메뉴 건너뛰기




Volumn 90, Issue 4, 1997, Pages 1501-1507

Interleukin-6 downregulates factor XII production by human hepatoma cell line (HepG2)

Author keywords

[No Author keywords available]

Indexed keywords

ACUTE PHASE PROTEIN; BLOOD CLOTTING FACTOR 12; FIBRINOGEN; INTERLEUKIN 2; MESSENGER RNA; PREALBUMIN; PREKALLIKREIN; RECOMBINANT INTERLEUKIN 6;

EID: 0030761483     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.v90.4.1501.1501_1501_1507     Document Type: Article
Times cited : (45)

References (67)
  • 1
    • 0020021627 scopus 로고
    • The biochemistry and pathophysiology of the contact system of plasma
    • Cochrane CG, Griffin JH: The biochemistry and pathophysiology of the contact system of plasma. Adv lmmunol 33:241, 1982
    • (1982) Adv Lmmunol , vol.33 , pp. 241
    • Cochrane, C.G.1    Griffin, J.H.2
  • 2
    • 0021348273 scopus 로고
    • Surface-mediated defense reactions. The plasma contact activation system
    • Colman RW: Surface-mediated defense reactions. The plasma contact activation system. J Clin Invest 73:1249, 1984
    • (1984) J Clin Invest , vol.73 , pp. 1249
    • Colman, R.W.1
  • 3
    • 0023134625 scopus 로고
    • Contact factors in health and disease
    • Saito H: Contact factors in health and disease. Thromb Haemost 13:36, 1987
    • (1987) Thromb Haemost , vol.13 , pp. 36
    • Saito, H.1
  • 4
    • 0023201944 scopus 로고
    • The coagulation-kinin pathway of human plasma
    • Kaplan AP, Silverberg M: The coagulation-kinin pathway of human plasma. Blood 70:1, 1987
    • (1987) Blood , vol.70 , pp. 1
    • Kaplan, A.P.1    Silverberg, M.2
  • 5
    • 0002172917 scopus 로고
    • The contact activation system of plasma: Biochemistry and pathophysiology
    • Gallin JI, Goldstein IM, Snyderman R (eds): New York, NY, Raven
    • Kozin F, Cochrane CG: The contact activation system of plasma: Biochemistry and pathophysiology, in Gallin JI, Goldstein IM, Snyderman R (eds): Inflammation: Basic Principles and Clinical Correlates. New York, NY, Raven, 1988, p 101
    • (1988) Inflammation: Basic Principles and Clinical Correlates , pp. 101
    • Kozin, F.1    Cochrane, C.G.2
  • 8
    • 0000619771 scopus 로고
    • Definition and classification of acute-phase proteins
    • Gordon AH, Koj A (eds): Amsterdam, The Netherlands, Elsevier
    • Koj A: Definition and classification of acute-phase proteins, in Gordon AH, Koj A (eds): The Acute-Phase Response to Injury and Infection. Amsterdam, The Netherlands, Elsevier, 1985, p 139
    • (1985) The Acute-Phase Response to Injury and Infection , pp. 139
    • Koj, A.1
  • 10
    • 0025228036 scopus 로고
    • Acute-phase response of human hepatocytes: Regulation of acute-phase protein synthesis by interleukin-6
    • Castell JV. Gómez-Lechón MJ, David M, Fabra R, Trullenque R, Heinrich P: Acute-phase response of human hepatocytes: Regulation of acute-phase protein synthesis by interleukin-6. Hepatology 12:1179, 1990
    • (1990) Hepatology , vol.12 , pp. 1179
    • Castell, J.V.1    Gómez-Lechón, M.J.2    David, M.3    Fabra, R.4    Trullenque, R.5    Heinrich, P.6
  • 11
    • 0025190892 scopus 로고
    • Interleukin-6 and the acute phase response
    • Heinrich PC, Castell JV, Andus T: Interleukin-6 and the acute phase response. Biochem J 265:621, 1990
    • (1990) Biochem J , vol.265 , pp. 621
    • Heinrich, P.C.1    Castell, J.V.2    Andus, T.3
  • 12
    • 0002473674 scopus 로고    scopus 로고
    • Acute phase response
    • Mackiewicz A, Kushner I, Baumann H (eds): Boca Raton, FL, CRC
    • Kushner I, Mackiewicz A: Acute phase response, in Mackiewicz A, Kushner I, Baumann H (eds): Acute Phase Proteins. Boca Raton, FL, CRC, 1996, p 4
    • (1996) Acute Phase Proteins , pp. 4
    • Kushner, I.1    Mackiewicz, A.2
  • 13
    • 0002275085 scopus 로고    scopus 로고
    • The negative acute phase proteins
    • Mackiewicz A, Kushner I, Baumann H (eds): Boca Raton, FL, CRC
    • Aldred AR, Schreiber G: The negative acute phase proteins, in Mackiewicz A, Kushner I, Baumann H (eds): Acute Phase Proteins. Boca Raton, FL, CRC, 1996, p 21
    • (1996) Acute Phase Proteins , pp. 21
    • Aldred, A.R.1    Schreiber, G.2
  • 16
    • 0023739278 scopus 로고
    • Functional discrimination between interleukin-6 and interleukin-1
    • Helle M, Boeije L, Aarden LA: Functional discrimination between interleukin-6 and interleukin-1. Eur J Immunol 18:1535, 1988
    • (1988) Eur J Immunol , vol.18 , pp. 1535
    • Helle, M.1    Boeije, L.2    Aarden, L.A.3
  • 17
    • 0022972464 scopus 로고
    • A highly sensitive cell line, WEHI 164 clone 13, for measuring cytotoxic factor/tumor necrosis from human monocytes
    • Espevik T, Nissen-Meyer J: A highly sensitive cell line, WEHI 164 clone 13, for measuring cytotoxic factor/tumor necrosis from human monocytes. J Immunol Methods 95:99, 1986
    • (1986) J Immunol Methods , vol.95 , pp. 99
    • Espevik, T.1    Nissen-Meyer, J.2
  • 18
    • 0029967088 scopus 로고    scopus 로고
    • Structure/function analysis of human factor XII using recombinant deletion mutants. Evidence for an additional region involved in the binding to negatively charged surfaces
    • Citarella F, Ravon DM, Pascucci B, Felici A, Fantoni A, Hack CE: Structure/function analysis of human factor XII using recombinant deletion mutants. Evidence for an additional region involved in the binding to negatively charged surfaces. Eur J Biochem 238:240, 1996
    • (1996) Eur J Biochem , vol.238 , pp. 240
    • Citarella, F.1    Ravon, D.M.2    Pascucci, B.3    Felici, A.4    Fantoni, A.5    Hack, C.E.6
  • 19
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P, Sacchi N: Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem 162:156, 1987
    • (1987) Anal Biochem , vol.162 , pp. 156
    • Chomczynski, P.1    Sacchi, N.2
  • 20
    • 0026649162 scopus 로고
    • Control of human coagulation by recombinant serine proteases. Blood clotting is activated by recombinant factor XII deleted of five regulatory domains
    • Citarella F, Aiuti A, La Porta C, Russo G, Pietropaolo C, Rinaldi M, Fantoni A: Control of human coagulation by recombinant serine proteases. Blood clotting is activated by recombinant factor XII deleted of five regulatory domains. Eur J Biochem 208:23, 1992
    • (1992) Eur J Biochem , vol.208 , pp. 23
    • Citarella, F.1    Aiuti, A.2    La Porta, C.3    Russo, G.4    Pietropaolo, C.5    Rinaldi, M.6    Fantoni, A.7
  • 23
    • 0019332750 scopus 로고
    • Human hepatocellular carcinoma cell lines secrete the major plasma proteins and hepatitis b surface antigen
    • Knowles BB, Howe CC, Aden DP: Human hepatocellular carcinoma cell lines secrete the major plasma proteins and hepatitis b surface antigen. Science 209:497, 1980
    • (1980) Science , vol.209 , pp. 497
    • Knowles, B.B.1    Howe, C.C.2    Aden, D.P.3
  • 25
    • 0024334846 scopus 로고
    • Interferon β2/interleukin-6 modulates synthesis of α1-antitrypsin in human mononuclear phagocytes and in human hepatoma cells
    • Perlmutter DH, May LT, Sehgal PB: Interferon β2/interleukin-6 modulates synthesis of α1-antitrypsin in human mononuclear phagocytes and in human hepatoma cells. J Clin Invest 84:138, 1989
    • (1989) J Clin Invest , vol.84 , pp. 138
    • Perlmutter, D.H.1    May, L.T.2    Sehgal, P.B.3
  • 26
    • 0023432812 scopus 로고
    • Interferon β2/B-cell stimulatory factor type 2 shares identity with monocyte-derived hepatocyte-stimulating factor and regulates the major acute phase protein response in liver cells
    • Gauldie J, Richards C, Harnish D, Lansdorp PM, Baumann H: Interferon β2/B-cell stimulatory factor type 2 shares identity with monocyte-derived hepatocyte-stimulating factor and regulates the major acute phase protein response in liver cells. Proc Natl Acad Sci USA 84:7251, 1987
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 7251
    • Gauldie, J.1    Richards, C.2    Harnish, D.3    Lansdorp, P.M.4    Baumann, H.5
  • 27
    • 0022976949 scopus 로고
    • Monocyte-conditioned medium, interleukin-1, and tumor necrosis factor stimulate the acute phase response in human hepatoma cells in vitro
    • Darlington GJ, Wilson DR, Lachman LB: Monocyte-conditioned medium, interleukin-1, and tumor necrosis factor stimulate the acute phase response in human hepatoma cells in vitro. J Cell Biol 103:787, 1986
    • (1986) J Cell Biol , vol.103 , pp. 787
    • Darlington, G.J.1    Wilson, D.R.2    Lachman, L.B.3
  • 28
    • 0023555212 scopus 로고
    • Interactions among hepatocyte-stimulating factors, interleukin 1, and glucocorticoids for regulation of acute phase plasma proteins in human hepatoma (HepG2) cells
    • Baumann H, Richards C, Gauldie J: Interactions among hepatocyte-stimulating factors, interleukin 1, and glucocorticoids for regulation of acute phase plasma proteins in human hepatoma (HepG2) cells. J Immunol 139:4122, 1987
    • (1987) J Immunol , vol.139 , pp. 4122
    • Baumann, H.1    Richards, C.2    Gauldie, J.3
  • 29
    • 0026763858 scopus 로고
    • Effects of interleukin-6 on the expression of thyroid hormone-binding protein genes in cultured human hepatoblastoma-derived (HepG2) cells
    • Bartalena L, Farsetti A, Flink IL, Robbins J: Effects of interleukin-6 on the expression of thyroid hormone-binding protein genes in cultured human hepatoblastoma-derived (HepG2) cells. Mol Endocrinol 6:935, 1992
    • (1992) Mol Endocrinol , vol.6 , pp. 935
    • Bartalena, L.1    Farsetti, A.2    Flink, I.L.3    Robbins, J.4
  • 30
    • 0023146694 scopus 로고
    • Purified interleukin-1 (IL-1) from human monocytes stimulates acute-phase protein synthesis by rodent hepatocytes in vitro
    • Gauldie J, Sauder DN, McAdams KPWJ, Dinarello CA: Purified interleukin-1 (IL-1) from human monocytes stimulates acute-phase protein synthesis by rodent hepatocytes in vitro. Immunology 60:203, 1987
    • (1987) Immunology , vol.60 , pp. 203
    • Gauldie, J.1    Sauder, D.N.2    McAdams, K.P.W.J.3    Dinarello, C.A.4
  • 31
    • 0023017916 scopus 로고
    • Cachectin/tumor necrosis factor regulates hepatic acute-phase gene expression
    • Perlmutter DH, Dinarello CA, Punsal PI, Colten HR: Cachectin/tumor necrosis factor regulates hepatic acute-phase gene expression. J Clin Invest 78:1349, 1986
    • (1986) J Clin Invest , vol.78 , pp. 1349
    • Perlmutter, D.H.1    Dinarello, C.A.2    Punsal, P.I.3    Colten, H.R.4
  • 32
    • 0023887261 scopus 로고
    • Recombinant human interleukin-6 (IL-6/BSF-2/HSF) regulates the synthesis of acute phase proteins in human hepatocytes
    • Castell JV, Gómez-Lechón MJ, David M, Hirano T, Kishimoto T, Heinrich PC: Recombinant human interleukin-6 (IL-6/BSF-2/HSF) regulates the synthesis of acute phase proteins in human hepatocytes. FEBS Lett 232:347, 1988
    • (1988) FEBS Lett , vol.232 , pp. 347
    • Castell, J.V.1    Gómez-Lechón, M.J.2    David, M.3    Hirano, T.4    Kishimoto, T.5    Heinrich, P.C.6
  • 35
    • 0023213963 scopus 로고
    • Distinct sets of acute phase plasma proteins are stimulated by separate human hepatocyte-stimulating factors and monokines in rat hepatoma cells
    • Baumann H, Onorato V, Gauldie J, Jahreis GP: Distinct sets of acute phase plasma proteins are stimulated by separate human hepatocyte-stimulating factors and monokines in rat hepatoma cells. J Biol Chem 262:9756, 1987
    • (1987) J Biol Chem , vol.262 , pp. 9756
    • Baumann, H.1    Onorato, V.2    Gauldie, J.3    Jahreis, G.P.4
  • 37
    • 0026081942 scopus 로고
    • Tumor necrosis factor (TNF) inhibits interleukin (IL)-1 and/or IL-6 stimulated synthesis of C-reactive protein (CRP) and serum amyloid A (SAA) in primary cultures of human hepatocytes
    • Yap SH, Moshage HJ, Hazenberg BPC, Roelofs HMJ, Bijzet J, Limburg PC, Aarden LA, van Rijswijk MH: Tumor necrosis factor (TNF) inhibits interleukin (IL)-1 and/or IL-6 stimulated synthesis of C-reactive protein (CRP) and serum amyloid A (SAA) in primary cultures of human hepatocytes. Biochim Biophys Acta Mol Cell Res 1091:405, 1991
    • (1991) Biochim Biophys Acta Mol Cell Res , vol.1091 , pp. 405
    • Yap, S.H.1    Moshage, H.J.2    Hazenberg, B.P.C.3    Roelofs, H.M.J.4    Bijzet, J.5    Limburg, P.C.6    Aarden, L.A.7    Van Rijswijk, M.H.8
  • 38
    • 0025311421 scopus 로고
    • IL-6 functions as an exocrine hormone in inflammation hepatocytes undergoing acute phase responses require exogenous IL-6
    • Gauldie J, Northemann W, Fey GH: IL-6 functions as an exocrine hormone in inflammation hepatocytes undergoing acute phase responses require exogenous IL-6. J Immunol 144:3804, 1990
    • (1990) J Immunol , vol.144 , pp. 3804
    • Gauldie, J.1    Northemann, W.2    Fey, G.H.3
  • 39
    • 0022387743 scopus 로고
    • Pretranslational modulation of acute phase hepatic protein synthesis by murine recombinant interleukin 1 (IL-1) and purified human IL-1
    • Ramadori G, Sipe JD, Dinarello CA, Mizel SB, Colten HR: Pretranslational modulation of acute phase hepatic protein synthesis by murine recombinant interleukin 1 (IL-1) and purified human IL-1. J Exp Med 162:930, 1985
    • (1985) J Exp Med , vol.162 , pp. 930
    • Ramadori, G.1    Sipe, J.D.2    Dinarello, C.A.3    Mizel, S.B.4    Colten, H.R.5
  • 41
    • 0024555358 scopus 로고
    • IL-6 modulates the synthesis of a specific set of acute phase plasma proteins in vivo
    • Marinkovic S, Jahreis GP, Wong GG, Baumann H: IL-6 modulates the synthesis of a specific set of acute phase plasma proteins in vivo. J Immunol 142:808, 1989
    • (1989) J Immunol , vol.142 , pp. 808
    • Marinkovic, S.1    Jahreis, G.P.2    Wong, G.G.3    Baumann, H.4
  • 42
    • 0022973587 scopus 로고
    • Transcriptional regulation of plasma protein synthesis during inflammation
    • Birch HE, Schreiber G: Transcriptional regulation of plasma protein synthesis during inflammation. J Biol Chem 261:8077, 1986
    • (1986) J Biol Chem , vol.261 , pp. 8077
    • Birch, H.E.1    Schreiber, G.2
  • 44
    • 0028804622 scopus 로고
    • Decreased expression of hepatocyte nuclear factor 3α during the acute-phase response influences transthyretin gene transcription
    • Qian X, Samadani U, Porcella A, Costa RH: Decreased expression of hepatocyte nuclear factor 3α during the acute-phase response influences transthyretin gene transcription. Mol Cell Biol 15:1364, 1995
    • (1995) Mol Cell Biol , vol.15 , pp. 1364
    • Qian, X.1    Samadani, U.2    Porcella, A.3    Costa, R.H.4
  • 45
    • 0027263560 scopus 로고
    • Liver-enriched HNF-3α and ubiquitous factors interact with the human transferrin gene enhancer
    • Auge-Gouillou C, Petropoulos I, Zakin MM: Liver-enriched HNF-3α and ubiquitous factors interact with the human transferrin gene enhancer. FEBS Lett 323:4, 1993
    • (1993) FEBS Lett , vol.323 , pp. 4
    • Auge-Gouillou, C.1    Petropoulos, I.2    Zakin, M.M.3
  • 46
    • 0024556115 scopus 로고
    • Multiple hepatocyte-enriched nuclear factor function in the regulation of transthyretin and α1-antitrypsin genes
    • Costa RH, Grayson DR, Darnell JE Jr: Multiple hepatocyte-enriched nuclear factor function in the regulation of transthyretin and α1-antitrypsin genes. Mol Cell Biol 9:1415, 1989
    • (1989) Mol Cell Biol , vol.9 , pp. 1415
    • Costa, R.H.1    Grayson, D.R.2    Darnell Jr., J.E.3
  • 47
    • 0027408905 scopus 로고
    • The 5' sequence of human factor XII gene contains transcription regulatory elements typical of liver specific, estrogen-modulated genes
    • Citarella F, Misiti S, Felici A, Aiuti A, La Porta C, Fantoni A: The 5' sequence of human factor XII gene contains transcription regulatory elements typical of liver specific, estrogen-modulated genes. Biochim Biophys Acta 1172:197, 1993
    • (1993) Biochim Biophys Acta , vol.1172 , pp. 197
    • Citarella, F.1    Misiti, S.2    Felici, A.3    Aiuti, A.4    La Porta, C.5    Fantoni, A.6
  • 48
    • 0028353904 scopus 로고
    • The DNA-binding specifity of the hepatocyte nuclear factor 3/forkhead domain is influenced by amino acid residues adiacent to the recognition helix
    • Overdier DG, Porcella A, Costa RH: The DNA-binding specifity of the hepatocyte nuclear factor 3/forkhead domain is influenced by amino acid residues adiacent to the recognition helix. Mol Cell Biol 14:2755, 1994
    • (1994) Mol Cell Biol , vol.14 , pp. 2755
    • Overdier, D.G.1    Porcella, A.2    Costa, R.H.3
  • 50
    • 0020565895 scopus 로고
    • Thrombosis or myocardial infarction in congenital clotting factor abnormalities and chronic thrombocytopenias: A report of 21 patients and a review of 50 previously reported cases
    • Goodnough LT, Saito H, Ratnoff OD: Thrombosis or myocardial infarction in congenital clotting factor abnormalities and chronic thrombocytopenias: A report of 21 patients and a review of 50 previously reported cases. Medicine 62:248, 1983
    • (1983) Medicine , vol.62 , pp. 248
    • Goodnough, L.T.1    Saito, H.2    Ratnoff, O.D.3
  • 51
    • 0026065260 scopus 로고
    • Thromboembolism and bleeding tendency in congenital factor XII deficiency. A study on 74 subjects from 14 Swiss families
    • Lammle B, Wuillemin WA, Huber I, Krauskopf M, Zürcher C, Pflugshaupt R, Furlan M: Thromboembolism and bleeding tendency in congenital factor XII deficiency. A study on 74 subjects from 14 Swiss families. Thromb Haemost 65:117, 1991
    • (1991) Thromb Haemost , vol.65 , pp. 117
    • Lammle, B.1    Wuillemin, W.A.2    Huber, I.3    Krauskopf, M.4    Zürcher, C.5    Pflugshaupt, R.6    Furlan, M.7
  • 53
    • 0026050749 scopus 로고
    • Reduction of contact activation related fibrinolytic activity in factor XII deficient patients. Further evidence for the role of the contact system in fibrinolysis in vivo
    • Levi M, Hack CE, De Boer JP, Brandjes DPM, Büller HR, ten Cate WJ: Reduction of contact activation related fibrinolytic activity in factor XII deficient patients. Further evidence for the role of the contact system in fibrinolysis in vivo. J Clin Invest 88:1155, 1991
    • (1991) J Clin Invest , vol.88 , pp. 1155
    • Levi, M.1    Hack, C.E.2    De Boer, J.P.3    Brandjes, D.P.M.4    Büller, H.R.5    Ten Cate, W.J.6
  • 54
    • 0029986326 scopus 로고    scopus 로고
    • Inhibition of factor XII in septic baboons attenuates the activation of complement and fibrinolytic systems and reduces the release of interleukin-6 and neutrophil elastase
    • Jansen PM, Pixley RA, Brouwer M, de Jong IW, Chang ACK, Hack CE, Taylor FB Jr, Colman RW: Inhibition of factor XII in septic baboons attenuates the activation of complement and fibrinolytic systems and reduces the release of interleukin-6 and neutrophil elastase. Blood 6:2337, 1996
    • (1996) Blood , vol.6 , pp. 2337
    • Jansen, P.M.1    Pixley, R.A.2    Brouwer, M.3    De Jong, I.W.4    Chang, A.C.K.5    Hack, C.E.6    Taylor Jr., F.B.7    Colman, R.W.8
  • 55
    • 0025495355 scopus 로고
    • Regulation of fibrinogen biosynthesis: Glucocorticoid and interleukin-6 control
    • Amrani DL: Regulation of fibrinogen biosynthesis: Glucocorticoid and interleukin-6 control. Blood Coagul Fibrinolysis 1:443, 1990
    • (1990) Blood Coagul Fibrinolysis , vol.1 , pp. 443
    • Amrani, D.L.1
  • 56
    • 0023262644 scopus 로고
    • Recombinant human B cell stimulatory factor 2 (BSF-2/IFN-β32) regulates β-fibrinogen and albumin mRNA levels in FAO-9 cells
    • Andus T, Geiger T, Hirano T, Northoff H, Ganter U, Bauer J, Kishimoto T, Heinrich PC: Recombinant human B cell stimulatory factor 2 (BSF-2/IFN-β32) regulates β-fibrinogen and albumin mRNA levels in FAO-9 cells. FEBS Lett 221:18, 1987
    • (1987) FEBS Lett , vol.221 , pp. 18
    • Andus, T.1    Geiger, T.2    Hirano, T.3    Northoff, H.4    Ganter, U.5    Bauer, J.6    Kishimoto, T.7    Heinrich, P.C.8
  • 57
    • 0023244665 scopus 로고
    • Induction of fibrinogen and a subset of acute phase response genes involves a novel monokine which is mimicked by phorbol esters
    • Evans E, Courtois GM, Kilian PL, Fuller GM, Crabtree GR: Induction of fibrinogen and a subset of acute phase response genes involves a novel monokine which is mimicked by phorbol esters. J Biol Chem 262:10850, 1987
    • (1987) J Biol Chem , vol.262 , pp. 10850
    • Evans, E.1    Courtois, G.M.2    Kilian, P.L.3    Fuller, G.M.4    Crabtree, G.R.5
  • 58
    • 0019804199 scopus 로고
    • Direct evidence of transcriptional control of fibrinogen and albumin synthesis in rat liver during the acute phase response
    • Princen JMG, Nieuwenhuizen W, Mol-Backx GPBM, Yap SH: Direct evidence of transcriptional control of fibrinogen and albumin synthesis in rat liver during the acute phase response. Biochem Biophys Res Commun 102:717, 1981
    • (1981) Biochem Biophys Res Commun , vol.102 , pp. 717
    • Princen, J.M.G.1    Nieuwenhuizen, W.2    Mol-Backx, G.P.B.M.3    Yap, S.H.4
  • 60
    • 0024562002 scopus 로고
    • Promotion and subsequent inhibition of plasminogen activator after administation of intravenous endotoxin to normal subjects
    • Suffredini AF, Harpel PC, Parillo JE: Promotion and subsequent inhibition of plasminogen activator after administation of intravenous endotoxin to normal subjects. N Engl J Med 18:1165, 1989
    • (1989) N Engl J Med , vol.18 , pp. 1165
    • Suffredini, A.F.1    Harpel, P.C.2    Parillo, J.E.3
  • 61
    • 0001104468 scopus 로고
    • The fast-acting inhibitor of tissue plasminogen activator is an acute phase reactant protein
    • Davidson JF, Donati MB, Coccheri S (eds): Edinburgh, UK, Churchill-Livingstone
    • Juhan-Vague I, Aillaud MF, de Cock F, Philip-Joet C, Arnaud C, Serradimigni A, Collen D: The fast-acting inhibitor of tissue plasminogen activator is an acute phase reactant protein, in Davidson JF, Donati MB, Coccheri S (eds): Progress in Fibrinolysis. Edinburgh, UK, Churchill-Livingstone, 1985, p 146
    • (1985) Progress in Fibrinolysis , pp. 146
    • Juhan-Vague, I.1    Aillaud, M.F.2    De Cock, F.3    Philip-Joet, C.4    Arnaud, C.5    Serradimigni, A.6    Collen, D.7
  • 62
    • 0022201001 scopus 로고
    • The postoperative fibrinolytic shutdown: A rapidly reverting acute phase pattern for the fast-acting inhibitor of tisue-type plasminogen activator after trauma
    • Kluft C, Verheijen JH, Jie AFH, Rijken DC, Preston FE. Sue-Ling HM, Jespersen J, Aasen AO: The postoperative fibrinolytic shutdown: A rapidly reverting acute phase pattern for the fast-acting inhibitor of tisue-type plasminogen activator after trauma. Scand J Clin Lab Invest 45:605, 1985
    • (1985) Scand J Clin Lab Invest , vol.45 , pp. 605
    • Kluft, C.1    Verheijen, J.H.2    Jie, A.F.H.3    Rijken, D.C.4    Preston, F.E.5    Sue-Ling, H.M.6    Jespersen, J.7    Aasen, A.O.8
  • 63
    • 0024376248 scopus 로고
    • Interleukin-1, endotoxin or tumor necrosis factor/cachectin enhance the level of plasminogen activator inhibitor messenger RNA in bovine aortic endothelial cells
    • Medina R, Socher SH, Han JH, Friedman PA: Interleukin-1, endotoxin or tumor necrosis factor/cachectin enhance the level of plasminogen activator inhibitor messenger RNA in bovine aortic endothelial cells. Thromb Res 54:41, 1989
    • (1989) Thromb Res , vol.54 , pp. 41
    • Medina, R.1    Socher, S.H.2    Han, J.H.3    Friedman, P.A.4
  • 64
    • 0022525897 scopus 로고
    • Interleukin 1 and lipopolysaccharide induce an inhibitor of tissue-type plasminogen activator in vivo and in cultured endothelial cells
    • Emeis JJ, Kooistra T: Interleukin 1 and lipopolysaccharide induce an inhibitor of tissue-type plasminogen activator in vivo and in cultured endothelial cells. J Exp Med 163:1260, 1986
    • (1986) J Exp Med , vol.163 , pp. 1260
    • Emeis, J.J.1    Kooistra, T.2
  • 65
    • 0022517446 scopus 로고
    • Interleukin 1 induces endothelial cell synthesis of plasminogen activator inhibitor
    • Nachman RL, Hajjar KA, Silverstein RL, Dinarello CA: Interleukin 1 induces endothelial cell synthesis of plasminogen activator inhibitor. J Exp Med 163:1595, 1986
    • (1986) J Exp Med , vol.163 , pp. 1595
    • Nachman, R.L.1    Hajjar, K.A.2    Silverstein, R.L.3    Dinarello, C.A.4
  • 66
    • 0023727896 scopus 로고
    • Tumor necrosis factor increases the production of plasminogen activator inhibitor in human endothelial cells in vitro and rats in vivo
    • Van Hinsbergh VWM, Kooistra T, van den Berg EA, Princen HMG, Fiers W, Emeis JJ: Tumor necrosis factor increases the production of plasminogen activator inhibitor in human endothelial cells in vitro and rats in vivo. Blood 72:1467, 1988
    • (1988) Blood , vol.72 , pp. 1467
    • Van Hinsbergh, V.W.M.1    Kooistra, T.2    Van Den Berg, E.A.3    Princen, H.M.G.4    Fiers, W.5    Emeis, J.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.