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Volumn 106, Issue , 2014, Pages 74-85

Inhibition of MMP-2 expression affects metabolic enzyme expression levels: Proteomic analysis of rat cardiomyocytes

Author keywords

ATP synthase; Cardiomyocytes; Contractility; Matrix metalloproteinase 2; Metabolic enzymes; SiRNA

Indexed keywords

ACYL COENZYME A DEHYDROGENASE; ATP SYNTHASE BETA SUBUNIT; CHAPERONIN 60; COPPER ZINC SUPEROXIDE DISMUTASE; CYTOCHROME C OXIDASE; DIHYDROLIPOYLLYSINE RESIDUE SUCCINYLTRANSFERASE; ELECTRON TRANSFERRING FLAVOPROTEIN; GELATINASE A; MITOCHONDRIAL ENZYME; OXOGLUTARATE DEHYDROGENASE; PROTEOME; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; SMALL INTERFERING RNA; UNCLASSIFIED DRUG; MATRIX METALLOPROTEINASE INHIBITOR; MMP2 PROTEIN, RAT; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

EID: 84899817877     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2014.04.026     Document Type: Article
Times cited : (10)

References (42)
  • 1
    • 35748974863 scopus 로고    scopus 로고
    • Myocardial matrix remodeling and the matrix metalloproteinases: influence on cardiac form and function
    • Spinale F.G. Myocardial matrix remodeling and the matrix metalloproteinases: influence on cardiac form and function. Physiol Rev 2007, 87:1285-1342.
    • (2007) Physiol Rev , vol.87 , pp. 1285-1342
    • Spinale, F.G.1
  • 2
    • 0019505565 scopus 로고
    • The effects of lysophosphatidylcholine, a toxic metabolite of ischemia, on the components of cardiac excitability in sheep Purkinje fibers
    • Arnsdorf M.F., Sawicki G.J. The effects of lysophosphatidylcholine, a toxic metabolite of ischemia, on the components of cardiac excitability in sheep Purkinje fibers. Circ Res 1981, 49:16-30.
    • (1981) Circ Res , vol.49 , pp. 16-30
    • Arnsdorf, M.F.1    Sawicki, G.J.2
  • 3
    • 34548820960 scopus 로고    scopus 로고
    • Matrix metalloproteinase-2 degrades the cytoskeletal protein alpha-actinin in peroxynitrite mediated myocardial injury
    • Sung M.M., Schulz C.G., Wang W., Sawicki G., Bautista-Lopez N.L., Schulz R. Matrix metalloproteinase-2 degrades the cytoskeletal protein alpha-actinin in peroxynitrite mediated myocardial injury. J Mol Cell Cardiol 2007, 43:429-436.
    • (2007) J Mol Cell Cardiol , vol.43 , pp. 429-436
    • Sung, M.M.1    Schulz, C.G.2    Wang, W.3    Sawicki, G.4    Bautista-Lopez, N.L.5    Schulz, R.6
  • 4
    • 0037126045 scopus 로고    scopus 로고
    • Intracellular action of matrix metalloproteinase-2 accounts for acute myocardial ischemia and reperfusion injury
    • Wang W., Schulze C.J., Suarez-Pinzon W.L., Dyck J.R., Sawicki G., Schulz R. Intracellular action of matrix metalloproteinase-2 accounts for acute myocardial ischemia and reperfusion injury. Circulation 2002, 106:1543-1549.
    • (2002) Circulation , vol.106 , pp. 1543-1549
    • Wang, W.1    Schulze, C.J.2    Suarez-Pinzon, W.L.3    Dyck, J.R.4    Sawicki, G.5    Schulz, R.6
  • 5
    • 23044497564 scopus 로고    scopus 로고
    • Degradation of myosin light chain in isolated rat hearts subjected to ischemia-reperfusion injury: a new intracellular target for matrix metalloproteinase-2
    • Sawicki G., Leon H., Sawicka J., Sariahmetoglu M., Schulze C.J., Scott P.G., et al. Degradation of myosin light chain in isolated rat hearts subjected to ischemia-reperfusion injury: a new intracellular target for matrix metalloproteinase-2. Circulation 2005, 112:544-552.
    • (2005) Circulation , vol.112 , pp. 544-552
    • Sawicki, G.1    Leon, H.2    Sawicka, J.3    Sariahmetoglu, M.4    Schulze, C.J.5    Scott, P.G.6
  • 6
    • 78549277458 scopus 로고    scopus 로고
    • Titin is a target of matrix metalloproteinase-2: implications in myocardial ischemia/reperfusion injury
    • Ali M.A., Cho W.J., Hudson B., Kassiri Z., Granzier H., Schulz R. Titin is a target of matrix metalloproteinase-2: implications in myocardial ischemia/reperfusion injury. Circulation 2010, 122:2039-2047.
    • (2010) Circulation , vol.122 , pp. 2039-2047
    • Ali, M.A.1    Cho, W.J.2    Hudson, B.3    Kassiri, Z.4    Granzier, H.5    Schulz, R.6
  • 7
    • 78649631500 scopus 로고    scopus 로고
    • Neonatal asphyxia induces the nitration of cardiac myosin light chain 2 that is associated with cardiac systolic dysfunction
    • Doroszko A., Polewicz D., Cadete V.J., Sawicka J., Jones M., Szczesna-Cordary D., et al. Neonatal asphyxia induces the nitration of cardiac myosin light chain 2 that is associated with cardiac systolic dysfunction. Shock 2010, 34:592-600.
    • (2010) Shock , vol.34 , pp. 592-600
    • Doroszko, A.1    Polewicz, D.2    Cadete, V.J.3    Sawicka, J.4    Jones, M.5    Szczesna-Cordary, D.6
  • 8
    • 84861856192 scopus 로고    scopus 로고
    • Cardiac sarcomeric proteins: novel intracellular targets of matrix metalloproteinase-2 in heart disease
    • Ali M.A., Fan X., Schulz R. Cardiac sarcomeric proteins: novel intracellular targets of matrix metalloproteinase-2 in heart disease. Trends Cardiovasc Med 2011, 21:112-118.
    • (2011) Trends Cardiovasc Med , vol.21 , pp. 112-118
    • Ali, M.A.1    Fan, X.2    Schulz, R.3
  • 11
    • 0032055067 scopus 로고    scopus 로고
    • Hypothyroidism decreases the ATP sensitivity of KATP channels from rat heart
    • Light P., Shimoni Y., Harbison S., Giles W., French R.J. Hypothyroidism decreases the ATP sensitivity of KATP channels from rat heart. J Membr Biol 1998, 162:217-223.
    • (1998) J Membr Biol , vol.162 , pp. 217-223
    • Light, P.1    Shimoni, Y.2    Harbison, S.3    Giles, W.4    French, R.J.5
  • 12
    • 0027723262 scopus 로고
    • Role of sodium-calcium exchange in activation of contraction in rat ventricle
    • Bouchard R.A., Clark R.B., Giles W.R. Role of sodium-calcium exchange in activation of contraction in rat ventricle. J Physiol 1993, 472:391-413.
    • (1993) J Physiol , vol.472 , pp. 391-413
    • Bouchard, R.A.1    Clark, R.B.2    Giles, W.R.3
  • 13
    • 0034681937 scopus 로고    scopus 로고
    • Matrix metalloproteinase-2 contributes to ischemia-reperfusion injury in the heart
    • Cheung P.Y., Sawicki G., Wozniak M., Wang W., Radomski M.W., Schulz R. Matrix metalloproteinase-2 contributes to ischemia-reperfusion injury in the heart. Circulation 2000, 101:1833-1839.
    • (2000) Circulation , vol.101 , pp. 1833-1839
    • Cheung, P.Y.1    Sawicki, G.2    Wozniak, M.3    Wang, W.4    Radomski, M.W.5    Schulz, R.6
  • 14
    • 50249125886 scopus 로고    scopus 로고
    • Inhibiting matrix metalloproteinase-2 reduces protein release into coronary effluent from isolated rat hearts during ischemia-reperfusion
    • Fert-Bober J., Leon H., Sawicka J., Basran R.S., Devon R.M., Schulz R., et al. Inhibiting matrix metalloproteinase-2 reduces protein release into coronary effluent from isolated rat hearts during ischemia-reperfusion. Basic Res Cardiol 2008, 103:431-443.
    • (2008) Basic Res Cardiol , vol.103 , pp. 431-443
    • Fert-Bober, J.1    Leon, H.2    Sawicka, J.3    Basran, R.S.4    Devon, R.M.5    Schulz, R.6
  • 15
    • 48249096734 scopus 로고    scopus 로고
    • Effect of duration of ischemia on myocardial proteome in ischemia/reperfusion injury
    • Fert-Bober J., Basran R.S., Sawicka J., Sawicki G. Effect of duration of ischemia on myocardial proteome in ischemia/reperfusion injury. Proteomics 2008, 8:2543-2555.
    • (2008) Proteomics , vol.8 , pp. 2543-2555
    • Fert-Bober, J.1    Basran, R.S.2    Sawicka, J.3    Sawicki, G.4
  • 16
    • 0142182382 scopus 로고    scopus 로고
    • Functional proteomics of neurokinin B in the placenta indicates a novel role in regulating cytotrophoblast antioxidant defences
    • Sawicki G., Dakour J., Morrish D.W. Functional proteomics of neurokinin B in the placenta indicates a novel role in regulating cytotrophoblast antioxidant defences. Proteomics 2003, 3:2044-2051.
    • (2003) Proteomics , vol.3 , pp. 2044-2051
    • Sawicki, G.1    Dakour, J.2    Morrish, D.W.3
  • 17
    • 3042771387 scopus 로고    scopus 로고
    • Detection of regional changes in protein levels in the in vivo canine model of acute heart failure following ischemia-reperfusion injury: functional proteomics studies
    • Sawicki G., Jugdutt B.I. Detection of regional changes in protein levels in the in vivo canine model of acute heart failure following ischemia-reperfusion injury: functional proteomics studies. Proteomics 2004, 4:2195-2202.
    • (2004) Proteomics , vol.4 , pp. 2195-2202
    • Sawicki, G.1    Jugdutt, B.I.2
  • 18
    • 25844437437 scopus 로고    scopus 로고
    • Proteome analysis of embryo and endosperm from germinating tomato seeds
    • Sheoran I.S., Olson D.J., Ross A.R., Sawhney V.K. Proteome analysis of embryo and endosperm from germinating tomato seeds. Proteomics 2005, 5:3752-3764.
    • (2005) Proteomics , vol.5 , pp. 3752-3764
    • Sheoran, I.S.1    Olson, D.J.2    Ross, A.R.3    Sawhney, V.K.4
  • 19
    • 12944269065 scopus 로고
    • Rapid identification of proteins by peptide-mass fingerprinting
    • Pappin D.J., Hojrup P., Bleasby A.J. Rapid identification of proteins by peptide-mass fingerprinting. Curr Biol 1993, 3:327-332.
    • (1993) Curr Biol , vol.3 , pp. 327-332
    • Pappin, D.J.1    Hojrup, P.2    Bleasby, A.J.3
  • 20
    • 84862507917 scopus 로고    scopus 로고
    • Ischemia/reperfusion-induced myosin light chain 1 phosphorylation increases its degradation by matrix metalloproteinase 2
    • Cadete V.J., Sawicka J., Jaswal J.S., Lopaschuk G.D., Schulz R., Szczesna-Cordary D., et al. Ischemia/reperfusion-induced myosin light chain 1 phosphorylation increases its degradation by matrix metalloproteinase 2. FEBS J 2012, 279:2444-2454.
    • (2012) FEBS J , vol.279 , pp. 2444-2454
    • Cadete, V.J.1    Sawicka, J.2    Jaswal, J.S.3    Lopaschuk, G.D.4    Schulz, R.5    Szczesna-Cordary, D.6
  • 21
    • 79957598460 scopus 로고    scopus 로고
    • Ischemia induced peroxynitrite dependent modifications of cardiomyocyte MLC1 increases its degradation by MMP-2 leading to contractile dysfunction
    • Polewicz D., Cadete V.J., Doroszko A., Hunter B.E., Sawicka J., Szczesna-Cordary D., et al. Ischemia induced peroxynitrite dependent modifications of cardiomyocyte MLC1 increases its degradation by MMP-2 leading to contractile dysfunction. J Cell Mol Med 2011, 15:1136-1147.
    • (2011) J Cell Mol Med , vol.15 , pp. 1136-1147
    • Polewicz, D.1    Cadete, V.J.2    Doroszko, A.3    Hunter, B.E.4    Sawicka, J.5    Szczesna-Cordary, D.6
  • 22
    • 34548746306 scopus 로고    scopus 로고
    • Myocardial reperfusion injury
    • Yellon D.M., Hausenloy D.J. Myocardial reperfusion injury. N Engl J Med 2007, 357:1121-1135.
    • (2007) N Engl J Med , vol.357 , pp. 1121-1135
    • Yellon, D.M.1    Hausenloy, D.J.2
  • 23
    • 79953189369 scopus 로고    scopus 로고
    • Tearin' up my heart: proteolysis in the cardiac sarcomere
    • Portbury A.L., Willis M.S., Patterson C. Tearin' up my heart: proteolysis in the cardiac sarcomere. J Biol Chem 2011, 286:9929-9934.
    • (2011) J Biol Chem , vol.286 , pp. 9929-9934
    • Portbury, A.L.1    Willis, M.S.2    Patterson, C.3
  • 24
    • 84875157276 scopus 로고    scopus 로고
    • Synergistic protection of MLC 1 against cardiac ischemia/reperfusion-induced degradation: a novel therapeutic concept for the future
    • Cadete V.J., Arcand S.A., Lin H.B., Sawicki G. Synergistic protection of MLC 1 against cardiac ischemia/reperfusion-induced degradation: a novel therapeutic concept for the future. Future Med Chem 2013, 5:389-398.
    • (2013) Future Med Chem , vol.5 , pp. 389-398
    • Cadete, V.J.1    Arcand, S.A.2    Lin, H.B.3    Sawicki, G.4
  • 25
    • 70349652283 scopus 로고    scopus 로고
    • Cardiac dysfunction in an animal model of neonatal asphyxia is associated with increased degradation of MLC1 by MMP-2
    • Doroszko A., Polewicz D., Sawicka J., Richardson J.S., Cheung P.Y., Sawicki G. Cardiac dysfunction in an animal model of neonatal asphyxia is associated with increased degradation of MLC1 by MMP-2. Basic Res Cardiol 2009, 104:669-679.
    • (2009) Basic Res Cardiol , vol.104 , pp. 669-679
    • Doroszko, A.1    Polewicz, D.2    Sawicka, J.3    Richardson, J.S.4    Cheung, P.Y.5    Sawicki, G.6
  • 26
    • 0034643336 scopus 로고    scopus 로고
    • Rapid degradation of a large fraction of newly synthesized proteins by proteasomes
    • Schubert U., Anton L.C., Gibbs J., Norbury C.C., Yewdell J.W., Bennink J.R. Rapid degradation of a large fraction of newly synthesized proteins by proteasomes. Nature 2000, 404:770-774.
    • (2000) Nature , vol.404 , pp. 770-774
    • Schubert, U.1    Anton, L.C.2    Gibbs, J.3    Norbury, C.C.4    Yewdell, J.W.5    Bennink, J.R.6
  • 28
    • 84865532057 scopus 로고    scopus 로고
    • Effect of the myosin light chain kinase inhibitor ML-7 on the proteome of hearts subjected to ischemia-reperfusion injury
    • Lin H.B., Cadete V.J., Sawicka J., Wozniak M., Sawicki G. Effect of the myosin light chain kinase inhibitor ML-7 on the proteome of hearts subjected to ischemia-reperfusion injury. J Proteomics 2012, 75:5386-5395.
    • (2012) J Proteomics , vol.75 , pp. 5386-5395
    • Lin, H.B.1    Cadete, V.J.2    Sawicka, J.3    Wozniak, M.4    Sawicki, G.5
  • 29
    • 78650068857 scopus 로고    scopus 로고
    • Effect of the Rho kinase inhibitor Y-27632 on the proteome of hearts with ischemia-reperfusion injury
    • Cadete V.J., Sawicka J., Polewicz D., Doroszko A., Wozniak M., Sawicki G. Effect of the Rho kinase inhibitor Y-27632 on the proteome of hearts with ischemia-reperfusion injury. Proteomics 2010, 10:4377-4385.
    • (2010) Proteomics , vol.10 , pp. 4377-4385
    • Cadete, V.J.1    Sawicka, J.2    Polewicz, D.3    Doroszko, A.4    Wozniak, M.5    Sawicki, G.6
  • 30
    • 84883250907 scopus 로고    scopus 로고
    • Combined subthreshold dose inhibition of myosin light chain phosphorylation and matrix metalloproteinase-2 activity provides cardioprotection from ischemic/reperfusion injury in isolated rat heart
    • Cadete V.J., Sawicka J., Bekar L.K., Sawicki G. Combined subthreshold dose inhibition of myosin light chain phosphorylation and matrix metalloproteinase-2 activity provides cardioprotection from ischemic/reperfusion injury in isolated rat heart. Br J Pharmacol 2013, 170:380-390.
    • (2013) Br J Pharmacol , vol.170 , pp. 380-390
    • Cadete, V.J.1    Sawicka, J.2    Bekar, L.K.3    Sawicki, G.4
  • 31
    • 0037841983 scopus 로고    scopus 로고
    • Imbalance between tissue inhibitor of metalloproteinase-4 and matrix metalloproteinases during acute myocardial [correction of myoctardial] ischemia-reperfusion injury
    • Schulze C.J., Wang W., Suarez-Pinzon W.L., Sawicka J., Sawicki G., Schulz R. Imbalance between tissue inhibitor of metalloproteinase-4 and matrix metalloproteinases during acute myocardial [correction of myoctardial] ischemia-reperfusion injury. Circulation 2003, 107:2487-2492.
    • (2003) Circulation , vol.107 , pp. 2487-2492
    • Schulze, C.J.1    Wang, W.2    Suarez-Pinzon, W.L.3    Sawicka, J.4    Sawicki, G.5    Schulz, R.6
  • 33
    • 0027254060 scopus 로고
    • A metalloproteinase inhibitor domain in Alzheimer amyloid protein precursor
    • Miyazaki K., Hasegawa M., Funahashi K., Umeda M. A metalloproteinase inhibitor domain in Alzheimer amyloid protein precursor. Nature 1993, 362:839-841.
    • (1993) Nature , vol.362 , pp. 839-841
    • Miyazaki, K.1    Hasegawa, M.2    Funahashi, K.3    Umeda, M.4
  • 34
    • 36749032794 scopus 로고    scopus 로고
    • Hypoxic inhibition of human cardiac fibroblast invasion and MMP-2 activation may impair adaptive myocardial remodelling
    • Morley M.E., Riches K., Peers C., Porter K.E. Hypoxic inhibition of human cardiac fibroblast invasion and MMP-2 activation may impair adaptive myocardial remodelling. Biochem Soc Trans 2007, 35:905-907.
    • (2007) Biochem Soc Trans , vol.35 , pp. 905-907
    • Morley, M.E.1    Riches, K.2    Peers, C.3    Porter, K.E.4
  • 35
    • 0028291737 scopus 로고
    • A matrix metalloproteinase expressed on the surface of invasive tumour cells
    • Sato H., Takino T., Okada Y., Cao J., Shinagawa A., Yamamoto E., et al. A matrix metalloproteinase expressed on the surface of invasive tumour cells. Nature 1994, 370:61-65.
    • (1994) Nature , vol.370 , pp. 61-65
    • Sato, H.1    Takino, T.2    Okada, Y.3    Cao, J.4    Shinagawa, A.5    Yamamoto, E.6
  • 36
    • 33847020733 scopus 로고    scopus 로고
    • Intracellular targets of matrix metalloproteinase-2 in cardiac disease: rationale and therapeutic approaches
    • Schulz R. Intracellular targets of matrix metalloproteinase-2 in cardiac disease: rationale and therapeutic approaches. Annu Rev Pharmacol Toxicol 2007, 47:211-242.
    • (2007) Annu Rev Pharmacol Toxicol , vol.47 , pp. 211-242
    • Schulz, R.1
  • 37
    • 77956784544 scopus 로고    scopus 로고
    • Intracellular substrate cleavage: a novel dimension in the biochemistry, biology and pathology of matrix metalloproteinases
    • Cauwe B., Opdenakker G. Intracellular substrate cleavage: a novel dimension in the biochemistry, biology and pathology of matrix metalloproteinases. Crit Rev Biochem Mol Biol 2010, 45:351-423.
    • (2010) Crit Rev Biochem Mol Biol , vol.45 , pp. 351-423
    • Cauwe, B.1    Opdenakker, G.2
  • 39
    • 84864572108 scopus 로고    scopus 로고
    • Proteomic analysis of right and left cardiac ventricles under aerobic conditions and after ischemia/reperfusion
    • Cadete V.J., Lin H.B., Sawicka J., Wozniak M., Sawicki G. Proteomic analysis of right and left cardiac ventricles under aerobic conditions and after ischemia/reperfusion. Proteomics 2012, 12:2366-2377.
    • (2012) Proteomics , vol.12 , pp. 2366-2377
    • Cadete, V.J.1    Lin, H.B.2    Sawicka, J.3    Wozniak, M.4    Sawicki, G.5
  • 40
    • 0037036399 scopus 로고    scopus 로고
    • Activation of matrix metalloproteinase-2 by overexpression of manganese superoxide dismutase in human breast cancer MCF-7 cells involves reactive oxygen species
    • Zhang H.J., Zhao W., Venkataraman S., Robbins M.E., Buettner G.R., Kregel K.C., et al. Activation of matrix metalloproteinase-2 by overexpression of manganese superoxide dismutase in human breast cancer MCF-7 cells involves reactive oxygen species. J Biol Chem 2002, 277:20919-20926.
    • (2002) J Biol Chem , vol.277 , pp. 20919-20926
    • Zhang, H.J.1    Zhao, W.2    Venkataraman, S.3    Robbins, M.E.4    Buettner, G.R.5    Kregel, K.C.6
  • 41
    • 75749134894 scopus 로고    scopus 로고
    • Regulation of ATPase activity of transglutaminase 2 by MT1-MMP: implications for mineralization of MC3T3-E1 osteoblast cultures
    • Nakano Y., Forsprecher J., Kaartinen M.T. Regulation of ATPase activity of transglutaminase 2 by MT1-MMP: implications for mineralization of MC3T3-E1 osteoblast cultures. J Cell Physiol 2010, 223:260-269.
    • (2010) J Cell Physiol , vol.223 , pp. 260-269
    • Nakano, Y.1    Forsprecher, J.2    Kaartinen, M.T.3
  • 42
    • 84867733931 scopus 로고    scopus 로고
    • Cardiac mitochondrial matrix and respiratory complex protein phosphorylation
    • Covian R., Balaban R.S. Cardiac mitochondrial matrix and respiratory complex protein phosphorylation. Am J Physiol Heart Circ Physiol 2012, 303:H940-H966.
    • (2012) Am J Physiol Heart Circ Physiol , vol.303
    • Covian, R.1    Balaban, R.S.2


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