Abstract
The development of congestive heart failure is associated with left ventricular dilation and myocardial remodeling. The matrix metalloproteinase (MMP) and tissue inhibitors of MMP (TIMP) activities play a significant role in extracellular remodeling. The inflammatory cytokine tumor necrosis factor-α (TNF-α) is proposed to affect myocardial remodeling and modulate myocyte cell growth and fibrosis. The synthesis of MMPs is also regulated by TNF-α in vitro study. However, it is not fully known that whether tissue TNF-α is associated with expressions for MMPs and TIMPs of infarcted myocardium in animal model.
Myocardial infarction (MI) was induced by surgical occlusion of the left main coronary artery in rats. Collagen content in infarcted tissues increased four folds at the first week after MI. In infarcted tissues, MMP-9 mRNA levels were early expressed within one week after MI. Those levels for MMP-13 and MMP-2 were both enhanced after from day 7 to day 14 and thereafter decreased at day 28. MMP-3 and MMP-14 mRNA expressions were expressed at day 14 and 28 after MI. The levels of TIMP-1 and TIMP-2 mRNA expression were elevated within one week and thereafter reduced. TIMP-3 mRNA expression was greater from day 14. TNF-α mRNA in the infarcted tissues increased within one week and those levels were still elevated by day 14. By the Western blotting and immunostaining studies, the maximal TNF-α protein levels were observed on day 7 in the infarcted tissues where large numbers of macrophage were infiltrated. Thus, MMP-9 was co-expressed with TNF-α at an early phase after MI. Other MMPs were more expressed after one week. We suggest that ventricular remodeling in infarcted tissue may be initially contributed to the enhancement of TNF-α expression, which can increase MMPs activity in cardiac fibroblasts.
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References
Weber KT, Brilla CG. 1991. Pathological hypertrophy and cardiac interstitume, Fibrosis and renin-angiotensin-aldosterone system. Circulation 83:1849–1865.
Tyagi SC. 1996. Role of extracellular matrix metalloproteinase in cardiac remoddeling. Heart Failure Rev 1:73–80.
Dollery CM, McEwan JR, Henney AM. 1995. Matrix metalloproteinases and cardiovascular disease. Cir Res 77:863–868.
Li YY, Feldman AM, Sun Y, McTierman CF. 1998. Differential expression of tissue inhibiotors of metalloproteinases in the failing human heart. Circulation 98:1728–1734.
Spinale FG, Coker ML, Krombach SR, Mukherjee R, Hallak H, Houck WV, Clair MJ, Kribbs SB, Johnson LL, Peterson JT, Zile MR. 1999. Matrix metalloproteinase inhibition during the development of congestive heart failure: Effects on left ventricular dimension and function. Circ Res 85:364–376.
Thomas CT, Coker ML, Zeller JL, Handy JR, Crumbley AJ III, Spinale GS. 1998. Increased matrix metalloproteinase activity and selective upregulation in LV myocardium from patients with end-stage dilated cardiomyopathy. Circulation 97:1708–1715.
Masutomo K, Makino N, Sugano M, Miyamoto S, Hata T, Yanaga T. 1999. Extracellular matrix regulation in the development of Syrian cardiomyopahtic Bio 14.6 and Bio 53.58 Hamsters. J Mol Cell Cardiol 31:1607–1616.
Pfeffer MA, Braunwald E. 1990. Ventricular remodeling after myocardial infarction: experimental observations and clinical implications. Circulation 81:1161–1172.
Weber KT, Sun Y, Tyagi SC, Cleutjens JP. 1994. Collagen network of the myocardum: function, structural remodeling and regulatory mechanisms. J Mol Cell Cardiol 26:279–292.
Pfeffer MA, Pfeffer JM, Steinberg C, Finn P. 1985. Survival after an experimental myocardial infarction: beneficial effects of long-term therapy with Captopril. Circulation 72:406–412.
Torre-Amione G, Kapadia S, Benedict C, Oral H, Young JB, Mann DL. 1996. Proinflammatory cytokine level in patients with depressed left ventricular ejection fraction: a report from the studies of left ventricular dysfunction (SOLVD). J Am Coll Cardiol 27:1201–1206.
Thaik CM, Calderone A, Takahashi N, Colucci WS. 1995. Interleukin-1β modulates the growth and phenotype of neonatal rat cardiac myocytes. J Clin Invest 96:1093–1099.
Yokoyama T, Nakano M, Bednarczyk JL, Mclntyre BW, Entman M, Mann DL. 1997. Tumor necro-sis factor-α provokes a hypertrophic growth response in adult cardiac myocytes. Circulation 95:1247–1252.
Krown KA, Page MT, Nguyen C, Zechner D, Gutierrez V, Comstock KL, Glembotski CC, Quintana PJ, Sabbadini RA. 1996. Tumor necrosis factor α-incuced apoptosis in cardiac myocytes; involvement of the sphingolipid signaling cascade in cardiac cell death. J Clin Invest 98:2854–2865.
Siwik DA, Chang DLF, Colucci WS. 2000. Interleukin-lβ and tumor necrosis factor-α decrease collagen synthesis and increase matrix metalloproteinase activity in cardiac fibroblasts in vitro. Cir Res 86:1259–1265.
Makino N, Hata T, Sugano M, Dixon IMC, Yanaga T. 1996. Regression of hypertrophy after myocardial infarction is produced by the chronic blockade of angiotensin type 1 receptor in rats. J Mol Cell Cardio 28:507–517.
Bergman I, Loxley R. 1961. Two improved and simplified methods for the spectrophotometric determination of hydroxyproline. Anal Chem 35:1961–1965.
Tyagi Sc, Matsubara L, Weber KT. 1993. Direct extraction and estimation of collagenase(s) activity by zymography in microquantities of rat myocardium and uterus. Clin Biochem 26:191–198.
Bryant D, Becker L, Richardson J, Shelton J, Franco F, Peshock R, Thompson M, Giroir B. 1998. Cardiac failure in transgenic mice with myocardial expression of tumor necrosis factor-α. Circulation 97:1375–1381.
Jacobs M, Staufenberger S, Gergs U, Meuter K, Brandstatter K, Hafner M, Ertl G, Schorb W. 1999. Tumor necrosis factor-α at acute myocardial infarction in rats and effects on cardiac fibroblasts. J Mol Cell Cardiol 31:1949–1959.
Shimizu N, Yoshiyama M, Takeuchi K, et al. 1998. Doppler echocardiographic assessment and cardiac gene expression analysis of the left ventricle in myovcardial infarcted rat. Jap Circ J 62:436–442.
Cleutjens JP. 1996. The role of matrix metalloproteinase in heart disease. Cardiovasc Res 32:814–821.
Jugdutt BI, Joljart MJ, Khan MI. 1996. Rate of collagen deposition during healing and ventricular remodeling after myocardial infarction in rat and dog models. Circulation 94:94–101.
Heymans S, Lutun A, Nuyens D, et al. 1999. Inhibition of plasminogen activators or matrix metal-loproteinases prevents cardiac rupture but impairs therapeutic angiogenesis and causes cardiac failure [see comments]. Nature Med 5:1135–1142.
Li YY, McTierman CF, Feldman AM. 1999. Proinflammatory cytokines regulate tissue inhibitors of metalloproteinases and disintegrin metalloproteinases in cardiac cells. Cardiovasc Res 42:162–172.
Fujisawa T, Hattori T, Takahashi K, Kuboki T, Yamashita A, Takigawa M. 1999. Cyclic mechanical stress induces extracellular matrix degradation in culture chondrocytes via gene expression of matrix metalloproteinase and interleukin-α. J Biochem (Tokyo) 125:966–975.
Ducharme A, Frantz S, Aikawa M, Rabkin E, Lindsey M, Rohde LE, Schoen F, Kelly RA, Werb Z, Libby P, Lee RT. 2000. Targeted deletion of mtrix metalloproteonase-9 attenuates left ventricular enlargement and collagen accumulation after experimental myocardial infarction. J Clin Invest 106:55–62.
Leibovich SJ, et al. 1987. Macrophage-induced angiogenesis is mediated by tumor necrosis factor-alpha. Nature 329:630–632.
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Makino, N., Sugano, M., Masutomo, K., Hata, T., Fushiki, S. (2003). Matrix Degradative Enzyme Activities on Cardiac Remodeling in Heart Failure. In: Singal, P.K., Dixon, I.M.C., Kirshenbaum, L.A., Dhalla, N.S. (eds) Cardiac Remodeling and Failure. Progress in Experimental Cardiology, vol 5. Springer, Boston, MA. https://doi.org/10.1007/978-1-4419-9262-8_21
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DOI: https://doi.org/10.1007/978-1-4419-9262-8_21
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