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Matrix metalloproteinases and cardiovascular diseases

https://doi.org/10.18705/1607-419X-2009-15-5-532-538

Abstract

The paper reviews the role of matrix metalloproteinases of proteolytic system that perform a great variety of function and control almost all biological processes. According to the classification all proteases are divided into four families serine, cysteine, aspartate and metalloproteinases (last also called matrix metalloproteinases (MMP)). Up to now 28 MMP are known (from MMP-1 to MMP-28). Based on structural features and substrate specificity MMP family was divided into identified 4 subfamilies: collagenases, gelatinases. stromelizines and unclassified MMP. Study of MMP family in cardiology significantly expands the understanding of the pathogenetic mechanisms of cardiovascular diseases and demonstrates different MMPs functions: stromelizine MMP-3, collagenase - MMP-8, gelatinase - MMP-9. It is assumed that MMP-3 and MMP-9 play an important role in acute myocardial infarction, unstable angina, rehabilitation after a heart attack, left ventricular remodeling. There are data of special role of MMP-3, MMP-9 gene polymorphism associated with susceptibility to cardiovascular disease, atherosclerosis of the arteries, heart attack, aneurysm of the aorta. However, role of MMP-2, MMP-7 and unclassified MMPs in cardiac pathology is not well investigated and remains controversial.

About the Authors

A. A. Tourna
FGUZ Clinical Hospital № 83 FMBA, Moscow, Russia
Russian Federation


R. T. Toguzov
GOU VPO RGMU FUB Department of Clinical Laboratory Diagnostics, Moscow, Russia
Russian Federation


References

1. Яровая Г.А. Биорегулируюшие функции и патогенетическая роль протеолиза. Современные представления и перспективы // Лаб. медицина. - 2000. - Т. 3. - С. 19-22.

2. Rawlings N.D. Barren A.J. Classification of peptidases by comparison of primary and tertiary structures. - Biomed. Health Res. - 1997. Mri.13. -P. 13-21.

3. Rawlings N.D., Barrett A.J. Evolutionary families of metallopeptidases // Meth. Enzymol. - 1995. - Vol. 248. - P. 183 -228.

4. Barrett A.J. Evolution and tlic structural classification of peptidases // Biomed. Health Res. - 1997. - Vol. 13. - P. 3-12.

5. Gross J., Lapiere C.M. Collagenolytic activity in amphibian tissues: atissue culture assay // Proc. Natl. Acad. Sci. USA. - 1962. - Vol. 48. - Р. 1014-1022.

6. Chow A.K., Cena J., Schul/ R. Acute actions and novel targets of matrix metalloproteinases in the heart and vasculature // Brit. J. Pharmacol. - 2007. - Vol. 152. № 2. - P. 189-205.

7. Creemers E.J.M., Cleutjens J.P.M., Smits J.F.M., Daemen M.J.A.P. Matrix metalloproteinase inhibition after myocardial infarction // Circ. Res. - 2001. - Vol. 89, № 3. - P. 201-210.

8. Davis L.S. A question of transformation. The synovial fibroblast in rheumatoid arthritis // Am. J. Pathol. - 2003. - Vol. 162. - № 5. - P. 1399-1402.

9. Hooper N.M. Families of zinc metalloproteases // FEBS Lett. 1994. - Vol. 354. - № 1. - P. 1-6.

10. Woessncr J.F.Jr. Matrix metalloproteinases and their inhibitors in connective tissue remodeling. FASFB J. - 1991. - Vol. 5, № 8, - P. 2145-2154.

11. Hidalgo M., Eckhardt G.S. Development of matrix metalloproteinase inhibitors in cancer therapy // J. Nation. Cancer Inst. - 2001. - Vol. 93, № 3, - Р. 178-193.

12. Close D.R. Matrix metalloproteinase inhibitors in rheumatic diseases // Ann. Rheum. Dis. - 2001. - Vol. 60, № 3. - P. 62-67.

13. Яровая Г.А. Биорегулируюшие функции и патогенезитческая роль протеолиза. Распространение, классификация и основы механизма действия протеиназ // Лаб. медицина. - 2001. - Т. 4. - С. 75-80.

14. Brinckerhoff C.E. Joint destruction in arthritis: metalloproteinase in the spotlight // Arthritis Rheum. - 1991. - Vol. 34. - P. 1073-1075.

15. Davies M.J. Reactive oxygen species, metalloproteinases, and plaque stability // Circulation. - 1998. - Vol. 97, № 24. - P. 2382-2383.

16. Li J., Schwimmbeck P.L. Tschope C. et al. Collagen degradation in a murine myocarditis model: relevance of matrix metalloproteinase in association with inflammatory induction //Cardiovasc. Res. - 2002. - Vol. 56, № 2. - P. 235-247.

17. Woessner J.F. Jr. Role of matrix proteases in processing enamel proteins It Connect. Tissue Res. - 1998. - Vol. 39, № 1-3. - P. 69-73.

18. Kleiner D.E., Steller-Stevcnson W.G. Matrix metalloproteinases and metastasis // Cancer Chemother. Pharmacol. - 1999. - Vol. 43 (Suppl.). - P. 42-51.

19. Nagase H. Activation mechanisms of matrix metalloproteinases // BioI.Chem. - 1997. - Vol. 378, №3-4. - P. 151-160.

20. Rudek M.A., Figg W.D., Dyer V. et al. Phase I clinical trial of oral COL 3. - a matrix metalloproteinase inhibitor, in patients with refractory metastatic cancer // J. Clin. Oncol. - 2001. - Vol. 19, № 2. - P. 584-592.

21. Iloekslra R. Hskens F.A.L.M., Verweij J. Matrix metalloproteinase inhibitors: current developments and future perspectives // The Oncologist. - 2001. - Vol. 6, № 5. - P. 415- 427.

22. Kim I.I.E., Dalai S.S., Young E. et al. Disruption of the myocardial extracellular matrix leads to cardiac dysfunction // J. Clin. Invest. 2000. - Vol. 106. - P. 857-866.

23. Mohammed P.P., Smookler D.S. Metalloproteinases, inflammation, and rheumatoid arthritis // Ann. Rheum. Dis., 2003. - Vol. 62, № 2. - P. 1143-1147.

24. Montfort I., Perez-Tamayo R. The distribution of collagenase in normal rat tissues // J. Histochem. Cytochcm. - 1975. - Vol. 23, № 12. - P. 910-920.

25. Cleutjens J.P.M., Kandala J.C., Guarda E. et al. Regulation of collagen degradation in the rat myocardium after infarction // J. Mol. Cell. Cardiol. - 1994. - Vol. 27, № 6. - P. 1281-1292.

26. Galis Z.S., Sukhova G.K., Lark M.W, Increased expression of matrix melalloproteinaseand matrix degrading activity in vulnerable regions of human atherosclerotic plaques // J. Clin. Invest. - 1994. - Vol. 94, № 6. - P. 2493-2503.

27. Loftus I.M., NaylorA.R., Goodall S. et al. Increased matrix MMP9 activity in unstable carotid plaques: a potential role in acute plaque disruption // Stroke. - 2000. - Vol. 31, № 1. - P. 40-47.

28. Tyagi S.C., Matsubara L., Weber K.T. Direct extraction and estimation of collagcnase(s) activity by zymography in microquantities of rat myocardium and uterus // Clin. Biochem. - 1993. - Vol. 26, № 3. - P. 191-198.

29. Nagase H., Barrett A.J., Woessncr J.F. Nomenclature and glossary of the matrix metalloproteinases // Matrix Suppl. - 1992. - Vol. 1. - P. 421-424.

30. Saffarian S., Collier I.E., Manner B.L. et al. Interstitial col-lagenase is a Brownian ratchet driven by proteolysis of collagen // Science. - 2004. - Vol. 306, № 5693. - P. 108-111.

31. Patterson C., Pourmotabbed I., Mainardi C.L., Hasty K.A. Structure-function relationship of human neutrophil eollagenasc: identification of regions responsible lor substrate specificity and general proteinase activity // PNAS. - 1993. - Vol. 90, № 7. - P. 2569-2573.

32. Mukherjec R., Brinsa T.A., Dowdy K.B. et al. Myocardial infarct expansion and matrix metalloproteinase inhibition / Circulation. - 2003. - Vol. 107, № 4. - P. 618-625.

33. Spinale P.O., Coker M.L., Heung L.J. et al. A matrix metalloproteinase induction/activation system exists in the human myocardium and is upregulated in heart failure // Circulation. 2000. - Vol. 102, № 16. - P. 1944-1949.

34. Волкова M.A. Клиническая онкогематология. М.: «МЕДИЦИНА». - 2001. - С. 9-21.

35. Webb C.S., Bonnema D.D., llinan A.S. et al. Specific temporal profile of matrix metalloproteinase release occurs in patients after myocardial infarction // Circulation. 2006. - Vol. 114, № 10. - P. 1020-1027.

36. Aimes R.T., Quigley J.P. Matrix metalloproteinase-2 is an interstitial collagenase: inhibitor-free enzyme catalyzes the cleavage of collagen fibrils and soluble native type I collagen generating the specific 3/4- and 1/4-length fragments // J. Biol. Chem. - 1995. - Vol. 270, № 11. - P. 5872-5876.

37. Kahari V.M., Saarialho-Kere U. Matrix metalloproteinases in skin // Exp. Dermatol. 1997. - Vol. 6, № 5. - P. 199-213.

38. Huhtala P., Tuuttila A., Chow L.T. et al. Complete structure of the human gene for 92-kDa type IV collagenase. Divergent regulation of expression for the 92- and 72-kilodalton enzyme genes in HT-1080 cells // J. Biol. Chem. - 1991. - Vol. 266, № 25. - P. 16485-16490.

39. Zhang В., Ye S., Herrmann S.M. el al. Functional polymorphism in the regulatory region of gelatinase В gene in relation to severity of coronary atherosclerosis // Circulation. - 1999. - Vol. 99, № 14. - P. 1788-1794.

40. Siwik D.A., Pagano P.J., Colucci W.S. Oxidative stress regulates collagen synthesis and matrix metalloproteinase activity in cardiac fibroblasts // Am. J. Physiol. Cell. Physiol. 2001. - Vol. 280, № 1. - P. 53-60.

41. Aljada A., Cihanim H., Mohanty P. et al. Hydrocortisone suppresses intranuclear activator-protein-1 (AР-1) binding activity in mononuclear cells and plasma matrix metalloproteinase 2 and 9 (MMP-2 and MMP-9) // J. Clin. Endocrinol. Metab. - 2001. - Vol. 86, № 12. - P. 5988-5991.

42. Potier M., Karl M., Elliot S.J. et al. Response to sex hormones differs in atherosclerosis-susceptible and -resistant mice // Am. J. Physiol. Endocrinol. Metab. - 2003. - Vol. 285, № 6. - P. E1237-E1245.

43. Heymans S., Luttun A., Nuyens I., et al. Inhibition of plasminogen activators or matrix metalloprolcinases prevent cardiac rupture but impairs therapeutic angiogenesis and causes cardiac failure // Nat. Med. - 1999. - Vol. 5, № 10. - P. 1135-1142.

44. Kai H., Ikeda H., Yasukawa II. et al. Peripheral blood levels of matrix metalloproteinase 2 and 9 are elevated in patients with acute coronary syndromes // J. Am. Coll. Cardiol. 1998. - Vol. 32, № 2. - P. 368-372.

45. Ardans J., F.conomou A., Martinson J. et al. Oxidised low density and high density lipoproteins regulate the production of matrix metallo-proteinases 1 and 9 by activated monocytes // J. Leukoc. Biol. - 2002. - Vol. 71, № 6. - P. 1012-1018.

46. Herzog E., Gu A., Kohmoto Т. Burkhoff D. Early activation of metalloproteinases after experimental myocardial infarction occurs in infarct and non-infarct zones // Cardiovasc. Pathol. - 1998. - Vol. 7, № 6. - P. 307-312.

47. Etoh Т., Joffs C., Deschamps A.M. et al. Myocardial and interstitial matrix metalloproteinase activity after acute myocardial infarction in pigs // Am. J. Physiol. Heart. Circ. Physiol. 2001. - Vol. 281, № 3. - P. H987-H994.

48. Lanone S., Zheng I., Zhu Z. et al. Overlapping and enzyme-specific contributions of matrix metalloproteinases-9 and -12 in IL-13-induced inflammation and remodeling // J. Clin. Invest. 2002, - Vol. 110, № 4. - P. 463-474.

49. Garvin P., Nilsson L., Carslensen J. et al. Circulating matrix metalloproteinase-9 is associated with cardiovascular risk factors in a middle-aged normal population // Oxford.J. Med. - 2008. - Vol. 101, № 10. - P. 785-791.

50. Borden P., Heller R.A. Transcriptional control of matrix metalloproteinases and the tissue inhibitors of matrix metalloproteinases // Crit. Rev. Eukaryot. Gene Expr. - 1997. - Vol. 7, № 1-2. - P. 159-178.

51. Moon S.K., Cha B.Y. Kim C.H. ERK1/2 mediates TNF-alpha-indueed matrix metalloproteinase-9 expression in human vascular smooth muscle cells via the regulation of NF-kappaB and AP I: involvement of the ras dependent pathway // J. Cell. Physiol. 2004. Vol. 198, № 3. - P. 417-427.

52. Inokubo Y., Hanada H., Ishizaka H. et al. Plasma levels of matrix metalloproteinase-9 and tissue inhibitor of metalloproteinase-1 are increased in the coronary circulation in patients with acute coronary syndrome // Am. Heart. J.- 2001. -Vol. 141, № 2. - P. 211- 217.

53. Ctezki J.P., Hafeli U.O., Song P. el al. Parenchymal cell proliferation in coronary arteries after percutaneous transluminal coronary angioplasty: a human tissue bank study // Int. J. Radial. Oncol. Biol.Phys. - 1999. - Vol. 45, № 4. - P. 963-968.

54. Sierevogel M.J., Pasterkamp G., de Kleijn D.P., Strauss B.H. Matrix metalloproteinases: a therapeutic target in cardiovascular disease // Curr. Pharm. Des. - 2003. - Vol. 9, № 13. - P. 1033-1040.

55. van Beusekom H.M., Post M.J., Whelan D.M. et al. Metalloproteinase inhibition by batimastat does not reduce neoinlimal thickening in stented atherosclerotic porcine femoral arteries // Cardiovasc. Radiant Med. - 2003. - Vol. 4, № 4. - P. 186-191.

56. Плеханова О.С., Соломатииа М.А., Меньшиков M.Ю. и др. Активаторы плазминогена и матриксные металлопротеиназы в экспериментальном ремоделировании артерии // Кардиология. - 2006. - Т. 9, № 46. - С. 47-56.

57. Collen D. The plasminogen (fibrinolytic) system // Тhromb. Haemost. - 1999. - Vol. 82, № 2. - P. 259-270.

58. Lijnen H.R., Van Hoef В., Lupu F. et al. Function of the plasminogen/plasmin and matrix metalloproteinase systems after vascular injur) i mice with targeted inactivation of fibrinolytic system genes // Thromb. Vast Biol. - 1998. - Vol. 18, № 7. - P. 1035-1045.

59. Ye S. Polymorphism in matrix metalloproteinase gene promoton implication in regulation of gene expression and susceptibility of variou diseases // Matrix. Biol. - 2000. Vol. 19, № 7. - P. 623-629.

60. Richardson P.D., Davies M.J., Born G.V.R. Influence of plaque configuration and stress distribution on lissuring of coronary athcrosclcroli plaques // Lancet. - 1989. - Vol. 2, № 8669. - P. 941-944.

61. Borgono C.A., Diamandis E.P. The emerging roles of human tissue kallikreins in cancer // Nat. Rev. Cancer. 2004. - Vol.4 №11. - P. 876-890.

62. Yamada Y., Izawa H., Ichihara S. et al. Prediction of the risk of myocardial infarction from polymorphisms in candidate genes // New Eng. J. Med. - 2002. - Vol. 347, № 24. - P. 1916-1923.

63. Humphries S.E., Martin S., Cooper J., Miller G. Interaction between smoking and the stromelysin-1 (MMP3) gene 5A/6A promote-polymorphism and risk of coronary heart disease in healthy men // Ann. Hum. Genet. - 2002. - Vol. 66. Pt. 5-6. - P. 343-352.

64. Ye S., Eriksson P., Hamstcn A. et al. 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. - Vol. 271. - P. 13055- 13060.

65. Ye S., Watts G.F., Mandalia S. et al. Preliminary report: genetic variation in the human stromelysin promoter is associated with progression of coronary atherosclerosis // Brit. Heart J. - 1995. - Vol. 73, № 3. - P. 209-215.

66. Humphries S.E., Luong L.-A., Talmud P.I. et al. The 5A/6A polymorphism in the promoter of the stromelysin-l (MMP 3) gene predict' progression of angiographically determined coronary artery disease in me in the LOCAT gemfibrozil study // Atherosclerosis. 1998. - Vol. 134, № 1. - P. 49-56.

67. Medley Т.Е., Kingwell B.A., Gatzka C.D. et al. Matrix metalloproteinase-3 genotype contributes to age-related aortic stiffening througf modulation of gene and protein expression // Circ. Res. - 2003. - Vol. 92, № 11. - P. 1254-1261.

68. Thrailkill K., Moreau C.S., Cockrell G. et al. Physiologies matrix metalloproteinase concentrations in serum during childhood an adolescence, using Luminex Multiplex technology // Clin. Chem. Lab Med. - 2005. - Vol. 43, № 12. - P. 1392-1399.

69. Jung K. Serum or plasma: what kind of blood sample should be used to measure circulating matrix metalloproteinases and their inhibitors? J. Neuroimmunol. - 2005, Vol. 162. - P. 1-2.

70. Thrailkill K., Cockrell G., Simpson P. et al. Physiologiea matrix metalloproteinase (MMP) concentrations: comparison of semi and plasma specimens // Clin. Chem. Lab. Med. 2006. - Vol. 44, № 4. - P. 503-504.

71. Rohde L.E., Ducharme A., Arroyo L.H. et al. Matrix metalloptoteinase inhibition attenuates early left ventricular enlargement after experimental myocardial infarction in mice // Circulation. - 1999. - Vol. 99, № 23. - P. 3063-3070.

72. Apple F.S. Pearce L.A., Chung A. et al. Multiple biomarker use for detection of adverse events in patients presenting with symptom suggestive of acute coronary syndrome // Clin. Chem. - 2007. - Vol. 53, № 5. - P. 874-881.

73. Li Y.Y., Feng Y., McTiernan C.F. et al. Down regulation of matrix metalloproteinases and regulation in collagen damage in the failing human heart after support with left ventricular assist devices // Circulation. - 2001. - Vol. 104, № 10. - P. 1147-1152.


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Tourna A.A., Toguzov R.T. Matrix metalloproteinases and cardiovascular diseases. "Arterial’naya Gipertenziya" ("Arterial Hypertension"). 2009;15(5):532-538. (In Russ.) https://doi.org/10.18705/1607-419X-2009-15-5-532-538

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