메뉴 건너뛰기




Volumn 117, Issue 6, 2007, Pages 1514-1526

Strain-dependent embryonic lethality and exaggerated vascular remodeling in heparin cofactor II-deficient mice

(26)  Aihara, Ken Ichi a,b,c   Azuma, Hiroyuki a   Akaike, Masashi a   Ikeda, Yasumasa a,b   Sata, Masataka c   Takamori, Nobuyuki a   Yagi, Shusuke a   Iwase, Takashi a   Sumitomo, Yuka a   Kawano, Hirotaka c   Yamada, Takashi c   Fukuda, Toru c   Matsumoto, Takahiro c,d   Sekine, Keisuke c   Sato, Takashi c   Nakamichi, Yuko c   Yamamoto, Yoko c   Yoshimura, Kimihiro c   Watanabe, Tomoyuki c   Nakamura, Takashi c   more..


Author keywords

[No Author keywords available]

Indexed keywords

APOLIPOPROTEIN E; CHEMOKINE; CYTOKINE; HEPARIN COFACTOR II; PROTEINASE ACTIVATED RECEPTOR 1; THROMBIN;

EID: 34249905656     PISSN: 00219738     EISSN: 15588238     Source Type: Journal    
DOI: 10.1172/JCI27095     Document Type: Article
Times cited : (42)

References (63)
  • 1
    • 0032723681 scopus 로고    scopus 로고
    • Multifunctional roles of thrombin
    • Narayanan, S. 1999. Multifunctional roles of thrombin. Ann. Clin. Lab Sci. 29:275-280.
    • (1999) Ann. Clin. Lab Sci , vol.29 , pp. 275-280
    • Narayanan, S.1
  • 2
    • 0020570701 scopus 로고    scopus 로고
    • Bar-Shavit, R., Kahn, A., Wilner, G.D., and Fenton, J.W., 2nd. 1983. Monocyte chemotaxis: stimulation by specific exosite region in thrombin. Science. 220:728-731.
    • Bar-Shavit, R., Kahn, A., Wilner, G.D., and Fenton, J.W., 2nd. 1983. Monocyte chemotaxis: stimulation by specific exosite region in thrombin. Science. 220:728-731.
  • 3
    • 0016432831 scopus 로고
    • Mitogenic activity of blood components. I. Thrombin and prothrombin
    • Chen, L.B., and Buchanan, J.M. 1975. Mitogenic activity of blood components. I. Thrombin and prothrombin. Proc. Natl. Acad. Sci. U. S. A. 72:131-135.
    • (1975) Proc. Natl. Acad. Sci. U. S. A , vol.72 , pp. 131-135
    • Chen, L.B.1    Buchanan, J.M.2
  • 4
    • 0027492461 scopus 로고
    • Thrombin stimulates proliferation of cultured rat aortic smooth muscle cells by a proteolytically activated receptor
    • McNamara, C.A., et al. 1993. Thrombin stimulates proliferation of cultured rat aortic smooth muscle cells by a proteolytically activated receptor. J. Clin. Invest. 91:94-98.
    • (1993) J. Clin. Invest , vol.91 , pp. 94-98
    • McNamara, C.A.1
  • 5
    • 0036371260 scopus 로고    scopus 로고
    • Thrombin regulation of cell function through protease-activated receptors: Implications for therapeutic intervention
    • Derian, C.K., Damiano, B.P., D'Andrea, M.R., and Andrade-Gordon, P. 2002. Thrombin regulation of cell function through protease-activated receptors: implications for therapeutic intervention. Biochemistry Mosc. 67:56-64.
    • (2002) Biochemistry Mosc , vol.67 , pp. 56-64
    • Derian, C.K.1    Damiano, B.P.2    D'Andrea, M.R.3    Andrade-Gordon, P.4
  • 6
    • 0035979691 scopus 로고    scopus 로고
    • A role for thrombin receptor signaling in endothelial cells during embryonic development
    • Griffin, C.T., Srinivasan, Y., Zheng, Y.W., Huang, W., and Coughlin, S.R. 2001. A role for thrombin receptor signaling in endothelial cells during embryonic development. Science. 293:1666-1670.
    • (2001) Science , vol.293 , pp. 1666-1670
    • Griffin, C.T.1    Srinivasan, Y.2    Zheng, Y.W.3    Huang, W.4    Coughlin, S.R.5
  • 8
    • 0026497368 scopus 로고
    • Thrombin receptor expression in normal and atherosclerotic human arteries
    • Nelken, N.A., et al. 1992. Thrombin receptor expression in normal and atherosclerotic human arteries. J. Clin. Invest. 90:1614-1621.
    • (1992) J. Clin. Invest , vol.90 , pp. 1614-1621
    • Nelken, N.A.1
  • 9
    • 0035817822 scopus 로고    scopus 로고
    • Role of thrombin signalling in platelets in haemostasis and thrombosis
    • Sambrano, G.R., Weiss, E.J., Zheng, Y.W., Huang, W., and Coughlin, S.R. 2001. Role of thrombin signalling in platelets in haemostasis and thrombosis. Nature. 413:74-78.
    • (2001) Nature , vol.413 , pp. 74-78
    • Sambrano, G.R.1    Weiss, E.J.2    Zheng, Y.W.3    Huang, W.4    Coughlin, S.R.5
  • 10
    • 0037783288 scopus 로고    scopus 로고
    • Extracellular mediators in atherosclerosis and thrombosis: Lessons from thrombin receptor knockout mice
    • Major, C.D., Santulli, R.J., Derian, C.K., and Andrade-Gordon, P. 2003. Extracellular mediators in atherosclerosis and thrombosis: lessons from thrombin receptor knockout mice. Arterioscler. Thromb. Vasc. Biol. 23:931-939.
    • (2003) Arterioscler. Thromb. Vasc. Biol , vol.23 , pp. 931-939
    • Major, C.D.1    Santulli, R.J.2    Derian, C.K.3    Andrade-Gordon, P.4
  • 11
    • 2142651737 scopus 로고    scopus 로고
    • Role of protease-activated receptors in the vascular system
    • Hirano, K., and Kanaide, H. 2003. Role of protease-activated receptors in the vascular system. J. Atheroscler. Thromb. 10:211-225.
    • (2003) J. Atheroscler. Thromb , vol.10 , pp. 211-225
    • Hirano, K.1    Kanaide, H.2
  • 12
    • 0035816731 scopus 로고    scopus 로고
    • Role for tissue factor pathway in murine model of vascular remodeling
    • Singh, R., et al. 2001. Role for tissue factor pathway in murine model of vascular remodeling. Circ. Res. 89:71-76.
    • (2001) Circ. Res , vol.89 , pp. 71-76
    • Singh, R.1
  • 13
    • 33645536018 scopus 로고    scopus 로고
    • Thrombomodulin plays an important role in arterial remodeling and neointima formation in mouse carotid ligation model
    • Li, Y.H., et al. 2006. Thrombomodulin plays an important role in arterial remodeling and neointima formation in mouse carotid ligation model. Thromb. Haemost. 95:128-133.
    • (2006) Thromb. Haemost , vol.95 , pp. 128-133
    • Li, Y.H.1
  • 14
    • 0036077426 scopus 로고    scopus 로고
    • Endogenous vitronectin and plasminogen activator inhibitor-1 promote neointima formation in murine carotid arteries
    • Peng, L., Bhatia, N., Parker, A.C., Zhu, Y., and Fay, W.P. 2002. Endogenous vitronectin and plasminogen activator inhibitor-1 promote neointima formation in murine carotid arteries. Arterioscler. Thromb. Vasc. Biol. 22:934-939.
    • (2002) Arterioscler. Thromb. Vasc. Biol , vol.22 , pp. 934-939
    • Peng, L.1    Bhatia, N.2    Parker, A.C.3    Zhu, Y.4    Fay, W.P.5
  • 15
    • 0029816753 scopus 로고    scopus 로고
    • Comparison of the effects of the thrombin inhibitor r-hirudin in four animal models of neointima formation after arterial injury
    • Gerdes, C., Faber-Steinfeld, V., Yalkinoglu, O., and Wohlfeil, S. 1996. Comparison of the effects of the thrombin inhibitor r-hirudin in four animal models of neointima formation after arterial injury. Arterioscler. Thromb. Vasc. Biol. 16:1306-1311.
    • (1996) Arterioscler. Thromb. Vasc. Biol , vol.16 , pp. 1306-1311
    • Gerdes, C.1    Faber-Steinfeld, V.2    Yalkinoglu, O.3    Wohlfeil, S.4
  • 16
    • 0025051257 scopus 로고
    • Localization of anticoagulantly active heparan sulfate proteoglycans in vascular endothelium: Antithrombin binding on cultured endothelial cells and perfused rat aorta
    • de Agostini, A.I., Watkins, S.C., Slayter, H.S., Youssoufian, H., and Rosenberg, R.D. 1990. Localization of anticoagulantly active heparan sulfate proteoglycans in vascular endothelium: antithrombin binding on cultured endothelial cells and perfused rat aorta. J. Cell Biol. 111:1293-1304.
    • (1990) J. Cell Biol , vol.111 , pp. 1293-1304
    • de Agostini, A.I.1    Watkins, S.C.2    Slayter, H.S.3    Youssoufian, H.4    Rosenberg, R.D.5
  • 17
    • 0020617887 scopus 로고
    • Activation of heparin cofactor II by dermatan sulfate
    • Tollefsen, D.M., Pestka, C.A., and Monafo, W.J. 1983. Activation of heparin cofactor II by dermatan sulfate. J. Biol. Chem. 258:6713-6716.
    • (1983) J. Biol. Chem , vol.258 , pp. 6713-6716
    • Tollefsen, D.M.1    Pestka, C.A.2    Monafo, W.J.3
  • 18
    • 0028784386 scopus 로고
    • Insight into the mechanism of action of heparin cofactor II
    • Tollefsen, D.M. 1995. Insight into the mechanism of action of heparin cofactor II. Thromb. Haemost. 74:1209-1214.
    • (1995) Thromb. Haemost , vol.74 , pp. 1209-1214
    • Tollefsen, D.M.1
  • 19
    • 0021792469 scopus 로고
    • Isolation of dermatan sulfate proteoglycans from mature bovine articular cartilages
    • Rosenberg, L.C., et al. 1985. Isolation of dermatan sulfate proteoglycans from mature bovine articular cartilages. J. Biol. Chem. 260:6304-6313.
    • (1985) J. Biol. Chem , vol.260 , pp. 6304-6313
    • Rosenberg, L.C.1
  • 20
    • 0024596126 scopus 로고
    • Characterization of the dermatan sulfate proteoglycans, DS-PGI and DS-PGII, from bovine articular cartilage and skin isolated by octyl-sepharose chromatography
    • Choi, H.U., et al. 1989. Characterization of the dermatan sulfate proteoglycans, DS-PGI and DS-PGII, from bovine articular cartilage and skin isolated by octyl-sepharose chromatography. J. Biol. Chem. 264:2876-2884.
    • (1989) J. Biol. Chem , vol.264 , pp. 2876-2884
    • Choi, H.U.1
  • 21
    • 0034674479 scopus 로고    scopus 로고
    • Altered dermatan sulfate structure and reduced heparin cofactor II-stimulating activity of biglycan and decorin from human atherosclerotic plaque
    • Shirk, R.A., Parthasarathy, N., San Antonio, J.D., Church, F.C., and Wagner, W.D. 2000. Altered dermatan sulfate structure and reduced heparin cofactor II-stimulating activity of biglycan and decorin from human atherosclerotic plaque. J. Biol. Chem. 275:18085-18092.
    • (2000) J. Biol. Chem , vol.275 , pp. 18085-18092
    • Shirk, R.A.1    Parthasarathy, N.2    San Antonio, J.D.3    Church, F.C.4    Wagner, W.D.5
  • 22
    • 0035171975 scopus 로고    scopus 로고
    • Molecular mechanism of type I congenital heparin cofactor (HC) II deficiency caused by a missense mutation at reactive P2 site: HC II Tokushima
    • Kanagawa, Y., et al. 2001. Molecular mechanism of type I congenital heparin cofactor (HC) II deficiency caused by a missense mutation at reactive P2 site: HC II Tokushima. Thromb. Haemost. 85:101-107.
    • (2001) Thromb. Haemost , vol.85 , pp. 101-107
    • Kanagawa, Y.1
  • 23
    • 0842264178 scopus 로고    scopus 로고
    • High plasma heparin cofactor II activity is associated with reduced incidence of in-stent restenosis after percutaneous coronary intervention
    • Takamori, N., et al. 2004. High plasma heparin cofactor II activity is associated with reduced incidence of in-stent restenosis after percutaneous coronary intervention. Circulation. 109:481-486.
    • (2004) Circulation , vol.109 , pp. 481-486
    • Takamori, N.1
  • 24
    • 2942532696 scopus 로고    scopus 로고
    • Heparin cofactor II is a novel protective factor against carotid atherosclerosis in elderly individuals
    • Aihara, K., et al. 2004. Heparin cofactor II is a novel protective factor against carotid atherosclerosis in elderly individuals. Circulation. 109:2761-2765.
    • (2004) Circulation , vol.109 , pp. 2761-2765
    • Aihara, K.1
  • 25
    • 0036155992 scopus 로고    scopus 로고
    • Heparin cofactor II inhibits arterial thrombosis after endothelial injury
    • doi:10.1172/JCI200213432
    • He, L., Vicente, C.P., Westrick, R.J., Eitzman, D.T., and Tollefsen, D.M. 2002. Heparin cofactor II inhibits arterial thrombosis after endothelial injury. J. Clin. Invest. 109:213-219. doi:10.1172/JCI200213432.
    • (2002) J. Clin. Invest , vol.109 , pp. 213-219
    • He, L.1    Vicente, C.P.2    Westrick, R.J.3    Eitzman, D.T.4    Tollefsen, D.M.5
  • 26
    • 0027967395 scopus 로고
    • Characterization of thrombin receptor expression during vascular lesion formation
    • Wilcox, J.N., et al. 1994. Characterization of thrombin receptor expression during vascular lesion formation. Circ. Res. 75:1029-1038.
    • (1994) Circ. Res , vol.75 , pp. 1029-1038
    • Wilcox, J.N.1
  • 27
    • 0032543264 scopus 로고    scopus 로고
    • Antibody to thrombin receptor inhibits neointimal smooth muscle cell accumulation without causing inhibition of platelet aggregation or altering hemostatic parameters after angioplasty in rat
    • Takada, M., et al. 1998. Antibody to thrombin receptor inhibits neointimal smooth muscle cell accumulation without causing inhibition of platelet aggregation or altering hemostatic parameters after angioplasty in rat. Circ. Res. 82:980-987.
    • (1998) Circ. Res , vol.82 , pp. 980-987
    • Takada, M.1
  • 28
    • 0034967927 scopus 로고    scopus 로고
    • Administration of a potent antagonist of protease-activated receptor-1 (PAR-1) attenuates vascular restenosis following balloon angioplasty in rats
    • Andrade-Gordon, P., et al. 2001. Administration of a potent antagonist of protease-activated receptor-1 (PAR-1) attenuates vascular restenosis following balloon angioplasty in rats. J. Pharmacol. Exp. Ther. 298:34-42.
    • (2001) J. Pharmacol. Exp. Ther , vol.298 , pp. 34-42
    • Andrade-Gordon, P.1
  • 29
    • 0036105149 scopus 로고    scopus 로고
    • Hematopoietic stem cells differentiate into vascular cells that participate in the pathogenesis of atherosclerosis
    • Sata, M., et al. 2002. Hematopoietic stem cells differentiate into vascular cells that participate in the pathogenesis of atherosclerosis. Nat. Med. 8:403-409.
    • (2002) Nat. Med , vol.8 , pp. 403-409
    • Sata, M.1
  • 30
    • 33750475625 scopus 로고    scopus 로고
    • Free radicals, mitochondria, and oxidized lipids: The emerging role in signal transduction in vascular cells
    • Gutierrez, J., Ballinger, S.W., Darley-Usmar, V.M., and Landar, A. 2006. Free radicals, mitochondria, and oxidized lipids: the emerging role in signal transduction in vascular cells. Circ. Res. 99:924-932.
    • (2006) Circ. Res , vol.99 , pp. 924-932
    • Gutierrez, J.1    Ballinger, S.W.2    Darley-Usmar, V.M.3    Landar, A.4
  • 31
    • 0033580382 scopus 로고    scopus 로고
    • Rapid changes in the exon/intron structure of a mammalian thrombin inhibitor gene
    • Kamp, P.B., and Ragg, H. 1999. Rapid changes in the exon/intron structure of a mammalian thrombin inhibitor gene. Gene. 229:137-144.
    • (1999) Gene , vol.229 , pp. 137-144
    • Kamp, P.B.1    Ragg, H.2
  • 32
    • 0032849534 scopus 로고    scopus 로고
    • Hereditary homozygous heparin cofactor II deficiency and the risk of developing venous thrombosis
    • Villa, P., et al. 1999. Hereditary homozygous heparin cofactor II deficiency and the risk of developing venous thrombosis. Thromb. Haemost. 82:1011-1014.
    • (1999) Thromb. Haemost , vol.82 , pp. 1011-1014
    • Villa, P.1
  • 33
    • 4444233600 scopus 로고    scopus 로고
    • Homozygous deficiency of heparin cofactor II: Relevance of P17 glutamate residue in serpins, relationship with conformational diseases, and role in thrombosis
    • Corral, J., et al. 2004. Homozygous deficiency of heparin cofactor II: relevance of P17 glutamate residue in serpins, relationship with conformational diseases, and role in thrombosis. Circulation. 110:1303-1307.
    • (2004) Circulation , vol.110 , pp. 1303-1307
    • Corral, J.1
  • 34
    • 0032524695 scopus 로고    scopus 로고
    • Anticoagulant dermatan sulfate proteoglycan (decorin) in the term human placenta
    • Delorme, M.A., Xu, L., Berry, L., Mitchell, L., and Andrew, M. 1998. Anticoagulant dermatan sulfate proteoglycan (decorin) in the term human placenta. Thromb. Res. 90:147-153.
    • (1998) Thromb. Res , vol.90 , pp. 147-153
    • Delorme, M.A.1    Xu, L.2    Berry, L.3    Mitchell, L.4    Andrew, M.5
  • 35
    • 0031966558 scopus 로고    scopus 로고
    • Heparin cofactor II: A new marker for pre-eclampsia
    • Bellart, J., et al. 1998. Heparin cofactor II: a new marker for pre-eclampsia. Blood Coagul. Fibrinolysis. 9:205-208.
    • (1998) Blood Coagul. Fibrinolysis , vol.9 , pp. 205-208
    • Bellart, J.1
  • 36
    • 33645513210 scopus 로고    scopus 로고
    • Placental dermatan sulfate: Isolation, anticoagulant activity, and association with heparin cofactor II
    • Giri, T.K., and Tollefsen, D.M. 2006. Placental dermatan sulfate: isolation, anticoagulant activity, and association with heparin cofactor II. Blood. 107:2753-2758.
    • (2006) Blood , vol.107 , pp. 2753-2758
    • Giri, T.K.1    Tollefsen, D.M.2
  • 37
    • 0036880595 scopus 로고    scopus 로고
    • Heparin cofactor II deficiency
    • Tollefsen, D.M. 2002. Heparin cofactor II deficiency. Arch. Pathol. Lab. Med. 126:1394-1400.
    • (2002) Arch. Pathol. Lab. Med , vol.126 , pp. 1394-1400
    • Tollefsen, D.M.1
  • 38
    • 2942612188 scopus 로고    scopus 로고
    • Does heparin cofactor II modulate atherosclerosis and restenosis?
    • Tollefsen, D.M. 2004. Does heparin cofactor II modulate atherosclerosis and restenosis? Circulation. 109:2682-2684.
    • (2004) Circulation , vol.109 , pp. 2682-2684
    • Tollefsen, D.M.1
  • 39
    • 20844443466 scopus 로고    scopus 로고
    • High plasma heparin cofactor II activity protects from restenosis after femoropopliteal stenting
    • Schillinger, M., et al. 2004. High plasma heparin cofactor II activity protects from restenosis after femoropopliteal stenting. Thromb. Haemost. 92:1108-1113.
    • (2004) Thromb. Haemost , vol.92 , pp. 1108-1113
    • Schillinger, M.1
  • 40
    • 0026035523 scopus 로고
    • Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation
    • Vu, T.K., Hung, D.T., Wheaton, V.I., and Coughlin, S.R. 1991. Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation. Cell. 64:1057-1068.
    • (1991) Cell , vol.64 , pp. 1057-1068
    • Vu, T.K.1    Hung, D.T.2    Wheaton, V.I.3    Coughlin, S.R.4
  • 41
    • 0030979972 scopus 로고    scopus 로고
    • Protease-activated receptor 3 is a second thrombin receptor in humans
    • Ishihara, H., et al. 1997. Protease-activated receptor 3 is a second thrombin receptor in humans. Nature. 386:502-506.
    • (1997) Nature , vol.386 , pp. 502-506
    • Ishihara, H.1
  • 42
    • 0032499696 scopus 로고    scopus 로고
    • Cloning and characterization of human protease-activated receptor 4
    • Xu, W.F., et al. 1998. Cloning and characterization of human protease-activated receptor 4. Proc. Natl. Acad. Sci. U. S. A. 95:6642-6646.
    • (1998) Proc. Natl. Acad. Sci. U. S. A , vol.95 , pp. 6642-6646
    • Xu, W.F.1
  • 43
    • 0033538516 scopus 로고    scopus 로고
    • Stimulation of a vascular smooth muscle cell NAD(P)H oxidase by thrombin. Evidence that p47(phox) may participate in forming this oxidase in vitro and in vivo
    • Patterson, C., et al. 1999. Stimulation of a vascular smooth muscle cell NAD(P)H oxidase by thrombin. Evidence that p47(phox) may participate in forming this oxidase in vitro and in vivo. J. Biol. Chem. 274:19814-19822.
    • (1999) J. Biol. Chem , vol.274 , pp. 19814-19822
    • Patterson, C.1
  • 44
    • 0034698062 scopus 로고    scopus 로고
    • Heparin blockade of thrombin-induced smooth muscle cell migration involves inhibition of epidermal growth factor (EGF) receptor transactivation by heparin-binding EGF-like growth factor
    • Kalmes, A., Vesti, B.R., Daum, G., Abraham, J.A., and Clowes, A.W. 2000. Heparin blockade of thrombin-induced smooth muscle cell migration involves inhibition of epidermal growth factor (EGF) receptor transactivation by heparin-binding EGF-like growth factor. Circ. Res. 87:92-98.
    • (2000) Circ. Res , vol.87 , pp. 92-98
    • Kalmes, A.1    Vesti, B.R.2    Daum, G.3    Abraham, J.A.4    Clowes, A.W.5
  • 45
    • 0042942985 scopus 로고    scopus 로고
    • Synergistic effect of sphingosine 1-phosphate on thrombin-induced tissue factor expression in endothelial cells
    • Takeya, H., Gabazza, E.C., Aoki, S., Ueno, H., and Suzuki, K. 2003. Synergistic effect of sphingosine 1-phosphate on thrombin-induced tissue factor expression in endothelial cells. Blood. 102:1693-1700.
    • (2003) Blood , vol.102 , pp. 1693-1700
    • Takeya, H.1    Gabazza, E.C.2    Aoki, S.3    Ueno, H.4    Suzuki, K.5
  • 46
    • 0033966202 scopus 로고    scopus 로고
    • Regulation of vascular smooth muscle cell proliferation by nuclear factor-kappaB and its inhibitor, I-kappaB
    • Hoshi, S., Goto, M., Koyama, N., Nomoto, K., and Tanaka, H. 2000. Regulation of vascular smooth muscle cell proliferation by nuclear factor-kappaB and its inhibitor, I-kappaB. J. Biol. Chem. 275:883-889.
    • (2000) J. Biol. Chem , vol.275 , pp. 883-889
    • Hoshi, S.1    Goto, M.2    Koyama, N.3    Nomoto, K.4    Tanaka, H.5
  • 47
    • 0029979369 scopus 로고    scopus 로고
    • Biologic basis for interleukin-1 in disease
    • Dinarello, C.A. 1996. Biologic basis for interleukin-1 in disease. Blood. 87:2095-2147.
    • (1996) Blood , vol.87 , pp. 2095-2147
    • Dinarello, C.A.1
  • 48
    • 0036347210 scopus 로고    scopus 로고
    • Kruppel-like zinc-finger transcription factor KLF5/BTEB2 is a target for angiotensin II signaling and an essential regulator of cardiovascular remodeling
    • Shindo, T., et al. 2002. Kruppel-like zinc-finger transcription factor KLF5/BTEB2 is a target for angiotensin II signaling and an essential regulator of cardiovascular remodeling. Nat. Med. 8:856-863.
    • (2002) Nat. Med , vol.8 , pp. 856-863
    • Shindo, T.1
  • 49
    • 0025216647 scopus 로고
    • Proliferating or interleukin 1-activated human vascular smooth muscle cells secrete copious interleukin 6
    • Loppnow, H., and Libby, P. 1990. Proliferating or interleukin 1-activated human vascular smooth muscle cells secrete copious interleukin 6. J. Clin. Invest. 85:731-738.
    • (1990) J. Clin. Invest , vol.85 , pp. 731-738
    • Loppnow, H.1    Libby, P.2
  • 50
    • 3943107538 scopus 로고    scopus 로고
    • Rat aortic MCP-1 and its receptor CCR2 increase with age and alter vascular smooth muscle cell function
    • Spinetti, G., et al. 2004. Rat aortic MCP-1 and its receptor CCR2 increase with age and alter vascular smooth muscle cell function. Arterioscler. Thromb. Vasc. Biol. 24:1397-1402.
    • (2004) Arterioscler. Thromb. Vasc. Biol , vol.24 , pp. 1397-1402
    • Spinetti, G.1
  • 51
    • 0043075883 scopus 로고    scopus 로고
    • Deficiency of interleukin-1 receptor antagonist promotes neointimal formation after injury
    • Isoda, K., et al. 2003. Deficiency of interleukin-1 receptor antagonist promotes neointimal formation after injury. Circulation. 108:516-518.
    • (2003) Circulation , vol.108 , pp. 516-518
    • Isoda, K.1
  • 52
    • 0030763857 scopus 로고    scopus 로고
    • Mice lacking the vitamin D receptor exhibit impaired bone formation, uterine hypoplasia and growth retardation after weaning
    • Yoshizawa, T., et al. 1997. Mice lacking the vitamin D receptor exhibit impaired bone formation, uterine hypoplasia and growth retardation after weaning. Nat. Genet. 16:391-396.
    • (1997) Nat. Genet , vol.16 , pp. 391-396
    • Yoshizawa, T.1
  • 53
    • 0032947346 scopus 로고    scopus 로고
    • Fgf10 is essential for limb and lung formation
    • Sekine, K., et al. 1999. Fgf10 is essential for limb and lung formation. Nat. Genet. 21:138-141.
    • (1999) Nat. Genet , vol.21 , pp. 138-141
    • Sekine, K.1
  • 54
    • 0041923632 scopus 로고    scopus 로고
    • Suppressive function of androgen receptor in bone resorption
    • Kawano, H., et al. 2003. Suppressive function of androgen receptor in bone resorption. Proc. Natl. Acad. Sci. U. S. A. 100:9416-9421.
    • (2003) Proc. Natl. Acad. Sci. U. S. A , vol.100 , pp. 9416-9421
    • Kawano, H.1
  • 55
    • 0037221067 scopus 로고    scopus 로고
    • Chondromodulin I is a bone remodeling factor
    • Nakamichi, Y., et al. 2003. Chondromodulin I is a bone remodeling factor. Mol. Cell. Biol. 23:636-644.
    • (2003) Mol. Cell. Biol , vol.23 , pp. 636-644
    • Nakamichi, Y.1
  • 56
    • 0026620047 scopus 로고
    • Location of the mouse complement factor H gene (cfh) by FISH analysis and replication R-banding
    • Matsuda, Y., et al. 1992. Location of the mouse complement factor H gene (cfh) by FISH analysis and replication R-banding. Cytogenet. Cell Genet. 61:282-285.
    • (1992) Cytogenet. Cell Genet , vol.61 , pp. 282-285
    • Matsuda, Y.1
  • 57
    • 4143096123 scopus 로고    scopus 로고
    • Disruption of nuclear vitamin D receptor gene causes enhanced thrombogenicity in mice
    • Aihara, K., et al. 2004. Disruption of nuclear vitamin D receptor gene causes enhanced thrombogenicity in mice. J. Biol. Chem. 279:35798-35802.
    • (2004) J. Biol. Chem , vol.279 , pp. 35798-35802
    • Aihara, K.1
  • 58
    • 33644791267 scopus 로고    scopus 로고
    • Heparin cofactor II levels do not predict the development of coronary heart disease: The Atherosclerosis Risk in Communities (ARIC) study
    • Giri, T.K., Ahn, C.W., Wu, K.K., and Tollefsen, D.M. 2005. Heparin cofactor II levels do not predict the development of coronary heart disease: the Atherosclerosis Risk in Communities (ARIC) study. Arterioscler. Thromb. Vasc. Biol. 25:2689-2690.
    • (2005) Arterioscler. Thromb. Vasc. Biol , vol.25 , pp. 2689-2690
    • Giri, T.K.1    Ahn, C.W.2    Wu, K.K.3    Tollefsen, D.M.4
  • 59
    • 0033750522 scopus 로고    scopus 로고
    • A mouse model of vascular injury that induces rapid onset of medial cell apoptosis followed by reproducible neointimal hyperplasia
    • Sata, M., et al. 2000. A mouse model of vascular injury that induces rapid onset of medial cell apoptosis followed by reproducible neointimal hyperplasia. J. Mol. Cell. Cardiol. 32:2097-2104.
    • (2000) J. Mol. Cell. Cardiol , vol.32 , pp. 2097-2104
    • Sata, M.1
  • 60
    • 23844436632 scopus 로고    scopus 로고
    • Androgen receptor gene knockout male mice exhibit impaired cardiac growth and exacerbation of angiotensin II-induced cardiac fibrosis
    • Ikeda, Y., et al. 2005. Androgen receptor gene knockout male mice exhibit impaired cardiac growth and exacerbation of angiotensin II-induced cardiac fibrosis. J. Biol. Chem. 280:29661-29666.
    • (2005) J. Biol. Chem , vol.280 , pp. 29661-29666
    • Ikeda, Y.1
  • 61
    • 0042190635 scopus 로고    scopus 로고
    • Absence of p53 leads to accelerated neointimal hyperplasia after vascular injury
    • Sata, M., Tanaka, K., Ishizaka, N., Hirata, Y., and Nagai, R. 2003. Absence of p53 leads to accelerated neointimal hyperplasia after vascular injury. Arterioscler. Thromb. Vasc. Biol. 23:1548-1552.
    • (2003) Arterioscler. Thromb. Vasc. Biol , vol.23 , pp. 1548-1552
    • Sata, M.1    Tanaka, K.2    Ishizaka, N.3    Hirata, Y.4    Nagai, R.5
  • 62
    • 0034002351 scopus 로고    scopus 로고
    • Heparin cofactor II inhibits thrombus formation in a rat thrombosis model
    • Yamanaga, K., et al. 2000. Heparin cofactor II inhibits thrombus formation in a rat thrombosis model. Thromb. Res. 98:95-101.
    • (2000) Thromb. Res , vol.98 , pp. 95-101
    • Yamanaga, K.1
  • 63
    • 17144419252 scopus 로고    scopus 로고
    • Activation of the unfolded protein response occurs at all stages of atherosclerotic lesion development in apolipoprotein E-deficient mice
    • Zhou, J., Lhotak, S., Hilditch, B.A., and Austin, R.C. 2005. Activation of the unfolded protein response occurs at all stages of atherosclerotic lesion development in apolipoprotein E-deficient mice. Circulation. 111:1814-1821.
    • (2005) Circulation , vol.111 , pp. 1814-1821
    • Zhou, J.1    Lhotak, S.2    Hilditch, B.A.3    Austin, R.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.