메뉴 건너뛰기




Volumn 1852, Issue 2, 2015, Pages 195-208

Proteases in cardiometabolic diseases: Pathophysiology, molecular mechanisms and clinical applications

Author keywords

Calpain; Cardiometabolic diseases; Caspase; Cathepsin; MMP

Indexed keywords

CALPAIN; CASPASE; CATHEPSIN; CELL PROTEIN; COLLAGENASE; ELASTASE; GELATINASE; GELATINASE A; GELATINASE B; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MATRIX METALLOPROTEINASE; PROTEINASE; STROMELYSIN; STROMELYSIN 2; STROMELYSIN 3; PEPTIDE HYDROLASE; PROTEINASE INHIBITOR;

EID: 84919794346     PISSN: 09254439     EISSN: 1879260X     Source Type: Journal    
DOI: 10.1016/j.bbadis.2014.04.032     Document Type: Review
Times cited : (79)

References (260)
  • 1
    • 0037126526 scopus 로고    scopus 로고
    • Expert panel on detection, evaluation, and treatment of high blood cholesterol in adults (adult treatment panel III) final report
    • Third Report of the National Cholesterol Education Program (NCEP) Expert panel on detection, evaluation, and treatment of high blood cholesterol in adults (adult treatment panel III) final report. Circulation 2002, 106:3143-3421.
    • (2002) Circulation , vol.106 , pp. 3143-3421
  • 2
    • 0024160877 scopus 로고
    • Banting lecture 1988. Role of insulin resistance in human disease
    • Reaven G.M. Banting lecture 1988. Role of insulin resistance in human disease. Diabetes 1988, 37:1595-1607.
    • (1988) Diabetes , vol.37 , pp. 1595-1607
    • Reaven, G.M.1
  • 4
    • 84871090162 scopus 로고    scopus 로고
    • Global obesity: trends, risk factors and policy implications
    • Malik V.S., Willett W.C., Hu F.B. Global obesity: trends, risk factors and policy implications. Nat. Rev. Endocrinol. 2013, 9:13-27.
    • (2013) Nat. Rev. Endocrinol. , vol.9 , pp. 13-27
    • Malik, V.S.1    Willett, W.C.2    Hu, F.B.3
  • 10
    • 37349082926 scopus 로고    scopus 로고
    • Matrix metalloproteinases and their inhibitors in vascular remodeling and vascular disease
    • Raffetto J.D., Khalil R.A. Matrix metalloproteinases and their inhibitors in vascular remodeling and vascular disease. Biochem. Pharmacol. 2008, 75:346-359.
    • (2008) Biochem. Pharmacol. , vol.75 , pp. 346-359
    • Raffetto, J.D.1    Khalil, R.A.2
  • 11
    • 0031656460 scopus 로고    scopus 로고
    • Matrix metalloproteinases: structures, evolution, and diversification
    • Massova I., Kotra L.P., Fridman R., Mobashery S. Matrix metalloproteinases: structures, evolution, and diversification. FASEB J. 1998, 12:1075-1095.
    • (1998) FASEB J. , vol.12 , pp. 1075-1095
    • Massova, I.1    Kotra, L.P.2    Fridman, R.3    Mobashery, S.4
  • 12
    • 0034680366 scopus 로고    scopus 로고
    • A matrix metalloproteinase induction/activation system exists in the human left ventricular myocardium and is upregulated in heart failure
    • Spinale F.G., Coker M.L., Heung L.J., Bond B.R., Gunasinghe H.R., Etoh T., Goldberg A.T., Zellner J.L., Crumbley A.J. A matrix metalloproteinase induction/activation system exists in the human left ventricular myocardium and is upregulated in heart failure. Circulation 2000, 102:1944-1949.
    • (2000) Circulation , vol.102 , pp. 1944-1949
    • Spinale, F.G.1    Coker, M.L.2    Heung, L.J.3    Bond, B.R.4    Gunasinghe, H.R.5    Etoh, T.6    Goldberg, A.T.7    Zellner, J.L.8    Crumbley, A.J.9
  • 14
    • 0025847582 scopus 로고
    • Matrix metalloproteinases and their inhibitors in connective tissue remodeling
    • Woessner J.F. Matrix metalloproteinases and their inhibitors in connective tissue remodeling. FASEB J. 1991, 5:2145-2154.
    • (1991) FASEB J. , vol.5 , pp. 2145-2154
    • Woessner, J.F.1
  • 15
    • 77956562826 scopus 로고    scopus 로고
    • Tetracyclines: a pleitropic family of compounds with promising therapeutic properties. Review of the literature
    • Griffin M.O., Fricovsky E., Ceballos G., Villarreal F. Tetracyclines: a pleitropic family of compounds with promising therapeutic properties. Review of the literature. Am. J. Physiol. Cell Physiol. 2010, 299:C539-C548.
    • (2010) Am. J. Physiol. Cell Physiol. , vol.299 , pp. C539-C548
    • Griffin, M.O.1    Fricovsky, E.2    Ceballos, G.3    Villarreal, F.4
  • 17
    • 20344386015 scopus 로고    scopus 로고
    • Calpains and disease
    • Zatz M., Starling A. Calpains and disease. N. Engl. J. Med. 2005, 352:2413-2423.
    • (2005) N. Engl. J. Med. , vol.352 , pp. 2413-2423
    • Zatz, M.1    Starling, A.2
  • 18
    • 84860623128 scopus 로고    scopus 로고
    • Physiologic and pathophysiologic role of calpain: implications for the occurrence of atrial fibrillation
    • Bukowska A., Lendeckel U., Bode-Boger S.M., Goette A. Physiologic and pathophysiologic role of calpain: implications for the occurrence of atrial fibrillation. Cardiovasc. Ther. 2010, 30:e115-e127.
    • (2010) Cardiovasc. Ther. , vol.30 , pp. e115-e127
    • Bukowska, A.1    Lendeckel, U.2    Bode-Boger, S.M.3    Goette, A.4
  • 20
    • 77956437195 scopus 로고    scopus 로고
    • Calpain inhibition attenuates intracellular changes in muscle cells in response to extracellular inflammatory stimulation
    • Nozaki K., Das A., Ray S.K., Banik N.L. Calpain inhibition attenuates intracellular changes in muscle cells in response to extracellular inflammatory stimulation. Exp. Neurol. 2010, 225:430-435.
    • (2010) Exp. Neurol. , vol.225 , pp. 430-435
    • Nozaki, K.1    Das, A.2    Ray, S.K.3    Banik, N.L.4
  • 21
    • 0029978058 scopus 로고    scopus 로고
    • Drug-induced apoptosis in B-cell chronic lymphocytic leukemia: relationship between p53 gene mutation and bcl-2/bax proteins in drug resistance
    • Thomas A., El Rouby S., Reed J.C., Krajewski S., Silber R., Potmesil M., Newcomb E.W. Drug-induced apoptosis in B-cell chronic lymphocytic leukemia: relationship between p53 gene mutation and bcl-2/bax proteins in drug resistance. Oncogene 1996, 12:1055-1062.
    • (1996) Oncogene , vol.12 , pp. 1055-1062
    • Thomas, A.1    El Rouby, S.2    Reed, J.C.3    Krajewski, S.4    Silber, R.5    Potmesil, M.6    Newcomb, E.W.7
  • 23
    • 0035971091 scopus 로고    scopus 로고
    • Synergistic activation of caspase-3 by m-calpain after neonatal hypoxia-ischemia: a mechanism of "pathological apoptosis"?
    • Blomgren K., Zhu C., Wang X., Karlsson J.O., Leverin A.L., Bahr B.A., Mallard C., Hagberg H. Synergistic activation of caspase-3 by m-calpain after neonatal hypoxia-ischemia: a mechanism of "pathological apoptosis"?. J. Biol. Chem. 2001, 276:10191-10198.
    • (2001) J. Biol. Chem. , vol.276 , pp. 10191-10198
    • Blomgren, K.1    Zhu, C.2    Wang, X.3    Karlsson, J.O.4    Leverin, A.L.5    Bahr, B.A.6    Mallard, C.7    Hagberg, H.8
  • 24
    • 0032493743 scopus 로고    scopus 로고
    • Calcium/calmodulin-dependent protein kinase IV is cleaved by caspase-3 and calpain in SH-SY5Y human neuroblastoma cells undergoing apoptosis
    • McGinnis K.M., Whitton M.M., Gnegy M.E., Wang K.K. Calcium/calmodulin-dependent protein kinase IV is cleaved by caspase-3 and calpain in SH-SY5Y human neuroblastoma cells undergoing apoptosis. J. Biol. Chem. 1998, 273:19993-20000.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19993-20000
    • McGinnis, K.M.1    Whitton, M.M.2    Gnegy, M.E.3    Wang, K.K.4
  • 25
    • 0028040099 scopus 로고
    • Brain G-protein proteolysis by calpain: enhancement by lithium
    • Greenwood A.F., Jope R.S. Brain G-protein proteolysis by calpain: enhancement by lithium. Brain Res. 1994, 636:320-326.
    • (1994) Brain Res. , vol.636 , pp. 320-326
    • Greenwood, A.F.1    Jope, R.S.2
  • 26
    • 0033534475 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha-inducible IkappaBalpha proteolysis mediated by cytosolic m-calpain. A mechanism parallel to the ubiquitin-proteasome pathway for nuclear factor-kappab activation
    • Han Y., Weinman S., Boldogh I., Walker R.K., Brasier A.R. Tumor necrosis factor-alpha-inducible IkappaBalpha proteolysis mediated by cytosolic m-calpain. A mechanism parallel to the ubiquitin-proteasome pathway for nuclear factor-kappab activation. J. Biol. Chem. 1999, 274:787-794.
    • (1999) J. Biol. Chem. , vol.274 , pp. 787-794
    • Han, Y.1    Weinman, S.2    Boldogh, I.3    Walker, R.K.4    Brasier, A.R.5
  • 27
    • 0028981050 scopus 로고
    • Activation of NF-kappa B requires proteolysis of the inhibitor I kappa B-alpha: signal-induced phosphorylation of I kappa B-alpha alone does not release active NF-kappa B
    • Lin Y.C., Brown K., Siebenlist U. Activation of NF-kappa B requires proteolysis of the inhibitor I kappa B-alpha: signal-induced phosphorylation of I kappa B-alpha alone does not release active NF-kappa B. Proc. Natl. Acad. Sci. U. S. A. 1995, 92:552-556.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 552-556
    • Lin, Y.C.1    Brown, K.2    Siebenlist, U.3
  • 28
    • 0031014946 scopus 로고    scopus 로고
    • Proteolytic cleavage of human p53 by calpain: a potential regulator of protein stability
    • Kubbutat M.H., Vousden K.H. Proteolytic cleavage of human p53 by calpain: a potential regulator of protein stability. Mol. Cell. Biol. 1997, 17:460-468.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 460-468
    • Kubbutat, M.H.1    Vousden, K.H.2
  • 31
    • 0028292616 scopus 로고
    • Calpain-induced downregulation of activated protein kinase C-alpha affects lung epithelial cell morphology
    • Dwyer L.D., Miller A.C., Parks A.L., Jaken S., Malkinson A.M. Calpain-induced downregulation of activated protein kinase C-alpha affects lung epithelial cell morphology. Am. J. Physiol. 1994, 266:L569-L576.
    • (1994) Am. J. Physiol. , vol.266 , pp. L569-L576
    • Dwyer, L.D.1    Miller, A.C.2    Parks, A.L.3    Jaken, S.4    Malkinson, A.M.5
  • 32
    • 0033595636 scopus 로고    scopus 로고
    • The PEST domain of IkappaBalpha is necessary and sufficient for in vitro degradation by mu-calpain
    • Shumway S.D., Maki M., Miyamoto S. The PEST domain of IkappaBalpha is necessary and sufficient for in vitro degradation by mu-calpain. J. Biol. Chem. 1999, 274:30874-30881.
    • (1999) J. Biol. Chem. , vol.274 , pp. 30874-30881
    • Shumway, S.D.1    Maki, M.2    Miyamoto, S.3
  • 33
    • 57749191674 scopus 로고    scopus 로고
    • Delayed recovery of intracellular acidosis during reperfusion prevents calpain activation and determines protection in postconditioned myocardium
    • Inserte J., Barba I., Hernando V., Garcia-Dorado D. Delayed recovery of intracellular acidosis during reperfusion prevents calpain activation and determines protection in postconditioned myocardium. Cardiovasc. Res. 2009, 81:116-122.
    • (2009) Cardiovasc. Res. , vol.81 , pp. 116-122
    • Inserte, J.1    Barba, I.2    Hernando, V.3    Garcia-Dorado, D.4
  • 35
    • 7744240369 scopus 로고    scopus 로고
    • Implication of prostaglandin E(2) in TNF-alpha-induced release of m-calpain from HCS-2/8 chondrocytes. Inhibition of m-calpain release by NSAIDs
    • Fushimi K., Nakashima S., Banno Y., Akaike A., Takigawa M., Shimizu K. Implication of prostaglandin E(2) in TNF-alpha-induced release of m-calpain from HCS-2/8 chondrocytes. Inhibition of m-calpain release by NSAIDs. Osteoarthr. Cart. 2004, 12:895-903.
    • (2004) Osteoarthr. Cart. , vol.12 , pp. 895-903
    • Fushimi, K.1    Nakashima, S.2    Banno, Y.3    Akaike, A.4    Takigawa, M.5    Shimizu, K.6
  • 41
    • 1942470581 scopus 로고    scopus 로고
    • A cathepsin L isoform that is devoid of a signal peptide localizes to the nucleus in S phase and processes the CDP/Cux transcription factor
    • Goulet B., Baruch A., Moon N.S., Poirier M., Sansregret L.L., Erickson A., Bogyo M., Nepveu A. A cathepsin L isoform that is devoid of a signal peptide localizes to the nucleus in S phase and processes the CDP/Cux transcription factor. Mol. Cell 2004, 14:207-219.
    • (2004) Mol. Cell , vol.14 , pp. 207-219
    • Goulet, B.1    Baruch, A.2    Moon, N.S.3    Poirier, M.4    Sansregret, L.L.5    Erickson, A.6    Bogyo, M.7    Nepveu, A.8
  • 42
    • 82755192921 scopus 로고    scopus 로고
    • Cysteine cathepsins in the secretory vesicle produce active peptides: cathepsin L generates peptide neurotransmitters and cathepsin B produces beta-amyloid of Alzheimer's disease
    • Hook V., Funkelstein L., Wegrzyn J., Bark S., Kindy M., Hook G. Cysteine cathepsins in the secretory vesicle produce active peptides: cathepsin L generates peptide neurotransmitters and cathepsin B produces beta-amyloid of Alzheimer's disease. Biochim. Biophys. Acta 2012, 1824:89-104.
    • (2012) Biochim. Biophys. Acta , vol.1824 , pp. 89-104
    • Hook, V.1    Funkelstein, L.2    Wegrzyn, J.3    Bark, S.4    Kindy, M.5    Hook, G.6
  • 45
    • 79952250111 scopus 로고    scopus 로고
    • Cathepsins (S and B) and their inhibitor cystatin C in immune cells: modulation by interferon-beta and role played in cell migration
    • Staun-Ram E., Miller A. Cathepsins (S and B) and their inhibitor cystatin C in immune cells: modulation by interferon-beta and role played in cell migration. J. Neuroimmunol. 2011, 232:200-206.
    • (2011) J. Neuroimmunol. , vol.232 , pp. 200-206
    • Staun-Ram, E.1    Miller, A.2
  • 46
    • 37549068912 scopus 로고    scopus 로고
    • Cathepsin K inhibitors: a novel target for osteoporosis therapy
    • Stoch S.A., Wagner J.A. Cathepsin K inhibitors: a novel target for osteoporosis therapy. Clin. Pharmacol. Ther. 2008, 83:172-176.
    • (2008) Clin. Pharmacol. Ther. , vol.83 , pp. 172-176
    • Stoch, S.A.1    Wagner, J.A.2
  • 48
    • 0037805704 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases regulate antigen presentation
    • Honey K., Rudensky A.Y. Lysosomal cysteine proteases regulate antigen presentation. Nat. Rev. Immunol. 2003, 3:472-482.
    • (2003) Nat. Rev. Immunol. , vol.3 , pp. 472-482
    • Honey, K.1    Rudensky, A.Y.2
  • 50
    • 0024284209 scopus 로고
    • Biosyntheses and processing of lysosomal cysteine proteinases in rat macrophages
    • Kominami E., Tsukahara T., Hara K., Katunuma N. Biosyntheses and processing of lysosomal cysteine proteinases in rat macrophages. FEBS Lett. 1988, 231:225-228.
    • (1988) FEBS Lett. , vol.231 , pp. 225-228
    • Kominami, E.1    Tsukahara, T.2    Hara, K.3    Katunuma, N.4
  • 51
    • 0025651746 scopus 로고
    • Inhibition of intracellular sorting and processing of lysosomal cathepsins H and L at reduced temperature in primary cultures of rat hepatocytes
    • Nishimura Y., Kawabata T., Yano S., Kato K. Inhibition of intracellular sorting and processing of lysosomal cathepsins H and L at reduced temperature in primary cultures of rat hepatocytes. Arch. Biochem. Biophys. 1990, 283:458-463.
    • (1990) Arch. Biochem. Biophys. , vol.283 , pp. 458-463
    • Nishimura, Y.1    Kawabata, T.2    Yano, S.3    Kato, K.4
  • 52
    • 0030038759 scopus 로고    scopus 로고
    • Potency and selectivity of the cathepsin L propeptide as an inhibitor of cysteine proteases
    • Carmona E., Dufour E., Plouffe C., Takebe S., Mason P., Mort J.S., Menard R. Potency and selectivity of the cathepsin L propeptide as an inhibitor of cysteine proteases. Biochemistry 1996, 35:8149-8157.
    • (1996) Biochemistry , vol.35 , pp. 8149-8157
    • Carmona, E.1    Dufour, E.2    Plouffe, C.3    Takebe, S.4    Mason, P.5    Mort, J.S.6    Menard, R.7
  • 53
    • 0037007965 scopus 로고    scopus 로고
    • Selective inhibition of the collagenolytic activity of human cathepsin K by altering its S2 subsite specificity
    • Lecaille F., Choe Y., Brandt W., Li Z., Craik C.S., Bromme D. Selective inhibition of the collagenolytic activity of human cathepsin K by altering its S2 subsite specificity. Biochemistry 2002, 41:8447-8454.
    • (2002) Biochemistry , vol.41 , pp. 8447-8454
    • Lecaille, F.1    Choe, Y.2    Brandt, W.3    Li, Z.4    Craik, C.S.5    Bromme, D.6
  • 54
    • 0022970858 scopus 로고
    • Cathepsin S. The cysteine proteinase from bovine lymphoid tissue is distinct from cathepsin L (EC 3.4.22.15)
    • Kirschke H., Schmidt I., Wiederanders B. Cathepsin S. The cysteine proteinase from bovine lymphoid tissue is distinct from cathepsin L (EC 3.4.22.15). Biochem. J. 1986, 240:455-459.
    • (1986) Biochem. J. , vol.240 , pp. 455-459
    • Kirschke, H.1    Schmidt, I.2    Wiederanders, B.3
  • 58
    • 0030837038 scopus 로고    scopus 로고
    • Selective induction of the secretion of cathepsins B and L by cytokines in synovial fibroblast-like cells
    • Lemaire R., Huet G., Zerimech F., Grard G., Fontaine C., Duquesnoy B., Flipo R.M. Selective induction of the secretion of cathepsins B and L by cytokines in synovial fibroblast-like cells. Br. J. Rheumatol. 1997, 36:735-743.
    • (1997) Br. J. Rheumatol. , vol.36 , pp. 735-743
    • Lemaire, R.1    Huet, G.2    Zerimech, F.3    Grard, G.4    Fontaine, C.5    Duquesnoy, B.6    Flipo, R.M.7
  • 60
    • 38849159247 scopus 로고    scopus 로고
    • Biochemical properties and regulation of cathepsin K activity
    • Lecaille F., Bromme D., Lalmanach G. Biochemical properties and regulation of cathepsin K activity. Biochimie 2008, 90:208-226.
    • (2008) Biochimie , vol.90 , pp. 208-226
    • Lecaille, F.1    Bromme, D.2    Lalmanach, G.3
  • 61
    • 0025028813 scopus 로고
    • Mechanism of interaction of cysteine proteinases and their protein inhibitors as compared to the serine proteinase-inhibitor interaction
    • (Suppl.)
    • Bode W., Engh R., Musil D., Laber B., Stubbs M., Huber R., Turk V. Mechanism of interaction of cysteine proteinases and their protein inhibitors as compared to the serine proteinase-inhibitor interaction. Biol. Chem. Hoppe Seyler 1990, 371:111-118. (Suppl.).
    • (1990) Biol. Chem. Hoppe Seyler , vol.371 , pp. 111-118
    • Bode, W.1    Engh, R.2    Musil, D.3    Laber, B.4    Stubbs, M.5    Huber, R.6    Turk, V.7
  • 62
    • 0033037118 scopus 로고    scopus 로고
    • Structural basis of inhibition of cysteine proteases by E-64 and its derivatives
    • Matsumoto K., Mizoue K., Kitamura K., Tse W.C., Huber C.P., Ishida T. Structural basis of inhibition of cysteine proteases by E-64 and its derivatives. Biopolymers 1999, 51:99-107.
    • (1999) Biopolymers , vol.51 , pp. 99-107
    • Matsumoto, K.1    Mizoue, K.2    Kitamura, K.3    Tse, W.C.4    Huber, C.P.5    Ishida, T.6
  • 63
    • 84887387835 scopus 로고    scopus 로고
    • Cathepsin K inhibitors: a novel target but promising approach in the treatment of osteoporosis
    • Helali A.M., Iti F.M., Mohamed I.N. Cathepsin K inhibitors: a novel target but promising approach in the treatment of osteoporosis. Curr. Drug Targets 2013, 14:1591-1600.
    • (2013) Curr. Drug Targets , vol.14 , pp. 1591-1600
    • Helali, A.M.1    Iti, F.M.2    Mohamed, I.N.3
  • 65
    • 0024510020 scopus 로고
    • Activation of interleukin-1 beta by a co-induced protease
    • Black R.A., Kronheim S.R., Sleath P.R. Activation of interleukin-1 beta by a co-induced protease. FEBS Lett. 1989, 247:386-390.
    • (1989) FEBS Lett. , vol.247 , pp. 386-390
    • Black, R.A.1    Kronheim, S.R.2    Sleath, P.R.3
  • 66
    • 0027525104 scopus 로고
    • The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 beta-converting enzyme
    • Yuan J., Shaham S., Ledoux S., Ellis H.M., Horvitz H.R. The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 beta-converting enzyme. Cell 1993, 75:641-652.
    • (1993) Cell , vol.75 , pp. 641-652
    • Yuan, J.1    Shaham, S.2    Ledoux, S.3    Ellis, H.M.4    Horvitz, H.R.5
  • 68
    • 0028168593 scopus 로고
    • Ich-1, an Ice/ced-3-related gene, encodes both positive and negative regulators of programmed cell death
    • Wang L., Miura M., Bergeron L., Zhu H., Yuan J. Ich-1, an Ice/ced-3-related gene, encodes both positive and negative regulators of programmed cell death. Cell 1994, 78:739-750.
    • (1994) Cell , vol.78 , pp. 739-750
    • Wang, L.1    Miura, M.2    Bergeron, L.3    Zhu, H.4    Yuan, J.5
  • 70
    • 0030011398 scopus 로고    scopus 로고
    • Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death
    • Boldin M.P., Goncharov T.M., Goltsev Y.V., Wallach D. Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death. Cell 1996, 85:803-815.
    • (1996) Cell , vol.85 , pp. 803-815
    • Boldin, M.P.1    Goncharov, T.M.2    Goltsev, Y.V.3    Wallach, D.4
  • 72
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li P., Nijhawan D., Budihardjo I., Srinivasula S.M., Ahmad M., Alnemri E.S., Wang X. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 1997, 91:479-489.
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6    Wang, X.7
  • 73
    • 0032555716 scopus 로고    scopus 로고
    • Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors
    • Luo X., Budihardjo I., Zou H., Slaughter C., Wang X. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell 1998, 94:481-490.
    • (1998) Cell , vol.94 , pp. 481-490
    • Luo, X.1    Budihardjo, I.2    Zou, H.3    Slaughter, C.4    Wang, X.5
  • 74
    • 0035038497 scopus 로고    scopus 로고
    • Distinct initiator caspases are required for the induction of apoptosis in cardiac myocytes during ischaemia versus reperfusion injury
    • Stephanou A., Brar B., Liao Z., Scarabelli T., Knight R.A., Latchman D.S. Distinct initiator caspases are required for the induction of apoptosis in cardiac myocytes during ischaemia versus reperfusion injury. Cell Death Differ. 2001, 8:434-435.
    • (2001) Cell Death Differ. , vol.8 , pp. 434-435
    • Stephanou, A.1    Brar, B.2    Liao, Z.3    Scarabelli, T.4    Knight, R.A.5    Latchman, D.S.6
  • 77
    • 0030698127 scopus 로고    scopus 로고
    • The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases
    • Roy N., Deveraux Q.L., Takahashi R., Salvesen G.S., Reed J.C. The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases. EMBO J. 1997, 16:6914-6925.
    • (1997) EMBO J. , vol.16 , pp. 6914-6925
    • Roy, N.1    Deveraux, Q.L.2    Takahashi, R.3    Salvesen, G.S.4    Reed, J.C.5
  • 78
    • 0035932465 scopus 로고    scopus 로고
    • Covalent inhibition revealed by the crystal structure of the caspase-8/p35 complex
    • Xu G., Cirilli M., Huang Y., Rich R.L., Myszka D.G., Wu H. Covalent inhibition revealed by the crystal structure of the caspase-8/p35 complex. Nature 2001, 410:494-497.
    • (2001) Nature , vol.410 , pp. 494-497
    • Xu, G.1    Cirilli, M.2    Huang, Y.3    Rich, R.L.4    Myszka, D.G.5    Wu, H.6
  • 79
    • 0035916324 scopus 로고    scopus 로고
    • The pyrin domain: a possible member of the death domain-fold family implicated in apoptosis and inflammation
    • Martinon F., Hofmann K., Tschopp J. The pyrin domain: a possible member of the death domain-fold family implicated in apoptosis and inflammation. Curr. Biol. 2001, 11:R118-R120.
    • (2001) Curr. Biol. , vol.11 , pp. R118-R120
    • Martinon, F.1    Hofmann, K.2    Tschopp, J.3
  • 80
    • 0035425256 scopus 로고    scopus 로고
    • The death domain superfamily: a tale of two interfaces?
    • Weber C.H., Vincenz C. The death domain superfamily: a tale of two interfaces?. Trends Biochem. Sci. 2001, 26:475-481.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 475-481
    • Weber, C.H.1    Vincenz, C.2
  • 81
    • 0029787268 scopus 로고    scopus 로고
    • Molecular ordering of apoptotic mammalian CED-3/ICE-like proteases
    • Orth K., O'Rourke K., Salvesen G.S., Dixit V.M. Molecular ordering of apoptotic mammalian CED-3/ICE-like proteases. J. Biol. Chem. 1996, 271:20977-20980.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20977-20980
    • Orth, K.1    O'Rourke, K.2    Salvesen, G.S.3    Dixit, V.M.4
  • 82
    • 0031615875 scopus 로고    scopus 로고
    • Autoproteolytic activation of pro-caspases by oligomerization
    • Yang X., Chang H.Y., Baltimore D. Autoproteolytic activation of pro-caspases by oligomerization. Mol. Cell 1998, 1:319-325.
    • (1998) Mol. Cell , vol.1 , pp. 319-325
    • Yang, X.1    Chang, H.Y.2    Baltimore, D.3
  • 83
    • 0031018914 scopus 로고    scopus 로고
    • FLICE induced apoptosis in a cell-free system. Cleavage of caspase zymogens
    • Muzio M., Salvesen G.S., Dixit V.M. FLICE induced apoptosis in a cell-free system. Cleavage of caspase zymogens. J. Biol. Chem. 1997, 272:2952-2956.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2952-2956
    • Muzio, M.1    Salvesen, G.S.2    Dixit, V.M.3
  • 84
    • 0030044324 scopus 로고    scopus 로고
    • ICE-LAP3, a novel mammalian homologue of the Caenorhabditis elegans cell death protein Ced-3 is activated during Fas- and tumor necrosis factor-induced apoptosis
    • Duan H., Chinnaiyan A.M., Hudson P.L., Wing J.P., He W.W., Dixit V.M. ICE-LAP3, a novel mammalian homologue of the Caenorhabditis elegans cell death protein Ced-3 is activated during Fas- and tumor necrosis factor-induced apoptosis. J. Biol. Chem. 1996, 271:1621-1625.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1621-1625
    • Duan, H.1    Chinnaiyan, A.M.2    Hudson, P.L.3    Wing, J.P.4    He, W.W.5    Dixit, V.M.6
  • 85
    • 0030977847 scopus 로고    scopus 로고
    • Target protease specificity of the viral serpin CrmA. Analysis of five caspases
    • Zhou Q., Snipas S., Orth K., Muzio M., Dixit V.M., Salvesen G.S. Target protease specificity of the viral serpin CrmA. Analysis of five caspases. J. Biol. Chem. 1997, 272:7797-7800.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7797-7800
    • Zhou, Q.1    Snipas, S.2    Orth, K.3    Muzio, M.4    Dixit, V.M.5    Salvesen, G.S.6
  • 86
    • 0030931876 scopus 로고    scopus 로고
    • Caspases: the executioners of apoptosis
    • Cohen G.M. Caspases: the executioners of apoptosis. Biochem. J. 1997, 326(Pt 1):1-16.
    • (1997) Biochem. J. , vol.326 , pp. 1-16
    • Cohen, G.M.1
  • 87
    • 0034440818 scopus 로고    scopus 로고
    • Proteases for cell suicide: functions and regulation of caspases
    • Chang H.Y., Yang X. Proteases for cell suicide: functions and regulation of caspases. Microbiol. Mol. Biol. Rev. 2000, 64:821-846.
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 821-846
    • Chang, H.Y.1    Yang, X.2
  • 88
    • 0026728952 scopus 로고
    • Viral inhibition of inflammation: cowpox virus encodes an inhibitor of the interleukin-1 beta converting enzyme
    • Ray C.A., Black R.A., Kronheim S.R., Greenstreet T.A., Sleath P.R., Salvesen G.S., Pickup D.J. Viral inhibition of inflammation: cowpox virus encodes an inhibitor of the interleukin-1 beta converting enzyme. Cell 1992, 69:597-604.
    • (1992) Cell , vol.69 , pp. 597-604
    • Ray, C.A.1    Black, R.A.2    Kronheim, S.R.3    Greenstreet, T.A.4    Sleath, P.R.5    Salvesen, G.S.6    Pickup, D.J.7
  • 89
    • 0028873964 scopus 로고
    • Fas- and tumor necrosis factor-induced apoptosis is inhibited by the poxvirus crmA gene product
    • Tewari M., Dixit V.M. Fas- and tumor necrosis factor-induced apoptosis is inhibited by the poxvirus crmA gene product. J. Biol. Chem. 1995, 270:3255-3260.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3255-3260
    • Tewari, M.1    Dixit, V.M.2
  • 91
    • 2242435231 scopus 로고    scopus 로고
    • Caspases and apoptosis: die and let live
    • Nalepa G., Zukowska-Szczechowska E. Caspases and apoptosis: die and let live. Wiad. Lek. 2002, 55:100-106.
    • (2002) Wiad. Lek. , vol.55 , pp. 100-106
    • Nalepa, G.1    Zukowska-Szczechowska, E.2
  • 94
    • 33745559712 scopus 로고    scopus 로고
    • Neutrophil serine proteases: specific regulators of inflammation
    • Pham C.T. Neutrophil serine proteases: specific regulators of inflammation. Nat. Rev. Immunol. 2006, 6:541-550.
    • (2006) Nat. Rev. Immunol. , vol.6 , pp. 541-550
    • Pham, C.T.1
  • 95
    • 0141539596 scopus 로고    scopus 로고
    • Calcium-dependent and aspartyl proteases in neurodegeneration and ageing in C. elegans
    • Samara C., Tavernarakis N. Calcium-dependent and aspartyl proteases in neurodegeneration and ageing in C. elegans. Ageing Res. Rev. 2003, 2:451-471.
    • (2003) Ageing Res. Rev. , vol.2 , pp. 451-471
    • Samara, C.1    Tavernarakis, N.2
  • 96
    • 20444375511 scopus 로고    scopus 로고
    • Proteolytic mechanisms in necrotic cell death and neurodegeneration
    • Artal-Sanz M., Tavernarakis N. Proteolytic mechanisms in necrotic cell death and neurodegeneration. FEBS Lett. 2005, 579:3287-3296.
    • (2005) FEBS Lett. , vol.579 , pp. 3287-3296
    • Artal-Sanz, M.1    Tavernarakis, N.2
  • 97
    • 33747613545 scopus 로고    scopus 로고
    • Matrix metalloproteinases, the pros and cons, in liver fibrosis
    • Han Y.P. Matrix metalloproteinases, the pros and cons, in liver fibrosis. J. Gastroenterol. Hepatol. 2006, 21(Suppl. 3):S88-S91.
    • (2006) J. Gastroenterol. Hepatol. , vol.21 , pp. S88-S91
    • Han, Y.P.1
  • 98
    • 64849116076 scopus 로고    scopus 로고
    • Serine proteases, inhibitors and receptors in renal fibrosis
    • Eddy A.A. Serine proteases, inhibitors and receptors in renal fibrosis. Thromb. Haemost. 2009, 101:656-664.
    • (2009) Thromb. Haemost. , vol.101 , pp. 656-664
    • Eddy, A.A.1
  • 99
    • 65749104602 scopus 로고    scopus 로고
    • Matrix metalloproteinases and cardiovascular diseases
    • Papazafiropoulou A., Tentolouris N. Matrix metalloproteinases and cardiovascular diseases. Hippokratia 2009, 13:76-82.
    • (2009) Hippokratia , vol.13 , pp. 76-82
    • Papazafiropoulou, A.1    Tentolouris, N.2
  • 101
    • 84866342680 scopus 로고    scopus 로고
    • Cardiac fibroblasts, fibrosis and extracellular matrix remodeling in heart disease
    • Fan D., Takawale A., Lee J., Kassiri Z. Cardiac fibroblasts, fibrosis and extracellular matrix remodeling in heart disease. Fibrogenesis Tissue Repair 2012, 5:15.
    • (2012) Fibrogenesis Tissue Repair , vol.5 , pp. 15
    • Fan, D.1    Takawale, A.2    Lee, J.3    Kassiri, Z.4
  • 103
    • 0038173265 scopus 로고    scopus 로고
    • High glucose alters matrix metalloproteinase expression in two key vascular cells: potential impact on atherosclerosis in diabetes
    • Death A.K., Fisher E.J., McGrath K.C., Yue D.K. High glucose alters matrix metalloproteinase expression in two key vascular cells: potential impact on atherosclerosis in diabetes. Atherosclerosis 2003, 168:263-269.
    • (2003) Atherosclerosis , vol.168 , pp. 263-269
    • Death, A.K.1    Fisher, E.J.2    McGrath, K.C.3    Yue, D.K.4
  • 105
    • 14644401767 scopus 로고    scopus 로고
    • Different involvement of extracellular matrix components in small and large arteries during chronic NO synthase inhibition
    • Bouvet C., Gilbert L.A., Girardot D., deBlois D., Moreau P. Different involvement of extracellular matrix components in small and large arteries during chronic NO synthase inhibition. Hypertension 2005, 45:432-437.
    • (2005) Hypertension , vol.45 , pp. 432-437
    • Bouvet, C.1    Gilbert, L.A.2    Girardot, D.3    deBlois, D.4    Moreau, P.5
  • 106
    • 25444502869 scopus 로고    scopus 로고
    • Angiotensin II stimulates matrix metalloproteinase secretion in human vascular smooth muscle cells via nuclear factor-kappaB and activator protein 1 in a redox-sensitive manner
    • Browatzki M., Larsen D., Pfeiffer C.A., Gehrke S.G., Schmidt J., Kranzhofer A., Katus H.A., Kranzhofer R. Angiotensin II stimulates matrix metalloproteinase secretion in human vascular smooth muscle cells via nuclear factor-kappaB and activator protein 1 in a redox-sensitive manner. J. Vasc. Res. 2005, 42:415-423.
    • (2005) J. Vasc. Res. , vol.42 , pp. 415-423
    • Browatzki, M.1    Larsen, D.2    Pfeiffer, C.A.3    Gehrke, S.G.4    Schmidt, J.5    Kranzhofer, A.6    Katus, H.A.7    Kranzhofer, R.8
  • 107
    • 0036227213 scopus 로고    scopus 로고
    • Modulation of adipose tissue expression of murine matrix metalloproteinases and their tissue inhibitors with obesity
    • Maquoi E., Munaut C., Colige A., Collen D., Lijnen H.R. Modulation of adipose tissue expression of murine matrix metalloproteinases and their tissue inhibitors with obesity. Diabetes 2002, 51:1093-1101.
    • (2002) Diabetes , vol.51 , pp. 1093-1101
    • Maquoi, E.1    Munaut, C.2    Colige, A.3    Collen, D.4    Lijnen, H.R.5
  • 108
    • 79953856935 scopus 로고    scopus 로고
    • Atherosclerotic coronary heart disease-epidemiology, classification and management
    • Negi S., Anand A. Atherosclerotic coronary heart disease-epidemiology, classification and management. Cardiovasc. Hematol. Disord. Drug Targets 2010, 10:257-261.
    • (2010) Cardiovasc. Hematol. Disord. Drug Targets , vol.10 , pp. 257-261
    • Negi, S.1    Anand, A.2
  • 109
    • 33845687065 scopus 로고    scopus 로고
    • Matrix metalloproteinases in cardiovascular disease
    • Liu P., Sun M., Sader S. Matrix metalloproteinases in cardiovascular disease. Can. J. Cardiol. 2006, 22(Suppl. B):25B-30B.
    • (2006) Can. J. Cardiol. , vol.22 , pp. 25B-30B
    • Liu, P.1    Sun, M.2    Sader, S.3
  • 110
    • 21544467275 scopus 로고    scopus 로고
    • Pathophysiology of coronary artery disease
    • Libby P., Theroux P. Pathophysiology of coronary artery disease. Circulation 2005, 111:3481-3488.
    • (2005) Circulation , vol.111 , pp. 3481-3488
    • Libby, P.1    Theroux, P.2
  • 111
    • 84919827367 scopus 로고    scopus 로고
    • Honokiol suppresses TNF-alpha-induced migration and matrix metalloproteinase expression by blocking NF-kappaB activation via the ERK signaling pathway in rat aortic smooth muscle cells
    • (press)
    • Zhu X., Wang Z., Hu C., Li Z., Hu J. Honokiol suppresses TNF-alpha-induced migration and matrix metalloproteinase expression by blocking NF-kappaB activation via the ERK signaling pathway in rat aortic smooth muscle cells. Acta Histochem. 2013, (in press).
    • (2013) Acta Histochem.
    • Zhu, X.1    Wang, Z.2    Hu, C.3    Li, Z.4    Hu, J.5
  • 112
    • 0031773610 scopus 로고    scopus 로고
    • Activation of matrix-degrading metalloproteinases by mast cell proteases in atherosclerotic plaques
    • Johnson J.L., Jackson C.L., Angelini G.D., George S.J. Activation of matrix-degrading metalloproteinases by mast cell proteases in atherosclerotic plaques. Arterioscler. Thromb. Vasc. Biol. 1998, 18:1707-1715.
    • (1998) Arterioscler. Thromb. Vasc. Biol. , vol.18 , pp. 1707-1715
    • Johnson, J.L.1    Jackson, C.L.2    Angelini, G.D.3    George, S.J.4
  • 114
    • 54849423350 scopus 로고    scopus 로고
    • Aspirin inhibits MMP-2 and MMP-9 expressions and activities through upregulation of PPARalpha/gamma and TIMP gene expressions in ox-LDL-stimulated macrophages derived from human monocytes
    • Hua Y., Xue J., Sun F., Zhu L., Xie M. Aspirin inhibits MMP-2 and MMP-9 expressions and activities through upregulation of PPARalpha/gamma and TIMP gene expressions in ox-LDL-stimulated macrophages derived from human monocytes. Pharmacology 2009, 83:18-25.
    • (2009) Pharmacology , vol.83 , pp. 18-25
    • Hua, Y.1    Xue, J.2    Sun, F.3    Zhu, L.4    Xie, M.5
  • 115
    • 84863543450 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibition therapy for vascular diseases
    • Newby A.C. Matrix metalloproteinase inhibition therapy for vascular diseases. Vasc. Pharmacol. 2012, 56:232-244.
    • (2012) Vasc. Pharmacol. , vol.56 , pp. 232-244
    • Newby, A.C.1
  • 116
    • 84891603907 scopus 로고    scopus 로고
    • Associations of matrix metalloproteinase-9 and monocyte chemoattractant protein-1 concentrations with carotid atherosclerosis, based on measurements of plaque and intima-media thickness
    • Tan C., Liu Y., Li W., Deng F., Liu X., Wang X., Gui Y., Qin L., Hu C., Chen L. Associations of matrix metalloproteinase-9 and monocyte chemoattractant protein-1 concentrations with carotid atherosclerosis, based on measurements of plaque and intima-media thickness. Atherosclerosis 2014, 232:199-203.
    • (2014) Atherosclerosis , vol.232 , pp. 199-203
    • Tan, C.1    Liu, Y.2    Li, W.3    Deng, F.4    Liu, X.5    Wang, X.6    Gui, Y.7    Qin, L.8    Hu, C.9    Chen, L.10
  • 117
    • 0028063408 scopus 로고
    • Increased expression of matrix metalloproteinases and matrix degrading activity in vulnerable regions of human atherosclerotic plaques
    • Galis Z.S., Sukhova G.K., Lark M.W., Libby P. Increased expression of matrix metalloproteinases and matrix degrading activity in vulnerable regions of human atherosclerotic plaques. J. Clin. Invest. 1994, 94:2493-2503.
    • (1994) J. Clin. Invest. , vol.94 , pp. 2493-2503
    • Galis, Z.S.1    Sukhova, G.K.2    Lark, M.W.3    Libby, P.4
  • 118
    • 0035019911 scopus 로고    scopus 로고
    • ApoE knockout mice expressing human matrix metalloproteinase-1 in macrophages have less advanced atherosclerosis
    • Lemaitre V., O'Byrne T.K., Borczuk A.C., Okada Y., Tall A.R., D'Armiento J. ApoE knockout mice expressing human matrix metalloproteinase-1 in macrophages have less advanced atherosclerosis. J. Clin. Invest. 2001, 107:1227-1234.
    • (2001) J. Clin. Invest. , vol.107 , pp. 1227-1234
    • Lemaitre, V.1    O'Byrne, T.K.2    Borczuk, A.C.3    Okada, Y.4    Tall, A.R.5    D'Armiento, J.6
  • 119
    • 31044446194 scopus 로고    scopus 로고
    • Macrophage expression of active MMP-9 induces acute plaque disruption in apoE-deficient mice
    • Gough P.J., Gomez I.G., Wille P.T., Raines E.W. Macrophage expression of active MMP-9 induces acute plaque disruption in apoE-deficient mice. J. Clin. Invest. 2006, 116:59-69.
    • (2006) J. Clin. Invest. , vol.116 , pp. 59-69
    • Gough, P.J.1    Gomez, I.G.2    Wille, P.T.3    Raines, E.W.4
  • 121
    • 1642362387 scopus 로고    scopus 로고
    • Loss of matrix metalloproteinase-9 or matrix metalloproteinase-12 protects apolipoprotein E-deficient mice against atherosclerotic media destruction but differentially affects plaque growth
    • Luttun A., Lutgens E., Manderveld A., Maris K., Collen D., Carmeliet P., Moons L. Loss of matrix metalloproteinase-9 or matrix metalloproteinase-12 protects apolipoprotein E-deficient mice against atherosclerotic media destruction but differentially affects plaque growth. Circulation 2004, 109:1408-1414.
    • (2004) Circulation , vol.109 , pp. 1408-1414
    • Luttun, A.1    Lutgens, E.2    Manderveld, A.3    Maris, K.4    Collen, D.5    Carmeliet, P.6    Moons, L.7
  • 123
    • 0035572899 scopus 로고    scopus 로고
    • Persistence of atherosclerotic plaque but reduced aneurysm formation in mice with stromelysin-1 (MMP-3) gene inactivation
    • Silence J., Lupu F., Collen D., Lijnen H.R. Persistence of atherosclerotic plaque but reduced aneurysm formation in mice with stromelysin-1 (MMP-3) gene inactivation. Arterioscler. Thromb. Vasc. Biol. 2001, 21:1440-1445.
    • (2001) Arterioscler. Thromb. Vasc. Biol. , vol.21 , pp. 1440-1445
    • Silence, J.1    Lupu, F.2    Collen, D.3    Lijnen, H.R.4
  • 124
    • 82955189882 scopus 로고    scopus 로고
    • Circulating adhesion molecules, matrix metalloproteinase-9, plasminogen activator inhibitor-1, and myeloperoxidase in coronary artery disease patients with stable and unstable angina
    • Tretjakovs P., Jurka A., Bormane I., Mikelsone I., Elksne K., Krievina G., Reihmane D., Verbovenko J., Bahs G. Circulating adhesion molecules, matrix metalloproteinase-9, plasminogen activator inhibitor-1, and myeloperoxidase in coronary artery disease patients with stable and unstable angina. Clin. Chim. Acta 2012, 413:25-29.
    • (2012) Clin. Chim. Acta , vol.413 , pp. 25-29
    • Tretjakovs, P.1    Jurka, A.2    Bormane, I.3    Mikelsone, I.4    Elksne, K.5    Krievina, G.6    Reihmane, D.7    Verbovenko, J.8    Bahs, G.9
  • 126
    • 0035874516 scopus 로고    scopus 로고
    • Proteolysis of the urokinase-type plasminogen activator receptor by metalloproteinase-12: implication for angiogenesis in fibrin matrices
    • Koolwijk P., Sidenius N., Peters E., Sier C.F., Hanemaaijer R., Blasi F., van Hinsbergh V.W. Proteolysis of the urokinase-type plasminogen activator receptor by metalloproteinase-12: implication for angiogenesis in fibrin matrices. Blood 2001, 97:3123-3131.
    • (2001) Blood , vol.97 , pp. 3123-3131
    • Koolwijk, P.1    Sidenius, N.2    Peters, E.3    Sier, C.F.4    Hanemaaijer, R.5    Blasi, F.6    van Hinsbergh, V.W.7
  • 127
    • 70350462242 scopus 로고    scopus 로고
    • Tissue-type plasminogen activator (t-PA) induces stromelysin-1 (MMP-3) in endothelial cells through activation of lipoprotein receptor-related protein
    • Suzuki Y., Nagai N., Yamakawa K., Kawakami J., Lijnen H.R., Umemura K. Tissue-type plasminogen activator (t-PA) induces stromelysin-1 (MMP-3) in endothelial cells through activation of lipoprotein receptor-related protein. Blood 2009, 114:3352-3358.
    • (2009) Blood , vol.114 , pp. 3352-3358
    • Suzuki, Y.1    Nagai, N.2    Yamakawa, K.3    Kawakami, J.4    Lijnen, H.R.5    Umemura, K.6
  • 128
    • 0034650486 scopus 로고    scopus 로고
    • Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis
    • Yu Q., Stamenkovic I. Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis. Genes Dev. 2000, 14:163-176.
    • (2000) Genes Dev. , vol.14 , pp. 163-176
    • Yu, Q.1    Stamenkovic, I.2
  • 129
    • 0142122225 scopus 로고    scopus 로고
    • Induction of matrix metalloproteinases-14 and -2 by cyclical mechanical stretch is mediated by tumor necrosis factor-alpha in cultured human umbilical vein endothelial cells
    • Wang B.W., Chang H., Lin S., Kuan P., Shyu K.G. Induction of matrix metalloproteinases-14 and -2 by cyclical mechanical stretch is mediated by tumor necrosis factor-alpha in cultured human umbilical vein endothelial cells. Cardiovasc. Res. 2003, 59:460-469.
    • (2003) Cardiovasc. Res. , vol.59 , pp. 460-469
    • Wang, B.W.1    Chang, H.2    Lin, S.3    Kuan, P.4    Shyu, K.G.5
  • 131
    • 0042178259 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinase-9 in endothelial cells is differentially regulated by shear stress. Role of c-Myc
    • Magid R., Murphy T.J., Galis Z.S. Expression of matrix metalloproteinase-9 in endothelial cells is differentially regulated by shear stress. Role of c-Myc. J. Biol. Chem. 2003, 278:32994-32999.
    • (2003) J. Biol. Chem. , vol.278 , pp. 32994-32999
    • Magid, R.1    Murphy, T.J.2    Galis, Z.S.3
  • 132
    • 25444522479 scopus 로고    scopus 로고
    • Role of angiogenesis in cardiovascular disease: a critical appraisal
    • Khurana R., Simons M., Martin J.F., Zachary I.C. Role of angiogenesis in cardiovascular disease: a critical appraisal. Circulation 2005, 112:1813-1824.
    • (2005) Circulation , vol.112 , pp. 1813-1824
    • Khurana, R.1    Simons, M.2    Martin, J.F.3    Zachary, I.C.4
  • 133
    • 70749162074 scopus 로고    scopus 로고
    • Matrix metalloproteinase-2 and -9 exacerbate arterial stiffening and angiogenesis in diabetes and chronic kidney disease
    • Chung A.W., Yang H.H., Sigrist M.K., Brin G., Chum E., Gourlay W.A., Levin A. Matrix metalloproteinase-2 and -9 exacerbate arterial stiffening and angiogenesis in diabetes and chronic kidney disease. Cardiovasc. Res. 2009, 84:494-504.
    • (2009) Cardiovasc. Res. , vol.84 , pp. 494-504
    • Chung, A.W.1    Yang, H.H.2    Sigrist, M.K.3    Brin, G.4    Chum, E.5    Gourlay, W.A.6    Levin, A.7
  • 134
    • 84879361082 scopus 로고    scopus 로고
    • An important role of matrix metalloproteinase-8 in angiogenesis in vitro and in vivo
    • Fang C., Wen G., Zhang L., Lin L., Moore A., Wu S., Ye S., Xiao Q. An important role of matrix metalloproteinase-8 in angiogenesis in vitro and in vivo. Cardiovasc. Res. 2013, 99:146-155.
    • (2013) Cardiovasc. Res. , vol.99 , pp. 146-155
    • Fang, C.1    Wen, G.2    Zhang, L.3    Lin, L.4    Moore, A.5    Wu, S.6    Ye, S.7    Xiao, Q.8
  • 135
    • 0035819050 scopus 로고    scopus 로고
    • Multiple signaling pathways involved in activation of matrix metalloproteinase-9 (MMP-9) by heregulin-beta1 in human breast cancer cells
    • Yao J., Xiong S., Klos K., Nguyen N., Grijalva R., Li P., Yu D. Multiple signaling pathways involved in activation of matrix metalloproteinase-9 (MMP-9) by heregulin-beta1 in human breast cancer cells. Oncogene 2001, 20:8066-8074.
    • (2001) Oncogene , vol.20 , pp. 8066-8074
    • Yao, J.1    Xiong, S.2    Klos, K.3    Nguyen, N.4    Grijalva, R.5    Li, P.6    Yu, D.7
  • 136
    • 0344586055 scopus 로고    scopus 로고
    • Induction of stromelysin-1 (MMP-3) by fibroblast growth factor-2 (FGF-2) in FGF-2-/-microvascular endothelial cells requires prolonged activation of extracellular signal-regulated kinases-1 and -2 (ERK-1/2)
    • Pintucci G., Yu P.J., Sharony R., Baumann F.G., Saponara F., Frasca A., Galloway A.C., Moscatelli D., Mignatti P. Induction of stromelysin-1 (MMP-3) by fibroblast growth factor-2 (FGF-2) in FGF-2-/-microvascular endothelial cells requires prolonged activation of extracellular signal-regulated kinases-1 and -2 (ERK-1/2). J. Cell. Biochem. 2003, 90:1015-1025.
    • (2003) J. Cell. Biochem. , vol.90 , pp. 1015-1025
    • Pintucci, G.1    Yu, P.J.2    Sharony, R.3    Baumann, F.G.4    Saponara, F.5    Frasca, A.6    Galloway, A.C.7    Moscatelli, D.8    Mignatti, P.9
  • 139
    • 2942675088 scopus 로고    scopus 로고
    • Obesity, metabolic syndrome, and cardiovascular disease
    • Grundy S.M. Obesity, metabolic syndrome, and cardiovascular disease. J. Clin. Endocrinol. Metab. 2004, 89:2595-2600.
    • (2004) J. Clin. Endocrinol. Metab. , vol.89 , pp. 2595-2600
    • Grundy, S.M.1
  • 140
    • 84874315293 scopus 로고    scopus 로고
    • Akt2 knockout preserves cardiac function in high-fat diet-induced obesity by rescuing cardiac autophagosome maturation
    • Xu X., Hua Y., Nair S., Zhang Y., Ren J. Akt2 knockout preserves cardiac function in high-fat diet-induced obesity by rescuing cardiac autophagosome maturation. J. Mol. Cell Biol. 2013, 5:61-63.
    • (2013) J. Mol. Cell Biol. , vol.5 , pp. 61-63
    • Xu, X.1    Hua, Y.2    Nair, S.3    Zhang, Y.4    Ren, J.5
  • 141
    • 84870023517 scopus 로고    scopus 로고
    • Increase in MMP-2 activity in overweight and obese women is associated with menopausal status
    • Miksztowicz V., Siseles N., Fernandez Machulsky N., Schreier L., Berg G. Increase in MMP-2 activity in overweight and obese women is associated with menopausal status. Climacteric 2012, 15:602-606.
    • (2012) Climacteric , vol.15 , pp. 602-606
    • Miksztowicz, V.1    Siseles, N.2    Fernandez Machulsky, N.3    Schreier, L.4    Berg, G.5
  • 142
    • 34248374205 scopus 로고    scopus 로고
    • Elevated matrix metalloproteinase 9 and tissue inhibitor of metalloproteinase 1 in obese children and adolescents
    • Glowinska-Olszewska B., Urban M. Elevated matrix metalloproteinase 9 and tissue inhibitor of metalloproteinase 1 in obese children and adolescents. Metab. Clin. Exp. 2007, 56:799-805.
    • (2007) Metab. Clin. Exp. , vol.56 , pp. 799-805
    • Glowinska-Olszewska, B.1    Urban, M.2
  • 147
    • 0141678871 scopus 로고    scopus 로고
    • Angiotensin II receptor blockade prevents microangiopathy and preserves diastolic function in the diabetic rat heart
    • Hayashi T., Sohmiya K., Ukimura A., Endoh S., Mori T., Shimomura H., Okabe M., Terasaki F., Kitaura Y. Angiotensin II receptor blockade prevents microangiopathy and preserves diastolic function in the diabetic rat heart. Heart 2003, 89:1236-1242.
    • (2003) Heart , vol.89 , pp. 1236-1242
    • Hayashi, T.1    Sohmiya, K.2    Ukimura, A.3    Endoh, S.4    Mori, T.5    Shimomura, H.6    Okabe, M.7    Terasaki, F.8    Kitaura, Y.9
  • 148
    • 84886690135 scopus 로고    scopus 로고
    • Fibulin-2 deficiency attenuates angiotensin II-induced cardiac hypertrophy by reducing transforming growth factor-beta signalling
    • Zhang H., Wu J., Dong H., Khan S.A., Chu M.L., Tsuda T. Fibulin-2 deficiency attenuates angiotensin II-induced cardiac hypertrophy by reducing transforming growth factor-beta signalling. Clin. Sci. 2014, 126:275-288.
    • (2014) Clin. Sci. , vol.126 , pp. 275-288
    • Zhang, H.1    Wu, J.2    Dong, H.3    Khan, S.A.4    Chu, M.L.5    Tsuda, T.6
  • 149
    • 84873157227 scopus 로고    scopus 로고
    • Simvastatin attenuates pulmonary vascular remodelling by down-regulating matrix metalloproteinase-1 and -9 expression in a carotid artery-jugular vein shunt pulmonary hypertension model in rats
    • Yao J., Xiong M., Tang B., Chen G., Liang M., Ma X., Wang Z., Wu Z. Simvastatin attenuates pulmonary vascular remodelling by down-regulating matrix metalloproteinase-1 and -9 expression in a carotid artery-jugular vein shunt pulmonary hypertension model in rats. Eur. J. Cardiothorac. Surg. 2012, 42:e121-e127.
    • (2012) Eur. J. Cardiothorac. Surg. , vol.42 , pp. e121-e127
    • Yao, J.1    Xiong, M.2    Tang, B.3    Chen, G.4    Liang, M.5    Ma, X.6    Wang, Z.7    Wu, Z.8
  • 150
    • 84870920351 scopus 로고    scopus 로고
    • Temporal changes in cardiac matrix metalloproteinase activity, oxidative stress, and TGF-beta in renovascular hypertension-induced cardiac hypertrophy
    • Rizzi E., Ceron C.S., Guimaraes D.A., Prado C.M., Rossi M.A., Gerlach R.F., Tanus-Santos J.E. Temporal changes in cardiac matrix metalloproteinase activity, oxidative stress, and TGF-beta in renovascular hypertension-induced cardiac hypertrophy. Exp. Mol. Pathol. 2013, 94:1-9.
    • (2013) Exp. Mol. Pathol. , vol.94 , pp. 1-9
    • Rizzi, E.1    Ceron, C.S.2    Guimaraes, D.A.3    Prado, C.M.4    Rossi, M.A.5    Gerlach, R.F.6    Tanus-Santos, J.E.7
  • 151
    • 79955870570 scopus 로고    scopus 로고
    • Lentivirus mediated IL-17R blockade improves diastolic cardiac function in spontaneously hypertensive rats
    • Liu W., Wang X., Feng W., Li S., Tian W., Xu T., Song Y., Zhang Z. Lentivirus mediated IL-17R blockade improves diastolic cardiac function in spontaneously hypertensive rats. Exp. Mol. Pathol. 2011, 91:362-367.
    • (2011) Exp. Mol. Pathol. , vol.91 , pp. 362-367
    • Liu, W.1    Wang, X.2    Feng, W.3    Li, S.4    Tian, W.5    Xu, T.6    Song, Y.7    Zhang, Z.8
  • 154
    • 44649188437 scopus 로고    scopus 로고
    • Transgenic expression of matrix metalloproteinase-1 inhibits myocardial fibrosis and prevents the transition to heart failure in a pressure overload mouse model
    • Foronjy R.F., Sun J., Lemaitre V., D'Armiento J.M. Transgenic expression of matrix metalloproteinase-1 inhibits myocardial fibrosis and prevents the transition to heart failure in a pressure overload mouse model. Hypertens. Res. 2008, 31:725-735.
    • (2008) Hypertens. Res. , vol.31 , pp. 725-735
    • Foronjy, R.F.1    Sun, J.2    Lemaitre, V.3    D'Armiento, J.M.4
  • 155
    • 33645820598 scopus 로고    scopus 로고
    • Targeted deletion of matrix metalloproteinase 2 ameliorates myocardial remodeling in mice with chronic pressure overload
    • Matsusaka H., Ide T., Matsushima S., Ikeuchi M., Kubota T., Sunagawa K., Kinugawa S., Tsutsui H. Targeted deletion of matrix metalloproteinase 2 ameliorates myocardial remodeling in mice with chronic pressure overload. Hypertension 2006, 47:711-717.
    • (2006) Hypertension , vol.47 , pp. 711-717
    • Matsusaka, H.1    Ide, T.2    Matsushima, S.3    Ikeuchi, M.4    Kubota, T.5    Sunagawa, K.6    Kinugawa, S.7    Tsutsui, H.8
  • 157
    • 2442457887 scopus 로고    scopus 로고
    • Activation of matrix metalloproteinases precedes left ventricular remodeling in hypertensive heart failure rats: its inhibition as a primary effect of angiotensin-converting enzyme inhibitor
    • Sakata Y., Yamamoto K., Mano T., Nishikawa N., Yoshida J., Hori M., Miwa T., Masuyama T. Activation of matrix metalloproteinases precedes left ventricular remodeling in hypertensive heart failure rats: its inhibition as a primary effect of angiotensin-converting enzyme inhibitor. Circulation 2004, 109:2143-2149.
    • (2004) Circulation , vol.109 , pp. 2143-2149
    • Sakata, Y.1    Yamamoto, K.2    Mano, T.3    Nishikawa, N.4    Yoshida, J.5    Hori, M.6    Miwa, T.7    Masuyama, T.8
  • 159
    • 59649091027 scopus 로고    scopus 로고
    • An ezrin/calpain/PI3K/AMPK/eNOSs1179 signaling cascade mediating VEGF-dependent endothelial nitric oxide production
    • Youn J.Y., Wang T., Cai H. An ezrin/calpain/PI3K/AMPK/eNOSs1179 signaling cascade mediating VEGF-dependent endothelial nitric oxide production. Circ. Res. 2009, 104:50-59.
    • (2009) Circ. Res. , vol.104 , pp. 50-59
    • Youn, J.Y.1    Wang, T.2    Cai, H.3
  • 160
    • 35048900480 scopus 로고    scopus 로고
    • 2+ influx- and phosphatidylinositol 3-kinase-mediated m-calpain activity for shear stress-induced endothelial cell polarity
    • 2+ influx- and phosphatidylinositol 3-kinase-mediated m-calpain activity for shear stress-induced endothelial cell polarity. Am. J. Physiol. Cell Physiol. 2007, 293:C1216-C1225.
    • (2007) Am. J. Physiol. Cell Physiol. , vol.293 , pp. C1216-C1225
    • Miyazaki, T.1    Honda, K.2    Ohata, H.3
  • 162
    • 36248949530 scopus 로고    scopus 로고
    • Proteolytic degradation of nitric oxide synthase isoforms by calpain is modulated by the expression levels of HSP90
    • Averna M., Stifanese R., De Tullio R., Salamino F., Bertuccio M., Pontremoli S., Melloni E. Proteolytic degradation of nitric oxide synthase isoforms by calpain is modulated by the expression levels of HSP90. FEBS J. 2007, 274:6116-6127.
    • (2007) FEBS J. , vol.274 , pp. 6116-6127
    • Averna, M.1    Stifanese, R.2    De Tullio, R.3    Salamino, F.4    Bertuccio, M.5    Pontremoli, S.6    Melloni, E.7
  • 164
    • 0041829109 scopus 로고    scopus 로고
    • Oxidized low-density lipoprotein induces calpain-dependent cell death and ubiquitination of caspase 3 in HMEC-1 endothelial cells
    • Porn-Ares M.I., Saido T.C., Andersson T., Ares M.P. Oxidized low-density lipoprotein induces calpain-dependent cell death and ubiquitination of caspase 3 in HMEC-1 endothelial cells. Biochem. J. 2003, 374:403-411.
    • (2003) Biochem. J. , vol.374 , pp. 403-411
    • Porn-Ares, M.I.1    Saido, T.C.2    Andersson, T.3    Ares, M.P.4
  • 166
    • 84873561998 scopus 로고    scopus 로고
    • Amiloride attenuates lipopolysaccharide-accelerated atherosclerosis via inhibition of NHE1-dependent endothelial cell apoptosis
    • Cui G.M., Zhao Y.X., Zhang N.N., Liu Z.S., Sun W.C., Peng Q.S. Amiloride attenuates lipopolysaccharide-accelerated atherosclerosis via inhibition of NHE1-dependent endothelial cell apoptosis. Acta Pharmacol. Sin. 2013, 34:231-238.
    • (2013) Acta Pharmacol. Sin. , vol.34 , pp. 231-238
    • Cui, G.M.1    Zhao, Y.X.2    Zhang, N.N.3    Liu, Z.S.4    Sun, W.C.5    Peng, Q.S.6
  • 167
    • 0030588325 scopus 로고    scopus 로고
    • Inhibition of IkappaB-alpha and IkappaB-beta proteolysis by calpain inhibitor I blocks nitric oxide synthesis
    • Milligan S.A., Owens M.W., Grisham M.B. Inhibition of IkappaB-alpha and IkappaB-beta proteolysis by calpain inhibitor I blocks nitric oxide synthesis. Arch. Biochem. Biophys. 1996, 335:388-395.
    • (1996) Arch. Biochem. Biophys. , vol.335 , pp. 388-395
    • Milligan, S.A.1    Owens, M.W.2    Grisham, M.B.3
  • 169
    • 79955086901 scopus 로고    scopus 로고
    • Endothelin-1 exacerbates lipid accumulation by increasing the protein degradation of the ATP-binding cassette transporter G1 in macrophages
    • Lin C.Y., Lee T.S., Chen C.C., Chang C.A., Lin Y.J., Hsu Y.P., Ho L.T. Endothelin-1 exacerbates lipid accumulation by increasing the protein degradation of the ATP-binding cassette transporter G1 in macrophages. J. Cell. Physiol. 2011, 226:2198-2205.
    • (2011) J. Cell. Physiol. , vol.226 , pp. 2198-2205
    • Lin, C.Y.1    Lee, T.S.2    Chen, C.C.3    Chang, C.A.4    Lin, Y.J.5    Hsu, Y.P.6    Ho, L.T.7
  • 170
    • 31344432567 scopus 로고    scopus 로고
    • Degraded collagen induces calpain-mediated apoptosis and destruction of the X-chromosome-linked inhibitor of apoptosis (xIAP) in human vascular smooth muscle cells
    • von Wnuck Lipinski K., Keul P., Lucke S., Heusch G., Wohlschlaeger J., Baba H.A., Levkau B. Degraded collagen induces calpain-mediated apoptosis and destruction of the X-chromosome-linked inhibitor of apoptosis (xIAP) in human vascular smooth muscle cells. Cardiovasc. Res. 2006, 69:697-705.
    • (2006) Cardiovasc. Res. , vol.69 , pp. 697-705
    • von Wnuck Lipinski, K.1    Keul, P.2    Lucke, S.3    Heusch, G.4    Wohlschlaeger, J.5    Baba, H.A.6    Levkau, B.7
  • 173
    • 0036092048 scopus 로고    scopus 로고
    • Atherosclerosis risk in communities, SNP43 of CAPN10 and the risk of type 2 diabetes in African-Americans: the Atherosclerosis Risk in Communities Study
    • Garant M.J., Kao W.H., Brancati F., Coresh J., Rami T.M., Hanis C.L., Boerwinkle E., Shuldiner A.R. Atherosclerosis risk in communities, SNP43 of CAPN10 and the risk of type 2 diabetes in African-Americans: the Atherosclerosis Risk in Communities Study. Diabetes 2002, 51:231-237.
    • (2002) Diabetes , vol.51 , pp. 231-237
    • Garant, M.J.1    Kao, W.H.2    Brancati, F.3    Coresh, J.4    Rami, T.M.5    Hanis, C.L.6    Boerwinkle, E.7    Shuldiner, A.R.8
  • 176
    • 0036321080 scopus 로고    scopus 로고
    • Variants in the calpain-10 gene predispose to insulin resistance and elevated free fatty acid levels
    • Orho-Melander M., Klannemark M., Svensson M.K., Ridderstrale M., Lindgren C.M., Groop L. Variants in the calpain-10 gene predispose to insulin resistance and elevated free fatty acid levels. Diabetes 2002, 51:2658-2664.
    • (2002) Diabetes , vol.51 , pp. 2658-2664
    • Orho-Melander, M.1    Klannemark, M.2    Svensson, M.K.3    Ridderstrale, M.4    Lindgren, C.M.5    Groop, L.6
  • 178
    • 0035123349 scopus 로고    scopus 로고
    • The prohormone convertase enzyme 2 (PC2) is essential for processing pro-islet amyloid polypeptide at the NH2-terminal cleavage site
    • Wang J., Xu J., Finnerty J., Furuta M., Steiner D.F., Verchere C.B. The prohormone convertase enzyme 2 (PC2) is essential for processing pro-islet amyloid polypeptide at the NH2-terminal cleavage site. Diabetes 2001, 50:534-539.
    • (2001) Diabetes , vol.50 , pp. 534-539
    • Wang, J.1    Xu, J.2    Finnerty, J.3    Furuta, M.4    Steiner, D.F.5    Verchere, C.B.6
  • 179
    • 0030606870 scopus 로고    scopus 로고
    • The insulin-induced down-regulation of IRS-1 in 3T3-L1 adipocytes is mediated by a calcium-dependent thiol protease
    • Smith L.K., Rice K.M., Garner C.W. The insulin-induced down-regulation of IRS-1 in 3T3-L1 adipocytes is mediated by a calcium-dependent thiol protease. Mol. Cell. Endocrinol. 1996, 122:81-92.
    • (1996) Mol. Cell. Endocrinol. , vol.122 , pp. 81-92
    • Smith, L.K.1    Rice, K.M.2    Garner, C.W.3
  • 180
    • 84865985511 scopus 로고    scopus 로고
    • Protective effects of adenosine on the diabetic myocardium against ischemia-reperfusion injury: role of calpain
    • Yang Y., Duan W., Zhou J., Yan J., Liu J., Zhang J., Jin Z., Yi D. Protective effects of adenosine on the diabetic myocardium against ischemia-reperfusion injury: role of calpain. Med. Hypotheses 2012, 79:462-464.
    • (2012) Med. Hypotheses , vol.79 , pp. 462-464
    • Yang, Y.1    Duan, W.2    Zhou, J.3    Yan, J.4    Liu, J.5    Zhang, J.6    Jin, Z.7    Yi, D.8
  • 181
    • 33745070887 scopus 로고    scopus 로고
    • Generation of constitutively active calcineurin by calpain contributes to delayed neuronal death following mouse brain ischemia
    • Shioda N., Moriguchi S., Shirasaki Y., Fukunaga K. Generation of constitutively active calcineurin by calpain contributes to delayed neuronal death following mouse brain ischemia. J. Neurochem. 2006, 98:310-320.
    • (2006) J. Neurochem. , vol.98 , pp. 310-320
    • Shioda, N.1    Moriguchi, S.2    Shirasaki, Y.3    Fukunaga, K.4
  • 182
    • 59849097814 scopus 로고    scopus 로고
    • Calcium, calpains, and cardiac hypertrophy: a new link
    • Heidrich F.M., Ehrlich B.E. Calcium, calpains, and cardiac hypertrophy: a new link. Circ. Res. 2009, 104:e19-e20.
    • (2009) Circ. Res. , vol.104 , pp. e19-e20
    • Heidrich, F.M.1    Ehrlich, B.E.2
  • 183
    • 41449084770 scopus 로고    scopus 로고
    • Targeting the calpain/calpastatin system as a new strategy to prevent cardiovascular remodeling in angiotensin II-induced hypertension
    • Letavernier E., Perez J., Bellocq A., Mesnard L., de Castro Keller A., Haymann J.P., Baud L. Targeting the calpain/calpastatin system as a new strategy to prevent cardiovascular remodeling in angiotensin II-induced hypertension. Circ. Res. 2008, 102:720-728.
    • (2008) Circ. Res. , vol.102 , pp. 720-728
    • Letavernier, E.1    Perez, J.2    Bellocq, A.3    Mesnard, L.4    de Castro Keller, A.5    Haymann, J.P.6    Baud, L.7
  • 184
    • 77953808043 scopus 로고    scopus 로고
    • Lack of beta3 integrin signaling contributes to calpain-mediated myocardial cell loss in pressure-overloaded myocardium
    • Suryakumar G., Kasiganesan H., Balasubramanian S., Kuppuswamy D. Lack of beta3 integrin signaling contributes to calpain-mediated myocardial cell loss in pressure-overloaded myocardium. J. Cardiovasc. Pharmacol. 2010, 55:567-573.
    • (2010) J. Cardiovasc. Pharmacol. , vol.55 , pp. 567-573
    • Suryakumar, G.1    Kasiganesan, H.2    Balasubramanian, S.3    Kuppuswamy, D.4
  • 185
    • 62749154948 scopus 로고    scopus 로고
    • Focal adhesion kinase signaling in cardiac hypertrophy and failure
    • (et al.)
    • Franchini K.G., Clemente C.F., Marin T.M. Focal adhesion kinase signaling in cardiac hypertrophy and failure. Braz. J. Med. Biol. Res. 2009, 42:44-52. (et al.).
    • (2009) Braz. J. Med. Biol. Res. , vol.42 , pp. 44-52
    • Franchini, K.G.1    Clemente, C.F.2    Marin, T.M.3
  • 186
    • 0035923477 scopus 로고    scopus 로고
    • Activated interstitial myofibroblasts express catabolic enzymes and mediate matrix remodeling in myxomatous heart valves
    • Rabkin E., Aikawa M., Stone J.R., Fukumoto Y., Libby P., Schoen F.J. Activated interstitial myofibroblasts express catabolic enzymes and mediate matrix remodeling in myxomatous heart valves. Circulation 2001, 104:2525-2532.
    • (2001) Circulation , vol.104 , pp. 2525-2532
    • Rabkin, E.1    Aikawa, M.2    Stone, J.R.3    Fukumoto, Y.4    Libby, P.5    Schoen, F.J.6
  • 187
    • 84873025790 scopus 로고    scopus 로고
    • Cathepsin K knockout mitigates high-fat diet-induced cardiac hypertrophy and contractile dysfunction
    • Hua Y., Zhang Y., Dolence J., Shi G.P., Ren J., Nair S. Cathepsin K knockout mitigates high-fat diet-induced cardiac hypertrophy and contractile dysfunction. Diabetes 2013, 62:498-509.
    • (2013) Diabetes , vol.62 , pp. 498-509
    • Hua, Y.1    Zhang, Y.2    Dolence, J.3    Shi, G.P.4    Ren, J.5    Nair, S.6
  • 188
    • 0014493424 scopus 로고
    • Increased activity of lysosomal enzymes in experimental atherosclerosis, and the effect of cortisone
    • Curreri P.W., Kothari H.V., Bonner M.J., Miller B.F. Increased activity of lysosomal enzymes in experimental atherosclerosis, and the effect of cortisone. Proc. Soc. Exp. Biol. Med. 1969, 130:1253-1256.
    • (1969) Proc. Soc. Exp. Biol. Med. , vol.130 , pp. 1253-1256
    • Curreri, P.W.1    Kothari, H.V.2    Bonner, M.J.3    Miller, B.F.4
  • 189
    • 0029007093 scopus 로고
    • Pericellular mobilization of the tissue-destructive cysteine proteinases, cathepsins B, L, and S, by human monocyte-derived macrophages
    • Reddy V.Y., Zhang Q.Y., Weiss S.J. Pericellular mobilization of the tissue-destructive cysteine proteinases, cathepsins B, L, and S, by human monocyte-derived macrophages. Proc. Natl. Acad. Sci. U. S. A. 1995, 92:3849-3853.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 3849-3853
    • Reddy, V.Y.1    Zhang, Q.Y.2    Weiss, S.J.3
  • 191
    • 33847747817 scopus 로고    scopus 로고
    • Expression of cathepsin K is regulated by shear stress in cultured endothelial cells and is increased in endothelium in human atherosclerosis
    • Platt M.O., Ankeny R.F., Shi G.P., Weiss D., Vega J.D., Taylor W.R., Jo H. Expression of cathepsin K is regulated by shear stress in cultured endothelial cells and is increased in endothelium in human atherosclerosis. Am. J. Physiol. Heart Circ. Physiol. 2007, 292:H1479-H1486.
    • (2007) Am. J. Physiol. Heart Circ. Physiol. , vol.292 , pp. H1479-H1486
    • Platt, M.O.1    Ankeny, R.F.2    Shi, G.P.3    Weiss, D.4    Vega, J.D.5    Taylor, W.R.6    Jo, H.7
  • 192
    • 0036735233 scopus 로고    scopus 로고
    • Differential expression of cysteine and aspartic proteases during progression of atherosclerosis in apolipoprotein E-deficient mice
    • Jormsjo S., Wuttge D.M., Sirsjo A., Whatling C., Hamsten A., Stemme S., Eriksson P. Differential expression of cysteine and aspartic proteases during progression of atherosclerosis in apolipoprotein E-deficient mice. Am. J. Pathol. 2002, 161:939-945.
    • (2002) Am. J. Pathol. , vol.161 , pp. 939-945
    • Jormsjo, S.1    Wuttge, D.M.2    Sirsjo, A.3    Whatling, C.4    Hamsten, A.5    Stemme, S.6    Eriksson, P.7
  • 195
    • 57649183693 scopus 로고    scopus 로고
    • Cathepsin L is significantly associated with apoptosis and plaque destabilization in human atherosclerosis
    • Li W., Kornmark L., Jonasson L., Forssell C., Yuan X.M. Cathepsin L is significantly associated with apoptosis and plaque destabilization in human atherosclerosis. Atherosclerosis 2009, 202:92-102.
    • (2009) Atherosclerosis , vol.202 , pp. 92-102
    • Li, W.1    Kornmark, L.2    Jonasson, L.3    Forssell, C.4    Yuan, X.M.5
  • 200
    • 59049103199 scopus 로고    scopus 로고
    • Usefulness of serum cathepsin L as an independent biomarker in patients with coronary heart disease
    • Liu Y., Li X., Peng D., Tan Z., Liu H., Qing Y., Xue Y., Shi G.P. Usefulness of serum cathepsin L as an independent biomarker in patients with coronary heart disease. Am. J. Cardiol. 2009, 103:476-481.
    • (2009) Am. J. Cardiol. , vol.103 , pp. 476-481
    • Liu, Y.1    Li, X.2    Peng, D.3    Tan, Z.4    Liu, H.5    Qing, Y.6    Xue, Y.7    Shi, G.P.8
  • 201
    • 84856096017 scopus 로고    scopus 로고
    • Serum and saliva levels of cathepsin L in patients with acute coronary syndrome
    • Mirzaii-Dizgah I., Riahi E. Serum and saliva levels of cathepsin L in patients with acute coronary syndrome. J. Contemp. Dent. Pract. 2011, 12:114-119.
    • (2011) J. Contemp. Dent. Pract. , vol.12 , pp. 114-119
    • Mirzaii-Dizgah, I.1    Riahi, E.2
  • 207
    • 62549136587 scopus 로고    scopus 로고
    • Cathepsin K regulates adipocyte differentiation: possible involvement of type I collagen degradation
    • Han J., Luo T., Gu Y., Li G., Jia W., Luo M. Cathepsin K regulates adipocyte differentiation: possible involvement of type I collagen degradation. Endocr. J. 2009, 56:55-63.
    • (2009) Endocr. J. , vol.56 , pp. 55-63
    • Han, J.1    Luo, T.2    Gu, Y.3    Li, G.4    Jia, W.5    Luo, M.6
  • 210
    • 84856613892 scopus 로고    scopus 로고
    • Cathepsin S as a biomarker: where are we now and what are the future challenges?
    • Arnlov J. Cathepsin S as a biomarker: where are we now and what are the future challenges?. Biomark. Med 2012, 6:9-11.
    • (2012) Biomark. Med , vol.6 , pp. 9-11
    • Arnlov, J.1
  • 213
    • 84904621905 scopus 로고    scopus 로고
    • Lysosomal cathepsin D contributes to cell death during adipocyte hypertrophy
    • Eguchi A., Feldstein A.E. Lysosomal cathepsin D contributes to cell death during adipocyte hypertrophy. Adipocyte 2013, 2:170-175.
    • (2013) Adipocyte , vol.2 , pp. 170-175
    • Eguchi, A.1    Feldstein, A.E.2
  • 214
    • 0042821989 scopus 로고    scopus 로고
    • Impaired cathepsin L gene expression in skeletal muscle is associated with type 2 diabetes
    • Huang X., Vaag A., Carlsson E., Hansson M., Ahren B., Groop L. Impaired cathepsin L gene expression in skeletal muscle is associated with type 2 diabetes. Diabetes 2003, 52:2411-2418.
    • (2003) Diabetes , vol.52 , pp. 2411-2418
    • Huang, X.1    Vaag, A.2    Carlsson, E.3    Hansson, M.4    Ahren, B.5    Groop, L.6
  • 215
    • 84872046229 scopus 로고    scopus 로고
    • Serum cathepsin S is associated with decreased insulin sensitivity and the development of type 2 diabetes in a community-based cohort of elderly men
    • Jobs E., Riserus U., Ingelsson E., Sundstrom J., Jobs M., Nerpin E., Iggman D., Basu S., Larsson A., Lind L., Arnlov J. Serum cathepsin S is associated with decreased insulin sensitivity and the development of type 2 diabetes in a community-based cohort of elderly men. Diabetes Care 2013, 36:163-165.
    • (2013) Diabetes Care , vol.36 , pp. 163-165
    • Jobs, E.1    Riserus, U.2    Ingelsson, E.3    Sundstrom, J.4    Jobs, M.5    Nerpin, E.6    Iggman, D.7    Basu, S.8    Larsson, A.9    Lind, L.10    Arnlov, J.11
  • 216
    • 84884784361 scopus 로고    scopus 로고
    • Correlation between serum cathepsin S and insulin resistance in type 2 diabetes
    • Chen R.P., Ren A., Ye S.D. Correlation between serum cathepsin S and insulin resistance in type 2 diabetes. Exp. Ther. Med. 2013, 6:1237-1242.
    • (2013) Exp. Ther. Med. , vol.6 , pp. 1237-1242
    • Chen, R.P.1    Ren, A.2    Ye, S.D.3
  • 217
    • 0016954695 scopus 로고
    • Proceedings: triglyceride, lipid peroxidation, and cathepsin in the serum of spontaneously hypertensive rats
    • Saito N., Mukaino S., Ogino K. Proceedings: triglyceride, lipid peroxidation, and cathepsin in the serum of spontaneously hypertensive rats. Jpn. Heart J. 1976, 17:345-347.
    • (1976) Jpn. Heart J. , vol.17 , pp. 345-347
    • Saito, N.1    Mukaino, S.2    Ogino, K.3
  • 218
    • 0017350448 scopus 로고
    • Lysosomal enzymes in the development and regression of myocardial hypertrophy induced by systemic hypertension
    • Wildenthal K., Mueller E.A. Lysosomal enzymes in the development and regression of myocardial hypertrophy induced by systemic hypertension. J. Mol. Cell. Cardiol. 1977, 9:121-130.
    • (1977) J. Mol. Cell. Cardiol. , vol.9 , pp. 121-130
    • Wildenthal, K.1    Mueller, E.A.2
  • 220
    • 0028937006 scopus 로고
    • Prevention of cardiac hypertrophy in experimental chronic renal failure by long-term ACE inhibitor administration: potential role of lysosomal proteinases
    • Suzuki H., Schaefer L., Ling H., Schaefer R.M., Dammrich J., Teschner M., Heidland A. Prevention of cardiac hypertrophy in experimental chronic renal failure by long-term ACE inhibitor administration: potential role of lysosomal proteinases. Am. J. Nephrol. 1995, 15:129-136.
    • (1995) Am. J. Nephrol. , vol.15 , pp. 129-136
    • Suzuki, H.1    Schaefer, L.2    Ling, H.3    Schaefer, R.M.4    Dammrich, J.5    Teschner, M.6    Heidland, A.7
  • 222
    • 60549104999 scopus 로고    scopus 로고
    • Lysosomal cysteine peptidase cathepsin L protects against cardiac hypertrophy through blocking AKT/GSK3beta signaling
    • Tang Q., Cai J., Shen D., Bian Z., Yan L., Wang Y.X., Lan J., Zhuang G.Q., Ma W.Z., Wang W. Lysosomal cysteine peptidase cathepsin L protects against cardiac hypertrophy through blocking AKT/GSK3beta signaling. J. Mol. Med. 2009, 87:249-260.
    • (2009) J. Mol. Med. , vol.87 , pp. 249-260
    • Tang, Q.1    Cai, J.2    Shen, D.3    Bian, Z.4    Yan, L.5    Wang, Y.X.6    Lan, J.7    Zhuang, G.Q.8    Ma, W.Z.9    Wang, W.10
  • 224
    • 84878922289 scopus 로고    scopus 로고
    • Cathepsin K knockout alleviates pressure overload-induced cardiac hypertrophy
    • Hua Y., Xu X., Shi G.P., Chicco A.J., Ren J., Nair S. Cathepsin K knockout alleviates pressure overload-induced cardiac hypertrophy. Hypertension 2013, 61:1184-1192.
    • (2013) Hypertension , vol.61 , pp. 1184-1192
    • Hua, Y.1    Xu, X.2    Shi, G.P.3    Chicco, A.J.4    Ren, J.5    Nair, S.6
  • 226
    • 0034604701 scopus 로고    scopus 로고
    • Free cholesterol loading of macrophages induces apoptosis involving the fas pathway
    • Yao P.M., Tabas I. Free cholesterol loading of macrophages induces apoptosis involving the fas pathway. J. Biol. Chem. 2000, 275:23807-23813.
    • (2000) J. Biol. Chem. , vol.275 , pp. 23807-23813
    • Yao, P.M.1    Tabas, I.2
  • 227
    • 0033456158 scopus 로고    scopus 로고
    • FLICE-inhibitory protein expression during macrophage differentiation confers resistance to fas-mediated apoptosis
    • Perlman H., Pagliari L.J., Georganas C., Mano T., Walsh K., Pope R.M. FLICE-inhibitory protein expression during macrophage differentiation confers resistance to fas-mediated apoptosis. J. Exp. Med. 1999, 190:1679-1688.
    • (1999) J. Exp. Med. , vol.190 , pp. 1679-1688
    • Perlman, H.1    Pagliari, L.J.2    Georganas, C.3    Mano, T.4    Walsh, K.5    Pope, R.M.6
  • 229
    • 0038447969 scopus 로고    scopus 로고
    • The p17 cleaved form of caspase-3 is present within viable macrophages in vitro and in atherosclerotic plaque
    • Nhan T.Q., Liles W.C., Chait A., Fallon J.T., Schwartz S.M. The p17 cleaved form of caspase-3 is present within viable macrophages in vitro and in atherosclerotic plaque. Arterioscler. Thromb. Vasc. Biol. 2003, 23:1276-1282.
    • (2003) Arterioscler. Thromb. Vasc. Biol. , vol.23 , pp. 1276-1282
    • Nhan, T.Q.1    Liles, W.C.2    Chait, A.3    Fallon, J.T.4    Schwartz, S.M.5
  • 231
    • 0035344697 scopus 로고    scopus 로고
    • Biologic effect and molecular regulation of vascular apoptosis in atherosclerosis
    • Geng Y.J. Biologic effect and molecular regulation of vascular apoptosis in atherosclerosis. Curr. Atheroscler. Rep. 2001, 3:234-242.
    • (2001) Curr. Atheroscler. Rep. , vol.3 , pp. 234-242
    • Geng, Y.J.1
  • 232
    • 42349104656 scopus 로고    scopus 로고
    • Endothelial dysfunction in hyperglycemia as a trigger of atherosclerosis
    • Nakagami H., Kaneda Y., Ogihara T., Morishita R. Endothelial dysfunction in hyperglycemia as a trigger of atherosclerosis. Curr. Diabetes Rev. 2005, 1:59-63.
    • (2005) Curr. Diabetes Rev. , vol.1 , pp. 59-63
    • Nakagami, H.1    Kaneda, Y.2    Ogihara, T.3    Morishita, R.4
  • 233
    • 0037203345 scopus 로고    scopus 로고
    • Lipoapoptosis: its mechanism and its diseases
    • Unger R.H., Orci L. Lipoapoptosis: its mechanism and its diseases. Biochim. Biophys. Acta 2002, 1585:202-212.
    • (2002) Biochim. Biophys. Acta , vol.1585 , pp. 202-212
    • Unger, R.H.1    Orci, L.2
  • 234
    • 1042266664 scopus 로고    scopus 로고
    • Apolipoprotein B production reduces lipotoxic cardiomyopathy: studies in heart-specific lipoprotein lipase transgenic mouse
    • Yokoyama M., Yagyu H., Hu Y., Seo T., Hirata K., Homma S., Goldberg I.J. Apolipoprotein B production reduces lipotoxic cardiomyopathy: studies in heart-specific lipoprotein lipase transgenic mouse. J. Biol. Chem. 2004, 279:4204-4211.
    • (2004) J. Biol. Chem. , vol.279 , pp. 4204-4211
    • Yokoyama, M.1    Yagyu, H.2    Hu, Y.3    Seo, T.4    Hirata, K.5    Homma, S.6    Goldberg, I.J.7
  • 235
    • 21444448717 scopus 로고    scopus 로고
    • High-fat diet enhances visceral advanced glycation end products, nuclear O-Glc-Nac modification, p38 mitogen-activated protein kinase activation and apoptosis
    • Li S.Y., Liu Y., Sigmon V.K., McCort A., Ren J. High-fat diet enhances visceral advanced glycation end products, nuclear O-Glc-Nac modification, p38 mitogen-activated protein kinase activation and apoptosis. Diabetes Obes. Metab. 2005, 7:448-454.
    • (2005) Diabetes Obes. Metab. , vol.7 , pp. 448-454
    • Li, S.Y.1    Liu, Y.2    Sigmon, V.K.3    McCort, A.4    Ren, J.5
  • 238
    • 38049009574 scopus 로고    scopus 로고
    • More activated cardiac mitochondrial-dependent apoptotic pathway in obese Zucker rats
    • Lu M.C., Tzang B.S., Kuo W.W., Wu F.L., Chen Y.S., Tsai C.H., Huang C.Y., Lee S.D. More activated cardiac mitochondrial-dependent apoptotic pathway in obese Zucker rats. Obesity 2007, 15:2634-2642.
    • (2007) Obesity , vol.15 , pp. 2634-2642
    • Lu, M.C.1    Tzang, B.S.2    Kuo, W.W.3    Wu, F.L.4    Chen, Y.S.5    Tsai, C.H.6    Huang, C.Y.7    Lee, S.D.8
  • 239
    • 57349129372 scopus 로고    scopus 로고
    • Mitochondrial apoptotic signaling is elevated in cardiac but not skeletal muscle in the obese Zucker rat and is reduced with aerobic exercise
    • Peterson J.M., Bryner R.W., Sindler A., Frisbee J.C., Alway S.E. Mitochondrial apoptotic signaling is elevated in cardiac but not skeletal muscle in the obese Zucker rat and is reduced with aerobic exercise. J. Appl. Physiol. 2008, 105:1934-1943.
    • (2008) J. Appl. Physiol. , vol.105 , pp. 1934-1943
    • Peterson, J.M.1    Bryner, R.W.2    Sindler, A.3    Frisbee, J.C.4    Alway, S.E.5
  • 241
    • 79958211266 scopus 로고    scopus 로고
    • Rutin attenuates metabolic changes, nonalcoholic steatohepatitis, and cardiovascular remodeling in high-carbohydrate, high-fat diet-fed rats
    • Panchal S.K., Poudyal H., Arumugam T.V., Brown L. Rutin attenuates metabolic changes, nonalcoholic steatohepatitis, and cardiovascular remodeling in high-carbohydrate, high-fat diet-fed rats. J. Nutr. 2011, 141:1062-1069.
    • (2011) J. Nutr. , vol.141 , pp. 1062-1069
    • Panchal, S.K.1    Poudyal, H.2    Arumugam, T.V.3    Brown, L.4
  • 242
    • 0033670330 scopus 로고    scopus 로고
    • Mechanisms of increased susceptibility to angiotensin II-induced apoptosis in ventricular cardiomyocytes of spontaneously hypertensive rats
    • Ravassa S., Fortuno M.A., Gonzalez A., Lopez B., Zalba G., Fortuno A., Diez J. Mechanisms of increased susceptibility to angiotensin II-induced apoptosis in ventricular cardiomyocytes of spontaneously hypertensive rats. Hypertension 2000, 36:1065-1071.
    • (2000) Hypertension , vol.36 , pp. 1065-1071
    • Ravassa, S.1    Fortuno, M.A.2    Gonzalez, A.3    Lopez, B.4    Zalba, G.5    Fortuno, A.6    Diez, J.7
  • 244
    • 0037373047 scopus 로고    scopus 로고
    • Reversal of interstitial fibroblast hyperplasia via apoptosis in hypertensive rat heart with valsartan or enalapril
    • Der Sarkissian S., Marchand E.L., Duguay D., Hamet P., deBlois D. Reversal of interstitial fibroblast hyperplasia via apoptosis in hypertensive rat heart with valsartan or enalapril. Cardiovasc. Res. 2003, 57:775-783.
    • (2003) Cardiovasc. Res. , vol.57 , pp. 775-783
    • Der Sarkissian, S.1    Marchand, E.L.2    Duguay, D.3    Hamet, P.4    deBlois, D.5
  • 245
    • 33745479230 scopus 로고    scopus 로고
    • Effects of exercise training on pathological cardiac hypertrophy related gene expression and apoptosis
    • Lee Y.I., Cho J.Y., Kim M.H., Kim K.B., Lee D.J., Lee K.S. Effects of exercise training on pathological cardiac hypertrophy related gene expression and apoptosis. Eur. J. Appl. Physiol. 2006, 97:216-224.
    • (2006) Eur. J. Appl. Physiol. , vol.97 , pp. 216-224
    • Lee, Y.I.1    Cho, J.Y.2    Kim, M.H.3    Kim, K.B.4    Lee, D.J.5    Lee, K.S.6
  • 246
    • 34748899474 scopus 로고    scopus 로고
    • Association of depressed cardiac gp130-mediated antiapoptotic pathways with stimulated cardiomyocyte apoptosis in hypertensive patients with heart failure
    • Gonzalez A., Ravassa S., Loperena I., Lopez B., Beaumont J., Querejeta R., Larman M., Diez J. Association of depressed cardiac gp130-mediated antiapoptotic pathways with stimulated cardiomyocyte apoptosis in hypertensive patients with heart failure. J. Hypertens. 2007, 25:2148-2157.
    • (2007) J. Hypertens. , vol.25 , pp. 2148-2157
    • Gonzalez, A.1    Ravassa, S.2    Loperena, I.3    Lopez, B.4    Beaumont, J.5    Querejeta, R.6    Larman, M.7    Diez, J.8
  • 249
    • 78650622627 scopus 로고    scopus 로고
    • Clinical significance of matrix metalloproteinase (MMP)-2 in patients with acute heart failure
    • Shirakabe A., Asai K., Hata N., Yokoyama S., Shinada T., Kobayashi N., Mizuno K. Clinical significance of matrix metalloproteinase (MMP)-2 in patients with acute heart failure. Int. Heart J. 2010, 51:404-410.
    • (2010) Int. Heart J. , vol.51 , pp. 404-410
    • Shirakabe, A.1    Asai, K.2    Hata, N.3    Yokoyama, S.4    Shinada, T.5    Kobayashi, N.6    Mizuno, K.7
  • 250
    • 84883511215 scopus 로고    scopus 로고
    • The co-existence of the IL-18+183 A/G and MMP-9-1562 C/T polymorphisms is associated with clinical events in coronary artery disease patients
    • Opstad T.B., Pettersen A.A., Arnesen H., Seljeflot I. The co-existence of the IL-18+183 A/G and MMP-9-1562 C/T polymorphisms is associated with clinical events in coronary artery disease patients. PLoS One 2013, 8:e74498.
    • (2013) PLoS One , vol.8 , pp. e74498
    • Opstad, T.B.1    Pettersen, A.A.2    Arnesen, H.3    Seljeflot, I.4
  • 251
    • 84877069808 scopus 로고    scopus 로고
    • Variations in matrix metalloproteinase-1, -3, and -9 genes and the risk of acute coronary syndrome and coronary artery disease in the Chinese Han population
    • Xu X., Wang L., Xu C., Zhang P., Yong F., Liu H., Wang J., Shi Y. Variations in matrix metalloproteinase-1, -3, and -9 genes and the risk of acute coronary syndrome and coronary artery disease in the Chinese Han population. Coron. Artery Dis. 2013, 24:259-265.
    • (2013) Coron. Artery Dis. , vol.24 , pp. 259-265
    • Xu, X.1    Wang, L.2    Xu, C.3    Zhang, P.4    Yong, F.5    Liu, H.6    Wang, J.7    Shi, Y.8
  • 256
    • 79961076739 scopus 로고    scopus 로고
    • The clinical impact of circulating caspase-3 p17 level: a potential new biomarker for myocardial injury and cardiovascular disease
    • Singh K.P., Jaffe A.S., Liang B.T. The clinical impact of circulating caspase-3 p17 level: a potential new biomarker for myocardial injury and cardiovascular disease. Futur. Cardiol. 2011, 7:443-445.
    • (2011) Futur. Cardiol. , vol.7 , pp. 443-445
    • Singh, K.P.1    Jaffe, A.S.2    Liang, B.T.3
  • 257
    • 33846120591 scopus 로고    scopus 로고
    • Matrix metalloproteinases as valid clinical targets
    • Fingleton B. Matrix metalloproteinases as valid clinical targets. Curr. Pharm. Des. 2007, 13:333-346.
    • (2007) Curr. Pharm. Des. , vol.13 , pp. 333-346
    • Fingleton, B.1
  • 258
    • 84887041961 scopus 로고    scopus 로고
    • Doxycycline reduces cardiac matrix metalloproteinase-2 activity but does not ameliorate myocardial dysfunction during reperfusion in coronary artery bypass patients undergoing cardiopulmonary bypass
    • Schulze C.J., Castro M.M., Kandasamy A.D., Cena J., Bryden C., Wang S.H., Koshal A., Tsuyuki R.T., Finegan B.A., Schulz R. Doxycycline reduces cardiac matrix metalloproteinase-2 activity but does not ameliorate myocardial dysfunction during reperfusion in coronary artery bypass patients undergoing cardiopulmonary bypass. Crit. Care Med. 2013, 41:2512-2520.
    • (2013) Crit. Care Med. , vol.41 , pp. 2512-2520
    • Schulze, C.J.1    Castro, M.M.2    Kandasamy, A.D.3    Cena, J.4    Bryden, C.5    Wang, S.H.6    Koshal, A.7    Tsuyuki, R.T.8    Finegan, B.A.9    Schulz, R.10
  • 259
    • 84876724230 scopus 로고    scopus 로고
    • Therapeutic inhibition of cathepsin K-reducing bone resorption while maintaining bone formation
    • Duong le T. Therapeutic inhibition of cathepsin K-reducing bone resorption while maintaining bone formation. Bone Key Rep. 2012, 67.
    • (2012) Bone Key Rep. , vol.67
    • Duong le, T.1
  • 260
    • 22744437978 scopus 로고    scopus 로고
    • Apoptosis-based therapies and drug targets
    • Fischer U., Schulze-Osthoff K. Apoptosis-based therapies and drug targets. Cell Death Differ. 2005, 12(Suppl. 1):942-961.
    • (2005) Cell Death Differ. , vol.12 , pp. 942-961
    • Fischer, U.1    Schulze-Osthoff, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.