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Volumn 7, Issue 1, 2009, Pages 111-120

Biochemical characterization of plasma-derived tissue factor pathway inhibitor: Post-translational modification of free, full-length form with particular reference to the sugar chain

Author keywords

Free form; Plasma derived; Post translational modification; Sugar chain; Tissue factor pathway inhibitor

Indexed keywords

ACETYLCYSTEINE DERIVATIVE; ASPARAGINE; BLOOD CLOTTING FACTOR 10; BLOOD CLOTTING FACTOR 8; GLYCOPROTEIN; GLYCOSIDASE; HEPARIN; SERINE; SIALIDASE; SIALOPROTEIN; SUGAR; THREONINE; TISSUE FACTOR PATHWAY INHIBITOR;

EID: 57749179741     PISSN: 15387933     EISSN: 15387836     Source Type: Journal    
DOI: 10.1111/j.1538-7836.2008.03222.x     Document Type: Article
Times cited : (9)

References (36)
  • 1
    • 0023924263 scopus 로고
    • Cloning and characterization of a cDNA coding for the lipoprotein-associated coagulation inhibitor shows that it consists of three tandem Kunitz-type inhibitory domains
    • Wun TC, Kretzmer KK, Girard TJ, Miletich JP, Broze GJ Jr. Cloning and characterization of a cDNA coding for the lipoprotein-associated coagulation inhibitor shows that it consists of three tandem Kunitz-type inhibitory domains. J Biol Chem 1988; 263: 6001-4.
    • (1988) J Biol Chem , vol.263 , pp. 6001-6004
    • Wun, T.C.1    Kretzmer, K.K.2    Girard, T.J.3    Miletich, J.P.4    Broze Jr., G.J.5
  • 2
    • 0026668480 scopus 로고
    • Tissue factor pathway inhibitor: The COOH-terminus is required for optimal inhibition of factor Xa
    • Wesselschmidt R, Likert K, Girard T, Wun TC, Broze GJ Jr. Tissue factor pathway inhibitor: The COOH-terminus is required for optimal inhibition of factor Xa. Blood 1992; 79: 2004-10.
    • (1992) Blood , vol.79 , pp. 2004-2010
    • Wesselschmidt, R.1    Likert, K.2    Girard, T.3    Wun, T.C.4    Broze Jr., G.J.5
  • 3
    • 10044255324 scopus 로고    scopus 로고
    • Role for the Kunitz-3 domain of tissue factor pathway inhibitor-α in cell surface binding
    • Piro O, Broze GJ Jr. Role for the Kunitz-3 domain of tissue factor pathway inhibitor-α in cell surface binding. Circulation 2004; 110: 3567-72.
    • (2004) Circulation , vol.110 , pp. 3567-3572
    • Piro, O.1    Broze Jr., G.J.2
  • 4
    • 0025222311 scopus 로고
    • Cultured normal human hepatocytes do not synthesize lipoprotein-associated coagulation inhibitor: Evidence that endothelium is the principal site of its synthesis
    • Bajaj MS, Kuppuswamy MN, Saito H, Spitzer SG, Bajaj SP. Cultured normal human hepatocytes do not synthesize lipoprotein-associated coagulation inhibitor: Evidence that endothelium is the principal site of its synthesis. Proc Natl Acad Sci U S A 1990; 87: 8869-73.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 8869-8873
    • Bajaj, M.S.1    Kuppuswamy, M.N.2    Saito, H.3    Spitzer, S.G.4    Bajaj, S.P.5
  • 5
    • 0025851449 scopus 로고
    • Plasma antigen levels of the lipoprotein-associated coagulation inhibitor in patient samples
    • Novotny WF, Brown SG, Miletich JP, Rader DJ, Broze GJ Jr. Plasma antigen levels of the lipoprotein-associated coagulation inhibitor in patient samples. Blood 1991; 78: 387-93.
    • (1991) Blood , vol.78 , pp. 387-393
    • Novotny, W.F.1    Brown, S.G.2    Miletich, J.P.3    Rader, D.J.4    Broze Jr., G.J.5
  • 6
    • 0019965397 scopus 로고
    • Studies of anti-Xa activity in human plasma II: The role of lipoproteins
    • Barrowcliffe TW, Eggleton CA, Stocks J. Studies of anti-Xa activity in human plasma II: The role of lipoproteins. Thromb Res 1982; 27: 185-95.
    • (1982) Thromb Res , vol.27 , pp. 185-195
    • Barrowcliffe, T.W.1    Eggleton, C.A.2    Stocks, J.3
  • 8
    • 0023778170 scopus 로고
    • Heparin induces release of extrinsic coagulation pathway inhibitor (EPI)
    • Sandset PM, Abildgaard U, Larsen ML. Heparin induces release of extrinsic coagulation pathway inhibitor (EPI). Thromb Res 1988; 50: 803-13.
    • (1988) Thromb Res , vol.50 , pp. 803-813
    • Sandset, P.M.1    Abildgaard, U.2    Larsen, M.L.3
  • 9
    • 0025871461 scopus 로고
    • Purification and properties of heparin-releasable lipoprotein-associated coagulation inhibitor
    • Novotny WF, Palmier M, Wun TC, Broze GJ Jr, Miletich JP. Purification and properties of heparin-releasable lipoprotein-associated coagulation inhibitor. Blood 1991; 78: 394-400.
    • (1991) Blood , vol.78 , pp. 394-400
    • Novotny, W.F.1    Palmier, M.2    Wun, T.C.3    Broze Jr., G.J.4    Miletich, J.P.5
  • 10
    • 0031439536 scopus 로고    scopus 로고
    • Tissue factor pathway inhibitor in endothelial cells colocalizes with glycolipid microdomains/caveolae - Regulatory mechanism(s) of the anticoagulant properties of the endothelium
    • Lupu C, Goodwin CA, Westmuckett AD, Emeis JJ, Scully MF, Kakkar VV, Lupu F. Tissue factor pathway inhibitor in endothelial cells colocalizes with glycolipid microdomains/caveolae - regulatory mechanism(s) of the anticoagulant properties of the endothelium. Arterioscler Thromb Vasc Biol 1997; 17: 2964-74.
    • (1997) Arterioscler Thromb Vasc Biol , vol.17 , pp. 2964-2974
    • Lupu, C.1    Goodwin, C.A.2    Westmuckett, A.D.3    Emeis, J.J.4    Scully, M.F.5    Kakkar, V.V.6    Lupu, F.7
  • 11
    • 0043074904 scopus 로고    scopus 로고
    • Glycosyl phosphatidylinositol anchorage of tissue factor pathway inhibitor
    • Zhang J, Piro O, Lu L, Broze GJ Jr. Glycosyl phosphatidylinositol anchorage of tissue factor pathway inhibitor. Circulation 2003; 108: 623-7.
    • (2003) Circulation , vol.108 , pp. 623-627
    • Zhang, J.1    Piro, O.2    Lu, L.3    Broze Jr., G.J.4
  • 12
    • 0024231919 scopus 로고
    • Platelets secrete a coagulation inhibitor functionally and antigenically similar to the lipoprotein associated coagulation inhibitor
    • Novotny WF, Girard TJ, Miletich JP, Broze GJ Jr. Platelets secrete a coagulation inhibitor functionally and antigenically similar to the lipoprotein associated coagulation inhibitor. Blood 1988; 72: 2020-5.
    • (1988) Blood , vol.72 , pp. 2020-2025
    • Novotny, W.F.1    Girard, T.J.2    Miletich, J.P.3    Broze Jr., G.J.4
  • 14
    • 0024434125 scopus 로고
    • Purification and characterization of the lipoprotein-associated coagulation inhibitor from human plasma
    • Novotny WF, Girard TJ, Miletich JP, Broze GJ Jr. Purification and characterization of the lipoprotein-associated coagulation inhibitor from human plasma. J Biol Chem 1989; 264: 18832-7.
    • (1989) J Biol Chem , vol.264 , pp. 18832-18837
    • Novotny, W.F.1    Girard, T.J.2    Miletich, J.P.3    Broze Jr., G.J.4
  • 15
    • 0031105294 scopus 로고    scopus 로고
    • Tissue factor pathway inhibitor in complex with low density lipoprotein isolated from human plasma does not possess anticoagulant function in tissue factor-induced coagulation in vitro
    • Hansen JB, Huseby KR, Huseby NE, Ezban M, Nordoy A. Tissue factor pathway inhibitor in complex with low density lipoprotein isolated from human plasma does not possess anticoagulant function in tissue factor-induced coagulation in vitro. Thromb Res 1997; 85: 413-25.
    • (1997) Thromb Res , vol.85 , pp. 413-425
    • Hansen, J.B.1    Huseby, K.R.2    Huseby, N.E.3    Ezban, M.4    Nordoy, A.5
  • 16
    • 23044459581 scopus 로고    scopus 로고
    • A novel anticoagulant activity assay of tissue factor pathway inhibitor I (TFPI)
    • Dahm AEA, Andersen TO, Rosendaal F, Sandset PM. A novel anticoagulant activity assay of tissue factor pathway inhibitor I (TFPI). J Thromb Haemost 2005; 3: 651-8.
    • (2005) J Thromb Haemost , vol.3 , pp. 651-658
    • Dahm, A.E.A.1    Andersen, T.O.2    Rosendaal, F.3    Sandset, P.M.4
  • 17
    • 0025043182 scopus 로고
    • Immunoaffinity purification and characterization of lipoprotein-associated coagulation inhibitors from Hep G2 hepatoma, Chang liver, and SK hepatoma cells -a comparative study
    • Wun TC, Huang MD, Kretzmer KK, Palmier MO, Day KC, Bulock JW, Fok KF, Broze GJ Jr. Immunoaffinity purification and characterization of lipoprotein-associated coagulation inhibitors from Hep G2 hepatoma, Chang liver, and SK hepatoma cells -a comparative study. J Biol Chem 1990; 265: 16096-101.
    • (1990) J Biol Chem , vol.265 , pp. 16096-16101
    • Wun, T.C.1    Huang, M.D.2    Kretzmer, K.K.3    Palmier, M.O.4    Day, K.C.5    Bulock, J.W.6    Fok, K.F.7    Broze, G.J.8
  • 24
    • 0029994708 scopus 로고    scopus 로고
    • Amino acid sequence and carbohydrate structure of a recombinant human tissue factor pathway inhibitor expressed in Chinese hamster ovary cells: One N- and two O-linked carbohydrate chains are located between Kunitz domains 2 and 3 and one N-linked carbohydrate chain is in Kunitz domain 2
    • Nakahara Y, Miyata T, Hamuro T, Funatsu A, Miyagi M, Tsunasawa S, Kato H. Amino acid sequence and carbohydrate structure of a recombinant human tissue factor pathway inhibitor expressed in Chinese hamster ovary cells: One N- and two O-linked carbohydrate chains are located between Kunitz domains 2 and 3 and one N-linked carbohydrate chain is in Kunitz domain 2. Biochemistry 1996; 35: 6450-9.
    • (1996) Biochemistry , vol.35 , pp. 6450-6459
    • Nakahara, Y.1    Miyata, T.2    Hamuro, T.3    Funatsu, A.4    Miyagi, M.5    Tsunasawa, S.6    Kato, H.7
  • 25
    • 0024991650 scopus 로고
    • Regulation of coagulation by a multivalent Kunitz-type inhibitor
    • Broze GJ Jr, Girard TJ, Novotny WF. Regulation of coagulation by a multivalent Kunitz-type inhibitor. Biochemistry 1990; 29: 7539-46.
    • (1990) Biochemistry , vol.29 , pp. 7539-7556
    • Broze Jr., G.J.1    Girard, T.J.2    Novotny, W.F.3
  • 26
    • 0029122652 scopus 로고
    • An anti-tissue factor pathway inhibitor (TFPI) monoclonal antibody recognized the third Kunitz domain (K3) of free-form TFPI but not lipoprotein-associated forms in plasma
    • Abumiya T, Enjyoji K, Kokawa T, Kamikubo Y, Kato H. An anti-tissue factor pathway inhibitor (TFPI) monoclonal antibody recognized the third Kunitz domain (K3) of free-form TFPI but not lipoprotein-associated forms in plasma. J Biochem (Tokyo) 1995; 118: 178-82.
    • (1995) J Biochem (Tokyo) , vol.118 , pp. 178-182
    • Abumiya, T.1    Enjyoji, K.2    Kokawa, T.3    Kamikubo, Y.4    Kato, H.5
  • 27
    • 0026659121 scopus 로고
    • Release of O-linked sugar chains from glycoproteins with anhydrous hydrazine and pyridylamination of the sugar chains with improved reaction conditions
    • Kuraya N, Hase S. Release of O-linked sugar chains from glycoproteins with anhydrous hydrazine and pyridylamination of the sugar chains with improved reaction conditions. J Biochem (Tokyo) 1992; 112: 122-6.
    • (1992) J Biochem (Tokyo) , vol.112 , pp. 122-126
    • Kuraya, N.1    Hase, S.2
  • 28
    • 0021308647 scopus 로고
    • Reexamination of the pyridylamination used for fluorescence labeling of oligosaccharides and its application to glycoproteins
    • Hase S, Ibuki T, Ikenaka T. Reexamination of the pyridylamination used for fluorescence labeling of oligosaccharides and its application to glycoproteins. J Biochem (Tokyo) 1984; 95: 197-203.
    • (1984) J Biochem (Tokyo) , vol.95 , pp. 197-203
    • Hase, S.1    Ibuki, T.2    Ikenaka, T.3
  • 29
    • 0030051116 scopus 로고    scopus 로고
    • Analysis of pyridylaminated O-linked sugar chains by two-dimensional sugar mapping
    • Kuraya N, Hase S. Analysis of pyridylaminated O-linked sugar chains by two-dimensional sugar mapping. Anal Biochem 1996; 233: 205-11.
    • (1996) Anal Biochem , vol.233 , pp. 205-211
    • Kuraya, N.1    Hase, S.2
  • 30
    • 0028207949 scopus 로고
    • High-performance liquid chromatography of pyridylaminated saccharides
    • In: Ginsburg V, ed. New York: Academic Press Inc
    • Hase S. High-performance liquid chromatography of pyridylaminated saccharides. In: Ginsburg V, ed. Methods in Enzymology vol. 230. New York: Academic Press Inc., 1994: 225-37.
    • (1994) Methods in Enzymology , vol.230 , pp. 225-237
    • Hase, S.1
  • 31
    • 0028343509 scopus 로고
    • Molecular cloning, expression, and partial characterization of a second human tissue-factor-pathway inhibitor
    • Sprecher CA, Kisiel W, Mathewes S, Foster DC. Molecular cloning, expression, and partial characterization of a second human tissue-factor-pathway inhibitor. Proc Natl Acad Sci U S A 1994; 91: 3353-7.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 3353-3357
    • Sprecher, C.A.1    Kisiel, W.2    Mathewes, S.3    Foster, D.C.4
  • 32
    • 0023056270 scopus 로고
    • The mRNA for a proteinase inhibitor related to the HI-30 domain of inter-alpha-trypsin inhibitor also encodes alpha-1-microglobulin (protein HC)
    • Kaumeyer JF, Polazzi JO, Kotick MP. The mRNA for a proteinase inhibitor related to the HI-30 domain of inter-alpha-trypsin inhibitor also encodes alpha-1-microglobulin (protein HC). Nucleic Acids Res 1986; 14: 7839-50.
    • (1986) Nucleic Acids Res , vol.14 , pp. 7839-7850
    • Kaumeyer, J.F.1    Polazzi, J.O.2    Kotick, M.P.3
  • 33
    • 0019631514 scopus 로고
    • Kunitz-type proteinase inhibitors derived by limited proteolysis of the inter-α-trypsin inhibitor, V
    • Hochstrasser K, Schonberger OL, Rossmanith I, Wachter E. Kunitz-type proteinase inhibitors derived by limited proteolysis of the inter-α-trypsin inhibitor, V. Hoppe Seylers Z Physiol Chem 1981; 362: 1357-62.
    • (1981) Hoppe Seylers Z Physiol Chem , vol.362 , pp. 1357-1362
    • Hochstrasser, K.1    Schonberger, O.L.2    Rossmanith, I.3    Wachter, E.4
  • 34
    • 0026456660 scopus 로고
    • Structural analysis of the N-linked oligosaccharides from human urinary trypsin inhibitor
    • Toyoda H, Ikei T, Demachi Y, Toida T, Imanari T. Structural analysis of the N-linked oligosaccharides from human urinary trypsin inhibitor. Chem Pharm Bull 1992; 40: 2882-4.
    • (1992) Chem Pharm Bull , vol.40 , pp. 2882-2884
    • Toyoda, H.1    Ikei, T.2    Demachi, Y.3    Toida, T.4    Imanari, T.5
  • 35
    • 0026638837 scopus 로고
    • Evolutionary origin of a Kunitz-type trypsin inhibitor domain inserted in the amyloid β precursor protein of Alzheimer's disease
    • Ikeo K, Takahashi K, Gojobori T. Evolutionary origin of a Kunitz-type trypsin inhibitor domain inserted in the amyloid β precursor protein of Alzheimer's disease. J Mol Evol 1992; 34: 536-43.
    • (1992) J Mol Evol , vol.34 , pp. 536-543
    • Ikeo, K.1    Takahashi, K.2    Gojobori, T.3
  • 36
    • 0034282877 scopus 로고    scopus 로고
    • Matrix metalloproteinases cleave tissue factor pathway inhibitor - Effects on coagulation
    • Belaaouaj AA, Li A, Wun TC, Welgus HG, Shapiro SD. Matrix metalloproteinases cleave tissue factor pathway inhibitor - Effects on coagulation. J Biol Chem 2000; 275: 27123-8.
    • (2000) J Biol Chem , vol.275 , pp. 27123-27128
    • Belaaouaj, A.A.1    Li, A.2    Wun, T.C.3    Welgus, H.G.4    Shapiro, S.D.5


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