МАТРИКСНЫЕ МЕТАЛЛОПРОТЕИНАЗЫВ РАЗВИТИИ ДЕСТРУКТИВНЫХ ПРОЦЕССОВПРИ РЕВМАТОИДНОМ АРТРИТЕ

1. <div><p>Яровая Г.А. Биорегулирующие функции и патогенетическая роль протеолиза. Современные представления и перспективы. Лаб мед 2000;3:19-22.</p><p>Rawlings N.D., Barrett A.J. Classification of peptidases by comparision of primary and tertiary structures. Biomed Health Res 1997;13:13-21.</p><p>Barrett A.J. Evolution and the structural classification of peptidases. Biomed Health Res 1997;13:3-12.</p><p>Rawlings N.D., Barrett A.J. Evolutionary families of metallopeptidases. Meth Enzymol 1995;248:183-228.</p><p>Hidalgo M., Eckhardt G.S. Development of мatrix мetalloproteinase inhibitors in cancer therapy. J Nation Cancer Inst 2001;93(3):178-93.</p><p>Яровая Г.А. Биорегулирующие функции и патогенетическая роль протеолиза. Распространение, классификация и основы механизма действия протеиназ. Лаб мед 2001;4:75-80.</p><p>Davies M.J. Reactive oxygen species, metalloproteinases, and plaque stability. Circulation 1998;97:2382-3.</p><p>Brinckerhoff C.E. Joint destruction in arthritis: metalloproteinase in the spotlight. Arthr Rheum 1991;34:1073-5.</p><p>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;56:235-47.</p><p>Pei D., Weiss S.J. Furindependent intracellular activation of the human stromelysin-3 zymogen. Nature 1995;375:244-7.</p><p>Nagase H. Activation mechanisms of matrix metalloproteinases. Biol Chem 1997;378:151-60.</p><p>Van Wart H.E., Birkedal-Hansen H. The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proc Natl Acad Sci USA 1990;87:5578-82.</p><p>Abramson S.R., Conner G.E., Nagase H. et al. Characterization of rat uterine matrilysin and its cDNA: Relationship to human pump-1 and activation of procollagenases. J Biol Chem 1995;270(27):16016-22.</p><p>Murphy G., Willenbrock F., Crabbe T. et al. Regulation of matrix metalloproteinase activity. Ann NY Acad Sci 1994;732:31-41.</p><p>Преображенский Д.В., Сидоренко Б.А., Батыралиев Т.А. Ингибиторы АПФ и АТ1-блокаторы в клинической практике. М.: ЗАО ?Пресид-Альянс?, 2002;224 с.</p><p>Zheng Y., Saftig P., Hartmann D. et al. Evaluation of the contribution of different ADAMs to TNF shedding and of the function of the TNF ectodomain in ensuring selective stimulated shedding by the TNF convertase TACE/ADAM17. J Biol Chem 2004;279:42898-906.</p><p>Sato H., Takino T., Kinoshita T. et al. Cell surface binding and activation of gelatinase A induced by expression of membranetype- 1-matrix metalloproteinase (MT1- MMP). FEBS Lett 1996;385:238-40.</p><p>Клишо Е.В., Кондакова И.В., Чойнзонов Е.Л. и др. Прогностическая значимость протеаз у больных плоскоклеточными карциномами головы и шеи. Бюл СО РАМН 2005;2(116):82-91.</p><p>Sternlicht M.D., Werb Z. How matrix metalloproteinases regulate cell behavior. Ann Rev Dev Biol 2001;17:463-516.</p><p>Brew K., Dinakarpandian D., Nagase H. Tissue inhibitors of metalloproteinases: evolution, structure and function. Biochim Biophys Acta 2000;1477:267-83.</p><p>Tchetverikov I., Lard L. R., De Groot J. Matrix metalloproteinases-3, -8, -9 as markers of disease activity and joint damage progression in early rheumatoid arthritis. Ann Rheum Dis 2003;62:1094-9.</p><p>Mohammed F.F., Smookler D.S. Metalloproteinases, inflammation, and rheumatoid arthritis. Ann Rheum Dis 2003;62(2):1143-7.</p><p>Creemers E., Davis J.N., Parkhurst A.M. et al. Deficiency of TIMP-1 exacerbates LV remodeling after myocardial infarction in mice. Am J Physiol Heart Circul Physiol 2003;284(1):364-71.</p><p>Рациональная фармако-терапия ревматических заболеваний: Руководство для практикующих врачей. Под ред. В.А. Насоновой, Е.Л. Насонова. М.: Изд-во Литтерра, 2003; 448 с.</p><p>Мазуров В.И. Клиническая ревматология. СПб.: ФОЛИАНТ, 2001;416 с.</p><p>Pincus T., Sokka T., Wolfe F. Premature mortality in patients with rheumatoid arthritis: evolving concepts. Arthr Rheum 2001;44:1234-6.</p><p>Sokka T., Toloza S., Cutolo M. et al. Women, men, and rheumatoid arthritis: analyses of disease activity, disease characteristics, and treatments in the QUEST-RA study. Arthr Res Ther 2009;11:R7.</p><p>Scherer S., de Souza T.B., de Paoli J. et al. Matrix metalloproteinase gene polymerphisms in patients with rheumatoid arthritis. Rheumatol Int 2010;30(3):369-73.</p><p>Tsukahara S., Shinozaki M., Ikari K. et al. Effect of matrix metalloproteinase-3 functional SNP on serum matrix metalloproteinase- 3 level and outcome measures in Japanese RA patients. Rheumatology (Oxford) 2008;47(1):41-4.</p><p>Мартынов А.И., Степура О.Б., Остроумова О.Д. Маркеры дисплазий соединительной ткани у больных с идиопатическим пролабированием атриовентрикулярных клапанов и с аномально расположенными хордами. Тер арх 1996;2:40-3.</p><p>Яковлев В.М., Глотов А.В., Нечаева Г.И. Клинико-иммунологический анализ клинических вариантов дисплазии соединительной ткани. Тер арх 1994;5:9-13.</p><p>Ровенский Ю.А. Как клетки ориентируются на местности. Соросовский образов журн 2001;7(3):4-11.</p><p>Seemayer C.A., Kuchen S., Kuenzler P. et al. Cartilage destruction mediated by synovial fibroblasts does not depend on proliferation in rheumatoid arthritis. Am J Pathol 2003;162:1549-57.</p><p>Nishikaku A.S., Ribeiro L.C., Molina R.F. et al. Matrix metalloproteinases with gelatinolytic activity induced by Paracoccidioides brasiliensis infection. Int J Exp Pathol 2009;90(5):527-37.</p><p>Butler G.S., Overall C.M. Updated biological roles for matrix metalloproteinases and new "intracellular" substrates revealed by degradomics. Biochemistry 2009;48(46):10830-45.</p><p>Gravallese E.M., Goldring S.R. Cellular mechanisms and the role of cytokines in bone erosions in rheumatoid arthritis. Arthr Rheum 2000;43:2143-51.</p><p>Ahn J.K., Koh E.M., Cha H.S. et al. Role of hypoxia-inducible factor-1alpha in hypoxia-induced expressions of IL-8, MMP-1 and MMP-3 in rheumatoid fibroblast- like synoviocytes. Rheumatology (Oxford) 2008;47(6):834-9.</p><p>Gross J., Lapiere C.M. Collagenolytic activity in amphibian tissues: a tissue culture assay. Proc Natl Acad Sci USA 1962;48:1014-22.</p><p>Yamagiwa H., Tokunaga K., Hayami T. et al. Expression of metalloproteinase-13 (collagenase-3) is induced during fracture healing in mice. Bone 1999;25:197-203.</p><p>Mitchell P.G., Magna H.A., Reeves L.M. et al. Cloning, expression and type II collagenolytic activity of matrix metalloproteinase- 13 from human osteoarthritic cartilage. J Clin Invert 1996;97(3):761-8.</p><p>Fosang A.J., Last K., Knд uper V. et al. Degradation of cartilage aggrecan by collagenase- 3 (MMP-13). FEBS Lett 1996;380:1-20.</p><p>Knд uper V., Will H., Lopez-Otin C. et al. Cellular Mechanisms for Human Procollagenase-3 (MMP-13) Activation. Am J Biochem Mol Biol 1996;271(29):17124-31.</p><p>Moore B.A., Aznavoorian S., Engler J.A. et al. Induction of collagenase-3 (MMP-13) in rheumatoid arthritis synovial fibroblasts. Biochem Biophis Acta 2000;1502(2):307-18.</p><p>Kim S.J., Shin H.H., Park S.Y. et al. Induction of MMP-13 expression by soluble human glucocorticoid-induced tumor necrosis factor receptor in fibroblast-like synovial cells. Osteoarthr Cartilage 2006;14(2):146-53.</p><p>Little C.B., Barai A., Burkhardt D. et al. Matrix metalloproteinase 13-deficient mice are resistant to osteoarthritic cartilage erosion but not chondrocyte hypertrophy or osteophyte development. Arthr Rheum 2009;60(12):3723-33.</p><p>Kennedy A.M., Inada M., Krane S.M. et al. MMP13 mutation causes spondyloepimetaphyseal dysplasia; Missouri type (SEMD (MO)). J Clin Invest 2005;115:2832-42.</p><p>Coussens L.M., Werb Z. Matrix metalloproteinases and the development of cancer. Chem Biol 1996;3(11):895-904.</p><p>Quinones S., Buttice G., Kurkinen M. Promoter elements in the transcriptional activation of the human stromelysin-1 gene by the inflammatory cytokine, interleukin 1. Biochem J 1994;302:471-7.</p><p>Murphy G., Cockett M.I., Stephens P.E. et al. Stromelysin is an activator of procollagenase. A study with natural and recombinant enzymes. Biochem J 1987;248:265-8.</p><p>Knд uper V., Wilhelm S.M., Seperack P.K. et al. Direct activation of human neutrophil procollagenase by recombinant stromelysin. Biochem J 1993;295(2):581-6.</p><p>Tetlow L.C., Lees M., Woolley D.E. Comparative studies of collagenase and stromelysin-1 expression by rheumatoid synoviocytes in vitro. Virchows Arch 1995;425:569-76.</p><p>Knд uper V., Lopez-Otin C., Smith B. et al. Biochemical characterization of human collagenase-3. J Biol Chem 1996;271:1544-50.</p><p>Milner J.M., Rowan A.D., Cawston T.E. et al. Metalloproteinase and inhibitor expression profiling of resorbing cartilage reveals pro-collagenase activation as a critical step for collagenolysis. Arthr Res Ther 2006;8(5):R142PMCID:PMC1779431</p><p>Yoshihara Y., Obata K., Fujimoto N. et al. Increased levels of stromelysin-1 and tissue inhibitor of metalloproteinases-1 in sera from patients with rheumatoid arthritis. Arthr Rheum 1995;38:969-75.</p><p>Kotajima L., Aotsuka S., Fujimani M. et al. Increased levels of matrix metalloproteinase- 3 in sera from patients with active lupus nephritis. Clin Exp Rheumatol 1998;16:409-15.</p><p>Keyszer G., Lambiri I., Nagel R. et al. Circulating levels of matrix metalloproteinases MMP-3 and MMP-1, tissue inhibitor of metalloproteinases 1 (TIMP-1), and MMP-1/TIMP-1 complex in rheumatic disease. Correlation with clinical activity of rheumatoid arthritis versus other surrogate markers. J Rheumatol 1999;26(2):251-8.</p><p>Posthumus M.D., Limburg P.C., Westra J. et al. Serum matrix metalloproteinase 3 levels in comparison to C-reactive protein in periods with and without progression of radiological damage in patients with early rheumatoid arthritis. Clin Exp Rheum 2003;21:465-72.</p><p>Mahmoud R.K., El-Ansary A.K., El-Eishi H.H. et al. Matrix metalloproteinases MMP-3 and MMP-1 levels in sera and synovial fluids in patients with rheumatoid arthritis and osteoarthritis. Ital J Biochem 2005;54(3-4):248-57.</p><p>Ribbens C., Andre B., Jaspar J.M. et al. Matrix metalloproteinase-3 serum levels are correlated with disease activity and predict clinical response in rheumatoid arthritis. J Rheumatol 2000;27:888-93.</p><p>Kahari V.M., Saarialho-Kere U. Matrix metalloproteinases in skin. Exp Dermatol 1997;6:199-213.</p><p>Gruber B.L., Sorbi D., French D.L. et al. Markedly elevated serum MMP-9 (gelatinase B) levels in rheumatoid arthritis: a potentially useful laboratory marker. Clin Immunol Immunopathol 1996;78(2):161-71.</p><p>Konttinen Y.T., Ceponis A., Takagi M. et al. New collagenolytic enzymes/cascade identified at the pannus-hard tissue junction in rheumatoid arthritis: destruction from above. Matrix Biol 1998;17:585-601.</p><p>Yoshida W., Uzuki M., Nishida J. et al. Examination of in vivo gelatinolytic activity in rheumatoid arthritis synovial tissue using newly developed in situ zymography and image analyzer. Clin Exp Rheumatol 2009;27(4):587-93.</p><p>Cauwe B., Martens E., Proost P. et al. Multidimensional degradomics identifies systemic autoantigens and intracellular matrix proteins as novel gelatinase B/MMP-9 substrates. Int Biol 2009;1(5- 6):404-26.</p><p>Ishiguro N., Ito T., Miyazaki K., Iwata H. Matrix metalloproteinases, tissue inhibitors of metalloproteinases, and glycosaminoglycans in synovial fluid from patients with rheumatoid arthritis. J Rheumatol 1999;26(1):34-40.</p><p>Yoshihara Y., Nakamura H., Obata K. et al. Matrix metalloproteinases and tissue inhibitors of metalloproteinases in synovial fluids from patients with rheumatoid arthritis or osteoarthritis. Ann Rheum Dis 2000;59(6):455-61.</p></div><br />