메뉴 건너뛰기




Volumn 172, Issue 2, 2004, Pages 229-238

Homocysteine enhances superoxide anion release and NADPH oxidase assembly by human neutrophils. Effects on MAPK activation and neutrophil migration

Author keywords

Homocysteine; MAPK; NADPH oxidase; Neutrophils; Reactive oxygen species

Indexed keywords

DIPHENYLIODONIUM SALT; ENZYME INHIBITOR; HOMOCYSTEINE; HYDROGEN PEROXIDE; MITOGEN ACTIVATED PROTEIN KINASE 1; PROTEIN P47; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE INHIBITOR; SUPEROXIDE; SUPEROXIDE DISMUTASE; SYNAPTOPHYSIN; UNCLASSIFIED DRUG;

EID: 10744230646     PISSN: 00219150     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.atherosclerosis.2003.11.005     Document Type: Article
Times cited : (67)

References (52)
  • 1
    • 0033671987 scopus 로고    scopus 로고
    • Activated polymorphonuclear leukocytes and monocytes in the peripheral blood of patients with ischemic heart and brain conditions correspond to the presence of multiple risk factors for atherothrombosis
    • Berliner S., Rogowski O., Rotstein R., Fusman R., Shapira I., Bornstein N.M. Activated polymorphonuclear leukocytes and monocytes in the peripheral blood of patients with ischemic heart and brain conditions correspond to the presence of multiple risk factors for atherothrombosis. Cardiology. 94:2000;19-25.
    • (2000) Cardiology , vol.94 , pp. 19-25
    • Berliner, S.1    Rogowski, O.2    Rotstein, R.3    Fusman, R.4    Shapira, I.5    Bornstein, N.M.6
  • 3
    • 0034808344 scopus 로고    scopus 로고
    • Correlations between peripheral differential leukocyte counts and carotid atherosclerosis in nonsmokers
    • Huang Z.S., Jeng J.S., Wang C.H., Yip P.K., Wu T.H., Lee T.K. Correlations between peripheral differential leukocyte counts and carotid atherosclerosis in nonsmokers. Atherosclerosis. 158:2001;431-436.
    • (2001) Atherosclerosis , vol.158 , pp. 431-436
    • Huang, Z.S.1    Jeng, J.S.2    Wang, C.H.3    Yip, P.K.4    Wu, T.H.5    Lee, T.K.6
  • 4
    • 0032499024 scopus 로고    scopus 로고
    • Homocysteine and atherothrombosis
    • Welch G.N., Loscalzo J. Homocysteine and atherothrombosis. N. Engl. J. Med. 338:1998;1042-1050.
    • (1998) N. Engl. J. Med. , vol.338 , pp. 1042-1050
    • Welch, G.N.1    Loscalzo, J.2
  • 6
    • 0033853452 scopus 로고    scopus 로고
    • Homocysteine and cardiovascular disease: Cause or effect?
    • Brattstrom L., Wilcken D.E. Homocysteine and cardiovascular disease: cause or effect? Am. J. Clin. Nutr. 72:2000;315-323.
    • (2000) Am. J. Clin. Nutr. , vol.72 , pp. 315-323
    • Brattstrom, L.1    Wilcken, D.E.2
  • 7
    • 0034837955 scopus 로고    scopus 로고
    • Roles of homocysteine in cell metabolism: Old and new functions
    • Medina M., Urdiales J.L., Amores-Sanchez M.I. Roles of homocysteine in cell metabolism: old and new functions. Eur. J. Biochem. 268:2001;3871-3882.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 3871-3882
    • Medina, M.1    Urdiales, J.L.2    Amores-Sanchez, M.I.3
  • 8
    • 0034332885 scopus 로고    scopus 로고
    • Homocysteine, a risk factor for coronary artery disease or not? a meta-analysis
    • Cleophas TJ, Hornstra N, van Hoogstraten B, van der MJ, Homocysteine, a risk factor for coronary artery disease or not? A meta-analysis, Am J Cardiol 86 (2000) 1005-9, A8.
    • (2000) Am J Cardiol , vol.86 , pp. 1005-1009
    • Cleophas, T.J.1    Hornstra, N.2    Van Hoogstraten, B.3    Van Der, M.J.4
  • 9
    • 0018858624 scopus 로고
    • Homocysteine-induced endothelial cell injury in vitro: A model for the study of vascular injury
    • Wall R.T., Harlan J.M., Harker L.A., Striker G.E. Homocysteine-induced endothelial cell injury in vitro: a model for the study of vascular injury. Thromb. Res. 18:1980;113-121.
    • (1980) Thromb. Res. , vol.18 , pp. 113-121
    • Wall, R.T.1    Harlan, J.M.2    Harker, L.A.3    Striker, G.E.4
  • 10
    • 0027288252 scopus 로고
    • Homocysteine-induced modulation of tissue plasminogen activator binding to its endothelial cell membrane receptor
    • Hajjar K.A. Homocysteine-induced modulation of tissue plasminogen activator binding to its endothelial cell membrane receptor. J. Clin. Invest. 91:1993;2873-2879.
    • (1993) J. Clin. Invest. , vol.91 , pp. 2873-2879
    • Hajjar, K.A.1
  • 11
    • 0033525542 scopus 로고    scopus 로고
    • Homocysteine enhances neutrophil-endothelial interactions in both cultured human cells and rats in vivo
    • Dudman N.P., Temple S.E., Guo X.W., Fu W., Perry M.A. Homocysteine enhances neutrophil-endothelial interactions in both cultured human cells and rats In vivo. Circ. Res. 84:1999;409-416.
    • (1999) Circ. Res. , vol.84 , pp. 409-416
    • Dudman, N.P.1    Temple, S.E.2    Guo, X.W.3    Fu, W.4    Perry, M.A.5
  • 12
    • 0036124199 scopus 로고    scopus 로고
    • Homocysteine increases monocyte and T-cell adhesion to human aortic endothelial cells
    • Koga T., Claycombe K., Meydani M. Homocysteine increases monocyte and T-cell adhesion to human aortic endothelial cells. Atherosclerosis. 161:2002;365-374.
    • (2002) Atherosclerosis , vol.161 , pp. 365-374
    • Koga, T.1    Claycombe, K.2    Meydani, M.3
  • 13
    • 0034254728 scopus 로고    scopus 로고
    • Induction of monocyte tissue factor expression by homocysteine: A possible mechanism for thrombosis
    • Khajuria A., Houston D.S. Induction of monocyte tissue factor expression by homocysteine: a possible mechanism for thrombosis. Blood. 96:2000;966-972.
    • (2000) Blood , vol.96 , pp. 966-972
    • Khajuria, A.1    Houston, D.S.2
  • 15
    • 0030814892 scopus 로고    scopus 로고
    • Mevalonate-dependent inhibition of transendothelial migration and chemotaxis of human peripheral blood neutrophils by pravastatin
    • Dunzendorfer S., Rothbucher D., Schratzberger P., Reinisch N., Kahler C.M., Wiedermann C.J. Mevalonate-dependent inhibition of transendothelial migration and chemotaxis of human peripheral blood neutrophils by pravastatin. Circ. Res. 81:1997;963-969.
    • (1997) Circ. Res. , vol.81 , pp. 963-969
    • Dunzendorfer, S.1    Rothbucher, D.2    Schratzberger, P.3    Reinisch, N.4    Kahler, C.M.5    Wiedermann, C.J.6
  • 16
    • 0031821779 scopus 로고    scopus 로고
    • Homocysteine and vitamins in cardiovascular disease
    • Jacobsen D.W. Homocysteine and vitamins in cardiovascular disease. Clin. Chem. 44:1998;1833-1843.
    • (1998) Clin. Chem. , vol.44 , pp. 1833-1843
    • Jacobsen, D.W.1
  • 17
    • 0027189961 scopus 로고
    • The biochemical basis of the NADPH oxidase of phagocytes
    • Segal A.W., Abo A. The biochemical basis of the NADPH oxidase of phagocytes. Trends Biochem. Sci. 18:1993;43-47.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 43-47
    • Segal, A.W.1    Abo, A.2
  • 18
    • 0031790002 scopus 로고    scopus 로고
    • Bacterial phagocytosis activates extracellular signal-regulated kinase and p38 mitogen-activated protein kinase cascades in human neutrophils
    • McLeish K.R., Klein J.B., Coxon P.Y., Head K.Z., Ward R.A. Bacterial phagocytosis activates extracellular signal-regulated kinase and p38 mitogen-activated protein kinase cascades in human neutrophils. J. Leukoc. Biol. 64:1998;835-844.
    • (1998) J. Leukoc. Biol. , vol.64 , pp. 835-844
    • McLeish, K.R.1    Klein, J.B.2    Coxon, P.Y.3    Head, K.Z.4    Ward, R.A.5
  • 19
    • 0028006744 scopus 로고
    • Activation of the mitogen-activated protein kinase signaling pathway in neutrophils. Role of oxidants
    • Fialkow L., Chan C.K., Rotin D., Grinstein S., Downey G.P. Activation of the mitogen-activated protein kinase signaling pathway in neutrophils. Role of oxidants. J. Biol. Chem. 269:1994;31234-31242.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31234-31242
    • Fialkow, L.1    Chan, C.K.2    Rotin, D.3    Grinstein, S.4    Downey, G.P.5
  • 20
    • 0027930914 scopus 로고
    • FMLP activates Ras and Raf in human neutrophils potential role in activation of MAP kinase
    • Worthen G.S., Avdi N., Buhl A.M., Suzuki N., Johnson G.L. FMLP activates Ras and Raf in human neutrophils potential role in activation of MAP kinase. J. Clin. Invest. 94:1994;815-823.
    • (1994) J. Clin. Invest. , vol.94 , pp. 815-823
    • Worthen, G.S.1    Avdi, N.2    Buhl, A.M.3    Suzuki, N.4    Johnson, G.L.5
  • 21
    • 0029918680 scopus 로고    scopus 로고
    • The mitogen-activated protein kinase phosphatases PAC1, MKP-1, and MKP-2 have unique substrate specificities and reduced activity in vivo toward the ERK2 sevenmaker mutation
    • Chu Y., Solski P.A., Khosravi-Far R., Der C.J., Kelly K. The mitogen-activated protein kinase phosphatases PAC1, MKP-1, and MKP-2 have unique substrate specificities and reduced activity in vivo toward the ERK2 sevenmaker mutation. J. Biol. Chem. 271:1996;6497-6501.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6497-6501
    • Chu, Y.1    Solski, P.A.2    Khosravi-Far, R.3    Der, C.J.4    Kelly, K.5
  • 22
    • 0014385564 scopus 로고
    • Isolation of mononuclear cells and granulocytes from human blood. Isolation of monuclear cells by one centrifugation, and of granulocytes by combining centrifugation and sedimentation at 1 g
    • Boyum A. Isolation of mononuclear cells and granulocytes from human blood. Isolation of monuclear cells by one centrifugation, and of granulocytes by combining centrifugation and sedimentation at 1 g. Scand J Clin Lab Invest Suppl. 97:1968;77-89.
    • (1968) Scand J Clin Lab Invest Suppl , vol.97 , pp. 77-89
    • Boyum, A.1
  • 23
    • 0024430910 scopus 로고
    • Cyclosporin a inhibits phorbol ester-induced activation of superoxide production in resident mouse peritoneal macrophages
    • Chiara M.D., Bedoya F., Sobrino F. Cyclosporin A inhibits phorbol ester-induced activation of superoxide production in resident mouse peritoneal macrophages. Biochem. J. 264:1989;21-26.
    • (1989) Biochem. J. , vol.264 , pp. 21-26
    • Chiara, M.D.1    Bedoya, F.2    Sobrino, F.3
  • 24
    • 0036486832 scopus 로고    scopus 로고
    • Activation of phagocytic cell NADPH oxidase by norfloxacin: A potential mechanism to explain its bactericidal action
    • El Bekay R., Alvarez M., Carballo M., Martin-Nieto J., Monteseirin J., Pintado E. Activation of phagocytic cell NADPH oxidase by norfloxacin: a potential mechanism to explain its bactericidal action. J. Leukoc. Biol. 71:2002;255-261.
    • (2002) J. Leukoc. Biol. , vol.71 , pp. 255-261
    • El Bekay, R.1    Alvarez, M.2    Carballo, M.3    Martin-Nieto, J.4    Monteseirin, J.5    Pintado, E.6
  • 25
    • 0035448083 scopus 로고    scopus 로고
    • Inhibition of the neutrophil NADPH oxidase and associated H+ channel by diethyl pyrocarbonate (DEPC), a histidine-modifying agent: Evidence for at least two target sites
    • Mankelow T.J., Henderson L.M. Inhibition of the neutrophil NADPH oxidase and associated H+ channel by diethyl pyrocarbonate (DEPC), a histidine-modifying agent: evidence for at least two target sites. Biochem. J. 358:2001;315-324.
    • (2001) Biochem. J. , vol.358 , pp. 315-324
    • Mankelow, T.J.1    Henderson, L.M.2
  • 26
    • 20244378630 scopus 로고    scopus 로고
    • Oxidative stress is a critical mediator of the angiotensin II signal in human neutrophils: Involvement of mitogen-activated protein kinase, calcineurin, and the transcription factor NF-κB
    • El Bekay R., Alvarez M., Monteseirin J., Alba G., Chacon P., Vega A. Oxidative stress is a critical mediator of the angiotensin II signal in human neutrophils: involvement of mitogen-activated protein kinase, calcineurin, and the transcription factor NF-κB. Blood. 102:2003;662-671.
    • (2003) Blood , vol.102 , pp. 662-671
    • El Bekay, R.1    Alvarez, M.2    Monteseirin, J.3    Alba, G.4    Chacon, P.5    Vega, A.6
  • 27
    • 0021027358 scopus 로고
    • Detection of picomole levels of hydroperoxides using a fluorescent dichlorofluorescein assay
    • Cathcart R., Schwiers E., Ames B.N. Detection of picomole levels of hydroperoxides using a fluorescent dichlorofluorescein assay. Anal Biochem. 134:1983;111-116.
    • (1983) Anal Biochem. , vol.134 , pp. 111-116
    • Cathcart, R.1    Schwiers, E.2    Ames, B.N.3
  • 28
    • 0017064979 scopus 로고
    • A fluorometric method for determination of oxidized and reduced glutathione in tissues
    • Hissin P.J., Hilf R. A fluorometric method for determination of oxidized and reduced glutathione in tissues. Anal. Biochem. 74:1976;214-226.
    • (1976) Anal. Biochem. , vol.74 , pp. 214-226
    • Hissin, P.J.1    Hilf, R.2
  • 29
    • 0019970508 scopus 로고
    • Human neutrophil-specific granule deficiency: A model to assess the role of neutrophilspecific granules in the evolution of the inflammatory response
    • Gallin J.I., Fletcher M.P., Seligmann B.E., Hoffstein S., Cehrs K., Mounessa N. Human neutrophil-specific granule deficiency: a model to assess the role of neutrophilspecific granules in the evolution of the inflammatory response. Blood. 59:1982;1317-1329.
    • (1982) Blood , vol.59 , pp. 1317-1329
    • Gallin, J.I.1    Fletcher, M.P.2    Seligmann, B.E.3    Hoffstein, S.4    Cehrs, K.5    Mounessa, N.6
  • 30
    • 0030711684 scopus 로고    scopus 로고
    • Cellular and molecular mechanisms of endothelial cell dysfunction
    • Harrison D.G. Cellular and molecular mechanisms of endothelial cell dysfunction. J. Clin. Invest. 100:1997;2153-2157.
    • (1997) J. Clin. Invest , vol.100 , pp. 2153-2157
    • Harrison, D.G.1
  • 31
    • 0023117805 scopus 로고
    • The inhibition by diphenyleneiodonium and its analogues of superoxide generation by macrophages
    • Hancock J.T., Jones O.T. The inhibition by diphenyleneiodonium and its analogues of superoxide generation by macrophages. Biochem. J. 242:1987;103-107.
    • (1987) Biochem. J. , vol.242 , pp. 103-107
    • Hancock, J.T.1    Jones, O.T.2
  • 32
    • 0025970033 scopus 로고
    • Neutrophil nicotinamide adenine dinucleotide phosphate oxidase assembly. Translocation of p47-phox and p67-phox requires interaction between p47-phox and cytochrome b558
    • Heyworth P.G., Curnutte J.T., Nauseef W.M., Volpp B.D., Pearson D.W., Rosen H.et al. Neutrophil nicotinamide adenine dinucleotide phosphate oxidase assembly. Translocation of p47-phox and p67-phox requires interaction between p47-phox and cytochrome b558. J. Clin. Invest. 87:1991;352-356.
    • (1991) J. Clin. Invest , vol.87 , pp. 352-356
    • Heyworth, P.G.1    Curnutte, J.T.2    Nauseef, W.M.3    Volpp, B.D.4    Pearson, D.W.5    Rosen, H.6
  • 33
    • 0028028859 scopus 로고
    • 2 production in adherent human neutrophils
    • 2 production in adherent human neutrophils. J. Immunol. 152:1994;290-300.
    • (1994) J. Immunol. , vol.152 , pp. 290-300
    • Suchard, S.J.1    Boxer, L.A.2
  • 35
    • 0023260229 scopus 로고
    • Ultrastructural localization of lysozyme in human neutrophils by immunogold
    • Cramer E.M., Breton-Gorius J. Ultrastructural localization of lysozyme in human neutrophils by immunogold. J. Leukoc. Biol. 41:1987;242-247.
    • (1987) J. Leukoc. Biol. , vol.41 , pp. 242-247
    • Cramer, E.M.1    Breton-Gorius, J.2
  • 36
    • 0028884033 scopus 로고
    • PD 098059 is a specific inhibitor of the activation of mitogen-activated protein kinase kinase in vitro and in vivo
    • Alessi D.R., Cuenda A., Cohen P., Dudley D.T., Saltiel A.R. PD 098059 is a specific inhibitor of the activation of mitogen-activated protein kinase kinase in vitro and in vivo. J. Biol. Chem. 270:1995;27489-27494.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27489-27494
    • Alessi, D.R.1    Cuenda, A.2    Cohen, P.3    Dudley, D.T.4    Saltiel, A.R.5
  • 37
    • 0028988138 scopus 로고
    • SB 203580 is a specific inhibitor of a MAP kinase homologue which is stimulated by cellular stresses and interleukin-1
    • Cuenda A., Rouse J., Doza Y.N.et al. SB 203580 is a specific inhibitor of a MAP kinase homologue which is stimulated by cellular stresses and interleukin-1. FEBS Lett. 364:1995;229-233.
    • (1995) FEBS Lett. , vol.364 , pp. 229-233
    • Cuenda, A.1    Rouse, J.2    Doza, Y.N.3
  • 39
    • 0036092467 scopus 로고    scopus 로고
    • Homocysteine and cardiovascular disease: Current evidence and future prospects
    • Mangoni A.A., Jackson S.H. Homocysteine and cardiovascular disease: current evidence and future prospects. Am. J. Med. 112:2002;556-565.
    • (2002) Am. J. Med. , vol.112 , pp. 556-565
    • Mangoni, A.A.1    Jackson, S.H.2
  • 40
    • 0029066299 scopus 로고
    • A quantitative assessment of plasma homocysteine as a risk factor for vascular disease. Probable benefits of increasing folic acid intakes
    • Boushey C.J., Beresford S.A., Omenn G.S., Motulsky A.G. A quantitative assessment of plasma homocysteine as a risk factor for vascular disease. Probable benefits of increasing folic acid intakes. J Am Med Assoc. 274:1995;1049-1057.
    • (1995) J Am Med Assoc , vol.274 , pp. 1049-1057
    • Boushey, C.J.1    Beresford, S.A.2    Omenn, G.S.3    Motulsky, A.G.4
  • 41
    • 0017197285 scopus 로고
    • Homocystine-induced arteriosclerosis. the role of endothelial cell injury and platelet response in its genesis
    • Harker L.A., Ross R., Slichter S.J., Scott C.R. Homocystine-induced arteriosclerosis. The role of endothelial cell injury and platelet response in its genesis. J. Clin. Invest. 58:1976;731-741.
    • (1976) J. Clin. Invest. , vol.58 , pp. 731-741
    • Harker, L.A.1    Ross, R.2    Slichter, S.J.3    Scott, C.R.4
  • 42
    • 1842331509 scopus 로고    scopus 로고
    • Plasma homocysteine as a risk factor for vascular disease. the European Concerted Action Project
    • Graham I.M., Daly L.E., Refsum H.M.et al. Plasma homocysteine as a risk factor for vascular disease. The European Concerted Action Project. J Am Med Assoc. 277:1997;1775-1781.
    • (1997) J Am Med Assoc , vol.277 , pp. 1775-1781
    • Graham, I.M.1    Daly, L.E.2    Refsum, H.M.3
  • 43
    • 0030866856 scopus 로고    scopus 로고
    • High homocysteine levels are independently related to isolated systolic hypertension in older adults
    • Sutton-Tyrrell K., Bostom A., Selhub J., Zeigler-Johnson C. High homocysteine levels are independently related to isolated systolic hypertension in older adults. Circulation. 96:1997;1745-1749.
    • (1997) Circulation , vol.96 , pp. 1745-1749
    • Sutton-Tyrrell, K.1    Bostom, A.2    Selhub, J.3    Zeigler-Johnson, C.4
  • 44
    • 0027142389 scopus 로고
    • Oxidation of low density lipoprotein by thiols: Superoxide-dependent and -independent mechanisms
    • Heinecke J.W., Kawamura M., Suzuki L., Chait A. Oxidation of low density lipoprotein by thiols: superoxide-dependent and -independent mechanisms. J. Lipid Res. 34:1993;2051-2061.
    • (1993) J. Lipid Res. , vol.34 , pp. 2051-2061
    • Heinecke, J.W.1    Kawamura, M.2    Suzuki, L.3    Chait, A.4
  • 45
    • 0030188563 scopus 로고    scopus 로고
    • The oxidant stress of hyperhomocyst(e)inemia
    • Loscalzo J. The oxidant stress of hyperhomocyst(e)inemia. J. Clin. Invest. 98:1996;5-7.
    • (1996) J. Clin. Invest. , vol.98 , pp. 5-7
    • Loscalzo, J.1
  • 46
    • 0030600365 scopus 로고    scopus 로고
    • The hemolytic activity of homocysteine is increased by the activated polymorphonuclear leukocytes
    • Olinescu R., Kummerow F.A., Handler B., Fleischer L. The hemolytic activity of homocysteine is increased by the activated polymorphonuclear leukocytes. Biochem. Biophys. Res. Commun. 226:1996;912-916.
    • (1996) Biochem. Biophys. Res. Commun. , vol.226 , pp. 912-916
    • Olinescu, R.1    Kummerow, F.A.2    Handler, B.3    Fleischer, L.4
  • 47
    • 0022394280 scopus 로고
    • The importance of free radicals and catalytic metal ions in human diseases
    • Halliwell B., Gutteridge J.M. The importance of free radicals and catalytic metal ions in human diseases. Mol. Aspects Med. 8:1985;89-193.
    • (1985) Mol. Aspects Med. , vol.8 , pp. 89-193
    • Halliwell, B.1    Gutteridge, J.M.2
  • 48
    • 0033938469 scopus 로고    scopus 로고
    • Homocysteine stimulates MAP kinase in bovine aortic smooth muscle cells
    • Woo D.K., Dudrick S.J., Sumpio B.E. Homocysteine stimulates MAP kinase in bovine aortic smooth muscle cells. Surgery. 128:2000;59-66.
    • (2000) Surgery , vol.128 , pp. 59-66
    • Woo, D.K.1    Dudrick, S.J.2    Sumpio, B.E.3
  • 49
    • 0034665653 scopus 로고    scopus 로고
    • Homocysteine-responsive ATF3 gene expression in human vascular endothelial cells: Activation of c-Jun NH2-terminal kinase and promoter response element
    • Cai Y., Zhang C., Nawa T., Aso T., Tanaka M., Oshiro S. Homocysteine-responsive ATF3 gene expression in human vascular endothelial cells: activation of c-Jun NH2-terminal kinase and promoter response element. Blood. 96:2000;2140-2148.
    • (2000) Blood , vol.96 , pp. 2140-2148
    • Cai, Y.1    Zhang, C.2    Nawa, T.3    Aso, T.4    Tanaka, M.5    Oshiro, S.6
  • 50
    • 0034176139 scopus 로고    scopus 로고
    • Polymorphonuclear leukocytes modulate tissue factor production by mononuclear cells: Role of reactive oxygen species
    • Cadroy Y., Dupouy D., Boneu B., Plaisancie H. Polymorphonuclear leukocytes modulate tissue factor production by mononuclear cells: role of reactive oxygen species. J. Immunol. 164:2000;3822-3828.
    • (2000) J. Immunol. , vol.164 , pp. 3822-3828
    • Cadroy, Y.1    Dupouy, D.2    Boneu, B.3    Plaisancie, H.4
  • 51
    • 0036760036 scopus 로고    scopus 로고
    • The evolving pathogenesis of systemic vasculitis
    • Savage C.O. The evolving pathogenesis of systemic vasculitis. Clin. Med. 2:2002;458-464.
    • (2002) Clin. Med. , vol.2 , pp. 458-464
    • Savage, C.O.1
  • 52
    • 0032430436 scopus 로고    scopus 로고
    • Can dietary supplements with folic acid or vitamin B6 reduce cardiovascular risk? Design of clinical trials to test the homocysteine hypothesis of vascular disease
    • Clarke R., Collins R. Can dietary supplements with folic acid or vitamin B6 reduce cardiovascular risk? Design of clinical trials to test the homocysteine hypothesis of vascular disease. J. Cardiovasc. Risk. 5:1998;249-255.
    • (1998) J. Cardiovasc. Risk , vol.5 , pp. 249-255
    • Clarke, R.1    Collins, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.