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Volumn 270, Issue 20, 2003, Pages 4059-4069

Probing plasma clearance of the thrombin-antithrombin complex with a monoclonal antibody against the putative serpin-enzyme complex receptor-binding site

Author keywords

Antithrombin; Monoclonal antibody; Serpin enzyme complex receptor; Thrombin; Thrombin antithrombin complex

Indexed keywords

ANTITHROMBIN; IMMUNOGLOBULIN F(AB) FRAGMENT; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY M27; SERINE PROTEINASE INHIBITOR; THROMBIN; THROMBIN ANTITHROMBIN COMPLEX; UNCLASSIFIED DRUG;

EID: 0142120491     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2003.03793.x     Document Type: Article
Times cited : (8)

References (50)
  • 1
    • 0030062157 scopus 로고    scopus 로고
    • The biostructural pathology of the serpins: Critical function of sheet opening mechanism
    • Carrell, R.W. & Stein, P.E. (1996) The biostructural pathology of the serpins: critical function of sheet opening mechanism. Biol. Chem. Hoppe-Seyler. 377, 1-17.
    • (1996) Biol. Chem. Hoppe-Seyler. , vol.377 , pp. 1-17
    • Carrell, R.W.1    Stein, P.E.2
  • 3
    • 0031755765 scopus 로고    scopus 로고
    • Structure-function relationships in serpins: Current concepts and controversies
    • Gils, A. & Declerck, P.J. (1998) Structure-function relationships in serpins: current concepts and controversies. Thromb. Haemost. 80, 531-541.
    • (1998) Thromb. Haemost. , vol.80 , pp. 531-541
    • Gils, A.1    Declerck, P.J.2
  • 4
    • 0028339523 scopus 로고
    • Structural aspects of serpin inhibition
    • Schulze, A.J., Huber, R., Bode, W. & Engh, R.A. (1994) Structural aspects of serpin inhibition. FEBS Lett. 334, 117-124.
    • (1994) FEBS Lett. , vol.334 , pp. 117-124
    • Schulze, A.J.1    Huber, R.2    Bode, W.3    Engh, R.A.4
  • 5
    • 0036882395 scopus 로고    scopus 로고
    • Serpin structure, mechanism, and function
    • Gettins, P.G.W. (2002) Serpin structure, mechanism, and function. Chem. Rev. 102, 4751-4803.
    • (2002) Chem. Rev. , vol.102 , pp. 4751-4803
    • Gettins, P.G.W.1
  • 7
    • 0031012256 scopus 로고    scopus 로고
    • Inherited thrombotic disorders: An update
    • Florell, S.R. & Rodgers, G.M. (1997) Inherited thrombotic disorders: an update. Am. J. Hematol. 54, 53-60.
    • (1997) Am. J. Hematol. , vol.54 , pp. 53-60
    • Florell, S.R.1    Rodgers, G.M.2
  • 8
    • 0018374956 scopus 로고
    • The production of an inactive form of antithrombin through limited proteolysis by thrombin
    • Fish, W.W., Orre, K. & Björk, I. (1979) The production of an inactive form of antithrombin through limited proteolysis by thrombin. FEBS Lett. 98, 103-106.
    • (1979) FEBS Lett. , vol.98 , pp. 103-106
    • Fish, W.W.1    Orre, K.2    Björk, I.3
  • 9
    • 0028773279 scopus 로고
    • Biological implications of a 3Å structure for dimeric antithrombin
    • Carrell, R.W., Stein, P.E., Fermi, G. & Wardell, M.R. (1994) Biological implications of a 3Å structure for dimeric antithrombin. Structure 2, 257-270.
    • (1994) Structure , vol.2 , pp. 257-270
    • Carrell, R.W.1    Stein, P.E.2    Fermi, G.3    Wardell, M.R.4
  • 10
    • 0034687422 scopus 로고    scopus 로고
    • Structure of a serpin-protease complex shows inhibition by deformation
    • Huntington, J.A., Read, R.J. & Carrell, R.W. (2000) Structure of a serpin-protease complex shows inhibition by deformation. Nature 407, 923-926.
    • (2000) Nature , vol.407 , pp. 923-926
    • Huntington, J.A.1    Read, R.J.2    Carrell, R.W.3
  • 11
    • 0033010830 scopus 로고    scopus 로고
    • The clearance of thrombin-antithrombin and related serpin-enzyme complexes from the circulation: Role of various hepatocyte receptors
    • Wells, M.J., Sheffield, W.P. & Blajckman, M.A. (1999) The clearance of thrombin-antithrombin and related serpin-enzyme complexes from the circulation: role of various hepatocyte receptors. Thromb. Haemost. 81, 325-337.
    • (1999) Thromb. Haemost. , vol.81 , pp. 325-337
    • Wells, M.J.1    Sheffield, W.P.2    Blajckman, M.A.3
  • 12
    • 0029866947 scopus 로고    scopus 로고
    • Probing serpin reactive-loop conformations by proteolytic cleavage
    • Chang, W.-S.W., Wardell, M.R., Lomas, D.A. & Carrell, R.W. (1996) Probing serpin reactive-loop conformations by proteolytic cleavage. Biochem. J. 314, 647-653.
    • (1996) Biochem. J. , vol.314 , pp. 647-653
    • Chang, W.-S.W.1    Wardell, M.R.2    Lomas, D.A.3    Carrell, R.W.4
  • 13
    • 0030700799 scopus 로고    scopus 로고
    • Preparative induction and chracterization of L-antithrombin: A structural homologue of latent plasminogen activator inhibitor-1
    • Wardell, M.R., Chang, M.-S.W., Bruce, D., Skinner, R., Lesk, A.M. & Carrell, R.W. (1997) Preparative induction and chracterization of L-antithrombin: a structural homologue of latent plasminogen activator inhibitor-1. Biochemistry 36, 13133-13142.
    • (1997) Biochemistry , vol.36 , pp. 13133-13142
    • Wardell, M.R.1    Chang, M.-S.W.2    Bruce, D.3    Skinner, R.4    Lesk, A.M.5    Carrell, R.W.6
  • 15
    • 0033570979 scopus 로고    scopus 로고
    • Formation of antithrombin heterodimer in vivo and the onset of thrombosis
    • Zhou, A., Huntington, J.A. & Carrell, R.W. (1999) Formation of antithrombin heterodimer in vivo and the onset of thrombosis. Blood 94, 3388-3396.
    • (1999) Blood , vol.94 , pp. 3388-3396
    • Zhou, A.1    Huntington, J.A.2    Carrell, R.W.3
  • 16
    • 0027999955 scopus 로고
    • Thromboembolic disease due to thermolabile conformational changes of antithrombin Rouen-VI (187 Asn → Asp)
    • Bruce, D., Perry, D.J., Borg, J.-Y., Carrell, R.W. & Wardell, M.R. (1994) Thromboembolic disease due to thermolabile conformational changes of antithrombin Rouen-VI (187 Asn → Asp). J. Clin. Invest. 94, 2265-2274.
    • (1994) J. Clin. Invest. , vol.94 , pp. 2265-2274
    • Bruce, D.1    Perry, D.J.2    Borg, J.-Y.3    Carrell, R.W.4    Wardell, M.R.5
  • 17
    • 0031059479 scopus 로고    scopus 로고
    • Commercial antithrombin concentrate contains inactive L-forms of antithrombin
    • Chang, W.-S.W. & Harper, P.L. (1997) Commercial antithrombin concentrate contains inactive L-forms of antithrombin. Thromb. Haemost. 77, 323-328.
    • (1997) Thromb. Haemost. , vol.77 , pp. 323-328
    • Chang, W.-S.W.1    Harper, P.L.2
  • 18
    • 0033578910 scopus 로고    scopus 로고
    • Antiangiogenic activity of the cleaved conformation of the serpin antithrombin
    • O'Reilly, M.S., Pirie-Shepherd, S., Lane, W.S. & Folkman, J. (1999) Antiangiogenic activity of the cleaved conformation of the serpin antithrombin. Science 285, 1926-1928.
    • (1999) Science , vol.285 , pp. 1926-1928
    • O'Reilly, M.S.1    Pirie-Shepherd, S.2    Lane, W.S.3    Folkman, J.4
  • 19
    • 0034544536 scopus 로고    scopus 로고
    • Antiangiogenic effects of latent antithrombin through perturbed cell-matrix interactions and apoptosis of endothelial cells
    • Larsson, H., Sjöblom, T., Dixelius, J., Östman, A., Ylinenjärvi, K., Björk, I. & Claesson-Welsh, L. (2000) Antiangiogenic effects of latent antithrombin through perturbed cell-matrix interactions and apoptosis of endothelial cells. Cancer Res. 60, 6723-6729.
    • (2000) Cancer Res. , vol.60 , pp. 6723-6729
    • Larsson, H.1    Sjöblom, T.2    Dixelius, J.3    Östman, A.4    Ylinenjärvi, K.5    Björk, I.6    Claesson-Welsh, L.7
  • 21
    • 0030658029 scopus 로고    scopus 로고
    • Cytokeratin 18 is expressed on the hepatocyte plasma membrane surface and interacts with thrombin-antithrombin complexes
    • Wells, M., Hatton, M.W.C., Hewlett, B., Podar, T.J., Scheffield, W.P. & Blajchman, M.A. (1997) Cytokeratin 18 is expressed on the hepatocyte plasma membrane surface and interacts with thrombin-antithrombin complexes. J. Biol. Chem. 272, 28574-28581.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28574-28581
    • Wells, M.1    Hatton, M.W.C.2    Hewlett, B.3    Podar, T.J.4    Scheffield, W.P.5    Blajchman, M.A.6
  • 22
    • 0029785660 scopus 로고    scopus 로고
    • Role of the proposed serpin-enzyme complex receptor recognition site in binding and internalization of thrombin-heparin cofactor II complexes by hepatocytes
    • Maekawa, H. & Tollefsen, D.M. (1996) Role of the proposed serpin-enzyme complex receptor recognition site in binding and internalization of thrombin-heparin cofactor II complexes by hepatocytes. J. Biol. Chem. 271, 18604-18609.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18604-18609
    • Maekawa, H.1    Tollefsen, D.M.2
  • 23
    • 0019472086 scopus 로고
    • A simple two-step procedure for the isolation of antithrombin III from biological fluids
    • McKay, E.J. (1981) A simple two-step procedure for the isolation of antithrombin III from biological fluids. Thromb. Res. 21, 375-382.
    • (1981) Thromb. Res. , vol.21 , pp. 375-382
    • McKay, E.J.1
  • 24
    • 0033582435 scopus 로고    scopus 로고
    • Topology of the stable serpin-protease complexes revealed by an autoantibody that fails to react with the monomeric conformers of antithrombin
    • Picard, V., Marque, P.-E., Paolucci, F., Aiach, M. & Le Bonniec, B.F. (1999) Topology of the stable serpin-protease complexes revealed by an autoantibody that fails to react with the monomeric conformers of antithrombin. J. Biol. Chem. 274, 4586-4593.
    • (1999) J. Biol. Chem. , vol.274 , pp. 4586-4593
    • Picard, V.1    Marque, P.-E.2    Paolucci, F.3    Aiach, M.4    Le Bonniec, B.F.5
  • 25
    • 0015739824 scopus 로고
    • Simultaneous purification of bovine prothrombin and factor X. Activation of prothrombin by trypsin-activated factor X
    • Bajaj, S.P. & Mann, K.G. (1973) Simultaneous purification of bovine prothrombin and factor X. Activation of prothrombin by trypsin-activated factor X. J. Biol. Chem. 248, 7729-7741.
    • (1973) J. Biol. Chem. , vol.248 , pp. 7729-7741
    • Bajaj, S.P.1    Mann, K.G.2
  • 26
    • 0022904908 scopus 로고
    • Prothrombin activation by an activator from the venom of Oxyuranus scutellatus (Taipan Snake)
    • Speijer, H., Govers-Reimslag, J.W.P., Zwall, R.F.A. & Rosing, J. (1986) Prothrombin activation by an activator from the venom of Oxyuranus scutellatus (Taipan Snake). J. Biol. Chem. 261, 13258-13267.
    • (1986) J. Biol. Chem. , vol.261 , pp. 13258-13267
    • Speijer, H.1    Govers-Reimslag, J.W.P.2    Zwall, R.F.A.3    Rosing, J.4
  • 27
    • 0034719165 scopus 로고    scopus 로고
    • Activated protein C-protein C inhibitor complex formation: Characterization of a neoepitope provides evidence for extensive insertion of the reactive center loop
    • Strandberg, K., Kjellberg, M., Erb, E.-M., Persson, U., Mosher, D.F., Villoutreix, B.O. & Stenflo, J. (2000) Activated protein C-protein C inhibitor complex formation: characterization of a neoepitope provides evidence for extensive insertion of the reactive center loop. Biochemistry 39, 15713-15720.
    • (2000) Biochemistry , vol.39 , pp. 15713-15720
    • Strandberg, K.1    Kjellberg, M.2    Erb, E.-M.3    Persson, U.4    Mosher, D.F.5    Villoutreix, B.O.6    Stenflo, J.7
  • 29
    • 0000896420 scopus 로고
    • Preparation and purification of active fragments from mouse monoclonal antibodies
    • (Weir, D.M., ed), 4th edn, Blackwell Scientific Publications, Maiden, MA
    • Parham, P. (1986) Preparation and purification of active fragments from mouse monoclonal antibodies. In: Cellular Immunology, (Weir, D.M., ed), 4th edn, Vol. 1, pp. 14.1-14.23. Blackwell Scientific Publications, Maiden, MA.
    • (1986) Cellular Immunology , vol.1 , pp. 141-1423
    • Parham, P.1
  • 30
    • 0034733659 scopus 로고    scopus 로고
    • Identification and purification of vitamin K-dependent proteins and peptides with monoclonal antibodies specific for γ-carboxyglutamyl (Gla) residues
    • Brown, M.A., Stenberg, L.M., Perrson, U. & Stenflo, J. (2000) Identification and purification of vitamin K-dependent proteins and peptides with monoclonal antibodies specific for γ-carboxyglutamyl (Gla) residues. J. Biol. Chem. 275, 19795-19802.
    • (2000) J. Biol. Chem. , vol.275 , pp. 19795-19802
    • Brown, M.A.1    Stenberg, L.M.2    Perrson, U.3    Stenflo, J.4
  • 31
    • 0016320003 scopus 로고
    • Intracellular immunoglobulin chain synthesis in non-secreting variants of a mouse myeloma: Detection of inactive light chain messenger RNA
    • Cowan, N.J., Secher, D.S. & Milstein, C.J. (1974) Intracellular immunoglobulin chain synthesis in non-secreting variants of a mouse myeloma: detection of inactive light chain messenger RNA. J. Mol. Biol. 90, 691-701.
    • (1974) J. Mol. Biol. , vol.90 , pp. 691-701
    • Cowan, N.J.1    Secher, D.S.2    Milstein, C.J.3
  • 33
    • 0031588685 scopus 로고    scopus 로고
    • The 2.6 Å structure of antithrombin indicates a conformational change at the heparin binding site
    • Skinner, R., Abrahams, J.P., Whisslock, J.C., Lesk, A.M., Carrell, R.W. & Wardell, M.R. (1997) The 2.6 Å structure of antithrombin indicates a conformational change at the heparin binding site. J. Mol. Biol. 266, 601-609.
    • (1997) J. Mol. Biol. , vol.266 , pp. 601-609
    • Skinner, R.1    Abrahams, J.P.2    Whisslock, J.C.3    Lesk, A.M.4    Carrell, R.W.5    Wardell, M.R.6
  • 34
    • 0027259312 scopus 로고
    • Crystal structure of cleaved bovine antithrombin III at 3.2 Å resolution
    • Mourny, L., Samama, J.P., Delarue, M., Petitou, M., Choay, J. & Moras, D. (1993) Crystal structure of cleaved bovine antithrombin III at 3.2 Å resolution. J. Mol. Biol. 232, 223-241.
    • (1993) J. Mol. Biol. , vol.232 , pp. 223-241
    • Mourny, L.1    Samama, J.P.2    Delarue, M.3    Petitou, M.4    Choay, J.5    Moras, D.6
  • 35
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee, B. & Richards, F.M. (1971) The interpretation of protein structures: estimation of static accessibility. J. Mol. Biol. 55, 379-400.
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 36
    • 0031977052 scopus 로고    scopus 로고
    • Heterogeneity of packing: Structural approach
    • Kurochking, N. & Privalov, G. (1998) Heterogeneity of packing: Structural approach. Protein Sci. 7, 897-905.
    • (1998) Protein Sci. , vol.7 , pp. 897-905
    • Kurochking, N.1    Privalov, G.2
  • 37
    • 0026807034 scopus 로고
    • Molecular cloning and cell-free expression of mouse antithrombin III
    • Wu, J.K., Sheffield, W.P. & Blajchman, M.A. (1992) Molecular cloning and cell-free expression of mouse antithrombin III. Thromb. Haemost. 68, 291-296.
    • (1992) Thromb. Haemost. , vol.68 , pp. 291-296
    • Wu, J.K.1    Sheffield, W.P.2    Blajchman, M.A.3
  • 39
    • 0029868041 scopus 로고    scopus 로고
    • 1-antitrypsin-trypsin complexes is mediated by the low density lipoprotein receptor-related protein
    • 1-antitrypsin-trypsin complexes is mediated by the low density lipoprotein receptor-related protein. J. Biol. Chem. 271, 6523-6529.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6523-6529
    • Kounnas, M.Z.1    Church, F.C.2    Argraves, W.S.3    Strickland, D.K.4
  • 40
    • 0024337511 scopus 로고
    • A monoclonal antibody that triggers deacylation of an intermediate thrombin-antithrombin III complex
    • Asakura, S., Matsuda, M., Yoshida, N., Terukina, S. & Kihara, H. (1989) A monoclonal antibody that triggers deacylation of an intermediate thrombin-antithrombin III complex. J. Biol. Chem. 264, 13736-13739.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13736-13739
    • Asakura, S.1    Matsuda, M.2    Yoshida, N.3    Terukina, S.4    Kihara, H.5
  • 41
    • 0025248027 scopus 로고
    • Hydrophobic residues 382-386 of antithrombin III, Ala-Ala-Ala-Ser-Thr, serve as the epitope for an antibody which facilitates hydrolysis of the inhibitor by thrombin
    • Asakura, S., Hirata, H., Okazaki, H., Hashimoto-Gotoh, T. & Matsuda, M. (1990) Hydrophobic residues 382-386 of antithrombin III, Ala-Ala-Ala-Ser-Thr, serve as the epitope for an antibody which facilitates hydrolysis of the inhibitor by thrombin. J. Biol. Chem. 265, 5135-5138.
    • (1990) J. Biol. Chem. , vol.265 , pp. 5135-5138
    • Asakura, S.1    Hirata, H.2    Okazaki, H.3    Hashimoto-Gotoh, T.4    Matsuda, M.5
  • 42
    • 0028325823 scopus 로고
    • Conformational change in antithrombin induced by heparin, probed with a monoclonal antibody against the 1C/4B region
    • Dawes, J., James, K. & Lane, D.A. (1994) Conformational change in antithrombin induced by heparin, probed with a monoclonal antibody against the 1C/4B region. Biochemistry 33, 4375-4383.
    • (1994) Biochemistry , vol.33 , pp. 4375-4383
    • Dawes, J.1    James, K.2    Lane, D.A.3
  • 43
    • 0025831251 scopus 로고
    • Predominant contribution of surface approximation to the mechanism of heparin acceleration of the antithrombin-thrombin reaction. Elucidation from salt concentration effects
    • Olson, S.T. & Björk, I. (1991) Predominant contribution of surface approximation to the mechanism of heparin acceleration of the antithrombin-thrombin reaction. Elucidation from salt concentration effects. J. Biol. Chem. 266, 6353-6364.
    • (1991) J. Biol. Chem. , vol.266 , pp. 6353-6364
    • Olson, S.T.1    Björk, I.2
  • 44
    • 0019182327 scopus 로고
    • Clearance of thrombin from circulation in rabbits by high-affinity binding sites on endothelium. Possible roles in the inactivation of thrombin by antithrombin III
    • Lollar, P. & Owen, W.G. (1980) Clearance of thrombin from circulation in rabbits by high-affinity binding sites on endothelium. Possible roles in the inactivation of thrombin by antithrombin III. J. Clin. Invest. 66, 1222-1230.
    • (1980) J. Clin. Invest. , vol.66 , pp. 1222-1230
    • Lollar, P.1    Owen, W.G.2
  • 46
    • 0023950380 scopus 로고
    • In vivo catabolism of heparin cofactor II and its complex with thrombin: Evidence for a common receptor-mediated clearance pathway for three serine proteinase inhibitors
    • Pratt, C.W., Church, F.C. & Pizzo, S.V. (1988) In vivo catabolism of heparin cofactor II and its complex with thrombin: evidence for a common receptor-mediated clearance pathway for three serine proteinase inhibitors. Arch. Biochem. Biophys. 262, 111-117.
    • (1988) Arch. Biochem. Biophys. , vol.262 , pp. 111-117
    • Pratt, C.W.1    Church, F.C.2    Pizzo, S.V.3
  • 49
    • 0035350602 scopus 로고    scopus 로고
    • A small synthetic peptide for gene delivery via the serpin-enzyme complex receptor
    • Patel, S., Zhang, X., Collins, L. & Fabre, J.W. (2001) A small synthetic peptide for gene delivery via the serpin-enzyme complex receptor. J. Gene Med. 3, 271-279.
    • (2001) J. Gene Med. , vol.3 , pp. 271-279
    • Patel, S.1    Zhang, X.2    Collins, L.3    Fabre, J.W.4
  • 50
    • 0033582456 scopus 로고    scopus 로고
    • Chain length of the polylysine in receptor-targeted transfer complexes affects duration of reporter gene expression both in vitro and in vivo
    • Zaidy, A.G., Ferkol, T., Dawson, D.V., Perlmutter, D.H. & Davis, P.B. (1999) Chain length of the polylysine in receptor-targeted transfer complexes affects duration of reporter gene expression both in vitro and in vivo. J. Biol. Chem. 274, 4908-4916.
    • (1999) J. Biol. Chem. , vol.274 , pp. 4908-4916
    • Zaidy, A.G.1    Ferkol, T.2    Dawson, D.V.3    Perlmutter, D.H.4    Davis, P.B.5


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