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Volumn 4 E, Issue 1, 2012, Pages 381-391

Posttranslational modifications of tissue factor

Author keywords

Carbohydrate composition; Factor VIIa; Factor X activation; Mass spectrometry; Review; Tissue factor

Indexed keywords

CARBOHYDRATE; CHOLESTEROL; MANNOSE; RECOMBINANT PROTEIN; THROMBOPLASTIN; DISULFIDE; PALMITIC ACID;

EID: 84860849256     PISSN: 19450494     EISSN: 19450508     Source Type: Journal    
DOI: 10.2741/e385     Document Type: Review
Times cited : (11)

References (91)
  • 1
    • 0024386731 scopus 로고
    • Selective cellular expression of tissue factor in human tissues. Implications for disorders of hemostasis and thrombosis
    • Drake, T. A., J. H. Morrissey & T. S. Edgington: Selective cellular expression of tissue factor in human tissues. Implications for disorders of hemostasis and thrombosis. Am J Pathol, 134, 1087-97 (1989)
    • (1989) Am J Pathol , vol.134 , pp. 1087-1097
    • Drake, T.A.1    Morrissey, J.H.2    Edgington, T.S.3
  • 2
    • 0025708079 scopus 로고
    • Localization of human tissue factor antigen by immunostaining with monospecific, polyclonal anti-human tissue factor antibody
    • Fleck, R. A., L. V. Rao, S. I. Rapaport & N. Varki: Localization of human tissue factor antigen by immunostaining with monospecific, polyclonal anti-human tissue factor antibody. Thromb Res, 59, 421-37 (1990)
    • (1990) Thromb Res , vol.59 , pp. 421-437
    • Fleck, R.A.1    Rao, L.V.2    Rapaport, S.I.3    Varki, N.4
  • 3
    • 0027220391 scopus 로고
    • Astrocytes are the primary source of tissue factor in the murine central nervous system. A role for astrocytes in cerebral hemostasis
    • Eddleston, M., J. C. de la Torre, M. B. Oldstone, D. J. Loskutoff, T. S. Edgington & N. Mackman: Astrocytes are the primary source of tissue factor in the murine central nervous system. A role for astrocytes in cerebral hemostasis. J Clin Invest, 92, 349-58 (1993)
    • (1993) J Clin Invest , vol.92 , pp. 349-358
    • Eddleston, M.1    De La Torre, J.C.2    Oldstone, M.B.3    Loskutoff, D.J.4    Edgington, T.S.5    Mackman, N.6
  • 4
    • 0030883109 scopus 로고    scopus 로고
    • Enhanced generation of monocyte tissue factor and increased plasma prothrombin fragment1+2 levels in patients with polycythemia vera: Mechanism of activation of blood coagulation
    • Kornberg, A., N. Rahimi-Levene, R. Yona, A. Mor & E. A. Rachmilewitz: Enhanced generation of monocyte tissue factor and increased plasma prothrombin fragment1+2 levels in patients with polycythemia vera: mechanism of activation of blood coagulation. Am J Hematol, 56, 5-11 (1997)
    • (1997) Am J Hematol , vol.56 , pp. 5-11
    • Kornberg, A.1    Rahimi-Levene, N.2    Yona, R.3    Mor, A.4    Rachmilewitz, E.A.5
  • 5
    • 0035137663 scopus 로고    scopus 로고
    • Tissue factor activity in human monocytes is regulated by plasma: Implications for the high and low responder phenomenon
    • Nijziel, M., R. van Oerle, C. van 't Veer, E. van Pampus, T. Lindhout & K. Hamulyak: Tissue factor activity in human monocytes is regulated by plasma: implications for the high and low responder phenomenon. Br J Haematol, 112, 98-104 (2001)
    • (2001) Br J Haematol , vol.112 , pp. 98-104
    • Nijziel, M.1    Van Oerle, R.2    Van'T Veer, C.3    Van Pampus, E.4    Lindhout, T.5    Hamulyak, K.6
  • 6
    • 0036303892 scopus 로고    scopus 로고
    • Adenosine inhibits tissue factor expression by LPS-stimulated human monocytes: Involvement of the A3 adenosine receptor
    • Broussas, M., P. Cornillet-Lefebvre, G. Potron & P. Nguyen: Adenosine inhibits tissue factor expression by LPS-stimulated human monocytes: involvement of the A3 adenosine receptor. Thromb Haemost, 88, 123-30 (2002)
    • (2002) Thromb Haemost , vol.88 , pp. 123-130
    • Broussas, M.1    Cornillet-Lefebvre, P.2    Potron, G.3    Nguyen, P.4
  • 8
    • 15244351287 scopus 로고    scopus 로고
    • Tissue factor in the myocardium: Evidence of roles in haemostasis and inflammation
    • Mumford, A. D. & J. H. McVey: Tissue factor in the myocardium: evidence of roles in haemostasis and inflammation. Dis Markers, 20, 353-8 (2004)
    • (2004) Dis Markers , vol.20 , pp. 353-358
    • Mumford, A.D.1    McVey, J.H.2
  • 9
    • 0027402655 scopus 로고
    • Quantitation of activated factor VII levels in plasma using a tissue factor mutant selectively deficient in promoting factor VII activation
    • Morrissey, J. H., B. G. Macik, P. F. Neuenschwander & P. C. Comp: Quantitation of activated factor VII levels in plasma using a tissue factor mutant selectively deficient in promoting factor VII activation. Blood, 81, 734-44 (1993)
    • (1993) Blood , vol.81 , pp. 734-744
    • Morrissey, J.H.1    Macik, B.G.2    Neuenschwander, P.F.3    Comp, P.C.4
  • 11
    • 0025662050 scopus 로고
    • Post-translational modifications of recombinant human tissue factor
    • Paborsky, L. R. & R. J. Harris: Post-translational modifications of recombinant human tissue factor. Thromb Res, 60, 367-76 (1990)
    • (1990) Thromb Res , vol.60 , pp. 367-376
    • Paborsky, L.R.1    Harris, R.J.2
  • 12
    • 0024286076 scopus 로고
    • Human tissue factor contains thioester-linked palmitate and stearate on the cytoplasmic half-cystine
    • Bach, R., W. H. Konigsberg & Y. Nemerson: Human tissue factor contains thioester-linked palmitate and stearate on the cytoplasmic half-cystine. Biochemistry, 27, 4227-31 (1988)
    • (1988) Biochemistry , vol.27 , pp. 4227-4231
    • Bach, R.1    Konigsberg, W.H.2    Nemerson, Y.3
  • 13
    • 0026782822 scopus 로고
    • The cytoplasmic domain of tissue factor is phosphorylated by a protein kinase C-dependent mechanism
    • Zioncheck, T. F., S. Roy & G. A. Vehar: The cytoplasmic domain of tissue factor is phosphorylated by a protein kinase C-dependent mechanism. J Biol Chem, 267, 3561-4 (1992)
    • (1992) J Biol Chem , vol.267 , pp. 3561-3634
    • Zioncheck, T.F.1    Roy, S.2    Vehar, G.A.3
  • 14
    • 0027096061 scopus 로고
    • Protein Syn thesis, posttranslational modifications, and aging
    • Rattan, S. I., A. Derventzi & B. F. Clark: Protein synthesis, posttranslational modifications, and aging. Ann N Y Acad Sci, 663, 48-62 (1992)
    • (1992) Ann N y Acad Sci , vol.663 , pp. 48-62
    • Rattan, S.I.1    Derventzi, A.2    Clark, B.F.3
  • 15
    • 0042266719 scopus 로고    scopus 로고
    • A genetic approach to Mammalian glycan function
    • Lowe, J. B. & J. D. Marth: A genetic approach to Mammalian glycan function. Annu Rev Biochem, 72, 643-91 (2003)
    • (2003) Annu Rev Biochem , vol.72 , pp. 643-691
    • Lowe, J.B.1    Marth, J.D.2
  • 16
    • 28444447140 scopus 로고    scopus 로고
    • Large-scale approaches for glycobiology
    • Campbell, C. T. & K. J. Yarema: Large-scale approaches for glycobiology. Genome Biol, 6, 236 (2005)
    • (2005) Genome Biol , vol.6 , pp. 236
    • Campbell, C.T.1    Yarema, K.J.2
  • 17
    • 0014958989 scopus 로고
    • Purification and characterization of the protein component of tissue factor
    • Nemerson, Y. & F. A. Pitlick: Purification and characterization of the protein component of tissue factor. Biochemistry, 9, 5100-5 (1970)
    • (1970) Biochemistry , vol.9 , pp. 5100-5155
    • Nemerson, Y.1    Pitlick, F.A.2
  • 18
    • 0016428569 scopus 로고
    • Concanavalin A inhibits tissue factor coagulant activity
    • Pitlick, F. A.: Concanavalin A inhibits tissue factor coagulant activity. J Clin Invest, 55, 175-9 (1975)
    • (1975) J Clin Invest , vol.55 , pp. 175-179
    • Pitlick, F.A.1
  • 19
    • 0001697163 scopus 로고
    • Protein-Carbohydrate Interaction. Ii. Inhibition Studies on the Interaction of Concanavalin a with Polysaccharides
    • Goldstein, I. J., C. E. Hollerman & E. E. Smith: Protein-Carbohydrate Interaction. Ii. Inhibition Studies on the Interaction of Concanavalin a with Polysaccharides. Biochemistry, 4, 876-83 (1965)
    • (1965) Biochemistry , vol.4 , pp. 876-883
    • Goldstein, I.J.1    Hollerman, C.E.2    Smith, E.E.3
  • 20
    • 0021179063 scopus 로고
    • Interaction of thromboplastin apoprotein of different tissues with concanavalin A-evidence for heterogeneous glycosylation of the human apoprotein
    • van den Besselaar, A. M. & R. M. Bertina: Interaction of thromboplastin apoprotein of different tissues with concanavalin A-evidence for heterogeneous glycosylation of the human apoprotein. Thromb Haemost, 52, 192-5 (1984)
    • (1984) Thromb Haemost , vol.52 , pp. 192-195
    • Van Den Besselaar, A.M.1    Bertina, R.M.2
  • 21
    • 0018721020 scopus 로고
    • Biological activities of the two major components of tunicamycin
    • Mahoney, W. C. & D. Duksin: Biological activities of the two major components of tunicamycin. J Biol Chem, 254, 6572-6 (1979)
    • (1979) J Biol Chem , vol.254 , pp. 6572-6666
    • Mahoney, W.C.1    Duksin, D.2
  • 22
    • 0021962871 scopus 로고
    • Macrophage factor X activator formation: Metabolic requirements for synthesis of components
    • Shands, J. W., Jr.: Macrophage factor X activator formation: metabolic requirements for synthesis of components. Blood, 65, 169-75 (1985)
    • (1985) Blood , vol.65 , pp. 169-175
    • Shands Jr., J.W.1
  • 23
    • 0026736047 scopus 로고
    • Tissue factor and its extracellular soluble domain: The relationship between intermolecular association with factor VIIa and enzymatic activity of the complex
    • Waxman, E., J. B. Ross, T. M. Laue, A. Guha, S. V. Thiruvikraman, T. C. Lin, W. H. Konigsberg & Y. Nemerson: Tissue factor and its extracellular soluble domain: the relationship between intermolecular association with factor VIIa and enzymatic activity of the complex. Biochemistry, 31, 3998-4003 (1992)
    • (1992) Biochemistry , vol.31 , pp. 3998-4003
    • Waxman, E.1    Ross, J.B.2    Laue, T.M.3    Guha, A.4    Thiruvikraman, S.V.5    Lin, T.C.6    Konigsberg, W.H.7    Nemerson, Y.8
  • 24
    • 0029051814 scopus 로고
    • Recombinant soluble human tissue factor secreted by Saccharomyces cerevisiae and refolded from Escherichia coli inclusion bodies: Glycosylation of mutants, activity and physical characterization
    • Stone, M. J., W. Ruf, D. J. Miles, T. S. Edgington & P. E. Wright: Recombinant soluble human tissue factor secreted by Saccharomyces cerevisiae and refolded from Escherichia coli inclusion bodies: glycosylation of mutants, activity and physical characterization. Biochem J, 310 (Pt 2), 605-14 (1995)
    • (1995) Biochem J , vol.310 , Issue.PART 2 , pp. 605-614
    • Stone, M.J.1    Ruf, W.2    Miles, D.J.3    Edgington, T.S.4    Wright, P.E.5
  • 25
    • 0028157535 scopus 로고
    • The biochemical basis for the apparent defect of soluble mutant tissue factor in enhancing the proteolytic activities of factor VIIa
    • Fiore, M. M., P. F. Neuenschwander & J. H. Morrissey: The biochemical basis for the apparent defect of soluble mutant tissue factor in enhancing the proteolytic activities of factor VIIa. J Biol Chem, 269, 143-9 (1994)
    • (1994) J Biol Chem , vol.269 , pp. 143-149
    • Fiore, M.M.1    Neuenschwander, P.F.2    Morrissey, J.H.3
  • 26
    • 77449161190 scopus 로고    scopus 로고
    • Carbohydrates and activity of natural and recombinant tissue factor
    • Krudysz-Amblo, J., M. E. Jennings, 2nd, K. G. Mann & S. Butenas: Carbohydrates and activity of natural and recombinant tissue factor. J Biol Chem, 285, 3371-82 (2010)
    • (2010) J Biol Chem , vol.285 , pp. 3371-3382
    • Krudysz-Amblo, J.1    Jennings, M.E.2    Mann II, K.G.3    Butenas, S.4
  • 27
    • 58249093866 scopus 로고    scopus 로고
    • Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms
    • Ruiz-Canada, C., D. J. Kelleher & R. Gilmore: Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms. Cell, 136, 272-83 (2009)
    • (2009) Cell , vol.136 , pp. 272-283
    • Ruiz-Canada, C.1    Kelleher, D.J.2    Gilmore, R.3
  • 28
    • 0017753965 scopus 로고
    • Synchronised transmembrane insertion and glycosylation of a nascent membrane protein
    • Rothman, J. E. & H. F. Lodish: Synchronised transmembrane insertion and glycosylation of a nascent membrane protein. Nature, 269, 775-80 (1977)
    • (1977) Nature , vol.269 , pp. 775-780
    • Rothman, J.E.1    Lodish, H.F.2
  • 29
    • 0029049090 scopus 로고
    • Cotranslational folding and calnexin binding during glycoprotein synthesis
    • Chen, W., J. Helenius, I. Braakman & A. Helenius: Cotranslational folding and calnexin binding during glycoprotein synthesis. Proc Natl Acad Sci U S A, 92, 6229-33 (1995)
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 6229-6233
    • Chen, W.1    Helenius, J.2    Braakman, I.3    Helenius, A.4
  • 30
    • 33645103490 scopus 로고    scopus 로고
    • An evolving view of the eukaryotic oligosaccharyltransferase
    • Kelleher, D. J. & R. Gilmore: An evolving view of the eukaryotic oligosaccharyltransferase. Glycobiology, 16, 47R-62R (2006)
    • (2006) Glycobiology , vol.16
    • Kelleher, D.J.1    Gilmore, R.2
  • 31
    • 7244254552 scopus 로고    scopus 로고
    • Comparing N-glycan processing in mammalian cell lines to native and engineered lepidopteran insect cell lines
    • Tomiya, N., S. Narang, Y. C. Lee & M. J. Betenbaugh: Comparing N-glycan processing in mammalian cell lines to native and engineered lepidopteran insect cell lines. Glycoconj J, 21, 343-60 (2004)
    • (2004) Glycoconj J , vol.21 , pp. 343-360
    • Tomiya, N.1    Narang, S.2    Lee, Y.C.3    Betenbaugh, M.J.4
  • 32
    • 0027772780 scopus 로고
    • Processing of asparagine-linked oligosaccharides in insect cells. N-acetylglucosaminyltransferase i and II activities in cultured lepidopteran cells
    • Altmann, F., G. Kornfeld, T. Dalik, E. Staudacher & J. Glossl: Processing of asparagine-linked oligosaccharides in insect cells. N-acetylglucosaminyltransferase I and II activities in cultured lepidopteran cells. Glycobiology, 3, 619-25 (1993)
    • (1993) Glycobiology , vol.3 , pp. 619-625
    • Altmann, F.1    Kornfeld, G.2    Dalik, T.3    Staudacher, E.4    Glossl, J.5
  • 33
    • 45549087961 scopus 로고    scopus 로고
    • A fused lobes gene encodes the processing beta-N-acetylglucosaminidase in Sf9 cells
    • Geisler, C., J. J. Aumiller & D. L. Jarvis: A fused lobes gene encodes the processing beta-N-acetylglucosaminidase in Sf9 cells. J Biol Chem, 283, 11330-9 (2008)
    • (2008) J Biol Chem , vol.283 , pp. 11330-12119
    • Geisler, C.1    Aumiller, J.J.2    Jarvis, D.L.3
  • 34
    • 0025821169 scopus 로고
    • The integrity of the cysteine 186-cysteine 209 bond of the second disulfide loop of tissue factor is required for binding of factor VII
    • Rehemtulla, A., W. Ruf & T. S. Edgington: The integrity of the cysteine 186-cysteine 209 bond of the second disulfide loop of tissue factor is required for binding of factor VII. J Biol Chem, 266, 10294-9 (1991)
    • (1991) J Biol Chem , vol.266 , pp. 10294-11109
    • Rehemtulla, A.1    Ruf, W.2    Edgington, T.S.3
  • 35
    • 0023614769 scopus 로고
    • Tissue factor apoprotein: Intracellular transport and expression in shed membrane vesicles
    • Bona, R., E. Lee & F. Rickles: Tissue factor apoprotein: intracellular transport and expression in shed membrane vesicles. Thromb Res, 48, 487-500 (1987)
    • (1987) Thromb Res , vol.48 , pp. 487-500
    • Bona, R.1    Lee, E.2    Rickles, F.3
  • 36
    • 0019982538 scopus 로고
    • The role of protein phosphorylation in neural and hormonal control of cellular activity
    • Cohen, P.: The role of protein phosphorylation in neural and hormonal control of cellular activity. Nature, 296, 613-20 (1982)
    • (1982) Nature , vol.296 , pp. 613-620
    • Cohen, P.1
  • 37
    • 0030751868 scopus 로고    scopus 로고
    • Tissue factor cytoplasmic domain peptide is multiply phosphorylated in vitro
    • Mody, R. S. & S. D. Carson: Tissue factor cytoplasmic domain peptide is multiply phosphorylated in vitro. Biochemistry, 36, 7869-75 (1997)
    • (1997) Biochemistry , vol.36 , pp. 7869-7875
    • Mody, R.S.1    Carson, S.D.2
  • 38
    • 0344826105 scopus 로고    scopus 로고
    • Regulation of tissue factor cytoplasmic domain phosphorylation by palmitoylation
    • Dorfleutner, A. & W. Ruf: Regulation of tissue factor cytoplasmic domain phosphorylation by palmitoylation. Blood, 102, 3998-4005 (2003)
    • (2003) Blood , vol.102 , pp. 3998-4005
    • Dorfleutner, A.1    Ruf, W.2
  • 39
    • 0025673917 scopus 로고
    • Endotoxin-mediated bovine alveolar macrophage procoagulant induction is dependent on protein kinase C activation
    • Car, B. D., D. O. Slauson, M. Dore & M. M. Suyemoto: Endotoxin-mediated bovine alveolar macrophage procoagulant induction is dependent on protein kinase C activation. Inflammation, 14, 681-9 (1990)
    • (1990) Inflammation , vol.14 , pp. 681-689
    • Car, B.D.1    Slauson, D.O.2    Dore, M.3    Suyemoto, M.M.4
  • 40
    • 0023052241 scopus 로고
    • Studies and perspectives of protein kinase C
    • Nishizuka, Y.: Studies and perspectives of protein kinase C. Science, 233, 305-12 (1986)
    • (1986) Science , vol.233 , pp. 305-312
    • Nishizuka, Y.1
  • 43
    • 2442647329 scopus 로고    scopus 로고
    • Protease-activated receptor 2-dependent phosphorylation of the tissue factor cytoplasmic domain
    • Ahamed, J. & W. Ruf: Protease-activated receptor 2-dependent phosphorylation of the tissue factor cytoplasmic domain. J Biol Chem, 279, 23038-44 (2004)
    • (2004) J Biol Chem , vol.279 , pp. 23038-23244
    • Ahamed, J.1    Ruf, W.2
  • 44
    • 77951209407 scopus 로고    scopus 로고
    • Evidence for tissue factor phosphorylation and its correlation with protease-activated receptor expression and the prognosis of primary breast cancer
    • Ryden, L., D. Grabau, F. Schaffner, P. E. Jonsson, W. Ruf & M. Belting: Evidence for tissue factor phosphorylation and its correlation with protease-activated receptor expression and the prognosis of primary breast cancer. Int J Cancer, 126, 2330-40 (2010)
    • (2010) Int J Cancer , vol.126 , pp. 2330-2340
    • Ryden, L.1    Grabau, D.2    Schaffner, F.3    Jonsson, P.E.4    Ruf, W.5    Belting, M.6
  • 45
    • 0022065554 scopus 로고
    • Two classes of fatty acid acylated proteins exist in eukaryotic cells
    • Magee, A. I. & S. A. Courtneidge: Two classes of fatty acid acylated proteins exist in eukaryotic cells. EMBO J, 4, 1137-44 (1985)
    • (1985) EMBO J , vol.4 , pp. 1137-1144
    • Magee, A.I.1    Courtneidge, S.A.2
  • 46
    • 0033540056 scopus 로고    scopus 로고
    • Ghrelin is a growth-hormonereleasing acylated peptide from stomach
    • Kojima, M., H. Hosoda, Y. Date, M. Nakazato, H. Matsuo & K. Kangawa: Ghrelin is a growth-hormonereleasing acylated peptide from stomach. Nature, 402, 656-60 (1999)
    • (1999) Nature , vol.402 , pp. 656-660
    • Kojima, M.1    Hosoda, H.2    Date, Y.3    Nakazato, M.4    Matsuo, H.5    Kangawa, K.6
  • 47
    • 0031596205 scopus 로고    scopus 로고
    • Acylation of Escherichia coli hemolysin: A unique protein lipidation mechanism underlying toxin function
    • Stanley, P., V. Koronakis & C. Hughes: Acylation of Escherichia coli hemolysin: a unique protein lipidation mechanism underlying toxin function. Microbiol Mol Biol Rev, 62, 309-33 (1998)
    • (1998) Microbiol Mol Biol Rev , vol.62 , pp. 309-333
    • Stanley, P.1    Koronakis, V.2    Hughes, C.3
  • 48
    • 0028151351 scopus 로고
    • Interactions between saturated acyl chains confer detergent resistance on lipids and glycosylphosphatidylinositol (GPI)-anchored proteins: GPI-anchored proteins in liposomes and cells show similar behavior
    • Schroeder, R., E. London & D. Brown: Interactions between saturated acyl chains confer detergent resistance on lipids and glycosylphosphatidylinositol (GPI)-anchored proteins: GPI-anchored proteins in liposomes and cells show similar behavior. Proc Natl Acad Sci U S A, 91, 12130-4 (1994)
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 12130-13124
    • Schroeder, R.1    London, E.2    Brown, D.3
  • 50
    • 0022472138 scopus 로고
    • Affinity purification of human tissue factor: Interaction of factor VII and tissue factor in detergent micelles
    • Guha, A., R. Bach, W. Konigsberg & Y. Nemerson: Affinity purification of human tissue factor: interaction of factor VII and tissue factor in detergent micelles. Proc Natl Acad Sci U S A, 83, 299-302 (1986)
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 299-302
    • Guha, A.1    Bach, R.2    Konigsberg, W.3    Nemerson, Y.4
  • 51
    • 0023830182 scopus 로고
    • Protein co-isolated with human tissue factor impairs recovery of activity
    • Carson, S. D., S. E. Ross & R. A. Gramzinski: Protein co-isolated with human tissue factor impairs recovery of activity. Blood, 71, 520-3 (1988)
    • (1988) Blood , vol.71 , pp. 520-523
    • Carson, S.D.1    Ross, S.E.2    Gramzinski, R.A.3
  • 52
    • 0025756188 scopus 로고
    • Selfassociation of tissue factor as revealed by chemical crosslinking
    • Roy, S., L. R. Paborsky & G. A. Vehar: Selfassociation of tissue factor as revealed by chemical crosslinking. J Biol Chem, 266, 4665-8 (1991)
    • (1991) J Biol Chem , vol.266 , pp. 4665-4748
    • Roy, S.1    Paborsky, L.R.2    Vehar, G.A.3
  • 53
    • 0031005422 scopus 로고    scopus 로고
    • Mechanism of tissue factor activation on HL-60 cells
    • Bach, R. R. & C. F. Moldow: Mechanism of tissue factor activation on HL-60 cells. Blood, 89, 3270-6 (1997)
    • (1997) Blood , vol.89 , pp. 3270-3336
    • Bach, R.R.1    Moldow, C.F.2
  • 55
    • 0034687096 scopus 로고    scopus 로고
    • Dimerization of tissue factor supports solution-phase autoactivation of factor VII without influencing proteolytic activation of factor X
    • Donate, F., C. R. Kelly, W. Ruf & T. S. Edgington: Dimerization of tissue factor supports solution-phase autoactivation of factor VII without influencing proteolytic activation of factor X. Biochemistry, 39, 11467-76 (2000)
    • (2000) Biochemistry , vol.39 , pp. 11467-12176
    • Donate, F.1    Kelly, C.R.2    Ruf, W.3    Edgington, T.S.4
  • 56
    • 0037959071 scopus 로고    scopus 로고
    • The state of lipid rafts: From model membranes to cells
    • Edidin, M.: The state of lipid rafts: from model membranes to cells. Annu Rev Biophys Biomol Struct, 32, 257-83 (2003)
    • (2003) Annu Rev Biophys Biomol Struct , vol.32 , pp. 257-283
    • Edidin, M.1
  • 57
    • 18044384665 scopus 로고    scopus 로고
    • Studies on rabbit natural and recombinant tissue factors: Intracellular retention and regulation of surface expression in cultured cells
    • Fortin, J. P., G. E. Rivard, A. Adam & F. Marceau: Studies on rabbit natural and recombinant tissue factors: intracellular retention and regulation of surface expression in cultured cells. Am J Physiol Heart Circ Physiol, 288, H2192-202 (2005)
    • (2005) Am J Physiol Heart Circ Physiol , vol.288
    • Fortin, J.P.1    Rivard, G.E.2    Adam, A.3    Marceau, F.4
  • 58
    • 33745063172 scopus 로고    scopus 로고
    • Cellular localization and trafficking of tissue factor
    • Mandal, S. K., U. R. Pendurthi & L. V. Rao: Cellular localization and trafficking of tissue factor. Blood, 107, 4746-53 (2006)
    • (2006) Blood , vol.107 , pp. 4746-4753
    • Mandal, S.K.1    Pendurthi, U.R.2    Rao, L.V.3
  • 59
    • 15844369922 scopus 로고    scopus 로고
    • Ligand-induced protease receptor translocation into caveolae: A mechanism for regulating cell surface proteolysis of the tissue factordependent coagulation pathway
    • Sevinsky, J. R., L. V. Rao & W. Ruf: Ligand-induced protease receptor translocation into caveolae: a mechanism for regulating cell surface proteolysis of the tissue factordependent coagulation pathway. J Cell Biol, 133, 293-304 (1996)
    • (1996) J Cell Biol , vol.133 , pp. 293-304
    • Sevinsky, J.R.1    Rao, L.V.2    Ruf, W.3
  • 60
    • 11144223766 scopus 로고    scopus 로고
    • Acute cholesterol depletion impairs functional expression of tissue factor in fibroblasts: Modulation of tissue factor activity by membrane cholesterol
    • Mandal, S. K., A. Iakhiaev, U. R. Pendurthi & L. V. Rao: Acute cholesterol depletion impairs functional expression of tissue factor in fibroblasts: modulation of tissue factor activity by membrane cholesterol. Blood, 105, 153-60 (2005)
    • (2005) Blood , vol.105 , pp. 153-160
    • Mandal, S.K.1    Iakhiaev, A.2    Pendurthi, U.R.3    Rao, L.V.4
  • 61
    • 1842526964 scopus 로고    scopus 로고
    • Lipid rafts are necessary for tonic inhibition of cellular tissue factor procoagulant activity
    • Dietzen, D. J., K. L. Page & T. A. Tetzloff: Lipid rafts are necessary for tonic inhibition of cellular tissue factor procoagulant activity. Blood, 103, 3038-44 (2004)
    • (2004) Blood , vol.103 , pp. 3038-3044
    • Dietzen, D.J.1    Page, K.L.2    Tetzloff, T.A.3
  • 62
    • 23944509766 scopus 로고    scopus 로고
    • Tissue-factor-bearing microvesicles arise from lipid rafts and fuse with activated platelets to initiate coagulation
    • Del Conde, I., C. N. Shrimpton, P. Thiagarajan & J. A. Lopez: Tissue-factor-bearing microvesicles arise from lipid rafts and fuse with activated platelets to initiate coagulation. Blood, 106, 1604-11 (2005)
    • (2005) Blood , vol.106 , pp. 1604-1611
    • Del Conde, I.1    Shrimpton, C.N.2    Thiagarajan, P.3    Lopez, J.A.4
  • 63
    • 0031455589 scopus 로고    scopus 로고
    • Caveolin interaction with protein kinase C. Isoenzymedependent regulation of kinase activity by the caveolin scaffolding domain peptide
    • Oka, N., M. Yamamoto, C. Schwencke, J. Kawabe, T. Ebina, S. Ohno, J. Couet, M. P. Lisanti & Y. Ishikawa: Caveolin interaction with protein kinase C. Isoenzymedependent regulation of kinase activity by the caveolin scaffolding domain peptide. J Biol Chem, 272, 33416-21 (1997)
    • (1997) J Biol Chem , vol.272 , pp. 33416-34321
    • Oka, N.1    Yamamoto, M.2    Schwencke, C.3    Kawabe, J.4    Ebina, T.5    Ohno, S.6    Couet, J.7    Lisanti, M.P.8    Ishikawa, Y.9
  • 65
    • 0028085405 scopus 로고
    • The effect of calcium ionophore A23187 on tissue factor activity and mRNA in endothelial cells
    • Wakita, K., D. J. Stearns-Kurosawa & Y. Marumoto: The effect of calcium ionophore A23187 on tissue factor activity and mRNA in endothelial cells. Thromb Res, 74, 95-103 (1994)
    • (1994) Thromb Res , vol.74 , pp. 95-103
    • Wakita, K.1    Stearns-Kurosawa, D.J.2    Marumoto, Y.3
  • 66
    • 0024996842 scopus 로고
    • Expression of tissue factor procoagulant activity: Regulation by cytosolic calcium
    • Bach, R. & D. B. Rifkin: Expression of tissue factor procoagulant activity: regulation by cytosolic calcium. Proc Natl Acad Sci U S A, 87, 6995-9 (1990)
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 6995-7069
    • Bach, R.1    Rifkin, D.B.2
  • 67
    • 33847239086 scopus 로고    scopus 로고
    • Calcium ionophore-induced de-encryption of tissue factor in monocytes is associated with extensive cell death
    • Henriksson, C. E., O. Klingenberg, M. Hellum, K. S. Landsverk, G. B. Joo, A. B. Westvik & P. Kierulf: Calcium ionophore-induced de-encryption of tissue factor in monocytes is associated with extensive cell death. Thromb Res, 119, 621-30 (2007)
    • (2007) Thromb Res , vol.119 , pp. 621-630
    • Henriksson, C.E.1    Klingenberg, O.2    Hellum, M.3    Landsverk, K.S.4    Joo, G.B.5    Westvik, A.B.6    Kierulf, P.7
  • 68
    • 45949085404 scopus 로고    scopus 로고
    • Membrane environment rather than tissue factor expression determines thrombin formation triggered by monocytic cells undergoing apoptosis
    • Stampfuss, J. J., P. Censarek, D. Bein, K. Schror, M. Grandoch, C. Naber & A. A. Weber: Membrane environment rather than tissue factor expression determines thrombin formation triggered by monocytic cells undergoing apoptosis. J Leukoc Biol, 83, 1379-81 (2008)
    • (2008) J Leukoc Biol , vol.83 , pp. 1379-1381
    • Stampfuss, J.J.1    Censarek, P.2    Bein, D.3    Schror, K.4    Grandoch, M.5    Naber, C.6    Weber, A.A.7
  • 69
    • 0028277701 scopus 로고
    • Fibroblast tissue factor: Calcium and ionophore induce shape changes, release of membrane vesicles, and redistribution of tissue factor antigen in addition to increased procoagulant activity
    • Carson, S. D., G. A. Perry & S. J. Pirruccello: Fibroblast tissue factor: calcium and ionophore induce shape changes, release of membrane vesicles, and redistribution of tissue factor antigen in addition to increased procoagulant activity. Blood, 84, 526-34 (1994)
    • (1994) Blood , vol.84 , pp. 526-534
    • Carson, S.D.1    Perry, G.A.2    Pirruccello, S.J.3
  • 71
    • 34547899924 scopus 로고    scopus 로고
    • Persistence of phosphatidylserine exposure on activated platelets in vivo in rabbits
    • Rand, M. L., H. Wang, K. W. Bang, M. A. Packham & J. Freedman: Persistence of phosphatidylserine exposure on activated platelets in vivo in rabbits. Thromb Haemost, 98, 477-8 (2007)
    • (2007) Thromb Haemost , vol.98 , pp. 477-478
    • Rand, M.L.1    Wang, H.2    Bang, K.W.3    Packham, M.A.4    Freedman, J.5
  • 72
    • 33846415830 scopus 로고    scopus 로고
    • Cholesterol enrichment of human monocyte/macrophages induces surface exposure of phosphatidylserine and the release of biologically-active tissue factor-positive microvesicles
    • Liu, M. L., M. P. Reilly, P. Casasanto, S. E. McKenzie & K. J. Williams: Cholesterol enrichment of human monocyte/macrophages induces surface exposure of phosphatidylserine and the release of biologically-active tissue factor-positive microvesicles. Arterioscler Thromb Vasc Biol, 27, 430-5 (2007)
    • (2007) Arterioscler Thromb Vasc Biol , vol.27 , pp. 430-435
    • Liu, M.L.1    Reilly, M.P.2    Casasanto, P.3    McKenzie, S.E.4    Williams, K.J.5
  • 73
    • 0022480078 scopus 로고
    • Enhancement of mononuclear procoagulant activity by platelet 12-hydroxyeicosatetraenoic acid
    • Lorenzet, R., J. Niemetz, A. J. Marcus & M. J. Broekman: Enhancement of mononuclear procoagulant activity by platelet 12-hydroxyeicosatetraenoic acid. J Clin Invest, 78, 418-23 (1986)
    • (1986) J Clin Invest , vol.78 , pp. 418-423
    • Lorenzet, R.1    Niemetz, J.2    Marcus, A.J.3    Broekman, M.J.4
  • 74
    • 0027440076 scopus 로고
    • Granulocytes enhance LPS-induced tissue factor activity in monocytes via an interaction with platelets
    • Halvorsen, H., J. O. Olsen & B. Osterud: Granulocytes enhance LPS-induced tissue factor activity in monocytes via an interaction with platelets. J Leukoc Biol, 54, 275-82 (1993)
    • (1993) J Leukoc Biol , vol.54 , pp. 275-282
    • Halvorsen, H.1    Olsen, J.O.2    Osterud, B.3
  • 75
    • 0034125350 scopus 로고    scopus 로고
    • Induction of tissue factor expression in whole blood: Lack of evidence for the presence of tissue factor expression in granulocytes
    • Osterud, B., L. V. Rao & J. O. Olsen: Induction of tissue factor expression in whole blood: lack of evidence for the presence of tissue factor expression in granulocytes. Thromb Haemost, 83, 861-7 (2000)
    • (2000) Thromb Haemost , vol.83 , pp. 861-867
    • Osterud, B.1    Rao, L.V.2    Olsen, J.O.3
  • 76
    • 33749366436 scopus 로고    scopus 로고
    • Evidence for activation of tissue factor by an allosteric disulfide bond
    • Chen, V. M., J. Ahamed, H. H. Versteeg, M. C. Berndt, W. Ruf & P. J. Hogg: Evidence for activation of tissue factor by an allosteric disulfide bond. Biochemistry, 45, 12020-8 (2006)
    • (2006) Biochemistry , vol.45 , pp. 12020-12128
    • Chen, V.M.1    Ahamed, J.2    Versteeg, H.H.3    Berndt, M.C.4    Ruf, W.5    Hogg, P.J.6
  • 77
    • 0024978434 scopus 로고
    • Chemical modification of chalcone isomerase by mercurials and tetrathionate. Evidence for a single cysteine residue in the active site
    • Bednar, R. A., W. B. Fried, Y. W. Lock & B. Pramanik: Chemical modification of chalcone isomerase by mercurials and tetrathionate. Evidence for a single cysteine residue in the active site. J Biol Chem, 264, 14272-6 (1989)
    • (1989) J Biol Chem , vol.264 , pp. 14272-15146
    • Bednar, R.A.1    Fried, W.B.2    Lock, Y.W.3    Pramanik, B.4
  • 79
    • 0028226060 scopus 로고
    • Mercury compounds induce a rapid increase in procoagulant activity of monocyte-like U937 cells
    • Kaneko, H., V. V. Kakkar & M. F. Scully: Mercury compounds induce a rapid increase in procoagulant activity of monocyte-like U937 cells. Br J Haematol, 87, 87-93 (1994)
    • (1994) Br J Haematol , vol.87 , pp. 87-93
    • Kaneko, H.1    Kakkar, V.V.2    Scully, M.F.3
  • 81
    • 77958522684 scopus 로고    scopus 로고
    • Effect of protein disulfide isomerase chaperone activity inhibition on tissue factor activity
    • Raturi, A. & W. Ruf: Effect of protein disulfide isomerase chaperone activity inhibition on tissue factor activity. J Thromb Haemost, 8, 1863-5 (2010)
    • (2010) J Thromb Haemost , vol.8 , pp. 1863-1915
    • Raturi, A.1    Ruf, W.2
  • 82
    • 34548494139 scopus 로고    scopus 로고
    • Tissue factor coagulant function is enhanced by protein-disulfide isomerase independent of oxidoreductase activity
    • Versteeg, H. H. & W. Ruf: Tissue factor coagulant function is enhanced by protein-disulfide isomerase independent of oxidoreductase activity. J Biol Chem, 282, 25416-24 (2007)
    • (2007) J Biol Chem , vol.282 , pp. 25416-26224
    • Versteeg, H.H.1    Ruf, W.2
  • 84
    • 48449100433 scopus 로고    scopus 로고
    • Protein disulfide isomerase as a trigger for tissue factor-dependent fibrin generation
    • Manukyan, D., M. L. von Bruehl, S. Massberg & B. Engelmann: Protein disulfide isomerase as a trigger for tissue factor-dependent fibrin generation. Thromb Res, 122 Suppl 1, S19-22 (2008)
    • (2008) Thromb Res , vol.122 , Issue.SUPPL. 1
    • Manukyan, D.1    Von Bruehl, M.L.2    Massberg, S.3    Engelmann, B.4
  • 85
    • 42449087287 scopus 로고    scopus 로고
    • Bovine protein disulfide isomerase-enhanced tissue factor coagulant function: Is phospholipid contaminant in it the real culprit?
    • Kothari, H., P. Sen, U. R. Pendurthi & L. V. Rao: Bovine protein disulfide isomerase-enhanced tissue factor coagulant function: is phospholipid contaminant in it the real culprit? Blood, 111, 3295-6 (2008)
    • (2008) Blood , vol.111 , pp. 3295-3336
    • Kothari, H.1    Sen, P.2    Pendurthi, U.R.3    Rao, L.V.4
  • 86
    • 54049143232 scopus 로고    scopus 로고
    • Protein disulfide isomerase has no stimulatory chaperone effect on factor X activation by factor VIIa-soluble tissue factor
    • Persson, E.: Protein disulfide isomerase has no stimulatory chaperone effect on factor X activation by factor VIIa-soluble tissue factor. Thromb Res, 123, 171-6 (2008)
    • (2008) Thromb Res , vol.123 , pp. 171-176
    • Persson, E.1
  • 87
    • 61849090924 scopus 로고    scopus 로고
    • Response: Tissue factor de-encryption: The cell model system
    • Pendurthi, U. R., Rao, L.V.: Response: Tissue factor de-encryption: the cell model system. Blood, 112, 913 (2008)
    • (2008) Blood , vol.112 , pp. 913
    • Pendurthi, U.R.1    Rao, L.V.2
  • 88
    • 77956533379 scopus 로고    scopus 로고
    • Extracellular protein disulfide isomerase regulates coagulation on endothelial cells through modulation of phosphatidylserine exposure
    • Popescu, N. I., C. Lupu & F. Lupu: Extracellular protein disulfide isomerase regulates coagulation on endothelial cells through modulation of phosphatidylserine exposure. Blood, 116, 993-1001 (2010)
    • (2010) Blood , vol.116 , pp. 993-1001
    • Popescu, N.I.1    Lupu, C.2    Lupu, F.3
  • 89
    • 77949266550 scopus 로고    scopus 로고
    • Role of PDI in regulating tissue factor: FVIIa activity
    • Popescu, N. I., C. Lupu & F. Lupu: Role of PDI in regulating tissue factor: FVIIa activity. Thromb Res, 125 Suppl 1, S38-41 (2010)
    • (2010) Thromb Res , vol.125 , Issue.SUPPL. 1
    • Popescu, N.I.1    Lupu, C.2    Lupu, F.3
  • 90
    • 84859801013 scopus 로고    scopus 로고
    • Tissue factor activation: Is disulfide bond switching a regulatory mechanism?
    • Pendurthi, U. R., Ghosh S., Mandal, S.K., Rao, L.V.: Tissue factor activation: is disulfide bond switching a regulatory mechanism? Blood, 112, 912-913 (2008)
    • (2008) Blood , vol.112 , pp. 912-913
    • Pendurthi, U.R.1    Ghosh, S.2    Mandal, S.K.3    Rao, L.V.4
  • 91
    • 77953625529 scopus 로고    scopus 로고
    • Cystine 186-cystine 209 disulfide bond is not essential for the procoagulant activity of tissue factor or for its deencryption
    • Kothari, H., R. C. Nayak, L. V. Rao & U. R. Pendurthi: Cystine 186-cystine 209 disulfide bond is not essential for the procoagulant activity of tissue factor or for its deencryption. Blood, 115, 4273-83 (2010)
    • (2010) Blood , vol.115 , pp. 4273-4283
    • Kothari, H.1    Nayak, R.C.2    Rao, L.V.3    Pendurthi, U.R.4


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