메뉴 건너뛰기




Volumn 94, Issue 3, 1999, Pages 959-967

Homocysteine-induced endoplasmic reticulum stress and growth arrest leads to specific changes in gene expression in human vascular endothelial cells

Author keywords

[No Author keywords available]

Indexed keywords

CLUSTERIN; COMPLEMENTARY DNA; GLUTATHIONE PEROXIDASE; HOMOCYSTEINE; MESSENGER RNA; SUPEROXIDE DISMUTASE;

EID: 0345535616     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.v94.3.959.415k20_959_967     Document Type: Article
Times cited : (331)

References (72)
  • 2
    • 0026633925 scopus 로고
    • Hyperhomocyst(e)inemia as a risk factor for occlusive vascular disease
    • Kang S-S, Wong PWK, Malinow MR: Hyperhomocyst(e)inemia as a risk factor for occlusive vascular disease. Annu Rev Nutr 12:279, 1992
    • (1992) Annu Rev Nutr , vol.12 , pp. 279
    • Kang, S.-S.1    Wong, P.W.K.2    Malinow, M.R.3
  • 5
    • 0029939676 scopus 로고    scopus 로고
    • Homocysteine and vascular disease
    • McCully KS: Homocysteine and vascular disease. Nature Med 2:386, 1996
    • (1996) Nature Med , vol.2 , pp. 386
    • McCully, K.S.1
  • 6
    • 0030971062 scopus 로고    scopus 로고
    • Homocysteine and thrombotic disease
    • D'Angelo A, Selhub J: Homocysteine and thrombotic disease. Blood 90:1, 1997
    • (1997) Blood , vol.90 , pp. 1
    • D'Angelo, A.1    Selhub, J.2
  • 10
    • 0021041780 scopus 로고
    • Effect of sulfinpyrazone on homocysteine-induced endothelial injury and arteriosclerosis in baboons
    • Harker LA, Harlan JM, Ross R: Effect of sulfinpyrazone on homocysteine-induced endothelial injury and arteriosclerosis in baboons. Circ Res 53:731, 1983
    • (1983) Circ Res , vol.53 , pp. 731
    • Harker, L.A.1    Harlan, J.M.2    Ross, R.3
  • 11
    • 0018743549 scopus 로고
    • Experimental homocysteinemia, endothelial lesions and thrombosis
    • Hladovec J: Experimental homocysteinemia, endothelial lesions and thrombosis. Blood Vessels 16:202, 1979
    • (1979) Blood Vessels , vol.16 , pp. 202
    • Hladovec, J.1
  • 12
    • 0018858624 scopus 로고
    • Homocysteine-induced endothelial cell injury in vitro: A model for the study of vascular injury
    • Wall RT, Harlan JM, Harker LA, Striker GE: Homocysteine-induced endothelial cell injury in vitro: A model for the study of vascular injury. Thromb Res 18:113, 1980
    • (1980) Thromb Res , vol.18 , pp. 113
    • Wall, R.T.1    Harlan, J.M.2    Harker, L.A.3    Striker, G.E.4
  • 13
    • 0022552919 scopus 로고
    • Endothelial cell injury due to copper-catalyzed hydrogen peroxide generation from homocysteine
    • Starkebaum G, Harlan JM: Endothelial cell injury due to copper-catalyzed hydrogen peroxide generation from homocysteine. J Clin Invest 77:1370, 1986
    • (1986) J Clin Invest , vol.77 , pp. 1370
    • Starkebaum, G.1    Harlan, J.M.2
  • 15
    • 0025989783 scopus 로고
    • Human arterial endothelial cell detachment in vitro: Its promotion by homocysteine and cysteine
    • Dudman NPB., Hicks C, Wang J, Wilcken DEL: Human arterial endothelial cell detachment in vitro: Its promotion by homocysteine and cysteine. Atherosclerosis 91:77, 1991
    • (1991) Atherosclerosis , vol.91 , pp. 77
    • Dudman, N.P.B.1    Hicks, C.2    Wang, J.3    Wilcken, D.E.L.4
  • 16
    • 0022472013 scopus 로고
    • Activation of endogenous factor V by a homocysteine-induced vascular endothelial cell activator
    • Rodgers GM, Kane, WH: Activation of endogenous factor V by a homocysteine-induced vascular endothelial cell activator. J Clin Invest 77:1909, 1986
    • (1986) J Clin Invest , vol.77 , pp. 1909
    • Rodgers, G.M.1    Kane, W.H.2
  • 17
    • 0025190042 scopus 로고
    • Homocysteine, an atherogenie stimulus, reduces protein C activation by arterial and venous endothelial cells
    • Rodgers GM, Conn MT: Homocysteine, an atherogenie stimulus, reduces protein C activation by arterial and venous endothelial cells. Blood 75:895, 1990
    • (1990) Blood , vol.75 , pp. 895
    • Rodgers, G.M.1    Conn, M.T.2
  • 18
    • 0026345948 scopus 로고
    • Inhibition of thrombomodulin surface expression and protein C activation by the thrombogenic agent homocysteine
    • Lentz SR, Sadler JE: Inhibition of thrombomodulin surface expression and protein C activation by the thrombogenic agent homocysteine. J Clin Invest 88:1906, 1991
    • (1991) J Clin Invest , vol.88 , pp. 1906
    • Lentz, S.R.1    Sadler, J.E.2
  • 19
    • 0027250615 scopus 로고
    • Homocysteine, a risk factor for premature vascular disease and thrombosis, induces tissue factor activity in endothelial cells
    • Fryer RH, Wilson BD, Gubler DB, Fitzgerald LA, Rodgers, GM: Homocysteine, a risk factor for premature vascular disease and thrombosis, induces tissue factor activity in endothelial cells. Arterioscler Thromb 13:1327, 1993
    • (1993) Arterioscler Thromb , vol.13 , pp. 1327
    • Fryer, R.H.1    Wilson, B.D.2    Gubler, D.B.3    Fitzgerald, L.A.4    Rodgers, G.M.5
  • 21
    • 0027531427 scopus 로고
    • Adverse vascular effects of homocysteine are modulated by endothelium-derived relaxing factor and related oxides of nitrogen
    • Stamler, JS, Osborne JA, Jaraki O, Rabbini LE, Mullins M, Singel S, Loscalzo J: Adverse vascular effects of homocysteine are modulated by endothelium-derived relaxing factor and related oxides of nitrogen. J Clin Invest 91:308, 1993
    • (1993) J Clin Invest , vol.91 , pp. 308
    • Stamler, J.S.1    Osborne, J.A.2    Jaraki, O.3    Rabbini, L.E.4    Mullins, M.5    Singel, S.6    Loscalzo, J.7
  • 24
    • 0029860742 scopus 로고    scopus 로고
    • Homocysteine-respondent genes in vascular endothelial cells identified by differential display analysis: GRP78 and novel genes
    • Kokame K, Kato H, Miyata T: Homocysteine-respondent genes in vascular endothelial cells identified by differential display analysis: GRP78 and novel genes. J Biol Chem 271:29659, 1996
    • (1996) J Biol Chem , vol.271 , pp. 29659
    • Kokame, K.1    Kato, H.2    Miyata, T.3
  • 25
    • 0031869090 scopus 로고    scopus 로고
    • Analysis of gene expression in homocysteine-injured vascular endothelial cells: Demonstration of GRP78/BiP expression, cloning and characterization of a novel reducing agent-tunicamycin regulated gene
    • Miyata T, Kokame K, Agarwala KL, Kato H: Analysis of gene expression in homocysteine-injured vascular endothelial cells: Demonstration of GRP78/BiP expression, cloning and characterization of a novel reducing agent-tunicamycin regulated gene. Semin Thromb Hemost 24:285, 1998
    • (1998) Semin Thromb Hemost , vol.24 , pp. 285
    • Miyata, T.1    Kokame, K.2    Agarwala, K.L.3    Kato, H.4
  • 27
    • 0026843954 scopus 로고
    • Mammalian stress response: Induction of the glucose-regulated protein family
    • Lee AS: Mammalian stress response: induction of the glucose-regulated protein family. Curr Opin Cell Biol 4:267, 1992
    • (1992) Curr Opin Cell Biol , vol.4 , pp. 267
    • Lee, A.S.1
  • 28
    • 0027472128 scopus 로고
    • Homocysteine inhibits von Willebrand factor processing and secretion by preventing transport from the endoplasmic reticulum
    • Lentz SR, Sadler JE: Homocysteine inhibits von Willebrand factor processing and secretion by preventing transport from the endoplasmic reticulum. Blood 81:683, 1993
    • (1993) Blood , vol.81 , pp. 683
    • Lentz, S.R.1    Sadler, J.E.2
  • 30
    • 0015822275 scopus 로고
    • Culture of human endothelial cells derived from umbilical veins: Identification by morphologic and immunologic criteria
    • Jaffe, EA, Nachmann RL, Becker CG, Minick CR: Culture of human endothelial cells derived from umbilical veins: Identification by morphologic and immunologic criteria. J Clin Invest 52:2745, 1973
    • (1973) J Clin Invest , vol.52 , pp. 2745
    • Jaffe, E.A.1    Nachmann, R.L.2    Becker, C.G.3    Minick, C.R.4
  • 31
    • 0022552149 scopus 로고
    • Expression of wild-type and mutant forms of influenza hemagglutinin: The role of folding in intracellular transport
    • Gething, M-J, McCammon K, Sambrook J: Expression of wild-type and mutant forms of influenza hemagglutinin: The role of folding in intracellular transport. Cell 46:939, 1986
    • (1986) Cell , vol.46 , pp. 939
    • Gething, M.-J.1    McCammon, K.2    Sambrook, J.3
  • 32
    • 0022536233 scopus 로고
    • Posttranslational association of immunoglobulin heavy chain binding protein with nascent heavy chains in nonsecreting and secreting hybridomas
    • Bole DG, Hendershot LM, Keaney JF: Posttranslational association of immunoglobulin heavy chain binding protein with nascent heavy chains in nonsecreting and secreting hybridomas. J Cell Biol 102:1558, 1986
    • (1986) J Cell Biol , vol.102 , pp. 1558
    • Bole, D.G.1    Hendershot, L.M.2    Keaney, J.F.3
  • 33
    • 0025784485 scopus 로고
    • A mutation in the ectodomain of herpes simplex virus 1 glycoprotein B causes defective processing and retention in the endoplasmic reticulum
    • Navarro D, Qadri I, Pereira L: A mutation in the ectodomain of herpes simplex virus 1 glycoprotein B causes defective processing and retention in the endoplasmic reticulum. Virology 184:253, 1991
    • (1991) Virology , vol.184 , pp. 253
    • Navarro, D.1    Qadri, I.2    Pereira, L.3
  • 34
    • 0031963203 scopus 로고    scopus 로고
    • DNA chips: State-of-the art
    • Ramsay G: DNA chips: State-of-the art. Nature Biotech 16:40, 1998
    • (1998) Nature Biotech , vol.16 , pp. 40
    • Ramsay, G.1
  • 39
    • 0032482438 scopus 로고    scopus 로고
    • Changes in gene expression during the growth arrest of HepG2 hepatoma cells induced by reducing agents or TGFß1
    • Cabibbo A, Consalez GG, Sardella M, Sitia R, Rubartelli A: Changes in gene expression during the growth arrest of HepG2 hepatoma cells induced by reducing agents or TGFß1. Oncogene 16:2935, 1998
    • (1998) Oncogene , vol.16 , pp. 2935
    • Cabibbo, A.1    Consalez, G.G.2    Sardella, M.3    Sitia, R.4    Rubartelli, A.5
  • 41
    • 0028849482 scopus 로고
    • Metabolism of homocysteine, its relation to the other cellular thiols and its mechanism of cell damage in a cell culture line (human histiocytic cell line U-937)
    • Hultberg B, Andersson A, Isaksson A: Metabolism of homocysteine, its relation to the other cellular thiols and its mechanism of cell damage in a cell culture line (human histiocytic cell line U-937). Biochim Biophys Acta 1269:6, 1995
    • (1995) Biochim Biophys Acta , vol.1269 , pp. 6
    • Hultberg, B.1    Andersson, A.2    Isaksson, A.3
  • 42
    • 0026546365 scopus 로고
    • CHOP, a novel developmentally regulated nuclear protein that dimerizes with transcription factors C/EBP and LAP and functions as a dominant negative inhibitor of gene transcription
    • Ron D, Habener JF: CHOP, a novel developmentally regulated nuclear protein that dimerizes with transcription factors C/EBP and LAP and functions as a dominant negative inhibitor of gene transcription. Genes Dev 6:439, 1992
    • (1992) Genes Dev , vol.6 , pp. 439
    • Ron, D.1    Habener, J.F.2
  • 44
    • 0026546246 scopus 로고
    • Activation of the gadd153 promoter by genotoxic agents: A rapid and specific response to DNA damage
    • Luethy JD, Holbrook NJ: Activation of the gadd153 promoter by genotoxic agents: a rapid and specific response to DNA damage. Cancer Res 52:5, 1992
    • (1992) Cancer Res , vol.52 , pp. 5
    • Luethy, J.D.1    Holbrook, N.J.2
  • 46
    • 0026632457 scopus 로고
    • Gadd45 and Gadd153 messenger RNA levels are increased during hypoxia and after exposure of cells to agents which elevate the levels of the glucose-regulated proteins
    • Price BD, Calderwood SK: Gadd45 and Gadd153 messenger RNA levels are increased during hypoxia and after exposure of cells to agents which elevate the levels of the glucose-regulated proteins. Cancer Res 52:3814, 1992
    • (1992) Cancer Res , vol.52 , pp. 3814
    • Price, B.D.1    Calderwood, S.K.2
  • 47
    • 0030820912 scopus 로고    scopus 로고
    • Reduction of trans-4,5-dihydroxy-1,2-dithiane by cellular oxidoreductases activates gadd153/chop and grp78 transcription and induces cellular tolerance in kidney epithelial cells
    • Halleck MM, Liu H, North J, Stevens JL: Reduction of trans-4,5-dihydroxy-1,2-dithiane by cellular oxidoreductases activates gadd153/chop and grp78 transcription and induces cellular tolerance in kidney epithelial cells. J Biol Chem 272:21760, 1997
    • (1997) J Biol Chem , vol.272 , pp. 21760
    • Halleck, M.M.1    Liu, H.2    North, J.3    Stevens, J.L.4
  • 49
    • 23444443039 scopus 로고
    • CHOP (GADD153) and its oncogenic variant, TLS-CHOP, differ in their ability to induce G1/s arrest
    • Barone MV, Crozat AY, Tabaee A, Philipson L, Ron D: CHOP (GADD153) and its oncogenic variant, TLS-CHOP, differ in their ability to induce G1/S arrest. Genes Dev 8:453, 1994
    • (1994) Genes Dev , vol.8 , pp. 453
    • Barone, M.V.1    Crozat, A.Y.2    Tabaee, A.3    Philipson, L.4    Ron, D.5
  • 50
    • 0027227651 scopus 로고
    • Fusion of CHOP to a novel RNA-binding protein in human myxoid liposarcoma with t(12;16)(q13;p11)
    • Crozat AY, Aman P, Mandahl N, Ron D: Fusion of CHOP to a novel RNA-binding protein in human myxoid liposarcoma with t(12;16)(q13;p11). Nature 363:640, 1993
    • (1993) Nature , vol.363 , pp. 640
    • Crozat, A.Y.1    Aman, P.2    Mandahl, N.3    Ron, D.4
  • 51
    • 0026019435 scopus 로고
    • Isolation of cDNAs for DNA-binding proteins which specifically bind to a tax-responsive enhancer element in the long terminal repeat of human T-cell leukemia virus type I
    • Tsujimoto A, Nyunoya H, Morita T, Sato T, Shimotohno K: Isolation of cDNAs for DNA-binding proteins which specifically bind to a tax-responsive enhancer element in the long terminal repeat of human T-cell leukemia virus type I. J Virol 65:1420. 1991
    • (1991) J Virol , vol.65 , pp. 1420
    • Tsujimoto, A.1    Nyunoya, H.2    Morita, T.3    Sato, T.4    Shimotohno, K.5
  • 52
    • 0029112861 scopus 로고
    • Normal fibroblasts induce the C/EBP beta and ATF-4 bZIP transcription factors in response to anoxia
    • Estes SD, Stoler DL, Andersen GR: Normal fibroblasts induce the C/EBP beta and ATF-4 bZIP transcription factors in response to anoxia. Exp Cell Res 220:47, 1995
    • (1995) Exp Cell Res , vol.220 , pp. 47
    • Estes, S.D.1    Stoler, D.L.2    Andersen, G.R.3
  • 53
    • 0031014395 scopus 로고    scopus 로고
    • 2+ depletion and formation of aberrant proteins: Activation of the conserved stress-inducible grp core promoter element by the human nuclear factor YY1
    • 2+ depletion and formation of aberrant proteins: Activation of the conserved stress-inducible grp core promoter element by the human nuclear factor YY1. Mol Cell Biol 17:54, 1997
    • (1997) Mol Cell Biol , vol.17 , pp. 54
    • Li, W.W.1    Hsiung, Y.2    Zhou, Y.3    Roy, B.4    Lee, A.S.5
  • 55
    • 0030930486 scopus 로고    scopus 로고
    • Multiple mechanims of transcriptional repression by YY1
    • Galvin KM, Shi Y: Multiple mechanims of transcriptional repression by YY1. Moll Cell Biol 17:3723, 1997
    • (1997) Moll Cell Biol , vol.17 , pp. 3723
    • Galvin, K.M.1    Shi, Y.2
  • 56
    • 0025238437 scopus 로고
    • The protein Id: A negative regulator of helix-loop-helix DNA binding proteins
    • Benezra R, Davis RL, Lockshon D, Turner DL, Weintraub H: The protein Id: a negative regulator of helix-loop-helix DNA binding proteins. Cell 61:49, 1990
    • (1990) Cell , vol.61 , pp. 49
    • Benezra, R.1    Davis, R.L.2    Lockshon, D.3    Turner, D.L.4    Weintraub, H.5
  • 57
    • 0029024931 scopus 로고
    • Suppression of mammary epithelial cell differentiation by the helix-loop-helix protein Id-1
    • Desprez PY, Hara E, Bissell MJ, Campisi J: Suppression of mammary epithelial cell differentiation by the helix-loop-helix protein Id-1. Mol Cell Biol 15:3398, 1995
    • (1995) Mol Cell Biol , vol.15 , pp. 3398
    • Desprez, P.Y.1    Hara, E.2    Bissell, M.J.3    Campisi, J.4
  • 58
    • 0028095488 scopus 로고
    • The helix-loop-helix protein Id inhibits differentiation of murine erythroleukemia cells
    • Shoji W, Yamamoto T, Obinata M: The helix-loop-helix protein Id inhibits differentiation of murine erythroleukemia cells. J Biol Chem 269:5078, 1994
    • (1994) J Biol Chem , vol.269 , pp. 5078
    • Shoji, W.1    Yamamoto, T.2    Obinata, M.3
  • 59
    • 0029783822 scopus 로고    scopus 로고
    • Developmental expression and activities of specific fos and jun proteins are functionally related to osteoblast maturation: Role of Fra-2 and Jun D during differentiation
    • McCabe LR, Banerjee C, Kundu R, Harrison RJ, Dobner PR, Stein JL, Lian JB, Stein GS: Developmental expression and activities of specific fos and jun proteins are functionally related to osteoblast maturation: Role of Fra-2 and Jun D during differentiation. Endocrinology 137:4398, 1996
    • (1996) Endocrinology , vol.137 , pp. 4398
    • McCabe, L.R.1    Banerjee, C.2    Kundu, R.3    Harrison, R.J.4    Dobner, P.R.5    Stein, J.L.6    Lian, J.B.7    Stein, G.S.8
  • 62
    • 0029124742 scopus 로고
    • Clusterin: Physiologic and pathophysiologic considerations
    • Rosenberg ME, Silkensen J: Clusterin: physiologic and pathophysiologic considerations. Int J Biochem Cell Biol 27:633, 1995
    • (1995) Int J Biochem Cell Biol , vol.27 , pp. 633
    • Rosenberg, M.E.1    Silkensen, J.2
  • 63
    • 0030753875 scopus 로고    scopus 로고
    • Increased immunolocalization of paraoxonase, clusterin, and apolipoprotein A-I in the human artery wall with the progression of atherosclerosis
    • Mackness B, Hunt R, Durrington PN, Mackness MI: Increased immunolocalization of paraoxonase, clusterin, and apolipoprotein A-I in the human artery wall with the progression of atherosclerosis. Arterioscler Thromb Vase Biol 17:1233, 1997
    • (1997) Arterioscler Thromb Vase Biol , vol.17 , pp. 1233
    • Mackness, B.1    Hunt, R.2    Durrington, P.N.3    Mackness, M.I.4
  • 64
    • 0031748528 scopus 로고    scopus 로고
    • Clusterin protects against oxidative stress in vitro through aggregative and nonaggregative properties
    • Schwochau GB, Nath KA, Rosenberg ME: Clusterin protects against oxidative stress in vitro through aggregative and nonaggregative properties. Kidney Int 53:1647, 1998
    • (1998) Kidney Int , vol.53 , pp. 1647
    • Schwochau, G.B.1    Nath, K.A.2    Rosenberg, M.E.3
  • 65
    • 0030803669 scopus 로고    scopus 로고
    • The PAG gene product, a stress-induced protein with antioxidant properties, is an Ab1 SH3-binding protein and a physiological inhibitor of c-Ab1 tyrosine kinase activity
    • Wen ST, Van Etten RA: The PAG gene product, a stress-induced protein with antioxidant properties, is an Ab1 SH3-binding protein and a physiological inhibitor of c-Ab1 tyrosine kinase activity. Genes Dev 11:2456, 1997
    • (1997) Genes Dev , vol.11 , pp. 2456
    • Wen, S.T.1    Van Etten, R.A.2
  • 66
    • 0345647078 scopus 로고    scopus 로고
    • The pag gene product, a physiological inhibitor of c-ab1 tyrosine kinase, is overexpressed in cells entering S phase and by contact with agents inducing oxidative stress
    • Prosperi MT, Ferbus D, Rouillard D, Goubin G: The pag gene product, a physiological inhibitor of c-ab1 tyrosine kinase, is overexpressed in cells entering S phase and by contact with agents inducing oxidative stress. FEBS Lett 423:39, 1998
    • (1998) FEBS Lett , vol.423 , pp. 39
    • Prosperi, M.T.1    Ferbus, D.2    Rouillard, D.3    Goubin, G.4
  • 67
    • 0029016985 scopus 로고
    • Induction of the antioxidant stress proteins heme oxygenase-1 and MSP23 by stress agents and oxidized LDL in cultured vascular smooth muscle cells
    • Siow RC, Ishii T, Sato H, Taketani S, Leake DS, Sweiry JH, Pearson JD, Bannai S, Mann GE: Induction of the antioxidant stress proteins heme oxygenase-1 and MSP23 by stress agents and oxidized LDL in cultured vascular smooth muscle cells. FEBS Lett 368:239, 1995
    • (1995) FEBS Lett , vol.368 , pp. 239
    • Siow, R.C.1    Ishii, T.2    Sato, H.3    Taketani, S.4    Leake, D.S.5    Sweiry, J.H.6    Pearson, J.D.7    Bannai, S.8    Mann, G.E.9
  • 68
    • 0029051274 scopus 로고
    • Increased lipid peroxidation as a mechanism of methionine-induced atherosclerosis in rabbits
    • Toborek M, Kopieczna-Grzebieniak E, Drozdz M, Wieczorek M: Increased lipid peroxidation as a mechanism of methionine-induced atherosclerosis in rabbits. Atherosclerosis 115:217, 1995
    • (1995) Atherosclerosis , vol.115 , pp. 217
    • Toborek, M.1    Kopieczna-Grzebieniak, E.2    Drozdz, M.3    Wieczorek, M.4
  • 71
    • 0025811786 scopus 로고
    • Competitive inhibition of a set of endoplasmic reticulum protein genes (GRP78, GRP94, and Erp72) retards cell growth and lowers viability after ionophore treatment
    • Li XA, Lee AS: Competitive inhibition of a set of endoplasmic reticulum protein genes (GRP78, GRP94, and Erp72) retards cell growth and lowers viability after ionophore treatment. Mol Cell Biol 11:3446, 1991
    • (1991) Mol Cell Biol , vol.11 , pp. 3446
    • Li, X.A.1    Lee, A.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.