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Volumn 15, Issue 4, 2011, Pages 519-527

Targets of chymase inhibitors

Author keywords

Angiotensin II; chymase; inhibitors; mast cells; matrix metalloproteianase 9; Transforming growth factor

Indexed keywords

ADVANCED GLYCATION END PRODUCT; ANGIOTENSIN I; ANGIOTENSIN II; CHYMASE; CHYMASE INHIBITOR; COLLAGEN TYPE 1; COLLAGEN TYPE 3; DIPEPTIDYL CARBOXYPEPTIDASE INHIBITOR; GELATINASE B; GLUCOSAMINE; GLUTAMINE; HISTIDINE; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE INHIBITOR; INSULIN; MACROPHAGE INFLAMMATORY PROTEIN 2; MITOGEN ACTIVATED PROTEIN KINASE 3; MONOCYTE CHEMOTACTIC PROTEIN 1; PHENYLALANINE; TRANSFORMING GROWTH FACTOR BETA; VASCULOTROPIN;

EID: 79952690181     PISSN: 14728222     EISSN: None     Source Type: Journal    
DOI: 10.1517/14728222.2011.555401     Document Type: Review
Times cited : (15)

References (99)
  • 1
    • 0023266455 scopus 로고
    • Measurement of the internal pH of mast cell granules using microvolumetric fluorescence and isotopic techniques
    • DOI 10.1016/0003-9861(87)90098-1
    • De Young MB, Nemeth EF, Scarpa A. Measurement of the internal pH of mast cell granules using microvolumetric fluorescence and isotopic techniques. Arch Biochem Biophys 1987;15:222-33 (Pubitemid 17068815)
    • (1987) Archives of Biochemistry and Biophysics , vol.254 , Issue.1 , pp. 222-233
    • De Young, M.B.1    Nemeth, E.F.2    Scarpa, A.3
  • 2
    • 0029020946 scopus 로고
    • Regulation of the activity of human chymase during storage and release from mast cells: The contributions of inorganic cations pH heparin and histamine
    • McEuen AR, Sharma B, Walls AF. Regulation of the activity of human chymase during storage and release from mast cells: the contributions of inorganic cations, pH, heparin and histamine. Biochim Biophys Acta 1995;1267:115-21
    • (1995) Biochim. Biophys. Acta. , vol.1267 , pp. 115-121
    • McEuen, A.R.1    Sharma, B.2    Walls, A.F.3
  • 3
    • 0030053083 scopus 로고    scopus 로고
    • Purification and characterization of angiotensin II-generating chymase from hamster cheek pouch
    • DOI 10.1016/0024-3205(95)02328-3
    • Takai S, Shiota N, Yamamoto D, et al. Purification and characterization of angiotensin II-generating chymase from hamster cheek pouch. Life Sci 1996;58:591-7 (Pubitemid 26046951)
    • (1996) Life Sciences , vol.58 , Issue.7 , pp. 591-597
    • Takai, S.1    Shiota, N.2    Yamamoto, D.3    Okunishi, H.4    Miyazaki, M.5
  • 5
    • 0034100147 scopus 로고    scopus 로고
    • Molecular and cellular mechanisms of angiotensin II-mediated cardiovascular and renal diseases
    • Kim S, Iwao H. Molecular and cellular mechanisms of angiotensin II-mediated cardiovascular and renal diseases. Pharmacol Rev 2000;52:11-34 (Pubitemid 30127593)
    • (2000) Pharmacological Reviews , vol.52 , Issue.1 , pp. 11-34
    • Kim, S.1    Iwao, H.2
  • 6
    • 0000136969 scopus 로고
    • Dose the new angiotensin converting enzyme inhibitor cilazapril prevent restenosis after percutaneous transluminal coronary angioplasty
    • MERCATOR Study Group
    • MERCATOR Study Group. Dose the new angiotensin converting enzyme inhibitor cilazapril prevent restenosis after percutaneous transluminal coronary angioplasty? Circulation 1992;86:100-10
    • (1992) Circulation , vol.86 , pp. 100-110
  • 7
    • 0035260346 scopus 로고    scopus 로고
    • Valsartan for prevention of restenosis after stenting of Type B2/C lesions: The Val-PREST trial
    • Peters S, Gotting B, Trummel M, et al. Valsartan for prevention of restenosis after stenting of type B2/C lesions: the VAL-PREST trial. J Invasive Cardiol 2001;13:93-7 (Pubitemid 33761992)
    • (2001) Journal of Invasive Cardiology , vol.13 , Issue.2 , pp. 93-97
    • Peters, S.1    Gotting, B.2    Trummel, M.3    Rust, H.4    Brattstrom, A.5
  • 9
    • 0025598309 scopus 로고
    • Identification of a highly specific chymase as the major angiotensin II-forming enzyme in the human heart
    • Urata H, Kinoshita A, Misono KS, et al. Identification of a highly specific chymase as the major angiotensin II-forming enzyme in the human heart. J Biol Chem 1990;265:22348-57 (Pubitemid 120014308)
    • (1990) Journal of Biological Chemistry , vol.265 , Issue.36 , pp. 22348-22357
    • Urata, H.1    Kinoshita, A.2    Misono, K.S.3    Bumpus, F.M.4    Husain, A.5
  • 10
    • 0031762019 scopus 로고    scopus 로고
    • Functional role of chymase in angiotensin II formation in human vascular tissue
    • DOI 10.1097/00005344-199811000-00020
    • Takai S, Shiota N, Jin D, Miyazaki M. Functional role of chymase in angiotensin II formation in human vascular tissue. J Cardiovasc Pharmacol 1998;32:826-33 (Pubitemid 28506655)
    • (1998) Journal of Cardiovascular Pharmacology , vol.32 , Issue.5 , pp. 826-833
    • Takai, S.1    Shiota, N.2    Jin, D.3    Miyazaki, M.4
  • 11
    • 0035106195 scopus 로고    scopus 로고
    • Different angiotensin II-forming pathways in human and rat vascular tissues
    • DOI 10.1016/S0009-8981(01)00379-5, PII S0009898101003795
    • Takai S, Sakaguchi M, Jin D, et al. Different angiotensin II-forming pathways in human and rat vascular tissues. Clin Chim Acta 2001;305:191-5 (Pubitemid 32201977)
    • (2001) Clinica Chimica Acta , vol.305 , Issue.1-2 , pp. 191-195
    • Takai, S.1    Sakaguchi, M.2    Jin, D.3    Yamada, M.4    Kirimura, K.5    Miyazaki, M.6
  • 13
    • 0037967318 scopus 로고    scopus 로고
    • Chymase is upregulated in diabetic nephropathy: Implications for an alternative pathway of angiotensin II-mediated diabetic renal and vascular disease
    • DOI 10.1097/01.ASN.0000071512.93927.4E
    • Huang XR, Chen WY, Truong LD, Lan HY. Chymase is upregulated in diabetic nephropathy: implications for an alternative pathway of angiotensin II-mediated diabetic renal and vascular disease. J Am Soc Nephrol 2003;14:1738-47 (Pubitemid 36750469)
    • (2003) Journal of the American Society of Nephrology , vol.14 , Issue.7 , pp. 1738-1747
    • Huang, X.R.1    Chen, W.Y.2    Truong, L.D.3    Lan, H.Y.4
  • 18
    • 0030845183 scopus 로고    scopus 로고
    • 92 bonds of the catalytic domain
    • DOI 10.1074/jbc.272.41.25628
    • Fang KC, Raymond WW, Blount JL, Caughey GH. Dog mast cell alpha-chymase activates progelatinase B by cleaving the Phe88-Gln89 andPhe91-Glu92 bonds of the catalytic domain. J Biol Chem 1997;272:25628-35 (Pubitemid 27438877)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.41 , pp. 25628-25635
    • Fang, K.C.1    Raymond, W.W.2    Blount, J.L.3    Caughey, G.H.4
  • 20
    • 0028945071 scopus 로고
    • Human prochymase activation a novel role for heparin in zymogen processing
    • Murakami M, Karnik SS, Husain A. Human prochymase activation. A novel role for heparin in zymogen processing. J Biol Chem 1995;270:2218-23
    • (1995) J. Biol. Chem. , vol.270 , pp. 2218-2223
    • Murakami, M.1    Karnik, S.S.2    Husain, A.3
  • 21
    • 0035947568 scopus 로고    scopus 로고
    • Dipeptidyl peptidase I is essential for activation of mast cell chymases but not tryptases in mice
    • Wolters PJ, Pham CT, Muilenburg DJ, et al. Dipeptidyl peptidase I is essential for activation of mast cell chymases, but not tryptases, in mice. J Biol Chem 2001;276:18551-6
    • (2001) J. Biol. Chem. , vol.276 , pp. 18551-18556
    • Wolters, P.J.1    Pham, C.T.2    Muilenburg, D.J.3
  • 22
    • 0023266455 scopus 로고
    • Measurement of the internal pH of mast cell granules using microvolumetric fluorescence and isotopic techniques
    • DOI 10.1016/0003-9861(87)90098-1
    • De Young MB, Nemeth EF, Scarpa A. Measurement of the internal pH of mast cell granules using microvolumetric fluorescence and isotopic techniques. Arch Biochem Biophys 1987;254:222-33 (Pubitemid 17068815)
    • (1987) Archives of Biochemistry and Biophysics , vol.254 , Issue.1 , pp. 222-233
    • De Young, M.B.1    Nemeth, E.F.2    Scarpa, A.3
  • 23
    • 0029020946 scopus 로고
    • Regulation of the activity of human chymase during storage and release from mast cells: The contributions of inorganic cations pH heparin and histamine
    • McEuen AR, Sharma B, Walls AF. Regulation of the activity of human chymase during storage and release from mast cells: the contributions of inorganic cations, pH, heparin and histamine. Biochim Biophys Acta 1995;1267:115-21
    • (1995) Biochim. Biophys. Acta. , vol.1267 , pp. 115-121
    • McEuen, A.R.1    Sharma, B.2    Walls, A.F.3
  • 25
    • 0030971415 scopus 로고    scopus 로고
    • Regulation of local angiotensin II formation in the human heart in the presence of interstitial fluid
    • Inhibition of chymase by protease inhibitors of interstitial fluid and of angiotensin-converting enzyme by Ang-1-9 formed by heart carboxypeptidase a-like activity
    • Kokkonen JO, Saarinen J, Kovanen PT. Regulation of local angiotensin II formation in the human heart in the presence of interstitial fluid. Inhibition of chymase by protease inhibitors of interstitial fluid and of angiotensin-converting enzyme by Ang-(1-9) formed by heart carboxypeptidase A-like activity. Circulation 1997;95:1455-63
    • (1997) Circulation , Issue.95 , pp. 1455-1463
    • Kokkonen, J.O.1    Saarinen, J.2    Kovanen, P.T.3
  • 26
    • 0033543089 scopus 로고    scopus 로고
    • Chymase-dependent angiotensin II formation in human vascular tissue
    • Takai S, Jin D, Sakaguchi M, Miyazaki M. Chymase-dependent angiotensin II formation in human vascular tissue. Circulation 1999;100:654-8 (Pubitemid 29379756)
    • (1999) Circulation , vol.100 , Issue.6 , pp. 654-658
    • Takai, S.1    Jin, D.2    Sakaguchi, M.3    Miyazaki, M.4
  • 27
    • 0033983720 scopus 로고    scopus 로고
    • Inhibition of chymase reduces vascular proliferation in dog grafted veins
    • DOI 10.1016/S0014-5793(00)01125-X, PII S001457930001125X
    • Takai S, Yuda A, Jin D, et al. Inhibition of chymase reduces vascular proliferation in dog grafted veins. FEBS Lett 2000;467:141-4 (Pubitemid 30081722)
    • (2000) FEBS Letters , vol.467 , Issue.2-3 , pp. 141-144
    • Takai, S.1    Yuda, A.2    Jin, D.3    Nishimoto, M.4    Sakagichi, M.5    Sasaki, S.6    Miyazaki, M.7
  • 30
    • 0030857181 scopus 로고    scopus 로고
    • Induction of chymase that forms angiotensin II in the monkey atherosclerotic aorta
    • DOI 10.1016/S0014-5793(97)00752-7, PII S0014579397007527
    • Takai S, Shiota N, Kobayashi S, et al. Induction of chymase that forms angiotensin II in the monkey atherosclerotic aorta. FEBS Lett 1997;412:86-90 (Pubitemid 27310005)
    • (1997) FEBS Letters , vol.412 , Issue.1 , pp. 86-90
    • Takai, S.1    Shiota, N.2    Kobayashi, S.3    Matsumura, E.4    Miyazaki, M.5
  • 32
    • 0031654651 scopus 로고    scopus 로고
    • Differences in tissue angiotensin II-forming pathways by species and organs in vitro
    • Akasu M, Urata H, Kinoshita A, et al. Differences in tissue angiotensin II-forming pathways by species and organs in vitro. Hypertension 1998;32:514-20 (Pubitemid 28429142)
    • (1998) Hypertension , vol.32 , Issue.3 , pp. 514-520
    • Akasu, M.1    Urata, H.2    Kinoshita, A.3    Sasaguri, M.4    Ideishi, M.5    Arakawa, K.6
  • 33
    • 0028956737 scopus 로고
    • Human mast cell chymase and leukocyte elastase release latent transforming growth factor-beta 1 from the extracellular matrix of cultured human epithelial and endothelial cells
    • Taipale J, Lohi J, Saarinen J, et al. Human mast cell chymase and leukocyte elastase release latent transforming growth factor-beta 1 from the extracellular matrix of cultured human epithelial and endothelial cells. J Biol Chem 1995;270:4689-96
    • (1995) J. Biol. Chem. , vol.270 , pp. 4689-4696
    • Taipale, J.1    Lohi, J.2    Saarinen, J.3
  • 35
    • 0029115532 scopus 로고
    • Production and localization of 92-kilodalton gelatinase in abdominal aortic aneurysms an elastolytic metalloproteinase expressed by aneurysm-infiltrating macrophages
    • Thompson RW, Holmes DR, Mertens RA, et al. Production and localization of 92-kilodalton gelatinase in abdominal aortic aneurysms. An elastolytic metalloproteinase expressed by aneurysm-infiltrating macrophages. J Clin Invest 1995;96:318-26
    • (1995) J. Clin. Invest. , vol.96 , pp. 318-326
    • Thompson, R.W.1    Holmes, D.R.2    Mertens, R.A.3
  • 36
    • 0029089366 scopus 로고
    • Inflammation and matrix metalloproteinases in the enlarging abdominal aortic aneurysm
    • Freestone T, Turner RJ, Coady A, et al. Inflammation and matrix metalloproteinases in the enlarging abdominal aortic aneurysm. Arterioscler Thromb Vasc Biol 1995;15:1145-51
    • (1995) Arterioscler. Thromb. Vasc. Biol. , vol.15 , pp. 1145-1151
    • Freestone, T.1    Turner, R.J.2    Coady, A.3
  • 37
    • 19044382607 scopus 로고    scopus 로고
    • Increased local angiotensin II formation in aneurysmal aorta
    • Nishimoto M, Takai S, Fukumoto H, et al. Increased local angiotensin II formation in aneurysmal aorta. Life Sci 2002;71:2195-205
    • (2002) Life Sci. , vol.71 , pp. 2195-2205
    • Nishimoto, M.1    Takai, S.2    Fukumoto, H.3
  • 39
    • 2442701523 scopus 로고    scopus 로고
    • A specific chymase inhibitor, 2-(5-formylamino-6-oxo-2-phenyl-1,6- dihydropyrimidine-1-yl)-N-[{3, 4-dioxo-1-phenyl-7-(2-pyridyloxy)}-2-heptyl] acetamide (NK3201), suppresses development of abdominal aortic aneurysm in hamsters
    • DOI 10.1124/jpet.103.063974
    • Tsunemi K, Takai S, Nishimoto M, et al. A specific chymase inhibitor, 2-(5-formylamino-6-oxo-2-phenyl-1,6- ihydropyrimidine-1-yl)-N-[[3,4-dioxo-1- phenyl-7-(2-pyridyloxy)]-2-heptyl] acetamide (NK3201), suppresses development of abdominal aortic aneurysm in hamsters. J Pharmacol Exp Ther 2004;309:879-83 (Pubitemid 38669674)
    • (2004) Journal of Pharmacology and Experimental Therapeutics , vol.309 , Issue.3 , pp. 879-883
    • Tsunemi, K.1    Takai, S.2    Nishimoto, M.3    Jin, D.4    Sakaguchi, M.5    Muramatsu, M.6    Yuda, A.7    Sasaki, S.8    Miyazaki, M.9
  • 41
    • 67349109176 scopus 로고    scopus 로고
    • Effects of chymase inhibitor on angiotensin II-induced abdominal aortic aneurysm development in apolipoprotein E-deficient mice
    • Inoue N, Muramatsu M, Jin D, et al. Effects of chymase inhibitor on angiotensin II-induced abdominal aortic aneurysm development in apolipoprotein E-deficient mice. Atherosclerosis 2009;204:359-64
    • (2009) Atherosclerosis , vol.204 , pp. 359-364
    • Inoue, N.1    Muramatsu, M.2    Jin, D.3
  • 42
    • 70349763716 scopus 로고    scopus 로고
    • Critical role of mast cell chymase in mouse abdominal aortic aneurysm formation
    • Sun J, Zhang J, Lindholt JS, et al. Critical role of mast cell chymase in mouse abdominal aortic aneurysm formation. Circulation 2009;120:973-82
    • (2009) Circulation , vol.120 , pp. 973-982
    • Sun, J.1    Zhang, J.2    Lindholt, J.S.3
  • 44
    • 0033758875 scopus 로고    scopus 로고
    • Suppression of invasion and MMP-9 expression in NIH 3T3 and v-H-Ras 3T3 fibroblasts by lovastatin through inhibition of ras isoprenylation
    • Wang IK, Lin-Shiau SY, Lin JK. Suppression of invasion and MMP-9 expression in NIH 3T3 and v-H-Ras 3T3 fibroblasts by lovastatin through inhibition of ras isoprenylation. Oncology 2000;59:245-54
    • (2000) Oncology , vol.59 , pp. 245-254
    • Wang, I.K.1    Lin-Shiau, S.Y.2    Lin, J.K.3
  • 45
    • 0027420322 scopus 로고
    • Captopril inhibits the 72 kDa and 92 kDa matrix metalloproteinases
    • Sorbi D, Fadly M, Hicks R, et al. Captopril inhibits the 72 kDa and 92 kDa matrix metalloproteinases. Kidney Int 1993;44:1266-72
    • (1993) Kidney Int. , vol.44 , pp. 1266-12672
    • Sorbi, D.1    Fadly, M.2    Hicks, R.3
  • 47
    • 68849084078 scopus 로고    scopus 로고
    • Chymase inhibition provides pancreatic islet protection in hamsters with streptozotocin-induced diabetes
    • Takai S, Jin D, Ohzu M, et al. Chymase inhibition provides pancreatic islet protection in hamsters with streptozotocin-induced diabetes. J Pharmacol Sci 2009;110:459-65
    • (2009) J. Pharmacol. Sci. , vol.110 , pp. 459-465
    • Takai, S.1    Jin, D.2    Ohzu, M.3
  • 48
    • 0025937755 scopus 로고
    • Multiple determinants for the high substrate specificity of an angiotensin II-forming chymase from the human heart
    • Kinoshita A, Urata H, Bumpus FM, Husain A. Multiple determinants for the high substrate specificity of an angiotensin II-forming chymase from the human heart. J Biol Chem 1991;266:19192-7 (Pubitemid 21908216)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.29 , pp. 19192-19197
    • Kinoshita, A.1    Urata, H.2    Bumpus, F.M.3    Husain, A.4
  • 49
    • 0037967318 scopus 로고    scopus 로고
    • Chymase is upregulated in diabetic nephropathy: Implications for an alternative pathway of angiotensin II-mediated diabetic renal and vascular disease
    • DOI 10.1097/01.ASN.0000071512.93927.4E
    • Huang XR, Chen WY, Truong LD, Lan HY. Chymase is upregulated in diabetic nephropathy: implications for an alternative pathway of angiotensin II-mediated diabetic renal and vascular disease. J Am Soc Nephrol 2003;14:1738-47 (Pubitemid 36750469)
    • (2003) Journal of the American Society of Nephrology , vol.14 , Issue.7 , pp. 1738-1747
    • Huang, X.R.1    Chen, W.Y.2    Truong, L.D.3    Lan, H.Y.4
  • 50
    • 78649951030 scopus 로고    scopus 로고
    • Inhibition of chymase protects against diabetes-induced oxidative stress and renal dysfunction in hamsters
    • Maeda Y, Inoguchi T, Takei R, et al. Inhibition of chymase protects against diabetes-induced oxidative stress and renal dysfunction in hamsters. Am J Physiol Renal Physiol 2010;299:F1328-38
    • (2010) Am. J. Physiol. Renal. Physiol. , vol.299
    • Maeda, Y.1    Inoguchi, T.2    Takei, R.3
  • 51
    • 33645746010 scopus 로고    scopus 로고
    • Advanced glycation end products activate a chymase-dependent angiotensin II-generating pathway in diabetic complications
    • DOI 10.1161/CIRCULATIONAHA.105.575589, PII 0000301720060314000013
    • Koka V, Wang W, Huang XR, et al. Advanced glycation end products activate a chymase-dependent angiotensin II-generating pathway in diabetic complications. Circulation 2006;113:1353-60 (Pubitemid 43739457)
    • (2006) Circulation , vol.113 , Issue.10 , pp. 1353-1360
    • Koka, V.1    Wang, W.2    Xiao, R.H.3    Shokei, K.-M.4    Truong, L.D.5    Lan, H.Y.6
  • 52
    • 34548319203 scopus 로고    scopus 로고
    • Mechanism of high glucose-induced angiotensin II production in rat vascular smooth muscle cells
    • DOI 10.1161/CIRCRESAHA.107.151852, PII 0000301220070831000006
    • Lavrentyev EN, Estes AM, Malik KU. Mechanism of high glucose induced angiotensin II production in rat vascular smooth muscle cells. Circ Res 2007;101:455-64 (Pubitemid 47347876)
    • (2007) Circulation Research , vol.101 , Issue.5 , pp. 455-464
    • Lavrentyev, E.N.1    Estes, A.M.2    Malik, K.U.3
  • 54
    • 53849107495 scopus 로고    scopus 로고
    • Involvement of angiotensin II-dependent vascular endothelial growth factor gene expression via NADPH oxidase in the retina in a type 2 diabetic rat model
    • Fukumoto M, Takai S, Ishizaki E, et al. Involvement of angiotensin II-dependent vascular endothelial growth factor gene expression via NADPH oxidase in the retina in a type 2 diabetic rat model. Curr Eye Res 2008;33:885-91
    • (2008) Curr. Eye Res. , vol.33 , pp. 885-891
    • Fukumoto, M.1    Takai, S.2    Ishizaki, E.3
  • 55
    • 0032547763 scopus 로고    scopus 로고
    • Vascular endothelial growth factor upregulates the expression of matrix metalloproteinases in vascular smooth muscle cells: Role of flt-1
    • Wang H, Keiser JA. Vascular endothelial growth factor upregulates the expression of matrix metalloproteinases in vascular smooth muscle cells: role of flt-1. Circ Res 1998;83:832-40 (Pubitemid 28489080)
    • (1998) Circulation Research , vol.83 , Issue.8 , pp. 832-840
    • Wang, H.1    Keiser, J.A.2
  • 57
    • 0031019612 scopus 로고    scopus 로고
    • Advanced glycation end products (AGEs) co-localize with AGE receptors in the retinal vasculature of diabetic and of AGE-infused rats
    • Stitt AW, Li YM, Gardiner TA, et al. Advanced glycation end products (AGEs) co-localize with AGE receptors in the retinal vasculature of diabetic and of AGE-infused rats. Am J Pathol 1997;150:523-31 (Pubitemid 27073782)
    • (1997) American Journal of Pathology , vol.150 , Issue.2 , pp. 523-531
    • Stitt, A.W.1    Li, Y.M.2    Gardiner, T.A.3    Bucala, R.4    Archer, D.B.5    Vlassara, H.6
  • 58
    • 33749873445 scopus 로고    scopus 로고
    • Activation of nicotinamide adenine dinucleotide phosphate (reduced form) oxidase by advanced glycation end products links oxidative stress to altered retinal vascular endothelial growth factor expression
    • DOI 10.1016/j.metabol.2006.06.022, PII S0026049506002411
    • Li L, Renier G. Activation of nicotinamide adenine dinucleotide phosphate (reduced form) oxidase by advanced glycation end products links oxidative stress to altered retinal vascular endothelial growth factor expression. Metabolism 2006;55:1516-23 (Pubitemid 44559685)
    • (2006) Metabolism: Clinical and Experimental , vol.55 , Issue.11 , pp. 1516-1523
    • Li, L.1    Renier, G.2
  • 59
  • 61
    • 13244295409 scopus 로고    scopus 로고
    • An antisense oligodeoxynucleotide against vascular endothelial growth factor in a nonhuman primate model of iris neovascularization
    • DOI 10.1001/archopht.123.2.214
    • Bhisitkul RB, Robinson GS, Moulton RS, et al. An antisense oligodeoxynucleotide against vascular endothelial growth factor in a nonhuman primate model of iris neovascularization. Arch Ophthalmol 2005;123:214-19 (Pubitemid 40189709)
    • (2005) Archives of Ophthalmology , vol.123 , Issue.2 , pp. 214-219
    • Bhisitkul, R.B.1    Robinson, G.S.2    Moulton, R.S.3    Claffey, K.P.4    Gragoudas, E.S.5    Miller, J.W.6
  • 62
    • 0032955659 scopus 로고    scopus 로고
    • Retinal neovascularization is suppressed with a matrix metalloproteinase inhibitor
    • Das A, McLamore A, Song W, McGuire PG. Retinal neovascularization is suppressed with a matrix metalloproteinase inhibitor. Arch Ophthalmol 1999;117:498-503 (Pubitemid 29169645)
    • (1999) Archives of Ophthalmology , vol.117 , Issue.4 , pp. 498-503
    • Das, A.1    McLamore, A.2    Song, W.3    McGuire, P.G.4
  • 66
    • 1642542466 scopus 로고    scopus 로고
    • Hypertensive myocardial fibrosis and diastolic dysfunction: Another model of inflammation?
    • DOI 10.1161/01.HYP.0000118584.33350.7d
    • Kuwahara F, Kai H, Tokuda K, et al. Hypertensive myocardial fibrosis and diastolic dysfunction: another model of inflammation? Hypertension 2004;43:739-45 (Pubitemid 38405580)
    • (2004) Hypertension , vol.43 , Issue.4 , pp. 739-745
    • Kuwahara, F.1    Kai, H.2    Tokuda, K.3    Takeya, M.4    Takeshita, A.5    Egashira, K.6    Imaizumi, T.7
  • 67
    • 0028592529 scopus 로고
    • Chronic administration of angiotensin II receptor antagonist TCV-116 in cardiomyopathic hamsters
    • Nakamura F, Nagano M, Kobayashi R, et al. Chronic administration of angiotensin II receptor antagonist, TCV-116, in cardiomyopathic hamsters. Am J Physiol 1994;267:H2297-304
    • (1994) Am. J. Physiol. , vol.267
    • Nakamura, F.1    Nagano, M.2    Kobayashi, R.3
  • 69
    • 0025178612 scopus 로고
    • The natural history of nonalcoholic steatohepatitis: A follow-up study of forty-two patients for up to 21 years
    • Powell EE, Cooksley WG, Hanson R, et al. The natural history of nonalcoholic steatohepatitis: a follow-up study of forty-two patients for up to 21 years. Hepatology 1990;11:74-80 (Pubitemid 20075105)
    • (1990) Hepatology , vol.11 , Issue.1 , pp. 74-80
    • Powell, E.E.1    Cooksley, W.G.E.2    Hanson, R.3    Searle, J.4    Halliday, J.W.5    Powell, L.W.6
  • 71
    • 0029157084 scopus 로고
    • Intrahepatic mast cells in chronic liver diseases
    • Farrell DJ, Hines JE, Walls AF, et al. Intrahepatic mast cells in chronic liver diseases. Hepatology 1995;22:1175-81
    • (1995) Hepatology , vol.22 , pp. 1175-1181
    • Farrell, D.J.1    Hines, J.E.2    Walls, A.F.3
  • 72
    • 0030967254 scopus 로고    scopus 로고
    • Mast cells distribution in human liver disease and experimental rat liver fibrosis. Indications for mast cell participation in development of liver fibrosis
    • DOI 10.1016/S0168-8278(97)80113-4
    • Armbrust T, Batusic D, Ringe B, Ramadori G. Mast cells distribution in human liver disease and experimental rat liver fibrosis. Indications for mast cell participation in development of liver fibrosis. J Hepatol 1997;26:1042-54 (Pubitemid 27242594)
    • (1997) Journal of Hepatology , vol.26 , Issue.5 , pp. 1042-1054
    • Armbrust, T.1    Batusic, D.2    Ringe, B.3    Ramadori, G.4
  • 73
    • 0033015309 scopus 로고    scopus 로고
    • Stromal mast cells and nerve fibers in various chronic liver diseases: Relevance to hepatic fibrosis
    • DOI 10.1111/j.1572-0241.1999.01232.x, PII S0002927099002889
    • Matsunaga Y, Kawasaki H, Terada T. Stromal mast cells and nerve fibers in various chronic liver diseases: relevance to hepatic fibrosis. Am J Gastroenterol 1999;94:1923-32 (Pubitemid 29315912)
    • (1999) American Journal of Gastroenterology , vol.94 , Issue.7 , pp. 1923-1932
    • Matsunaga, Y.1    Kawasaki, H.2    Terada, T.3
  • 75
    • 77954373221 scopus 로고    scopus 로고
    • Chymase inhibitor prevents the nonalcoholic steatohepatitis in hamsters fed a methionine-and choline-deficient diet
    • Tashiro K, Takai S, Jin D, et al. Chymase inhibitor prevents the nonalcoholic steatohepatitis in hamsters fed a methionine- and choline-deficient diet. Hepatol Res 2010;40:514-23
    • (2010) Hepatol. Res. , vol.40 , pp. 514-523
    • Tashiro, K.1    Takai, S.2    Jin, D.3
  • 77
    • 0027425864 scopus 로고
    • Effect of antibody to transforming growth factor β on bleomycin induced accumulation of lung collagen in mice
    • Giri SN, Hyde DM, Hollinger MA. Effect of antibody to transforming growth factor beta on bleomycin induced accumulation of lung collagen in mice. Thorax 1993;48:959-66 (Pubitemid 23319618)
    • (1993) Thorax , vol.48 , Issue.10 , pp. 959-966
    • Giri, S.N.1    Hyde, D.M.2    Hollinger, M.A.3
  • 78
    • 0036857328 scopus 로고    scopus 로고
    • Development of the chymase inhibitor as an anti-tissue-remodeling drug: Myocardial infarction and some other possibilities
    • DOI 10.1254/jjp.90.218
    • Sukenaga Y, Kamoshita K, Takai S, Miyazaki M. Development of the chymase inhibitor as an anti-tissue-remodeling drug: myocardial infarction and some other possibilities. Jpn J Pharmacol 2002;90:218-22 (Pubitemid 35422939)
    • (2002) Japanese Journal of Pharmacology , vol.90 , Issue.3 , pp. 218-222
    • Sukenaga, Y.1    Kamoshita, K.2    Takai, S.3    Miyazaki, M.4
  • 81
    • 79951907179 scopus 로고    scopus 로고
    • The specific chymase inhibitor TY-51469 suppresses the accumulation of neutrophils in the lung and reduces silica-induced pulmonary fibrosis in mice
    • published online 4 December 2010:10.3109/01902148.2010.520815
    • Takato H, Yasui M, Ichikawa Y, et al. The specific chymase inhibitor TY-51469 suppresses the accumulation of neutrophils in the lung and reduces silica-induced pulmonary fibrosis in mice. Exp Lung Res 2011: published online 4 December 2010 doi:10.3109/01902148.2010.520815
    • (2011) Exp. Lung. Res.
    • Takato, H.1    Yasui, M.2    Ichikawa, Y.3
  • 85
    • 77955259493 scopus 로고    scopus 로고
    • Chymase inhibition attenuates tetrachloride-induced liver fibrosis in hamsters
    • Komeda K, Takai S, Jin D, et al. Chymase inhibition attenuates tetrachloride-induced liver fibrosis in hamsters. Hepatol Res 2010;40:832-40
    • (2010) Hepatol. Res. , vol.40 , pp. 832-840
    • Komeda, K.1    Takai, S.2    Jin, D.3
  • 90
    • 0026788165 scopus 로고
    • Gastrointestinal damage associated with the use of nonsteroidal antiinflammatory drugs
    • Allison MC, Howatson AG, Torrance CJ, et al. Gastrointestinal damage associated with the use of nonsteroidal antiinflammatory drugs. N Engl J Med 1992;327:749-54
    • (1992) N. Engl. J. Med. , vol.327 , pp. 749-754
    • Allison, M.C.1    Howatson, A.G.2    Torrance, C.J.3
  • 91
    • 19044396444 scopus 로고    scopus 로고
    • A quantitative analysis of NSAID-induced small bowel pathology by capsule enteroscopy
    • Maiden L, Thjodleifsson B, Theodors A, et al. A quantitative analysis of NSAID-induced small bowel pathology by capsule enteroscopy. Gastroenterology 2005;128:1172-8
    • (2005) Gastroenterology , vol.128 , pp. 1172-1178
    • Maiden, L.1    Thjodleifsson, B.2    Theodors, A.3
  • 92
    • 76749123383 scopus 로고    scopus 로고
    • Significance of chymase-dependent matrix metalloproteinase-9 activation on indomethacin-induced small intestinal damages in rats
    • Kakimoto K, Takai S, Murano M, et al. Significance of chymase-dependent matrix metalloproteinase-9 activation on indomethacin-induced small intestinal damages in rats. J Pharmacol Exp Ther 2010;332:684-9
    • (2010) J. Pharmacol. Exp. Ther. , vol.332 , pp. 684-689
    • Kakimoto, K.1    Takai, S.2    Murano, M.3
  • 93
    • 33646507490 scopus 로고    scopus 로고
    • Mast cell chymase induces expression of chemokines for neutrophils in eosinophilic EoL-1 cells and mouse peritonitis eosinophils
    • Terakawa M, Tomimori Y, Goto M, Fukuda Y. Mast cell chymase induces expression of chemokines for neutrophils in eosinophilic EoL-1 cells and mouse peritonitis eosinophils. Eur J Pharmacol 2006;538:175-81
    • (2006) Eur. J. Pharmacol. , vol.538 , pp. 175-181
    • Terakawa, M.1    Tomimori, Y.2    Goto, M.3    Fukuda, Y.4
  • 94
    • 0033850005 scopus 로고    scopus 로고
    • Chymase is a potent chemoattractant for human monocytes and neutrophils
    • Tani K, Ogushi F, Kido H, et al. Chymase is a potent chemoattractant for human monocytes and neutrophils. J Leukoc Biol 2000;67:585-9
    • (2000) J. Leukoc. Biol. , vol.67 , pp. 585-589
    • Tani, K.1    Ogushi, F.2    Kido, H.3
  • 95
    • 0029779005 scopus 로고    scopus 로고
    • Basic science of abdominal aortic aneurysms: Emerging therapeutic strategies for an unresolved clinical problem
    • Thompson RW. Basic science of abdominal aortic aneurysms: emerging therapeutic strategies for an unresolved clinical problem. Curr Opin Cardiol 1996;11:504-18 (Pubitemid 26320991)
    • (1996) Current Opinion in Cardiology , vol.11 , Issue.5 , pp. 504-518
    • Thompson, R.W.1
  • 96
    • 0037015537 scopus 로고    scopus 로고
    • Small abdominal aortic aneurysms
    • Ballotta E, Toniato A. Small abdominal aortic aneurysms. N Engl J Med 2002;347:1112-15
    • (2002) N. Engl. J. Med. , vol.347 , pp. 1112-1115
    • Ballotta, E.1    Toniato, A.2
  • 97
    • 0034008405 scopus 로고    scopus 로고
    • Chymase as a proangiogenic factor. A possible involvement of chymase- angiotensin-dependent pathway in the hamster sponge angiogenesis model
    • DOI 10.1074/jbc.275.8.5545
    • Muramatsu M, Katada J, Hayashi I, Majima M. Chymase as a proangiogenic factor. A possible involvement of chymase-angiotensin-dependent pathway in the hamster sponge angiogenesis model. J Biol Chem 2000;275:5545-52 (Pubitemid 30115190)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.8 , pp. 5545-5552
    • Muramatsu, M.1    Katada, J.2    Hayashi, I.3    Majima, M.4
  • 98
    • 0036800652 scopus 로고    scopus 로고
    • Suppression of basic fibroblast growth factor-induced angiogenesis by a specific chymase inhibitor, BCEAB, through the chymase-angiotensin-dependent pathway in hamster sponge granulomas
    • DOI 10.1038/sj.bjp.0704893
    • Muramatsu M, Yamada M, Takai S, Miyazaki M. Suppression of basic fibroblast growth factor-induced angiogenesis by a specific chymase inhibitor, BCEAB, through the chymase-angiotensin-dependent pathway in hamster sponge granulomas. Br J Pharmacol 2002;137:554-60 (Pubitemid 35221910)
    • (2002) British Journal of Pharmacology , vol.137 , Issue.4 , pp. 554-560
    • Muramatsu, M.1    Yamada, M.2    Takai, S.3    Miyazaki, M.4
  • 99
    • 53749108177 scopus 로고    scopus 로고
    • Effect of candesartan on progression and regression of retinopathy in type 2 diabetes direct-protect 2: A randomised placebo-controlled trial
    • Sjolie AK, Klein R, Porta M, et al. Effect of candesartan on progression and regression of retinopathy in type 2 diabetes (DIRECT-Protect 2): a randomised placebo-controlled trial. Lancet 2008;372:1385-93
    • (2008) Lancet , vol.372 , pp. 1385-1393
    • Sjolie, A.K.1    Klein, R.2    Porta, M.3


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