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Volumn 26, Issue 1, 2008, Pages 24-37

Inhibiting metalloproteases with PD 166793 in heart failure: Impact on cardiac remodeling and beyond

Author keywords

AMP deaminase; Cardiac energetics; Heart failure; Metalloproteinases; Myocardial fibrosis; PD166793; Ventricular remodeling

Indexed keywords

ACTINONIN; ALPHA 2 MACROGLOBULIN; BATIMASTAT; BISPHOSPHONIC ACID DERIVATIVE; CATHECIN; CP 471 474; CURCUMIN; DOXYCYCLINE HYCLATE; GENISTEIN; ILOMASTAT; MARIMASTAT; MATRIX METALLOPROTEINASE INHIBITOR; METALLOPROTEINASE; N1 [2,2 DIMETHYL 1 [(METHYLAMINO)CARBONYL]PROPYL] N4 HYDROXY 2 (2 METHYLPROPYL)BUTANEDIAMIDE; PD 166793; PEROXYNITRITE; POLYPHENOL; RESVERATROL; RO 28 2653; TETRACYCLINE DERIVATIVE; THROMBOSPONDIN 1; THROMBOSPONDIN 2; TISSUE INHIBITOR OF METALLOPROTEINASE; UNCLASSIFIED DRUG;

EID: 47049121031     PISSN: 17555914     EISSN: 17555922     Source Type: Journal    
DOI: 10.1111/j.1527-3466.2007.00034.x     Document Type: Review
Times cited : (28)

References (84)
  • 2
    • 0036800192 scopus 로고    scopus 로고
    • Metalloproteinase inhibitors: Biological actions and therapeutic opportunities
    • Baker AH, Edwards DR, Murphy G (2002) Metalloproteinase inhibitors: Biological actions and therapeutic opportunities. J Cell Sci 115 : 3719 3727.
    • (2002) J Cell Sci , vol.115 , pp. 3719-3727
    • Baker, A.H.1    Edwards, D.R.2    Murphy, G.3
  • 4
  • 5
    • 33749991812 scopus 로고    scopus 로고
    • Mechanisms of diastolic dysfunction in heart failure
    • Borlaug BA, Kass DA (2006) Mechanisms of diastolic dysfunction in heart failure. Trends Cardiovasc Med 16 : 273 279.
    • (2006) Trends Cardiovasc Med , vol.16 , pp. 273-279
    • Borlaug, B.A.1    Kass, D.A.2
  • 6
    • 32944473831 scopus 로고    scopus 로고
    • MMPs - Role in cardiovascular development and disease
    • Brauer PR (2006) MMPs - role in cardiovascular development and disease. Front Biosci 11 : 447 478.
    • (2006) Front Biosci , vol.11 , pp. 447-478
    • Brauer, P.R.1
  • 7
    • 34447507856 scopus 로고    scopus 로고
    • Inhibition of matrix metalloproteinase activity by ACE inhibitors prevents left ventricular remodeling in a rat model of heart failure
    • Brower GL, Levick SP, Janicki JS (2007) Inhibition of matrix metalloproteinase activity by ACE inhibitors prevents left ventricular remodeling in a rat model of heart failure. Am J Physiol Heart Circ Physiol 292 : H3057 H3064.
    • (2007) Am J Physiol Heart Circ Physiol , vol.292
    • Brower, G.L.1    Levick, S.P.2    Janicki, J.S.3
  • 8
    • 0020684765 scopus 로고
    • Substrate specificity and kinetic characteristics of angiotensin converting enzyme
    • Bunning P, Holmquist B, Riordan JF (1983) Substrate specificity and kinetic characteristics of angiotensin converting enzyme. Biochemistry 22 : 103 110.
    • (1983) Biochemistry , vol.22 , pp. 103-110
    • Bunning, P.1    Holmquist, B.2    Riordan, J.F.3
  • 10
    • 0037161371 scopus 로고    scopus 로고
    • Effects of matrix metalloproteinase inhibition on ventricular remodeling due to volume overload
    • Chancey AL, Brower GL, Peterson JT, Janicki JS (2002) Effects of matrix metalloproteinase inhibition on ventricular remodeling due to volume overload. Circulation 105 : 1983 1988.
    • (2002) Circulation , vol.105 , pp. 1983-1988
    • Chancey, A.L.1    Brower, G.L.2    Peterson, J.T.3    Janicki, J.S.4
  • 11
    • 0037961698 scopus 로고    scopus 로고
    • Matrix metalloproteinase abundance in human myocardial fibroblasts: Effects of sustained pharmacologic matrix metalloproteinase inhibition
    • Chapman RE, Scott AA, Deschamps AM, Lowry AS, Stroud RE, Ikonomidis JS, Spinale FG (2003) Matrix metalloproteinase abundance in human myocardial fibroblasts: Effects of sustained pharmacologic matrix metalloproteinase inhibition. J Mo Cell Cardio 35 : 539 548.
    • (2003) J Mo Cell Cardio , vol.35 , pp. 539-548
    • Chapman, R.E.1    Scott, A.A.2    Deschamps, A.M.3    Lowry, A.S.4    Stroud, R.E.5    Ikonomidis, J.S.6    Spinale, F.G.7
  • 12
    • 0034638377 scopus 로고    scopus 로고
    • Structure-based design of a novel, potent, and selective inhibitor for MMP-13 Utilizing NMR spectroscopy and computer-aided molecular design
    • Chen JM, Nelson FC, Levin JI, Mobilio D, Moy FJ, Nilakantan R, Zask A, Powers R (2000) Structure-based design of a novel, potent, and selective inhibitor for MMP-13 Utilizing NMR spectroscopy and computer-aided molecular design. J Am Chem Soc 122 : 9648 9654.
    • (2000) J Am Chem Soc , vol.122 , pp. 9648-9654
    • Chen, J.M.1    Nelson, F.C.2    Levin, J.I.3    Mobilio, D.4    Moy, F.J.5    Nilakantan, R.6    Zask, A.7    Powers, R.8
  • 14
    • 34948852291 scopus 로고    scopus 로고
    • Acute actions and novel targets of matrix metalloproteinases in the heart and vasculature
    • Chow AK, Cena J, Schulz R (2007) Acute actions and novel targets of matrix metalloproteinases in the heart and vasculature. Br J Pharmacol 152 : 189 205.
    • (2007) Br J Pharmacol , vol.152 , pp. 189-205
    • Chow, A.K.1    Cena, J.2    Schulz, R.3
  • 15
    • 0029035551 scopus 로고
    • Tissue inhibitor of metalloproteinase-2 stimulates fibroblast proliferation via a cAMP-dependent mechanism
    • Corcoran ML, Stetler-Stevenson WG (1995) Tissue inhibitor of metalloproteinase-2 stimulates fibroblast proliferation via a cAMP-dependent mechanism. J Biol Chem 270 : 13453 13459.
    • (1995) J Biol Chem , vol.270 , pp. 13453-13459
    • Corcoran, M.L.1    Stetler-Stevenson, W.G.2
  • 16
    • 33748799968 scopus 로고    scopus 로고
    • Molecular balance of capillary tube formation versus regression in wound repair: Role of matrix metalloproteinases and their inhibitors
    • Davis GE, Saunders WB (2006) Molecular balance of capillary tube formation versus regression in wound repair: Role of matrix metalloproteinases and their inhibitors. J Investig Dermatol Symp Proc 11 : 44 56.
    • (2006) J Investig Dermatol Symp Proc , vol.11 , pp. 44-56
    • Davis, G.E.1    Saunders, W.B.2
  • 17
    • 0026714363 scopus 로고
    • Post-transcriptional regulation of collagenase and stromelysin gene expression by epidermal growth factor and dexamethasone in cultured human fibroblasts
    • Delany AM, Brinckerhoff CE (1992) Post-transcriptional regulation of collagenase and stromelysin gene expression by epidermal growth factor and dexamethasone in cultured human fibroblasts. J Cell Biochem 50 : 400 410.
    • (1992) J Cell Biochem , vol.50 , pp. 400-410
    • Delany, A.M.1    Brinckerhoff, C.E.2
  • 18
    • 31344466167 scopus 로고    scopus 로고
    • Pathways of matrix metalloproteinase induction in heart failure: Bioactive molecules and transcriptional regulation
    • Deschamps AM, Spinale FG (2006) Pathways of matrix metalloproteinase induction in heart failure: Bioactive molecules and transcriptional regulation. Cardiovasc Res 69 : 666 676.
    • (2006) Cardiovasc Res , vol.69 , pp. 666-676
    • Deschamps, A.M.1    Spinale, F.G.2
  • 19
    • 0033932709 scopus 로고    scopus 로고
    • Targeted deletion of matrix metalloproteinase-9 attenuates left ventricular enlargement and collagen accumulation after experimental myocardial infarction
    • Ducharme A, Frantz S, Aikawa M, Rabkin E, Lindsey M, Rohde LE, Schoen FJ, Kelly RA, Werb Z, Libby P, et al 2000) Targeted deletion of matrix metalloproteinase-9 attenuates left ventricular enlargement and collagen accumulation after experimental myocardial infarction. J Clin Invest 106 : 55 62.
    • (2000) J Clin Invest , vol.106 , pp. 55-62
    • Ducharme, A.1    Frantz, S.2    Aikawa, M.3    Rabkin, E.4    Lindsey, M.5    Rohde, L.E.6    Schoen, F.J.7    Kelly, R.A.8    Werb, Z.9    Libby, P.10    Al, E.11
  • 20
    • 0036512208 scopus 로고    scopus 로고
    • New functions for the matrix metalloproteinases in cancer progression
    • Egeblad M, Werb Z (2002) New functions for the matrix metalloproteinases in cancer progression. Nat Rev Cancer 2 : 161 174.
    • (2002) Nat Rev Cancer , vol.2 , pp. 161-174
    • Egeblad, M.1    Werb, Z.2
  • 22
    • 2342624494 scopus 로고    scopus 로고
    • Carbamoylphosphonate- based matrix metalloproteinase inhibitor metal complexes: Solution studies and stability constants
    • Towards a zinc-selective binding group
    • Farkas E, Katz Y, Bhusare S, Reich R, Roschenthaler GV, Konigsmann M, Breuer E (2004) Carbamoylphosphonate- based matrix metalloproteinase inhibitor metal complexes: Solution studies and stability constants. Towards a zinc-selective binding group. J Biol Inorg Chem 9 : 307 315.
    • (2004) J Biol Inorg Chem , vol.9 , pp. 307-315
    • Farkas, E.1    Katz, Y.2    Bhusare, S.3    Reich, R.4    Roschenthaler, G.V.5    Konigsmann, M.6    Breuer, E.7
  • 23
    • 0032719798 scopus 로고    scopus 로고
    • Vascular matrix metalloproteinase-2 cleaves big endothelin-1 yielding a novel vasoconstrictor
    • Fernandez-Patron C, Radomski MW, Davidge ST (1999) Vascular matrix metalloproteinase-2 cleaves big endothelin-1 yielding a novel vasoconstrictor. Circ Res 85 : 906 911.
    • (1999) Circ Res , vol.85 , pp. 906-911
    • Fernandez-Patron, C.1    Radomski, M.W.2    Davidge, S.T.3
  • 24
    • 33846120591 scopus 로고    scopus 로고
    • Matrix metalloproteinases as valid clinical targets
    • Fingleton B (2007) Matrix metalloproteinases as valid clinical targets. Curr Pharm Des 13 : 333 346.
    • (2007) Curr Pharm des , vol.13 , pp. 333-346
    • Fingleton, B.1
  • 26
    • 0030717692 scopus 로고    scopus 로고
    • Tissue inhibitors of metalloproteinases: Structure, regulation and biological functions
    • Gomez DE, Alonso DF, Yoshiji H, Thorgeirsson UP (1997) Tissue inhibitors of metalloproteinases: Structure, regulation and biological functions. Eur J Cell Biol 74 : 111 122.
    • (1997) Eur J Cell Biol , vol.74 , pp. 111-122
    • Gomez, D.E.1    Alonso, D.F.2    Yoshiji, H.3    Thorgeirsson, U.P.4
  • 27
    • 33751229302 scopus 로고    scopus 로고
    • Oxidative mechanism and homeostasis of proteinase/antiproteinase in congestive heart failure
    • Henderson BC, Tyagi SC (2006) Oxidative mechanism and homeostasis of proteinase/antiproteinase in congestive heart failure. J Mol Cell Cardiol 41 : 959 962.
    • (2006) J Mol Cell Cardiol , vol.41 , pp. 959-962
    • Henderson, B.C.1    Tyagi, S.C.2
  • 29
    • 0030861387 scopus 로고    scopus 로고
    • Time dependent alterations of serum matrix metalloproteinase-1 and metalloproteinase-1 tissue inhibitor after successful reperfusion of acute myocardial infarction
    • Hirohata S, Kusachi S, Murakami M, Murakami T, Sano I, Watanabe T, Komatsubara I, Kondo J, Tsuji T (1997) Time dependent alterations of serum matrix metalloproteinase-1 and metalloproteinase-1 tissue inhibitor after successful reperfusion of acute myocardial infarction. Heart 78 : 278 284.
    • (1997) Heart , vol.78 , pp. 278-284
    • Hirohata, S.1    Kusachi, S.2    Murakami, M.3    Murakami, T.4    Sano, I.5    Watanabe, T.6    Komatsubara, I.7    Kondo, J.8    Tsuji, T.9
  • 31
    • 23844523196 scopus 로고    scopus 로고
    • Structure and mechanics of healing myocardial infarcts
    • Holmes JW, Borg TK, Covell JW (2005) Structure and mechanics of healing myocardial infarcts. Annu Rev Biomed Eng 7 : 223 253.
    • (2005) Annu Rev Biomed Eng , vol.7 , pp. 223-253
    • Holmes, J.W.1    Borg, T.K.2    Covell, J.W.3
  • 34
    • 0035147051 scopus 로고    scopus 로고
    • Plasma levels of matrix metalloproteinase-9 and tissue inhibitor of metalloproteinase-1 are increased in the coronary circulation in patients with acute coronary syndrome
    • Inokubo Y, Hanada H, Ishizaka H, Fukushi T, Kamada T, Okumura K (2001) 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 141 : 211 217.
    • (2001) Am Heart J , vol.141 , pp. 211-217
    • Inokubo, Y.1    Hanada, H.2    Ishizaka, H.3    Fukushi, T.4    Kamada, T.5    Okumura, K.6
  • 35
    • 33947692118 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Influence on smooth muscle cells and atherosclerotic plaque stability
    • Johnson JL (2007) Matrix metalloproteinases: Influence on smooth muscle cells and atherosclerotic plaque stability. Expert Rev Cardiovasc Ther 5 : 265 282.
    • (2007) Expert Rev Cardiovasc Ther , vol.5 , pp. 265-282
    • Johnson, J.L.1
  • 38
    • 24044458235 scopus 로고    scopus 로고
    • Combination of tumor necrosis factor-alpha ablation and matrix metalloproteinase inhibition prevents heart failure after pressure overload in tissue inhibitor of metalloproteinase-3 knock-out mice
    • Kassiri Z, Oudit GY, Sanchez O, Dawood F, Mohammed FF, Nuttall RK, Edwards DR, Liu PP, Backx PH, Khokha R (2005) Combination of tumor necrosis factor-alpha ablation and matrix metalloproteinase inhibition prevents heart failure after pressure overload in tissue inhibitor of metalloproteinase-3 knock-out mice. Circ Res 97 : 380 390.
    • (2005) Circ Res , vol.97 , pp. 380-390
    • Kassiri, Z.1    Oudit, G.Y.2    Sanchez, O.3    Dawood, F.4    Mohammed, F.F.5    Nuttall, R.K.6    Edwards, D.R.7    Liu, P.P.8    Backx, P.H.9    Khokha, R.10
  • 40
    • 0000393540 scopus 로고    scopus 로고
    • Proinflammatory cytokines regulate tissue inhibitors of metalloproteinases and disintegrin metalloproteinase in cardiac cells
    • Li YY, McTiernan CF, Feldman AM (1999) Proinflammatory cytokines regulate tissue inhibitors of metalloproteinases and disintegrin metalloproteinase in cardiac cells. Cardiovasc Res 42 : 162 172.
    • (1999) Cardiovasc Res , vol.42 , pp. 162-172
    • Li, Y.Y.1    McTiernan, C.F.2    Feldman, A.M.3
  • 41
    • 0034115630 scopus 로고    scopus 로고
    • MMP/TIMP expression in spontaneously hypertensive heart failure rats: The effect of ACE- and MMP-inhibition
    • Li H, Simon H, Bocan TM, Peterson JT (2000) MMP/TIMP expression in spontaneously hypertensive heart failure rats: The effect of ACE- and MMP-inhibition. Cardiovasc Res 46 : 298 306.
    • (2000) Cardiovasc Res , vol.46 , pp. 298-306
    • Li, H.1    Simon, H.2    Bocan, T.M.3    Peterson, J.T.4
  • 42
    • 1042280329 scopus 로고    scopus 로고
    • MMP induction and inhibition in myocardial infarction
    • Lindsey ML (2004) MMP induction and inhibition in myocardial infarction. Heart Fail Rev 9 : 7 19.
    • (2004) Heart Fail Rev , vol.9 , pp. 7-19
    • Lindsey, M.L.1
  • 44
    • 16344367552 scopus 로고    scopus 로고
    • Peripheral levels of matrix metalloproteinase-9, interleukin-6, and C-reactive protein are elevated in patients with acute coronary syndromes: Correlations with serum troponin I
    • Manginas A, Bei E, Chaidaroglou A, Degiannis D, Koniavitou K, Voudris V, Pavlides G, Panagiotakos D, Cokkinos DV (2005) Peripheral levels of matrix metalloproteinase-9, interleukin-6, and C-reactive protein are elevated in patients with acute coronary syndromes: Correlations with serum troponin I. Clin Cardiol 28 : 182 186.
    • (2005) Clin Cardiol , vol.28 , pp. 182-186
    • Manginas, A.1    Bei, E.2    Chaidaroglou, A.3    Degiannis, D.4    Koniavitou, K.5    Voudris, V.6    Pavlides, G.7    Panagiotakos, D.8    Cokkinos, D.V.9
  • 45
    • 0025230509 scopus 로고
    • Metalloproteinases and their inhibitors in matrix remodeling
    • Matrisian LM (1990) Metalloproteinases and their inhibitors in matrix remodeling. Trends Genet 6 : 121 125.
    • (1990) Trends Genet , vol.6 , pp. 121-125
    • Matrisian, L.M.1
  • 50
    • 31344458952 scopus 로고    scopus 로고
    • Structure and function of matrix metalloproteinases and TIMPs
    • Nagase H, Visse R, Murphy G (2006) Structure and function of matrix metalloproteinases and TIMPs. Cardiovasc Res 69 : 562 573.
    • (2006) Cardiovasc Res , vol.69 , pp. 562-573
    • Nagase, H.1    Visse, R.2    Murphy, G.3
  • 51
    • 31344447802 scopus 로고    scopus 로고
    • Matrix metalloproteinases regulate migration, proliferation, and death of vascular smooth muscle cells by degrading matrix and nonmatrix substrates
    • Newby AC (2006) Matrix metalloproteinases regulate migration, proliferation, and death of vascular smooth muscle cells by degrading matrix and nonmatrix substrates. Cardiovasc Res 69 : 614 624.
    • (2006) Cardiovasc Res , vol.69 , pp. 614-624
    • Newby, A.C.1
  • 52
    • 0034719482 scopus 로고    scopus 로고
    • Structure-activity relationships and pharmacokinetic analysis for a series of potent, systemically available biphenylsulfonamide matrix metalloproteinase inhibitors
    • O'Brien PM, Ortwine DF, Pavlovsky AG, Picard JA, Sliskovic DR, Roth BD, Dyer RD, Johnson LL, Man CF, Hallak H (2000) Structure-activity relationships and pharmacokinetic analysis for a series of potent, systemically available biphenylsulfonamide matrix metalloproteinase inhibitors. J Med Chem 43 : 156 166.
    • (2000) J Med Chem , vol.43 , pp. 156-166
    • O'Brien, P.M.1    Ortwine, D.F.2    Pavlovsky, A.G.3    Picard, J.A.4    Sliskovic, D.R.5    Roth, B.D.6    Dyer, R.D.7    Johnson, L.L.8    Man, C.F.9    Hallak, H.10
  • 53
    • 33645738383 scopus 로고    scopus 로고
    • Towards third generation matrix metalloproteinase inhibitors for cancer therapy
    • Overall CM, Kleifeld O (2006) Towards third generation matrix metalloproteinase inhibitors for cancer therapy. Br J Cancer 94 : 941 946.
    • (2006) Br J Cancer , vol.94 , pp. 941-946
    • Overall, C.M.1    Kleifeld, O.2
  • 54
    • 0025866180 scopus 로고
    • Transcriptional and post-transcriptional regulation of 72-kDa gelatinase/type IV collagenase by transforming growth factor-beta 1 in human fibroblasts. Comparisons with collagenase and tissue inhibitor of matrix metalloproteinase gene expression
    • Overall CM, Wrana JL, Sodek J (1991) Transcriptional and post-transcriptional regulation of 72-kDa gelatinase/type IV collagenase by transforming growth factor-beta 1 in human fibroblasts. Comparisons with collagenase and tissue inhibitor of matrix metalloproteinase gene expression. J Biol Chem 266 : 14064 14071.
    • (1991) J Biol Chem , vol.266 , pp. 14064-14071
    • Overall, C.M.1    Wrana, J.L.2    Sodek, J.3
  • 55
    • 33847195428 scopus 로고    scopus 로고
    • Matrix metalloproteinases and the regulation of tissue remodelling
    • Page-McCaw A, Ewald AJ, Werb Z (2007) Matrix metalloproteinases and the regulation of tissue remodelling. Nat Rev Mol Cell Biol 8 : 221 233.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 221-233
    • Page-Mccaw, A.1    Ewald, A.J.2    Werb, Z.3
  • 57
    • 1042263796 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitor development and the remodeling of drug discovery
    • Peterson JT (2004) Matrix metalloproteinase inhibitor development and the remodeling of drug discovery. Heart Fail Rev 9 : 63 79.
    • (2004) Heart Fail Rev , vol.9 , pp. 63-79
    • Peterson, J.T.1
  • 58
    • 31344456635 scopus 로고    scopus 로고
    • The importance of estimating the therapeutic index in the development of matrix metalloproteinase inhibitors
    • Peterson JT (2006) The importance of estimating the therapeutic index in the development of matrix metalloproteinase inhibitors. Cardiovasc Res 69 : 677 687.
    • (2006) Cardiovasc Res , vol.69 , pp. 677-687
    • Peterson, J.T.1
  • 59
    • 0034032314 scopus 로고    scopus 로고
    • Evolution of matrix metalloprotease and tissue inhibitor expression during heart failure progression in the infarcted rat
    • Peterson JT, Li H, Dillon L, Bryant JW (2000) Evolution of matrix metalloprotease and tissue inhibitor expression during heart failure progression in the infarcted rat. Cardiovasc Res 46 : 307 315.
    • (2000) Cardiovasc Res , vol.46 , pp. 307-315
    • Peterson, J.T.1    Li, H.2    Dillon, L.3    Bryant, J.W.4
  • 61
    • 0037474256 scopus 로고    scopus 로고
    • Isolation by zinc-affinity chromatography of the histidine-proline-rich- glycoprotein molecule associated with rabbit skeletal muscle AMP deaminase. Evidence that the formation of a protein-protein complex between the catalytic subunit and the novel component is critical for the stability of the enzyme
    • Ranieri-Raggi M, Martini D, Sabbatini AR, Moir AJ, Raggi A (2003) Isolation by zinc-affinity chromatography of the histidine-proline-rich- glycoprotein molecule associated with rabbit skeletal muscle AMP deaminase. Evidence that the formation of a protein-protein complex between the catalytic subunit and the novel component is critical for the stability of the enzyme. Biochim Biophys Acta 1645 : 81 88.
    • (2003) Biochim Biophys Acta , vol.1645 , pp. 81-88
    • Ranieri-Raggi, M.1    Martini, D.2    Sabbatini, A.R.3    Moir, A.J.4    Raggi, A.5
  • 62
    • 14044274265 scopus 로고    scopus 로고
    • Recent developments in the design of specific Matrix Metalloproteinase inhibitors aided by structural and computational studies
    • Rao BG (2005) Recent developments in the design of specific Matrix Metalloproteinase inhibitors aided by structural and computational studies. Curr Pharm Des 11 : 295 322.
    • (2005) Curr Pharm des , vol.11 , pp. 295-322
    • Rao, B.G.1
  • 64
    • 31344477494 scopus 로고    scopus 로고
    • Myocardial proteases and matrix remodeling in inflammatory heart disease
    • Rutschow S, Li J, Schultheiss HP, Pauschinger M (2006) Myocardial proteases and matrix remodeling in inflammatory heart disease. Cardiovasc Res 69 : 646 656.
    • (2006) Cardiovasc Res , vol.69 , pp. 646-656
    • Rutschow, S.1    Li, J.2    Schultheiss, H.P.3    Pauschinger, M.4
  • 65
    • 0029157653 scopus 로고
    • Matrix metalloproteinase matrilysin is constitutively expressed in adult human exocrine epithelium
    • Saarialho-Kere UK, Crouch EC, Parks WC (1995) Matrix metalloproteinase matrilysin is constitutively expressed in adult human exocrine epithelium. J Invest Dermatol 105 : 190 196.
    • (1995) J Invest Dermatol , vol.105 , pp. 190-196
    • Saarialho-Kere, U.K.1    Crouch, E.C.2    Parks, W.C.3
  • 66
    • 33646032130 scopus 로고    scopus 로고
    • Lower serum concentration of matrix metalloproteinase-3 in the acute stage of myocardial infarction
    • Samnegard A, Silveira A, Tornvall P, Hamsten A, Ericsson CG, Eriksson P (2006) Lower serum concentration of matrix metalloproteinase-3 in the acute stage of myocardial infarction. J Intern Med 259 : 530 536.
    • (2006) J Intern Med , vol.259 , pp. 530-536
    • Samnegard, A.1    Silveira, A.2    Tornvall, P.3    Hamsten, A.4    Ericsson, C.G.5    Eriksson, P.6
  • 67
    • 0030946445 scopus 로고    scopus 로고
    • Release of gelatinase a during platelet activation mediates aggregation
    • Sawicki G, Salas E, Murat J, Miszta-Lane H, Radomski MW (1997) Release of gelatinase A during platelet activation mediates aggregation. Nature 386 : 616 619.
    • (1997) Nature , vol.386 , pp. 616-619
    • Sawicki, G.1    Salas, E.2    Murat, J.3    Miszta-Lane, H.4    Radomski, M.W.5
  • 68
    • 33847020733 scopus 로고    scopus 로고
    • Intracellular targets of matrix metalloproteinase-2 in cardiac disease: Rationale and therapeutic approaches
    • Schulz R (2007) Intracellular targets of matrix metalloproteinase-2 in cardiac disease: Rationale and therapeutic approaches. Annu Rev Pharmacol Toxicol 47 : 211 242.
    • (2007) Annu Rev Pharmacol Toxicol , vol.47 , pp. 211-242
    • Schulz, R.1
  • 69
    • 0344372732 scopus 로고
    • Common acute lymphoblastic leukemia antigen (CALLA) is active neutral endopeptidase 24.11 ("enkephalinase"): Direct evidence by cDNA transfection analysis
    • Shipp MA, Vijayaraghavan J, Schmidt EV, Masteller EL, D'Adamio L, Hersh LB, Reinherz EL (1989) Common acute lymphoblastic leukemia antigen (CALLA) is active neutral endopeptidase 24.11 ("enkephalinase"): Direct evidence by cDNA transfection analysis. Proc Natl Acad Sci U.S.A 86 : 297 301.
    • (1989) Proc Natl Acad Sci U.S.A , vol.86 , pp. 297-301
    • Shipp, M.A.1    Vijayaraghavan, J.2    Schmidt, E.V.3    Masteller, E.L.4    D'Adamio, L.5    Hersh, L.B.6    Reinherz, E.L.7
  • 70
    • 0034995893 scopus 로고    scopus 로고
    • Oxidative stress regulates collagen synthesis and matrix metalloproteinase activity in cardiac fibroblasts
    • Siwik DA, Pagano PJ, Colucci WS (2001) Oxidative stress regulates collagen synthesis and matrix metalloproteinase activity in cardiac fibroblasts. Am J Physiol Cell Physiol : C53 C60.
    • (2001) Am J Physiol Cell Physiol
    • Siwik, D.A.1    Pagano, P.J.2    Colucci, W.S.3
  • 72
    • 35748974863 scopus 로고    scopus 로고
    • Myocardial matrix remodeling and the matrix metalloproteinases: Influence on cardiac form and function
    • Spinale FG (2007) Myocardial matrix remodeling and the matrix metalloproteinases: Influence on cardiac form and function. Physiol Rev 87 : 1285 1342.
    • (2007) Physiol Rev , vol.87 , pp. 1285-1342
    • Spinale, F.G.1
  • 74
    • 27744607688 scopus 로고    scopus 로고
    • Proprotein convertases furin and PC5: Targeting atherosclerosis and restenosis at multiple levels
    • Stawowy P, Fleck E (2005) Proprotein convertases furin and PC5: Targeting atherosclerosis and restenosis at multiple levels. J Mol Med 83 : 865 875.
    • (2005) J Mol Med , vol.83 , pp. 865-875
    • Stawowy, P.1    Fleck, E.2
  • 75
    • 0027238419 scopus 로고
    • Direct extraction and estimation of collagenase(s) activity by zymography in microquantities of rat myocardium and uterus
    • 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.
    • (1993) Clin Biochem , vol.26 , pp. 191-198
    • Tyagi, S.C.1    Matsubara, L.2    Weber, K.T.3
  • 76
    • 31344477231 scopus 로고    scopus 로고
    • Relevance of matrix metalloproteinases and their inhibitors after myocardial infarction: A temporal and spatial window
    • Vanhoutte D, Schellings M, Pinto Y, Heymans S (2006) Relevance of matrix metalloproteinases and their inhibitors after myocardial infarction: A temporal and spatial window. Cardiovasc Res 69 : 604 613.
    • (2006) Cardiovasc Res , vol.69 , pp. 604-613
    • Vanhoutte, D.1    Schellings, M.2    Pinto, Y.3    Heymans, S.4
  • 77
    • 33846906016 scopus 로고    scopus 로고
    • Matrix metalloproteinases (MMPs): Chemical-biological functions and (Q)SARs
    • Verma RP, Hansch C (2007) Matrix metalloproteinases (MMPs): Chemical-biological functions and (Q)SARs. Bioorg Med Chem 15 : 2223 2268.
    • (2007) Bioorg Med Chem , vol.15 , pp. 2223-2268
    • Verma, R.P.1    Hansch, C.2
  • 81
    • 31344438587 scopus 로고    scopus 로고
    • Influence of matrix metalloproteinase genotype on cardiovascular disease susceptibility and outcome
    • Ye S (2006) Influence of matrix metalloproteinase genotype on cardiovascular disease susceptibility and outcome. Cardiovasc Res 69 : 636 645.
    • (2006) Cardiovasc Res , vol.69 , pp. 636-645
    • Ye, S.1
  • 82
    • 0026447262 scopus 로고
    • Purification and characterization of the human stromelysin catalytic domain expressed in Escherichia coli
    • Ye QZ, Johnson LL, Hupe DJ, Baragi V (1992) Purification and characterization of the human stromelysin catalytic domain expressed in Escherichia coli. Biochemistry 31 : 11231 11235.
    • (1992) Biochemistry , vol.31 , pp. 11231-11235
    • Ye, Q.Z.1    Johnson, L.L.2    Hupe, D.J.3    Baragi, V.4
  • 83
    • 0028118824 scopus 로고
    • A recombinant human stromelysin catalytic domain identifying tryptophan derivatives as human stromelysin inhibitors
    • Ye QZ, Johnson LL, Nordan I, Hupe D, Hupe L (1994) A recombinant human stromelysin catalytic domain identifying tryptophan derivatives as human stromelysin inhibitors. J Med Chem 37 : 206 209.
    • (1994) J Med Chem , vol.37 , pp. 206-209
    • Ye, Q.Z.1    Johnson, L.L.2    Nordan, I.3    Hupe, D.4    Hupe, L.5
  • 84
    • 0028914517 scopus 로고
    • Reconstructed 19 kDa catalytic domain of gelatinase a is an active proteinase
    • Ye QZ, Johnson LL, Yu AE, Hupe D (1995) Reconstructed 19 kDa catalytic domain of gelatinase A is an active proteinase. Biochemistry 34 : 4702 4708.
    • (1995) Biochemistry , vol.34 , pp. 4702-4708
    • Ye, Q.Z.1    Johnson, L.L.2    Yu, A.E.3    Hupe, D.4


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