69(3): 562–73.
  6. McCawley LJ, Matrisian LM. Matrix metalloproteinases: they're not just for matrix anymore! Curr Opin Cell Biol. 2001;13(5): 534–40.
  7. Cieplak P, Strongin AY. Matrix metalloproteinases – From the cleavage data to the prediction tools and beyond. Biochim Biophys Acta. 2017. pii: S0167-4889(17)30064-2. doi: 10.1016/j.bbamcr.2017.03.010.
  8. Li J, Wang JM, Liu YH, Zhang Z, Han N, Wang JY, Xue SH, Wang P. Effect of microRNA- 106b on the invasion and proliferation of trophoblasts through targeting MMP-2. Zhonghua Fu Chan Ke Za Zhi. 2017;52(5): 327–332. doi: 10.3760/cma.j.issn.0529-567X.2017.05.007.
  9. Yang L, Song X, Zhu J, Li M, Ji Y, Wu F, Chen Y, Cui X, Hu J, Wang L, Cao Y, Wei Y, Zhang W, Li F. Tumor suppressor microRNA-34a inhibits cell migration and invasion by targeting MMP- 2/MMP-9/FNDC3B in esophageal squamous cell carcinoma. Int J Oncol. 2017;51(1): 378–88. doi: 10.3892/ijo.2017.4015.
  10. Yan C, Boyd DD. Regulation of matrix metalloproteinase gene expression. J Cell Physiol. 2007;211(1): 19–26.
  11. Chen Q, Jin M, Yang F, Zhu J, Xiao Q, Zhang L. Matrix metalloproteinases: inflammatory regulators of cell behaviors in vascular formation and remodeling. Mediators Inflamm. 2013;2013:928315. doi: 10.1155/2013/928315.
  12. Chase AJ, Newby AC. Regulation of matrix metalloproteinase (matrixin) genes in blood vessels: a multi-step recruitment model for pathological remodelling. J Vasc Res. 2003;40(4): 329–43.
  13. Levin M, Udi Y, Solomonov I, Sagi I. Next Generation Matrix Metalloproteinase Inhibitors – Novel Strategies Bring New Prospects. Biochim Biophys Acta. 2017. pii: S0167- 4889(17)30161- 1. doi: 10.1016/j.bbamcr.2017.06.009.
  14. Freitas-Rodríguez S, Folgueras AR, López-Otín C. The role of matrix metalloproteinases in aging: Tissue remodeling and beyond. Biochim Biophys Acta. 2017. pii: S0167- 4889(17)30118-0. doi: 10.1016/j.bbamcr.2017.05.007.
  15. Cheng Z, Limbu MH, Wang Z, Liu J, Liu L, Zhang X, Chen P, Liu B. MMP-2 and 9 in Chronic Kidney Disease. Int J Mol Sci. 2017;18(4). pii: E776. doi: 10.3390/ijms18040776.
  16. Герштейн ЕС, Огнерубов НА, Кушлинский НЕ. Ассоциированные с опухолью протеазы и их тканевые ингибиторы. В: Кушлинский НЕ, Красильников МА, ред. Биологические маркеры опухолей: фундаментальные и клинические исследования. М.: Издательство РАМН; 2017. с. 197–230.
  17. Кушлинский НЕ, Герштейн ЕС. Матриксные металлопротеиназы и компоненты системы активации плазминогена в патогенезе и клиническом течении рака толстой кишки. Патогенез. 2013;11(3): 4–12.
  18. Кушлинский НЕ, Бабкина ИВ, Кузнецов ИН, Короткова ЕА, Тен ЕА, Булычева ИВ, Соловьев ЮН, Алиев МД. Ассоциированные с опухолью матриксные металлопротеиназы в сыворотке крови больных первичными саркомами костей. Молекулярная медицина. 2014;(1): 43–6.
  19. Герштейн ЕС, Муштенко ВВ, Короткова ЕА, Бежанова СД, Морозов АА, Алферов АА, Казанцева ИА, Кушлинский НЕ. Матриксные металлопротеиназы-2, 7, 8, 9 и их тканевой ингибитор 1-го типа в сыворотке крови больных раком почки: клинико- морфологические корреляции. Альманах клинической медицины. 2017;45(2): 94–101. doi: 10.18786/2072-0505-2017-45-2-94-101.
  20. Bui TP, Hoang AN, Le PL, Pham BT, Nguyen LTT, Do HM, Ta TV, Trinh TH. Matrix metalloproteinases in Vietnamese patients with colorectal cancer. Oncol Lett. 2017;13(4): 2097–2104. doi: 10.3892/ol.2017.5680.
  21. Miao C, Liang C, Zhu J, Xu A, Zhao K, Hua Y, Zhang J, Chen W, Suo C, Zhang C, Liu Y, Su S, Wang Z. Prognostic role of matrix metalloproteinases in bladder carcinoma: a systematic review and meta-analysis. Oncotarget. 2017;8(19): 32309–21. doi: 10.18632/oncotarget.15907.
  22. Wu S, Ma C, Shan S, Zhou L, Li W. High expression of matrix metalloproteinases 16 is associated with the aggressive malignant behavior and poor survival outcome in colorectal carcinoma. Sci Rep. 2017;7:46531. doi: 10.1038/srep46531.
  23. Merchant N, Nagaraju GP, Rajitha B, Lammata S, Jella KK, Buchwald ZS, Lakka SS, Ali AN. Matrix metalloproteinases: their functional role in lung cancer. Carcinogenesis. 2017. doi: 10.1093/carcin/bgx063.
  24. Hieronimus B, Pfohl J, Busch C, Graeve L. Expression and Characterization of Membrane- Type 4 Matrix Metalloproteinase (MT4- MMP) and its Different Forms in Melanoma. Cell Physiol Biochem. 2017;42(1): 198–210. doi: 10.1159/000477311.
  25. Juchniewicz A, Kowalczuk O, Milewski R, Laudański W, Dzięgielewski P, Kozłowski M, Nikliński J. MMP-10, MMP-7, TIMP-1 and TIMP- 2 mRNA expression in esophageal cancer. Acta Biochim Pol. 2017;64(2): 295–9. doi: 10.18388/abp.2016_1408.
  26. Amar S, Minond D, Fields GB. Clinical implications of compounds designed to inhibit ECM-modifying metalloproteinases. Proteomics. 2017. doi: 10.1002/pmic.201600389.
  27. Rutter JL, Mitchell TI, Butticè G, Meyers J, Gusella JF, Ozelius LJ, Brinckerhoff CE. A single nucleotide polymorphism in the matrix metalloproteinase- 1 promoter creates an Ets binding site and augments transcription. Cancer Res. 1998;58(23): 5321–5.
  28. Trombone AP, Cavalla F, Silveira EM, Andreo CB, Francisconi CF, Fonseca AC, Letra A, Silva RM, Garlet GP. MMP1-1607 polymorphism increases the risk for periapical lesion development through the upregulation MMP-1 expression in association with pro- inflammatory milieu elements. J Appl Oral Sci. 2016;24(4): 366–75. doi: 10.1590/1678-775720160112.
  29. Sri Manjari K, Nallari P, Balakrishna N, Vidyasagar A, Prabhakar B, Jyothy A, Venkateshwari A. Influence of matrix metalloproteinase-1 gene -1607 (1G/2G) (rs1799750) promoter polymorphism on circulating levels of MMP-1 in chronic pancreatitis. Biochem Genet. 2013;51(7–8): 644–54. doi: 10.1007/s10528-013-9594-9.
  30. Huang HL, Wu S, Hsu LA, Teng MS, Lin JF, Sun YC, Ko YL. Genetic variants associated with circulating MMP1 levels near matrix metalloproteinase genes on chromosome 11q21-22 in Taiwanese: interaction with obesity. BMC Med Genet. 2013;14:30. doi: 10.1186/1471-2350-14-30.
  31. Yang H, Liu J, Fan Y, Guo Q, Ge L, Yu N, Zheng X, Dou Y, Zheng S. Associations between various possible promoter polymorphisms of MMPs genes and endometriosis risk: a meta- analysis. Eur J Obstet Gynecol Reprod Biol. 2016;205:174–88. doi: 10.1016/j.ejogrb.2016.08.015.
  32. He M, Wang W, Han X, Huang W. Matrix metalloproteinase-1 rs1799750 polymorphism and glaucoma: A meta-analysis. Ophthalmic Genet. 2017;38(3): 211–6. doi: 10.1080/13816810.2016.1193877.
  33. Micheal S, Yousaf S, Khan MI, Akhtar F, Islam F, Khan WA, den Hollander AI, Qamar R, Ahmed A. Mol Vis. 2013;19:441–7.
  34. Montes AH, Valle-Garay E, Alvarez V, Pevida M, García Pérez E, Paz J, Meana A, Asensi V. A functional polymorphism in MMP1 could influence osteomyelitis development. J Bone Miner Res. 2010;25(4): 912–9. doi: 10.1359/jbmr.091013.
  35. Checa M, Ruiz V, Montaño M, Velázquez-Cruz R, Selman M, Pardo A. MMP-1 polymorphisms and the risk of idiopathic pulmonary fibrosis. Hum Genet. 2008;124(5): 465– 72. doi: 10.1007/s00439-008-0571-z.
  36. Pei JS, Hsu PC, Chou AK, Tsai CW, Chang WS, Hsiao CL, Hsu YN, Cheng SP, Bau DT. Matrix Metalloproteinase-1 Genotype Contributes to the Risk of Non-solid Tumor in Childhood Leukemia. Anticancer Res. 2016;36(10): 5127–32.
  37. Han G, Wei Z, Lu Z, Cui H, Bai X, Ge H, Zhang W. Association between matrix metalloproteinase 1 -1607 1G>2G polymorphism and cancer risk: a meta-analysis including 19706 subjects. Int J Clin Exp Med. 2014;7(9): 2992–9.
  38. Ricketts C, Zeegers MP, Lubinski J, Maher ER. Analysis of germline variants in CDH1, IGFBP3, MMP1, MMP3, STK15 and VEGF in familial and sporadic renal cell carcinoma. PLoS One. 2009;4(6):e6037. doi: 10.1371/journal.pone.0006037.
  39. Peng Q, Xu Y. Association between promoter polymorphisms of matrix metalloproteinase-1 and risk of gastric cancer. Onco Targets Ther. 2015;8:2519–26. doi: 10.2147/OTT.S83004.
  40. Liu D, Duan W, Guo H, Xu X, Bai Y. Meta-analysis of associations between polymorphisms in the promoter regions of matrix metalloproteinases and the risk of colorectal cancer. Int J Colorectal Dis. 2011;26(9): 1099–105. doi: 10.1007/s00384-011-1198-4.
  41. Yan Y, Liang H, Li T, Li M, Li R, Qin X, Li S. The MMP-1, MMP-2, and MMP-9 gene polymorphisms and susceptibility to bladder cancer: a meta-analysis. Tumour Biol. 2014;35(4): 3047–52. doi: 10.1007/s13277-013-1395-6.
  42. Yu C, Zhou Y, Miao X, Xiong P, Tan W, Lin D. Functional haplotypes in the promoter of matrix metalloproteinase-2 predict risk of the occurrence and metastasis of esophageal cancer. Cancer Res. 2004;64(20): 7622–8.
  43. Yari K, Rahimi Z, Moradi MT, Rahimi Z. The MMP-2 -735 C allele is a risk factor for susceptibility to breast cancer. Asian Pac J Cancer Prev. 2014;15(15): 6199–203.
  44. Zhou G, Zhai Y, Cui Y, Qiu W, Yang H, Zhang X, Dong X, He Y, Yao K, Zhang H, Peng Y, Yuan X, Zhi L, Zhang X, He F. Functional polymorphisms and haplotypes in the promoter of the MMP2 gene are associated with risk of nasopharyngeal carcinoma. Hum Mutat. 2007;28(11): 1091–7.
  45. Price SJ, Greaves DR, Watkins H. Identification of novel, functional genetic variants in the human matrix metalloproteinase-2 gene: role of Sp1 in allele-specific transcriptional regulation. J Biol Chem. 2001;276(10): 7549–58.
  46. Belo VA, Luizon MR, Carneiro PC, Gomes VA, Lacchini R, Lanna CM, Souza-Costa DC, Tanus- Santos JE. Effect of metabolic syndrome risk factors and MMP-2 genetic variations on circulating MMP-2 levels in childhood obesity. Mol Biol Rep. 2013;40(3): 2697–704. doi: 10.1007/s11033-012-2356-7.
  47. Kurzawski M, Modrzejewski A, Pawlik A, Droździk M. Polymorphism of matrix metalloproteinase genes (MMP1 and MMP3) in patients with varicose veins. Clin Exp Dermatol. 2009;34(5): 613–7. doi: 10.1111/j.1365-2230.2008.03166.x.
  48. Ye S, Eriksson P, Hamsten A, Kurkinen M, Humphries SE, Henney AM. Progression of coronary atherosclerosis is associated with a common genetic variant of the human stromelysin- 1 promoter which results in reduced gene expression. J Biol Chem. 1996;271(22): 13055–60.
  49. Morris DR, Biros E, Cronin O, Kuivaniemi H, Golledge J. The association of genetic variants of matrix metalloproteinases with abdominal aortic aneurysm: a systematic review and meta- analysis. Heart. 2014;100(4): 295–302. doi: 10.1136/heartjnl-2013-304129.
  50. Ma AJ, Fan LY, Li WJ, Zhao HQ, Han Y, Jiang XS, Yi P, Li CL, Song S, Ma CL, Yao RY, Pan XD. Association of matrix metalloproteinase-3 gene polymorphisms with subtypes of ischemic stroke. Zhonghua Yi Xue Yi Chuan Xue Za Zhi. 2013;30(4): 461–6. doi: 10.3760/cma.j.issn.1003-9406.2013.04.018.
  51. Abd-Allah SH, Shalaby SM, Pasha HF, El-Shal AS, Abou El-Saoud AM. Variation of matrix metalloproteinase 1 and 3 haplotypes and their serum levels in patients with rheumatoid arthritis and osteoarthritis. Genet Test Mol Biomarkers. 2012;16(1): 15–20. doi: 10.1089/gtmb.2011.0003.
  52. Huang R, Deng L, Shen A, Liu J, Ren H, Xu DL. Associations of MMP1, 3, 9 and TIMP3 genes polymorphism with isolated systolic hypertension in Chinese Han population. Int J Med Sci. 2013;10(7): 840–7. doi: 10.7150/ijms.5728.
  53. Kesh K, Subramanian L, Ghosh N, Gupta V, Gupta A, Bhattacharya S, Mahapatra NR, Swarnakar S. Association of MMP7 -181AG Promoter Polymorphism with Gastric Cancer Risk: Influence of Nicotine in Differential Allele- Specific Transcription via Increased Phosphorylation of cAMP-Response Element-Binding Protein (CREB). J Biol Chem. 2015;290(23): 14391–406. doi: 10.1074/jbc.M114.630129.
  54. Kazantseva MG, Hung NA, Highton J, Hessian PA. MMP expression in rheumatoid inflammation: the rs11568818 polymorphism is associated with MMP-7 expression at an extra-articular site. Genes Immun. 2013;14(3): 162–9. doi: 10.1038/gene.2012.65.
  55. Richards TJ, Park C, Chen Y, Gibson KF, Peter Di Y, Pardo A, Watkins SC, Choi AM, Selman M, Pilewski J, Kaminski N, Zhang Y. Allele-specific transactivation of matrix metalloproteinase 7 by FOXA2 and correlation with plasma levels in idiopathic pulmonary fibrosis. Am J Physiol Lung Cell Mol Physiol. 2012;302(8):L746–54. doi: 10.1152/ajplung.00319.2011.
  56. Fang WL, Liang WB, Gao LB, Zhou B, Xiao FL, Zhang L. Genetic polymorphisms in Matrix Metalloproteinases -1 and -7 and susceptibility to gastric cancer: an association study and meta-analysis. Iran J Allergy Asthma Immunol. 2013;12(3): 203–10.
  57. Yi YC, Chou PT, Chen LY, Kuo WH, Ho ES, Han CP, Yang SF. Matrix metalloproteinase-7 (MMP-7) polymorphism is a risk factor for endometrial cancer susceptibility. Clin Chem Lab Med. 2010;48(3): 337–44. doi: 10.1515/CCLM.2010.082.
  58. Manjari KS, Jyothy A, Kumar PS, Prabhakar B, Nallari P, Venkateshwari A. Association of matrix metalloproteinase-7 (-181A/G) promoter polymorphism in chronic pancreatitis. Indian J Med Res. 2014;140(5): 609–15.
  59. Eeles RA, Olama AA, Benlloch S, Saunders EJ, Leongamornlert DA, Tymrakiewicz M, Ghoussaini M, Luccarini C, Dennis J, Jugurnauth-Little S, Dadaev T, Neal DE, Hamdy FC, Donovan JL, Muir K, Giles GG, Severi G, Wiklund F, Gronberg H, Haiman CA, Schumacher F, Henderson BE, Le Marchand L, Lindstrom S, Kraft P, Hunter DJ, Gapstur S, Chanock SJ, Berndt SI; UK ProtecT (Prostate PRACTICAL (Prostate Cancer Association Group to Investigate Cancer-Associated Alterations in the Genome) Consortium, Kote-Jarai Z, Easton DF. Identification of 23 new prostate cancer susceptibility loci using the iCOGS custom genotyping array. Nat Genet. 2013;45(4): 385–91, 391e1–2. doi: 10.1038/ng.2560.
  60. Zhang B, Ye S, Herrmann SM, Eriksson P, de Maat M, Evans A, Arveiler D, Luc G, Cambien F, Hamsten A, Watkins H, Henney AM. Functional polymorphism in the regulatory region of gelatinase B gene in relation to severity of coronary atherosclerosis. Circulation. 1999;99(14): 1788–94.
  61. Mahmoodi K, Kamali K, Karami E, Soltanpour MS. Plasma concentration, genetic variation, and gene expression levels of matrix metalloproteinase 9 in Iranian patients with coronary artery disease. J Res Med Sci. 2017;22:8. doi: 10.4103/1735-1995.199088.
  62. Kukkonen MK, Tiili E, Vehmas T, Oksa P, Piirilä P, Hirvonen A. Association of genes of protease-antiprotease balance pathway to lung function and emphysema subtypes. BMC Pulm Med. 2013;13:36. doi: 10.1186/1471-2466-13-36.
  63. Rodríguez-Pérez JM, Vargas-Alarcón G, Posadas-Sánchez R, Zagal-Jiménez TX, Ortíz- Alarcón R, Valente-Acosta B, Tovilla- Zárate C, Nostroza-Hernández C, Pérez-Méndez O, Pérez-Hernández N. rs3918242 MMP9 gene polymorphism is associated with myocardial infarction in Mexican patients. Genet Mol Res. 2016;15(1): 15017776. doi: 10.4238/gmr.15017776.
  64. He T, Wang J, Wang XL, Deng WS, Sun P. Association between the Matrix Metalloproteinase- 9 rs3918242 Polymorphism and Ischemic Stroke Susceptibility: A Meta- Analysis. J Stroke Cerebrovasc Dis. 2017;26(5): 1136–43. doi: 10.1016/j.jstrokecerebrovasdis.2016.12.036.
  65. Jiang S, Yang ZH, Chen YY, He Z, Zhou Y, Gao Y, Zhang Q, Tan MQ. MMP-9 genetic polymorphism may confer susceptibility to COPD. Genet Mol Res. 2016;15(2). doi: 10.4238/gmr.15026272.
  66. Qin LM, Qin GM, Shi XH, Wang AL, Zuo H. Association between matrix metalloproteinase-9 rs3918242 polymorphism and development of coronary artery disease in a Chinese population. Genet Mol Res. 2016;15(2). doi: 10.4238/gmr.15027632.
  67. Singh K, Agrawal NK, Gupta SK, Singh K. A functional single nucleotide polymorphism -1562C>T in the matrix metalloproteinase- 9 promoter is associated with type 2 diabetes and diabetic foot ulcers. Int J Low Extrem Wounds. 2013;12(3): 199–204. doi: 10.1177/1534734613493289.
  68. Goncharov SV, Gurianova VL, Stroy DO, Drevytska TI, Kaplinskii SP, Nastenko EA, Litvinenko M, Terletskiy RV, Khaitovych MV, Moibenko OO, Dosenko VE. Genetic predisposition to essential hypertension in children: analysis of 17 single nucleotide polymorphisms. Fiziol Zh. 2013;59(6): 12–24.
  69. Jormsjö S, Ye S, Moritz J, Walter DH, Dimmeler S, Zeiher AM, Henney A, Hamsten A, Eriksson P. Allele-specific regulation of matrix metalloproteinase-12 gene activity is associated with coronary artery luminal dimensions in diabetic patients with manifest coronary artery disease. Circ Res. 2000;86(9): 998–1003.
  70. Chen SS, Song J, Tu XY, Zhao JH, Ye XQ. The association between MMP-12 82 A/G polymorphism and susceptibility to various malignant tumors: a meta-analysis. Int J Clin Exp Med. 2015;8(7): 10845–54.
  71. Шевела АИ, Новак ЕВ, Серяпина ЮВ, Морозов ВВ, Воронина ЕН. Полиморфные варианты генов матриксных металлопротеиназ и VEGF – предикторы варикозной болезни? Фундаментальные исследования. 2014;(10-7): 1399–403.
  72. Van Nguyen S, Skarstedt M, Löfgren S, Zar N, Andersson RE, Lindh M, Matussek A, Dimberg J. Gene polymorphism of matrix metalloproteinase- 12 and -13 and association with colorectal cancer in Swedish patients. Anticancer Res. 2013;33(8): 3247–50.
  73. Manetti M, Ibba-Manneschi L, Fatini C, Guiducci S, Cuomo G, Bonino C, Bazzichi L, Liakouli V, Giacomelli R, Abbate R, Bombardieri S, Montecucco C, Valentini G, Matucci- Cerinic M. Association of a functional polymorphism in the matrix metalloproteinase-12 promoter region with systemic sclerosis in an Italian population. J Rheumatol. 2010;37(9): 1852–7. doi: 10.3899/jrheum.100237.
  74. Haq I, Chappell S, Johnson SR, Lotya J, Daly L, Morgan K, Guetta-Baranes T, Roca J, Rabinovich R, Millar AB, Donnelly SC, Keatings V, MacNee W, Stolk J, Hiemstra PS, Miniati M, Monti S, O'Connor CM, Kalsheker N. Association of MMP-2 polymorphisms with severe and very severe COPD: a case control study of MMPs-1, 9 and 12 in a European population. BMC Med Genet. 2010;11:7. doi: 10.1186/1471-2350-11-7.
  75. Yoon S, Kuivaniemi H, Gatalica Z, Olson JM, Butticè G, Ye S, Norris BA, Malcom GT, Strong JP, Tromp G. MMP13 promoter polymorphism is associated with atherosclerosis in the abdominal aorta of young black males. Matrix Biol. 2002;21(6): 487–98.
  76. Shi M, Xia J, Xing H, Yang W, Xiong X, Pan W, Han S, Shang J, Zhou C, Zhou L, Yang M. The Sp1-mediaded allelic regulation of MMP13 expression by an ESCC susceptibility SNP rs2252070. Sci Rep. 2016;6:27013. doi: 10.1038/srep27013.
  77. Tannure PN, Küchler EC, Falagan-Lotsch P, Amorim LM, Raggio Luiz R, Costa MC, Vieira AR, Granjeiro JM. MMP13 polymorphism decreases risk for dental caries. Caries Res. 2012;46(4): 401–7. doi: 10.1159/000339379.
  78. Fernandez-Cadenas I, Mendioroz M, Domingues-Montanari S, Del Rio-Espinola A, Delgado P, Ruiz A, Hernandez-Guillamon M, Giralt D, Chacon P, Navarro-Sobrino M, Ribo M, Molina CA, Alvarez-Sabin J, Rosell A, Montaner J. Leukoaraiosis is associated with genes regulating blood-brain barrier homeostasis in ischaemic stroke patients. Eur J Neurol. 2011;18(6): 826–35. doi: 10.1111/j.1468-1331.2010.03243.x.
  79. Hu J, Pan J, Luo ZG. MMP1 rs1799750 single nucleotide polymorphism and lung cancer risk: a meta-analysis. Asian Pac J Cancer Prev. 2012;13(12): 5981–4.

Supplementary files

Supplementary Files
Action
1. JATS XML
Download

Copyright (c) 2017 Shadrina A.S., Plieva Y.Z., Kushlinskiy D.N., Morozov A.A., Filipenko M.L., Chang V.L., Kushlinskii N.E.

Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 International License.

This website uses cookies

You consent to our cookies if you continue to use our website.

About Cookies