Ablation of matrix metalloproteinase-9 prevents cardiomyocytes contractile dysfunction in diabetics

Frontiers in Physiology

Volumn 7, Issue MAR, 2016, Pages

  Prathipati, Priyanka ^a   Metreveli, Naira ^b   Nandi, Shyam Sundar ^a   Tyagi, Suresh C ^b   Mishra, Paras K ^a  

^a UNIVERSITY OF NEBRASKA MEDICAL CENTER   (United States)

^b University of Louisville School of Medicine   (United States)

Author keywords

Akita; Calcium transient; Diabetes; Heart failure; SERCA 2a

Indexed keywords

GELATINASE B; MESSENGER RNA; SARCOENDOPLASMIC RETICULUM CALCIUM ADENOSINE TRIPHOSPHATASE 2A; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE; UNCLASSIFIED DRUG;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; CALCIUM CURRENT; CONTROLLED STUDY; DIABETES MELLITUS; DOWN REGULATION; HEART MUSCLE CELL; HEART MUSCLE CONTRACTILITY; IMMUNOPRECIPITATION; MALE; MOUSE; MUSCLE CONTRACTION; MUSCLE RELAXATION; NONHUMAN; POLYMERASE CHAIN REACTION; UPREGULATION; WESTERN BLOTTING;

EID: 84964688015     PISSN: None     EISSN: 1664042X     Source Type: Journal    
DOI: 10.3389/fphys.2016.00093     Document Type: Article

References (31)

1. Annabi, B., Vaillancourt-Jean, E., Weil, A. G., and Beliveau, R. (2010). Pharmacological targeting of beta-adrenergic receptor functions abrogates NF-kappaB signaling and MMP-9 secretion in medulloblastoma cells. Onco Targets Ther. 3, 219-226. doi: 10.2147/OTT.S14503
2. Boudina, S., and Abel, E. D. (2007). Diabetic cardiomyopathy revisited. Circulation 115, 3213-3223. doi: 10.1161/circulationaha.106.679597
3. Buralli, S., Dini, F. L., Ballo, P., Conti, U., Fontanive, P., Duranti, E., et al. (2010). Circulating matrix metalloproteinase-3 and metalloproteinase-9 and tissue Doppler measures of diastolic dysfunction to risk stratify patients with systolic heart failure. Am. J. Cardiol. 105, 853-856. doi: 10.1016/j.amjcard.2009.11.038
4. Chavali, V., Nandi, S. S., Singh, S. R., and Mishra, P. K. (2014a). Generating double knockout mice to model genetic intervention for diabetic cardiomyopathy in humans. Methods Mol. Biol. 1194, 385-400. doi: 10.1007/978-1-4939-1215-5_22
5. Chavali, V., Tyagi, S. C., and Mishra, P. K. (2014b). Differential expression of dicer, miRNAs, and inflammatory markers in diabetic Ins2+/-Akita hearts. Cell Biochem. Biophys. 68, 25-35. doi: 10.1007/s12013-013-9679-4
6. Chiao, Y. A., Ramirez, T. A., Zamilpa, R., Okoronkwo, S. M., Dai, Q., Zhang, J., et al. (2012). Matrix metalloproteinase-9 deletion attenuates myocardial fibrosis and diastolic dysfunction in ageing mice. Cardiovasc. Res. 96, 444-455. doi: 10.1093/cvr/cvs275
7. Chu, J. W., Jones, G. T., Tarr, G. P., Phillips, L. V., Wilkins, G. T., van Rij, A. M., et al. (2013). Plasma active matrix metalloproteinase 9 and indices of diastolic function in patients with preserved systolic function. Int. J. Cardiol. 167, 1242-1246. doi: 10.1016/j.ijcard.2012.03.147
8. Cutler, M. J., Wan, X., Plummer, B. N., Liu, H., Deschenes, I., Laurita, K. R., et al. (2012). Targeted sarcoplasmic reticulum Ca2+ ATPase 2a gene delivery to restore electrical stability in the failing heart. Circulation 126, 2095-2104. doi: 10.1161/CIRCULATIONAHA.111.071480
9. del Monte, F., Harding, S. E., Schmidt, U., Matsui, T., Kang, Z. B., Dec, G. W., et al. (1999). Restoration of contractile function in isolated cardiomyocytes from failing human hearts by gene transfer of SERCA2a. Circulation 100, 2308-2311. doi: 10.1161/01.CIR.100.23.2308
10. Giordano, F. J., He, H., McDonough, P., Meyer, M., Sayen, M. R., and Dillmann, W. H. (1997). Adenovirus-mediated gene transfer reconstitutes depressed sarcoplasmic reticulum Ca2+-ATPase levels and shortens prolonged cardiac myocyte Ca2+ transients. Circulation 96, 400-403. doi: 10.1161/01.CIR.96.2.400
11. Halade, G. V., Jin, Y. F., and Lindsey, M. L. (2013). Matrix metalloproteinase (MMP)-9: a proximal biomarker for cardiac remodeling and a distal biomarker for inflammation. Pharmacol. Ther. 139, 32-40. doi: 10.1016/j.pharmthera.2013.03.009
12. He, H., Giordano, F. J., Hilal-Dandan, R., Choi, D. J., Rockman, H. A., McDonough, P. M., et al. (1997). Overexpression of the rat sarcoplasmic reticulum Ca2+ ATPase gene in the heart of transgenic mice accelerates calcium transients and cardiac relaxation. J. Clin. Invest. 100, 380-389. doi: 10.1172/JCI119544
13. Karakikes, I., Kim, M., Hadri, L., Sakata, S., Sun, Y., Zhang, W., et al. (2009). Gene remodeling in type 2 diabetic cardiomyopathy and its phenotypic rescue with SERCA2a. PLoS ONE 4:e6474. doi: 10.1371/journal.pone.0006474
14. Lindsey, M. L., Escobar, G. P., Dobrucki, L. W., Goshorn, D. K., Bouges, S., Mingoia, J. T., et al. (2006). Matrix metalloproteinase-9 gene deletion facilitates angiogenesis after myocardial infarction. Am. J. Physiol. Heart Circ. Physiol. 290, H232-H239. doi: 10.1152/ajpheart.00457.2005
15. Luo, M., and Anderson, M. E. (2013). Mechanisms of altered Ca(2)(+) handling in heart failure. Circ. Res. 113, 690-708. doi: 10.1161/CIRCRESAHA.113.301651
16. Malhotra, A., and Sanghi, V. (1997). Regulation of contractile proteins in diabetic heart. Cardiovasc. Res. 34, 34-40. doi: 10.1016/j.ceca.2014.09.005
17. Mann, D. L., and Spinale, F. G. (1998). Activation of matrix metalloproteinases in the failing human heart: breaking the tie that binds. Circulation 98, 1699-1702. doi: 10.1161/01.CIR.98.17.1699
18. Mishra, P. K., Givvimani, S., Metreveli, N., and Tyagi, S. C. (2010a). Attenuation of beta2-adrenergic receptors and homocysteine metabolic enzymes cause diabetic cardiomyopathy. Biochem. Biophys. Res. Commun. 401, 175-181. doi: 10.1016/j.bbrc.2010.09.006
19. Mishra, P. K., Metreveli, N., and Tyagi, S. C. (2010c). MMP-9 gene ablation and TIMP-4 mitigate PAR-1-mediated cardiomyocyte dysfunction: a plausible role of dicer and miRNA. Cell Biochem. Biophys. 57, 67-76. doi: 10.1007/s12013-010-9084-1
20. Mishra, P. K., Tyagi, N., Sen, U., Joshua, I. G., and Tyagi, S. C. (2010b). Synergism in hyperhomocysteinemia and diabetes: role of PPAR gamma and tempol. Cardiovasc. Diabetol. 9, 49. doi: 10.1186/1475-2840-9-49
21. Mishra, P. K., Chavali, V., Metreveli, N., and Tyagi, S. C. (2012). Ablation of MMP9 induces survival and differentiation of cardiac stem cells into cardiomyocytes in the heart of diabetics: a role of extracellular matrix. Can. J. Physiol. Pharmacol. 90, 353-360. doi: 10.1139/y11-131
22. Moshal, K. S., Tipparaju, S. M., Vacek, T. P., Kumar, M., Singh, M., Frank, I. E., et al. (2008a). Mitochondrial matrix metalloproteinase activation decreases myocyte contractility in hyperhomocysteinemia. Am. J. Physiol. Heart Circ. Physiol. 295, H890-H897. doi: 10.1152/ajpheart.00099.2008
23. Moshal, K. S., Rodriguez, W. E., Sen, U., and Tyagi, S. C. (2008b). Targeted deletion of MMP-9 attenuates myocardial contractile dysfunction in heart failure. Physiol. Res. 57, 379-384.
24. Rietz, A., and Spiers, J. (2012). The relationship between the MMP system, adrenoceptors and phosphoprotein phosphatases. Br. J. Pharmacol. 166, 1225-1243. doi: 10.1111/j.1476-5381.2012.01917.x
25. Rodrigues, S. F., Tran, E. D., Fortes, Z. B., and Schmid-Schonbein, G. W. (2010). Matrix metalloproteinases cleave the beta2-adrenergic receptor in spontaneously hypertensive rats. Am. J. Physiol. Heart Circ. Physiol. 299, H25-H35. doi: 10.1152/ajpheart.00620.2009
26. Romanic, A. M., Harrison, S. M., Bao, W., Burns-Kurtis, C. L., Pickering, S., Gu, J., et al. (2002). Myocardial protection from ischemia/reperfusion injury by targeted deletion of matrix metalloproteinase-9. Cardiovasc. Res. 54, 549-558. doi: 10.1016/S0008-6363(02)00254-7
27. Rubler, S., Dlugash, J., Yuceoglu, Y. Z., Kumral, T., Branwood, A. W., and Grishman, A. (1972). New type of cardiomyopathy associated with diabetic glomerulosclerosis. Am. J. Cardiol. 30, 595-602. doi: 10.1016/0002-9149(72)90595-4
28. Tayebjee, M. H., Lim, H. S., MacFadyen, R. J., and Lip, G. Y. (2004). Matrix metalloproteinase-9 and tissue inhibitor of metalloproteinase-1 and-2 in type 2 diabetes: effect of 1 year's cardiovascular risk reduction therapy. Diabetes Care 27, 2049-2051. doi: 10.2337/diacare.27.8.2049
29. ter Keurs, H. E. (2012). The interaction of Ca2+ with sarcomeric proteins: role in function and dysfunction of the heart. Am. J. Physiol. Heart Circ. Physiol. 302, H38-H50. doi: 10.1152/ajpheart.00219.2011
30. Thomas, C. V., Coker, M. L., Zellner, J. L., Handy, J. R., Crumbley, A. J. III, and Spinale, F. G. (1998). Increased matrix metalloproteinase activity and selective upregulation in LV myocardium from patients with end-stage dilated cardiomyopathy. Circulation 97, 1708-1715. doi: 10.1161/01.CIR.97.17.1708
31. Zarain-Herzberg, A., Garcia-Rivas, G., and Estrada-Aviles, R. (2014). Regulation of SERCA pumps expression in diabetes. Cell Calcium 56, 302-310. doi: 10.1016/j.ceca.2014.09.005