메뉴 건너뛰기




Volumn 5, Issue 1, 2010, Pages 13-25

Erratum to Matrix metalloproteinases and peripheral arterial disease (Intern Emerg Med, DOI 10.1007/s11739-009-0283-y);Matrix metalloproteinases and peripheral arterial disease

Author keywords

Atherosclerosis; Biomarkers; Inflammation; Matrix metalloproteinases; Peripheral arterial disease; Platelets; Thrombosis

Indexed keywords


EID: 76049125185     PISSN: 18280447     EISSN: 19709366     Source Type: Journal    
DOI: 10.1007/s11739-009-0308-6     Document Type: Erratum
Times cited : (88)

References (77)
  • 1
    • 0027276427 scopus 로고
    • Introduction to serial reviews: The extracellular matrix
    • Woessner JF (1993) Introduction to serial reviews: the extracellular matrix. FASEB J 7: 735-736.
    • (1993) FASEB J , vol.7 , pp. 735-736
    • Woessner, J.F.1
  • 2
    • 33947608239 scopus 로고    scopus 로고
    • Matrix metalloproteinases in peripheral vascular disease
    • Hobeika MJ (2007) Matrix metalloproteinases in peripheral vascular disease. J Vasc Surg 45: 849-857.
    • (2007) J Vasc Surg , vol.45 , pp. 849-857
    • Hobeika, M.J.1
  • 3
    • 12844286997 scopus 로고    scopus 로고
    • Dual role of matrix metalloproteinases (Matrixins) in intimal thickening and atherosclerotic plaque rupture
    • Newby AC (2005) Dual role of matrix metalloproteinases (Matrixins) in intimal thickening and atherosclerotic plaque rupture. Physiol Rev 85: 1-31.
    • (2005) Physiol Rev , vol.85 , pp. 1-31
    • Newby, A.C.1
  • 4
    • 0033523040 scopus 로고    scopus 로고
    • Structure of human pro-matrix metalloproteinase-2: Activation mechanism revealed
    • Morgunova E, Tuuttila A, Bergmann U et al (1999) Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed. Science 284: 1667-1670.
    • (1999) Science , vol.284 , pp. 1667-1670
    • Morgunova, E.1    Tuuttila, A.2    Bergmann, U.3
  • 5
    • 0025025442 scopus 로고
    • The cysteine switch: A principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family
    • van Wart HE, Birkedal-Hansen H (1990) 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 87: 5578-5582.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 5578-5582
    • van Wart, H.E.1    Birkedal-Hansen, H.2
  • 6
    • 0032516473 scopus 로고    scopus 로고
    • Flow regulation of 72 KD-collagenase IV (MMP-2) after experimental arterial injury
    • Bassiouny HS, Song RH, Hong XF et al (1998) Flow regulation of 72 KD-collagenase IV (MMP-2) after experimental arterial injury. Circulation 98: 157-163.
    • (1998) Circulation , vol.98 , pp. 157-163
    • Bassiouny, H.S.1    Song, R.H.2    Hong, X.F.3
  • 7
    • 0034610468 scopus 로고    scopus 로고
    • Remodelling of carotid artery is associated with increased expression of matrix metalloproteinases in mouse blood flow cessation model
    • Godin D, Ivan E, Johnson C et al (2000) Remodelling of carotid artery is associated with increased expression of matrix metalloproteinases in mouse blood flow cessation model. Circulation 102: 2861-2866.
    • (2000) Circulation , vol.102 , pp. 2861-2866
    • Godin, D.1    Ivan, E.2    Johnson, C.3
  • 8
    • 0032754564 scopus 로고    scopus 로고
    • Transmural pressure induces matrix-degrading activity in porcine arteries ex vivo
    • Chesler NC, Ku DN, Galis ZS (1999) Transmural pressure induces matrix-degrading activity in porcine arteries ex vivo. Am J Physiol 277: H2002-H2009.
    • (1999) Am J Physiol , vol.277
    • Chesler, N.C.1    Ku, D.N.2    Galis, Z.S.3
  • 10
    • 10544246489 scopus 로고    scopus 로고
    • Reactive oxygen species produced by macrophage-derived foam cells regulate activity of vascular matrix metalloproteinases in vitro
    • Rajagopalan S, Meng XP, Ramasamy S et al (1996) Reactive oxygen species produced by macrophage-derived foam cells regulate activity of vascular matrix metalloproteinases in vitro. J Clin Invest 98: 2572-2579.
    • (1996) J Clin Invest , vol.98 , pp. 2572-2579
    • Rajagopalan, S.1    Meng, X.P.2    Ramasamy, S.3
  • 11
    • 0030028593 scopus 로고    scopus 로고
    • Inactivation of tissue inhibitor of metalloproteinase-1 by peroxynitrite
    • Frears ER, Zhang Z, Blake DR et al (1996) Inactivation of tissue inhibitor of metalloproteinase-1 by peroxynitrite. FEBS Lett 381: 21-24.
    • (1996) FEBS Lett , vol.381 , pp. 21-24
    • Frears, E.R.1    Zhang, Z.2    Blake, D.R.3
  • 12
    • 11144277482 scopus 로고    scopus 로고
    • Effects of age, gender, ethnicity, diurnal variation and exercise on circulating levels of matrix metalloproteinases MMP-2 and -9, and their inhibitors, tissue inhibitors of matrix metalloproteinases TIMP-1 and -2
    • Tayebjee MH, Lip GY, Blann AD et al (2005) Effects of age, gender, ethnicity, diurnal variation and exercise on circulating levels of matrix metalloproteinases MMP-2 and -9, and their inhibitors, tissue inhibitors of matrix metalloproteinases TIMP-1 and -2. Thromb Res 115: 205-210.
    • (2005) Thromb Res , vol.115 , pp. 205-210
    • Tayebjee, M.H.1    Lip, G.Y.2    Blann, A.D.3
  • 13
    • 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
  • 14
    • 38649136309 scopus 로고    scopus 로고
    • Role of metalloproteinases in platelet function
    • Santos-Martínez MJ, Medina C, Jurasz P et al (2008) Role of metalloproteinases in platelet function. Thromb Res 121: 535-542.
    • (2008) Thromb Res , vol.121 , pp. 535-542
    • Santos-Martínez, M.J.1    Medina, C.2    Jurasz, P.3
  • 15
    • 0030946445 scopus 로고    scopus 로고
    • Release of gelatinase A during platelet activation mediates aggregation
    • Sawicki G, Salas E, Murat J et al (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
  • 16
    • 28444487916 scopus 로고    scopus 로고
    • Intraplatelet signaling mechanisms of the priming effect of matrix metalloproteinase-2 on platelet aggregation
    • Falcinelli E, Guglielmini G, Torti M et al (2005) Intraplatelet signaling mechanisms of the priming effect of matrix metalloproteinase-2 on platelet aggregation. J Thromb Haemost 3: 2526-2535.
    • (2005) J Thromb Haemost , vol.3 , pp. 2526-2535
    • Falcinelli, E.1    Guglielmini, G.2    Torti, M.3
  • 17
    • 0037205285 scopus 로고    scopus 로고
    • Outside-in signals delivered by matrix metalloproteinase-1 regulate platelet function
    • Galt SW, Lindemann S, Allen L et al (2002) Outside-in signals delivered by matrix metalloproteinase-1 regulate platelet function. Circ Res 90: 1093-1099.
    • (2002) Circ Res , vol.90 , pp. 1093-1099
    • Galt, S.W.1    Lindemann, S.2    Allen, L.3
  • 18
    • 40949141930 scopus 로고    scopus 로고
    • Allergen induces the migration of platelets to lung tissue in allergic asthma
    • Pitchford SC, Momi S, Baglioni S et al (2008) Allergen induces the migration of platelets to lung tissue in allergic asthma. Am J Respir Crit Care Med 177: 604-612.
    • (2008) Am J Respir Crit Care Med , vol.177 , pp. 604-612
    • Pitchford, S.C.1    Momi, S.2    Baglioni, S.3
  • 19
  • 20
    • 2942546273 scopus 로고    scopus 로고
    • Release of soluble CD40L from platelets is regulated by glycoprotein IIb/IIIa and actin polymerization
    • Furman MI, Krueger LA, Linden MD et al (2004) Release of soluble CD40L from platelets is regulated by glycoprotein IIb/IIIa and actin polymerization. J Am Coll Cardiol 43: 2319-2325.
    • (2004) J Am Coll Cardiol , vol.43 , pp. 2319-2325
    • Furman, M.I.1    Krueger, L.A.2    Linden, M.D.3
  • 21
    • 0035019911 scopus 로고    scopus 로고
    • ApoE knockout mice expressing human matrix metalloproteinase-1 in macrophages have less advanced atherosclerosis
    • Emaitre V, O'Byrne TK, Borczuk AC et al (2001) ApoE knockout mice expressing human matrix metalloproteinase-1 in macrophages have less advanced atherosclerosis. J Clin Invest 107: 1227-1234.
    • (2001) J Clin Invest , vol.107 , pp. 1227-1234
    • Emaitre, V.1    O'Byrne, T.K.2    Borczuk, A.C.3
  • 22
    • 0035572899 scopus 로고    scopus 로고
    • Persistence of atherosclerotic plaque but reduced aneurysm formation in mice with stromelysin-1 (MMP-3) gene inactivation
    • Ilence J, Lupu F, Collen D et al (2001) Persistence of atherosclerotic plaque but reduced aneurysm formation in mice with stromelysin-1 (MMP-3) gene inactivation. Arterioscler Thromb Vasc Biol 21: 1440-1445.
    • (2001) Arterioscler Thromb Vasc Biol , vol.21 , pp. 1440-1445
    • Ilence, J.1    Lupu, F.2    Collen, D.3
  • 23
    • 0031903487 scopus 로고    scopus 로고
    • Function of the plasminogen/plasmin and matrix metalloproteinase systems after vascular injury in mice with targeted inactivation of fibrinolytic system genes
    • Lijnen HR, van Hoef B, Lupu F et al (1998) Function of the plasminogen/plasmin and matrix metalloproteinase systems after vascular injury in mice with targeted inactivation of fibrinolytic system genes. Arterioscler Thromb Vasc Biol 18: 1035-1045.
    • (1998) Arterioscler Thromb Vasc Biol , vol.18 , pp. 1035-1045
    • Lijnen, H.R.1    van Hoef, B.2    Lupu, F.3
  • 24
    • 0028063408 scopus 로고
    • Increased expression of matrix metalloproteinases and matrix degrading activity in vulnerable regions of human atherosclerotic plaques
    • Galis ZS, Sukhova GK, Lark MW et al (1994) Increased expression of matrix metalloproteinases and matrix degrading activity in vulnerable regions of human atherosclerotic plaques. J Clin Invest 94: 2493-2503.
    • (1994) J Clin Invest , vol.94 , pp. 2493-2503
    • Galis, Z.S.1    Sukhova, G.K.2    Lark, M.W.3
  • 25
    • 0031003372 scopus 로고    scopus 로고
    • Differential expression of 92-kDa gelatinase in primary atherosclerotic versus restenotic coronary lesions
    • Brown DL, Hibbs MS, Kearney M et al (1997) Differential expression of 92-kDa gelatinase in primary atherosclerotic versus restenotic coronary lesions. Am J Cardiol 79: 878-882.
    • (1997) Am J Cardiol , vol.79 , pp. 878-882
    • Brown, D.L.1    Hibbs, M.S.2    Kearney, M.3
  • 26
    • 1642390201 scopus 로고    scopus 로고
    • Matrix metalloproteinases: A review of their structure and role in acute coronary syndromes
    • Jones CB, Sane DC, Herrington DM (2003) Matrix metalloproteinases: a review of their structure and role in acute coronary syndromes. Cardiovasc Res 59: 812-823.
    • (2003) Cardiovasc Res , vol.59 , pp. 812-823
    • Jones, C.B.1    Sane, D.C.2    Herrington, D.M.3
  • 27
    • 0036186650 scopus 로고    scopus 로고
    • Matrix metalloproteinase expression in the coronary circulation induced by coronary angioplasty
    • Hojo Y, Ikeda U, Katsuki T et al (2002) Matrix metalloproteinase expression in the coronary circulation induced by coronary angioplasty. Atherosclerosis 161: 185-192.
    • (2002) Atherosclerosis , vol.161 , pp. 185-192
    • Hojo, Y.1    Ikeda, U.2    Katsuki, T.3
  • 28
    • 0030896416 scopus 로고    scopus 로고
    • Thrombin promotes activation of matrix metalloproteinase-2 produced by cultured vascular smooth muscle cells
    • Galis ZS, Kranzhofer R, Fenton JW 2nd et al (1997) Thrombin promotes activation of matrix metalloproteinase-2 produced by cultured vascular smooth muscle cells. Arterioscler Thromb Vasc Biol 17: 483-489.
    • (1997) Arterioscler Thromb Vasc Biol , vol.17 , pp. 483-489
    • Galis, Z.S.1    Kranzhofer, R.2    Fenton 2nd, J.W.3
  • 29
    • 45849092207 scopus 로고    scopus 로고
    • Potentiation and priming of platelet activation: A potential target of antiplatelet therapy
    • Gresele P, Falcinelli E, Momi S (2008) Potentiation and priming of platelet activation: a potential target of antiplatelet therapy. Trends Pharmacol Sci 29: 352-360.
    • (2008) Trends Pharmacol Sci , vol.29 , pp. 352-360
    • Gresele, P.1    Falcinelli, E.2    Momi, S.3
  • 30
    • 0031014499 scopus 로고    scopus 로고
    • Evidence for altered balance between matrix metalloproteinases and their inhibitors in human aortic diseases
    • Knox JB, Sukhova GK, Whittemore AD et al (1997) Evidence for altered balance between matrix metalloproteinases and their inhibitors in human aortic diseases. Circulation 95: 205-212.
    • (1997) Circulation , vol.95 , pp. 205-212
    • Knox, J.B.1    Sukhova, G.K.2    Whittemore, A.D.3
  • 31
    • 0035902584 scopus 로고    scopus 로고
    • Ubiquitous elevation of matrix metalloproteinase-2 expression in the vasculature of patients with abdominal aneurysms
    • Goodall S, Crowther M, Hemingway DM et al (2001) Ubiquitous elevation of matrix metalloproteinase-2 expression in the vasculature of patients with abdominal aneurysms. Circulation 104: 304-309.
    • (2001) Circulation , vol.104 , pp. 304-309
    • Goodall, S.1    Crowther, M.2    Hemingway, D.M.3
  • 32
    • 49349107741 scopus 로고    scopus 로고
    • Potential circulating biomarkers for abdominal aortic aneurysm expansion and rupture-a systematic review
    • Urbonavicius S, Urbonaviciene G, Honorè B et al (2008) Potential circulating biomarkers for abdominal aortic aneurysm expansion and rupture-a systematic review. Eur J Vasc Endovasc Surg 36: 273-280.
    • (2008) Eur J Vasc Endovasc Surg , vol.36 , pp. 273-280
    • Urbonavicius, S.1    Urbonaviciene, G.2    Honorè, B.3
  • 33
    • 0032160033 scopus 로고    scopus 로고
    • Complex role of matrix metalloproteinases in angiogenesis
    • Sang QX (1998) Complex role of matrix metalloproteinases in angiogenesis. Cell Res 8: 171-177.
    • (1998) Cell Res , vol.8 , pp. 171-177
    • Sang, Q.X.1
  • 34
    • 0038047053 scopus 로고    scopus 로고
    • Temporal expression and activation of matrix metalloproteinases-2, -9, and membrane type 1-matrix metalloproteinase following acute hindlimb ischemia
    • Muhs BE, Plitas G, Delgado Y et al (2003) Temporal expression and activation of matrix metalloproteinases-2, -9, and membrane type 1-matrix metalloproteinase following acute hindlimb ischemia. J Surg Res 111: 8-15.
    • (2003) J Surg Res , vol.111 , pp. 8-15
    • Muhs, B.E.1    Plitas, G.2    Delgado, Y.3
  • 35
    • 22344437713 scopus 로고    scopus 로고
    • Processing of VEGF-A by matrix metalloproteinases regulates bioavailability and vascular patterning in tumors
    • Lee S, Jilani SM, Nikolova GV et al (2005) Processing of VEGF-A by matrix metalloproteinases regulates bioavailability and vascular patterning in tumors. J Cell Biol 169: 681-691.
    • (2005) J Cell Biol , vol.169 , pp. 681-691
    • Lee, S.1    Jilani, S.M.2    Nikolova, G.V.3
  • 36
    • 0036791588 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9-dependent exposure of a cryptic migratory control site in collagen is required before retinal angiogenesis
    • Hangai M, Kitaya N, Xu J et al (2002) Matrix metalloproteinase-9-dependent exposure of a cryptic migratory control site in collagen is required before retinal angiogenesis. Am J Pathol 161: 1429-1437.
    • (2002) Am J Pathol , vol.161 , pp. 1429-1437
    • Hangai, M.1    Kitaya, N.2    Xu, J.3
  • 37
    • 18444389451 scopus 로고    scopus 로고
    • Recruitment of stem and progenitor cells from the bone marrow niche requires MMP-9-mediated release of kit-ligand
    • Hessig B, Hattori K, Dias S et al (2002) Recruitment of stem and progenitor cells from the bone marrow niche requires MMP-9-mediated release of kit-ligand. Cell 109: 625-637.
    • (2002) Cell , vol.109 , pp. 625-637
    • Hessig, B.1    Hattori, K.2    Dias, S.3
  • 39
    • 0345516003 scopus 로고    scopus 로고
    • Increased expression of membrane-type matrix metalloproteinase and preferential localization of matrix metalloproteinase-2 to the neointima of balloon-injured rat carotid arteries
    • Jenkins GM, Crow MT, Bilato C et al (1998) Increased expression of membrane-type matrix metalloproteinase and preferential localization of matrix metalloproteinase-2 to the neointima of balloon-injured rat carotid arteries. Circulation 97: 82-90.
    • (1998) Circulation , vol.97 , pp. 82-90
    • Jenkins, G.M.1    Crow, M.T.2    Bilato, C.3
  • 40
    • 57149133404 scopus 로고    scopus 로고
    • Molecular imaging of activated matrix metalloproteinases in vascular remodeling
    • Zang J, Nie L, Razavian M et al (2008) Molecular imaging of activated matrix metalloproteinases in vascular remodeling. Circulation 118: 1953-1960.
    • (2008) Circulation , vol.118 , pp. 1953-1960
    • Zang, J.1    Nie, L.2    Razavian, M.3
  • 41
    • 0033533995 scopus 로고    scopus 로고
    • Tissue inhibitor of matrix metalloproteinases-1 impairs arterial neointima formation after vascular injury in mice
    • Lijnen HR, Soloway P, Collen D (1999) Tissue inhibitor of matrix metalloproteinases-1 impairs arterial neointima formation after vascular injury in mice. Circ Res 85: 1186-1191.
    • (1999) Circ Res , vol.85 , pp. 1186-1191
    • Lijnen, H.R.1    Soloway, P.2    Collen, D.3
  • 42
    • 34249294496 scopus 로고    scopus 로고
    • Clinical, cellular, and molecular aspects of arterial calcification
    • Guzman JR (2007) Clinical, cellular, and molecular aspects of arterial calcification. J Vasc Surg 45: A57-A63.
    • (2007) J Vasc Surg , vol.45
    • Guzman, J.R.1
  • 43
    • 0029954662 scopus 로고    scopus 로고
    • Risk factors predicting lower extremity amputations in patients with NIDDM
    • Lehto S, Rönnemaa T, Pyörälä K et al (1996) Risk factors predicting lower extremity amputations in patients with NIDDM. Diabetes Care 19: 607-612.
    • (1996) Diabetes Care , vol.19 , pp. 607-612
    • Lehto, S.1    Rönnemaa, T.2    Pyörälä, K.3
  • 44
    • 10044280353 scopus 로고    scopus 로고
    • Elastin degradation and calcification in an abdominal aorta injury model
    • Basalyga DM, Simionescu DT, Xiong W et al (2004) Elastin degradation and calcification in an abdominal aorta injury model. Circulation 110: 3480-3487.
    • (2004) Circulation , vol.110 , pp. 3480-3487
    • Basalyga, D.M.1    Simionescu, D.T.2    Xiong, W.3
  • 45
    • 33745936075 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibition attenuates aortic calcification
    • Qin X, Corriere MA, Matrisian LM et al (2006) Matrix metalloproteinase inhibition attenuates aortic calcification. Arterioscler Thromb Vasc Biol 26: 1510-1516.
    • (2006) Arterioscler Thromb Vasc Biol , vol.26 , pp. 1510-1516
    • Qin, X.1    Corriere, M.A.2    Matrisian, L.M.3
  • 46
    • 38449083353 scopus 로고    scopus 로고
    • Risk assessment in the patient with established peripheral arterial disease
    • Haugen S, Casserly IP, Regensteiner JG et al (2007) Risk assessment in the patient with established peripheral arterial disease. Vasc Med 12: 343-350.
    • (2007) Vasc Med , vol.12 , pp. 343-350
    • Haugen, S.1    Casserly, I.P.2    Regensteiner, J.G.3
  • 47
    • 34548684818 scopus 로고    scopus 로고
    • B2-Microglobulin as a biomarker in peripheral arterial disease: Proteomic profiling and clinical studies
    • Wilson AM, Kimura E, Harada RK et al (2007) B2-Microglobulin as a biomarker in peripheral arterial disease: proteomic profiling and clinical studies. Circulation 116: 1396-1403.
    • (2007) Circulation , vol.116 , pp. 1396-1403
    • Wilson, A.M.1    Kimura, E.2    Harada, R.K.3
  • 48
    • 60649092316 scopus 로고    scopus 로고
    • Plasma levels of beta(2)-microglobulin, a biomarker of peripheral arterial disease, are not affected by maximal leg exercise in patients with intermittent claudication
    • Busti C, Migliacci R, Falcinelli E et al (2009) Plasma levels of beta(2)-microglobulin, a biomarker of peripheral arterial disease, are not affected by maximal leg exercise in patients with intermittent claudication. Atherosclerosis 203: 38-40.
    • (2009) Atherosclerosis , vol.203 , pp. 38-40
    • Busti, C.1    Migliacci, R.2    Falcinelli, E.3
  • 49
    • 47649090393 scopus 로고    scopus 로고
    • Cystatine C-a marker of peripheral arterial disease?
    • Arpegrad J, Ostergren J, de Faire U et al (2008) Cystatine C-a marker of peripheral arterial disease? Atherosclerosis 199: 397-401.
    • (2008) Atherosclerosis , vol.199 , pp. 397-401
    • Arpegrad, J.1    Ostergren, J.2    de Faire, U.3
  • 50
    • 34547959390 scopus 로고    scopus 로고
    • Different roles of MMP-2 and-9 after human ischaemic stroke
    • Lucivero V, Prontera M, Mezzapesa DM et al (2007) Different roles of MMP-2 and-9 after human ischaemic stroke. Neurol Sci 28: 165-170.
    • (2007) Neurol Sci , vol.28 , pp. 165-170
    • Lucivero, V.1    Prontera, M.2    Mezzapesa, D.M.3
  • 51
    • 23044482635 scopus 로고    scopus 로고
    • Plasma matrix metalloproteinase-9 tissue inhibitor of metalloproteinase-2, and CD40 ligand levels in patients with stable coronary artery disease
    • Tayebjee MH, Lip GY, Tan KT et al (2005) Plasma matrix metalloproteinase-9 tissue inhibitor of metalloproteinase-2, and CD40 ligand levels in patients with stable coronary artery disease. Am J Cardiol 96: 339-345.
    • (2005) Am J Cardiol , vol.96 , pp. 339-345
    • Tayebjee, M.H.1    Lip, G.Y.2    Tan, K.T.3
  • 52
    • 0037381597 scopus 로고    scopus 로고
    • Plasma concentrations and genetic variation of matrix metalloproteinase 9 and prognosis of patients with cardiovascular disease
    • Blankenberg S, Rupprecht HJ, Poirier O et al (2003) Plasma concentrations and genetic variation of matrix metalloproteinase 9 and prognosis of patients with cardiovascular disease. Circulation 107: 1579-1585.
    • (2003) Circulation , vol.107 , pp. 1579-1585
    • Blankenberg, S.1    Rupprecht, H.J.2    Poirier, O.3
  • 53
    • 33750558522 scopus 로고    scopus 로고
    • Elevated matrix metalloproteinase-9 associated with stroke or cardiovascular death in patients with carotid stenosis
    • Eldrup N, Gronholdt ML, Sillesen H et al (2006) Elevated matrix metalloproteinase-9 associated with stroke or cardiovascular death in patients with carotid stenosis. Circulation 114: 1847-1854.
    • (2006) Circulation , vol.114 , pp. 1847-1854
    • Eldrup, N.1    Gronholdt, M.L.2    Sillesen, H.3
  • 54
    • 20844448886 scopus 로고    scopus 로고
    • Plasma levels and zymographic activities of matrix metalloproteinases 2 and 9 in type II diabetics with peripheral arterial disease
    • Signorelli SS, Malaponte G, Libra M et al (2005) Plasma levels and zymographic activities of matrix metalloproteinases 2 and 9 in type II diabetics with peripheral arterial disease. Vasc Med 10: 1-6.
    • (2005) Vasc Med , vol.10 , pp. 1-6
    • Signorelli, S.S.1    Malaponte, G.2    Libra, M.3
  • 55
    • 12344263631 scopus 로고    scopus 로고
    • Abnormal circulating levels of metalloprotease 9 and its tissue inhibitor 1 in angiographically proven peripheral arterial disease: Relationship to disease severity
    • Tayebjee MH, Tan KT, MacFadyen RJ et al (2005) Abnormal circulating levels of metalloprotease 9 and its tissue inhibitor 1 in angiographically proven peripheral arterial disease: relationship to disease severity. J Intern Med 257: 110-116.
    • (2005) J Intern Med , vol.257 , pp. 110-116
    • Tayebjee, M.H.1    Tan, K.T.2    MacFadyen, R.J.3
  • 56
    • 34250817676 scopus 로고    scopus 로고
    • Platelets release active matrix metalloproteinase-2 in vivo in humans at a site of vascular injury
    • Falcinelli E, Giannini S, Boschetti E, Gresele P (2007) Platelets release active matrix metalloproteinase-2 in vivo in humans at a site of vascular injury. Brit J Haematol 138: 221-230.
    • (2007) Brit J Haematol , vol.138 , pp. 221-230
    • Falcinelli, E.1    Giannini, S.2    Boschetti, E.3    Gresele, P.4
  • 57
    • 0030681317 scopus 로고    scopus 로고
    • Platelet activation markers in patients with peripheral arterial disease-a prospective comparison of different platelet function tests
    • Gresele P, Catalano M, Giammarresi C et al (1997) Platelet activation markers in patients with peripheral arterial disease-a prospective comparison of different platelet function tests. Thromb Haemost 78: 1434-1437.
    • (1997) Thromb Haemost , vol.78 , pp. 1434-1437
    • Gresele, P.1    Catalano, M.2    Giammarresi, C.3
  • 58
    • 34347204142 scopus 로고    scopus 로고
    • Pro-inflammatory genetic profiles in subjects with peripheral arterial occlusive disease and critical limb ischemia
    • Flex A, Gaetani E, Angelini F et al (2007) Pro-inflammatory genetic profiles in subjects with peripheral arterial occlusive disease and critical limb ischemia. J Intern Med 262: 124-130.
    • (2007) J Intern Med , vol.262 , pp. 124-130
    • Flex, A.1    Gaetani, E.2    Angelini, F.3
  • 59
    • 48649109765 scopus 로고    scopus 로고
    • Nuclear factor-kappaB induction by visfatin in human vascular endothelial cells: Its role in MMP-2/9 production and activation
    • Adya R, Tan BK, Chen J et al (2008) Nuclear factor-kappaB induction by visfatin in human vascular endothelial cells: its role in MMP-2/9 production and activation. Diabets Care 31: 758-760.
    • (2008) Diabets Care , vol.31 , pp. 758-760
    • Adya, R.1    Tan, B.K.2    Chen, J.3
  • 60
    • 35548969339 scopus 로고    scopus 로고
    • Low density lipoprotein from patients with Type 2 diabetes increases expression of monocyte matrix metalloproteinase and ADAM metalloproteinase genes
    • Worley JR, Hughes DA, Dozio N et al (2007) Low density lipoprotein from patients with Type 2 diabetes increases expression of monocyte matrix metalloproteinase and ADAM metalloproteinase genes. Cardiovasc Diabetol 22: 6-21.
    • (2007) Cardiovasc Diabetol , vol.22 , pp. 6-21
    • Worley, J.R.1    Hughes, D.A.2    Dozio, N.3
  • 61
    • 0141757272 scopus 로고    scopus 로고
    • Angiostatin antagonizes the action of VEGF-A in human endothelial cells via two distinct pathways
    • Chen YH, Wu HL, Chen CK, Huang YH, Yang BC, Wu LW (2003) Angiostatin antagonizes the action of VEGF-A in human endothelial cells via two distinct pathways. Biochem Biophys Res Commun 310: 804-810.
    • (2003) Biochem Biophys Res Commun , vol.310 , pp. 804-810
    • Chen, Y.H.1    Wu, H.L.2    Chen, C.K.3    Huang, Y.H.4    Yang, B.C.5    Wu, L.W.6
  • 62
    • 0036831302 scopus 로고    scopus 로고
    • The antitumoral effect of endostatin and angiostatin is associated with a down-regulation of vascular endothelial growth factor expression in tumor cells
    • Hajitou A, Grignet C, Devy L, Berndt S, Blacher S, Deroanne CF, Bajou K, Fong T, Chiang Y, Foidart JM, Noel A (2002) The antitumoral effect of endostatin and angiostatin is associated with a down-regulation of vascular endothelial growth factor expression in tumor cells. FASEB J 16: 1802-1804.
    • (2002) FASEB J , vol.16 , pp. 1802-1804
    • Hajitou, A.1    Grignet, C.2    Devy, L.3    Berndt, S.4    Blacher, S.5    Deroanne, C.F.6    Bajou, K.7    Fong, T.8    Chiang, Y.9    Foidart, J.M.10    Noel, A.11
  • 63
    • 33747611521 scopus 로고    scopus 로고
    • Reduced expression of vascular endothelial growth factor paralleled with the increased angiostatin expression resulting from the upregulated activities of matrix metalloproteinase-2 and -9 in human type 2 diabetic arterial vasculature
    • Chung AW, Hsiang YN, Matzke LA et al (2006) Reduced expression of vascular endothelial growth factor paralleled with the increased angiostatin expression resulting from the upregulated activities of matrix metalloproteinase-2 and -9 in human type 2 diabetic arterial vasculature. Circ Res 99: 140-148.
    • (2006) Circ Res , vol.99 , pp. 140-148
    • Chung, A.W.1    Hsiang, Y.N.2    Matzke, L.A.3
  • 64
    • 42449126565 scopus 로고    scopus 로고
    • Urinary matrix metalloproteinase -8, -9, -14 and their regulators (TRY-1, TRY-2, TATI) in patients with diabetic nephropathy
    • Lauhio A, Sorsa T, Srinivas R et al (2008) Urinary matrix metalloproteinase -8, -9, -14 and their regulators (TRY-1, TRY-2, TATI) in patients with diabetic nephropathy. Ann Med 40: 312-320.
    • (2008) Ann Med , vol.40 , pp. 312-320
    • Lauhio, A.1    Sorsa, T.2    Srinivas, R.3
  • 65
    • 64849101304 scopus 로고    scopus 로고
    • Increased circulating levels of matrix metalloproteinase (MMP)-8, MMP-9, and pro-inflammatory markers in patients with metabolic syndrome
    • Gonçalves FM, Jacob-Ferreira AL, Gomes VA et al (2009) Increased circulating levels of matrix metalloproteinase (MMP)-8, MMP-9, and pro-inflammatory markers in patients with metabolic syndrome. Clin Chim Acta 403: 173-177.
    • (2009) Clin Chim Acta , vol.403 , pp. 173-177
    • Gonçalves, F.M.1    Jacob-Ferreira, A.L.2    Gomes, V.A.3
  • 66
    • 76049089249 scopus 로고    scopus 로고
    • The oral anti-diabetic agent, gliclazide, inhibits oxidized LDL-mediated LOX-1 expression, metalloproteinase-9 secretion and apoptosis in human aortic endothelial cells
    • Li L, Renier G (2008) The oral anti-diabetic agent, gliclazide, inhibits oxidized LDL-mediated LOX-1 expression, metalloproteinase-9 secretion and apoptosis in human aortic endothelial cells. Atherosclerosis [Epub ahead of print].
    • (2008) Atherosclerosis [Epub ahead of print]
    • Li, L.1    Renier, G.2
  • 67
    • 39449138164 scopus 로고    scopus 로고
    • Pleiotrophic and anti-inflammatory effects of pioglitazone precede the metabolic activity in type 2 diabetic patients with coronary artery disease
    • Forst T, Karagiannis E, Lübben G et al (2008) Pleiotrophic and anti-inflammatory effects of pioglitazone precede the metabolic activity in type 2 diabetic patients with coronary artery disease. Atherosclerosis 197: 311-317.
    • (2008) Atherosclerosis , vol.197 , pp. 311-317
    • Forst, T.1    Karagiannis, E.2    Lübben, G.3
  • 68
    • 33749036035 scopus 로고    scopus 로고
    • Reductions in biomarkers of cardiovascular risk in type 2 diabetes with rosiglitazone added to metformin compared with dose escalation of metformin: An EMPIRE trial sub-study
    • Goldstein BJ, Weissman PN, Wooddell MJ et al (2006) Reductions in biomarkers of cardiovascular risk in type 2 diabetes with rosiglitazone added to metformin compared with dose escalation of metformin: an EMPIRE trial sub-study. Curr Med Res Opin 22: 1715-1723.
    • (2006) Curr Med Res Opin , vol.22 , pp. 1715-1723
    • Goldstein, B.J.1    Weissman, P.N.2    Wooddell, M.J.3
  • 69
    • 63449092586 scopus 로고    scopus 로고
    • New mechanism of rosiglitazone to reduce neointimal hyperplasia: Activation of glycogen synthase kinase-3beta followed by inhibition of MMP-9
    • Lee CS, Kwon YW, Yang HM et al (2009) New mechanism of rosiglitazone to reduce neointimal hyperplasia: activation of glycogen synthase kinase-3beta followed by inhibition of MMP-9. Arterioscler Thromb Vasc Biol 29: 472-479.
    • (2009) Arterioscler Thromb Vasc Biol , vol.29 , pp. 472-479
    • Lee, C.S.1    Kwon, Y.W.2    Yang, H.M.3
  • 70
    • 3242720779 scopus 로고    scopus 로고
    • Comparative effects of AT1-antagonism and angiotensin-converting enzyme inhibition on markers of inflammation and platelet aggregation in patients with coronary artery disease
    • Schieffer B, Bünte C, Witte J et al (2004) Comparative effects of AT1-antagonism and angiotensin-converting enzyme inhibition on markers of inflammation and platelet aggregation in patients with coronary artery disease. J Am Coll Cardiol 44: 362-368.
    • (2004) J Am Coll Cardiol , vol.44 , pp. 362-368
    • Schieffer, B.1    Bünte, C.2    Witte, J.3
  • 71
    • 44649197091 scopus 로고    scopus 로고
    • Inhibitory profiles of captopril on matrix metalloproteinase-9 activity
    • Yamamoto D, Takai S, Miyazaki M (2008) Inhibitory profiles of captopril on matrix metalloproteinase-9 activity. Eur J Pharmacol 588: 277-279.
    • (2008) Eur J Pharmacol , vol.588 , pp. 277-279
    • Yamamoto, D.1    Takai, S.2    Miyazaki, M.3
  • 72
    • 0031775709 scopus 로고    scopus 로고
    • HMG-CoA reductase inhibitors reduce MMP-9 secretion by macrophages
    • Bellosta S, Via D, Canavesi M et al (1998) HMG-CoA reductase inhibitors reduce MMP-9 secretion by macrophages. Arterioscler Thromb Vasc Biol 18: 1671-1678.
    • (1998) Arterioscler Thromb Vasc Biol , vol.18 , pp. 1671-1678
    • Bellosta, S.1    Via, D.2    Canavesi, M.3
  • 73
    • 0035916233 scopus 로고    scopus 로고
    • Pravastatin treatment increases collagen content and decreases lipid content, inflammation, metalloproteinases, and cell death in human carotid plaques implications for plaque stabilization
    • Crisby M, Nordin-Fredriksson G, Shah PK et al (2001) Pravastatin treatment increases collagen content and decreases lipid content, inflammation, metalloproteinases, and cell death in human carotid plaques implications for plaque stabilization. Circulation 103: 926-933.
    • (2001) Circulation , vol.103 , pp. 926-933
    • Crisby, M.1    Nordin-Fredriksson, G.2    Shah, P.K.3
  • 74
    • 1842556117 scopus 로고    scopus 로고
    • Atorvastatin lowers plasma matrix metalloproteinase-9 in patients with acute coronary syndrome
    • Xu Z, Zhao S, Zhou H et al (2004) Atorvastatin lowers plasma matrix metalloproteinase-9 in patients with acute coronary syndrome. Clin Chem 50: 750-753.
    • (2004) Clin Chem , vol.50 , pp. 750-753
    • Xu, Z.1    Zhao, S.2    Zhou, H.3
  • 75
    • 33847050858 scopus 로고    scopus 로고
    • The inflammation hypothesis and its potential relevance to statin therapy
    • Forrester JS, Libby P (2007) The inflammation hypothesis and its potential relevance to statin therapy. Am J Cardiol 99: 732-738.
    • (2007) Am J Cardiol , vol.99 , pp. 732-738
    • Forrester, J.S.1    Libby, P.2
  • 76
    • 0028344129 scopus 로고
    • Heparin inhibits the induction of three matrix metalloproteinases (stromelysin, 92-kD gelatinase, and collagenase) in primate arterial smooth muscle cells
    • Kenagy RD, Nikkari ST, Welgus HG et al (1994) Heparin inhibits the induction of three matrix metalloproteinases (stromelysin, 92-kD gelatinase, and collagenase) in primate arterial smooth muscle cells. J Clin Invest 93: 1987-1993.
    • (1994) J Clin Invest , vol.93 , pp. 1987-1993
    • Kenagy, R.D.1    Nikkari, S.T.2    Welgus, H.G.3
  • 77
    • 38549119554 scopus 로고    scopus 로고
    • Low molecular weight heparin treatment decreases MMP-9 plasma activity in patients with abdominal aortic aneurysm
    • Grzela T, Brawura-Biskupski-Samaha R et al (2008) Low molecular weight heparin treatment decreases MMP-9 plasma activity in patients with abdominal aortic aneurysm. Eur Vasc Endovasc Surg 35: 159-161.
    • (2008) Eur Vasc Endovasc Surg , vol.35 , pp. 159-161
    • Grzela, T.1    Brawura-Biskupski-Samaha, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.