메뉴 건너뛰기




Volumn 16, Issue 10, 1996, Pages 1292-1297

Thrombin inhibition by antithrombin III on the subendothelium is explained by the isoform ATβ

Author keywords

antithrombin III; antithrombin isoform; fibrin; thrombin; vascular injury

Indexed keywords

ANTITHROMBIN III; FIBRIN; THROMBIN;

EID: 0029846138     PISSN: 10795642     EISSN: None     Source Type: Journal    
DOI: 10.1161/01.ATV.16.10.1292     Document Type: Article
Times cited : (40)

References (43)
  • 1
    • 0019861825 scopus 로고
    • Functional properties of an endothelial cell cofactor for thrombin-catalyzed activation of protein C
    • Owen WG, Esmon CT. Functional properties of an endothelial cell cofactor for thrombin-catalyzed activation of protein C. J Biol Chem. 1981;256:5532-5535.
    • (1981) J Biol Chem , vol.256 , pp. 5532-5535
    • Owen, W.G.1    Esmon, C.T.2
  • 2
    • 0021133167 scopus 로고
    • Acceleration of thrombin-antithrombin complex formation in rat hindquarters via heparinlike molecules bound to the endothelium
    • Marcum JA, McKenney JB, Rosenberg RD. Acceleration of thrombin-antithrombin complex formation in rat hindquarters via heparinlike molecules bound to the endothelium. J Clin Invest. 1984;74:341-350.
    • (1984) J Clin Invest , vol.74 , pp. 341-350
    • Marcum, J.A.1    McKenney, J.B.2    Rosenberg, R.D.3
  • 3
    • 0020404408 scopus 로고
    • Complex formation between thrombin and thrombomodulin inhibits both thrombin-catalyzed fibrin formation and factor V activation
    • Esmon CT, Esmon NL, Harris KW. Complex formation between thrombin and thrombomodulin inhibits both thrombin-catalyzed fibrin formation and factor V activation. J Biol Chem. 1982;257:7944-7947.
    • (1982) J Biol Chem , vol.257 , pp. 7944-7947
    • Esmon, C.T.1    Esmon, N.L.2    Harris, K.W.3
  • 4
    • 0025051257 scopus 로고
    • Localization of anticoagulantly active heparan sulfate proteoglycans in vascular endothelium: Antithrombin binding on cultured endothelial cells and perfused rat aorta
    • de Agostini AI, Watkins SC, Slayter HS, Youssoufian H, Rosenberg RD. Localization of anticoagulantly active heparan sulfate proteoglycans in vascular endothelium: antithrombin binding on cultured endothelial cells and perfused rat aorta. J Cell Biol. 1990;111:1293-1304.
    • (1990) J Cell Biol , vol.111 , pp. 1293-1304
    • De Agostini, A.I.1    Watkins, S.C.2    Slayter, H.S.3    Youssoufian, H.4    Rosenberg, R.D.5
  • 5
    • 0024460632 scopus 로고
    • Biochemistry of heparin antithrombin interactions, and the physiologic role of this natural anticoagulant mechanism
    • Rosenberg RD. Biochemistry of heparin antithrombin interactions, and the physiologic role of this natural anticoagulant mechanism. Am J Med. 1989;87:2S-9S.
    • (1989) Am J Med , vol.87
    • Rosenberg, R.D.1
  • 7
    • 0022477437 scopus 로고
    • Distribution of the thrombomodulin antigen in the rabbit vasculature
    • DeBault LE, Esmon NL, Olson JR, Esmon CT, Distribution of the thrombomodulin antigen in the rabbit vasculature. Lab Invest. 1986;54:172-178.
    • (1986) Lab Invest , vol.54 , pp. 172-178
    • DeBault, L.E.1    Esmon, N.L.2    Olson, J.R.3    Esmon, C.T.4
  • 8
    • 0027490521 scopus 로고
    • Thrombomodulin and thrombin localization on the vascular endothelium: Their internalization and transcytosis by plasmalemmal vesicles
    • Horvat R, Palade GE. Thrombomodulin and thrombin localization on the vascular endothelium: their internalization and transcytosis by plasmalemmal vesicles. Eur J Cell Biol. 1993;61:299-313.
    • (1993) Eur J Cell Biol , vol.61 , pp. 299-313
    • Horvat, R.1    Palade, G.E.2
  • 9
    • 0018575465 scopus 로고
    • Distribution of glycosaminoglycans in consecutive layers of the rabbit aorta
    • Massaro TA, Glatz CE, Peppas NA, Chisolm GM, Colton CK. Distribution of glycosaminoglycans in consecutive layers of the rabbit aorta. Artery. 1979;5:1-13.
    • (1979) Artery , vol.5 , pp. 1-13
    • Massaro, T.A.1    Glatz, C.E.2    Peppas, N.A.3    Chisolm, G.M.4    Colton, C.K.5
  • 10
    • 0023491494 scopus 로고
    • Mapping of proteoglycans in human arterial tissue
    • Völker W, Schmidt A, Buddecke E. Mapping of proteoglycans in human arterial tissue. Eur J Cell Biol. 1987;45:72-79.
    • (1987) Eur J Cell Biol , vol.45 , pp. 72-79
    • Völker, W.1    Schmidt, A.2    Buddecke, E.3
  • 11
    • 0023195691 scopus 로고
    • Uptake and inactivation of thrombin on the subendothelium: Comparisons with endothelium
    • Frebelius S, Swedenborg J. Uptake and inactivation of thrombin on the subendothelium: comparisons with endothelium. Thromb Res. 1987;47:223-233.
    • (1987) Thromb Res , vol.47 , pp. 223-233
    • Frebelius, S.1    Swedenborg, J.2
  • 12
    • 0024789231 scopus 로고
    • Inhibition of thrombin on sub-endothelium: Studies on rabbit aorta, ex vivo
    • Nydahl S, Frebelius S, Swedenborg J. Inhibition of thrombin on sub-endothelium: studies on rabbit aorta, ex vivo. Eur Surg Res. 1989;21:287-295.
    • (1989) Eur Surg Res , vol.21 , pp. 287-295
    • Nydahl, S.1    Frebelius, S.2    Swedenborg, J.3
  • 13
    • 0027955262 scopus 로고
    • Thrombogenicity of the injured vessel wall: Role of antithrombin and heparin
    • Frebelius S, Hedin U, Swedenborg J. Thrombogenicity of the injured vessel wall: role of antithrombin and heparin. Thromb Haemost. 1994;71:147-153.
    • (1994) Thromb Haemost , vol.71 , pp. 147-153
    • Frebelius, S.1    Hedin, U.2    Swedenborg, J.3
  • 14
    • 0023818186 scopus 로고
    • Evidence that rabbit 125I-antithrombin III binds to proteoheparan sulphate at the subendothelium of the rabbit aorta in vitro
    • Hatton MW, Moar SL, Richardson M. Evidence that rabbit 125I-antithrombin III binds to proteoheparan sulphate at the subendothelium of the rabbit aorta in vitro. Blood Vessels. 1988;25:12-27.
    • (1988) Blood Vessels , vol.25 , pp. 12-27
    • Hatton, M.W.1    Moar, S.L.2    Richardson, M.3
  • 15
    • 0022350392 scopus 로고
    • Thrombin activity appearing on the vessel wall after trauma
    • Dryjski M, Olsson P, Swedenborg J. Thrombin activity appearing on the vessel wall after trauma. Thromb Haemost. 1985;54:773-775.
    • (1985) Thromb Haemost , vol.54 , pp. 773-775
    • Dryjski, M.1    Olsson, P.2    Swedenborg, J.3
  • 17
    • 0028202551 scopus 로고
    • Radiolabeled r-hirudin as a measure of thrombin activity at, or within, the rabbit aorta wall in vitro and in vivo
    • Hatton MW, Ross-Ouellet B. Radiolabeled r-hirudin as a measure of thrombin activity at, or within, the rabbit aorta wall in vitro and in vivo. Thromb Haemost. 1994;71:499-506.
    • (1994) Thromb Haemost , vol.71 , pp. 499-506
    • Hatton, M.W.1    Ross-Ouellet, B.2
  • 18
    • 0024463903 scopus 로고
    • Deendothelialization in vivo initiates a thrombogenic reaction at the rabbit aorta surface: Correlation of uptake of fibrinogen and antithrombin III with thrombin generation by the exposed subendothelium
    • Hatton MW, Moar SL, Richardson M. Deendothelialization in vivo initiates a thrombogenic reaction at the rabbit aorta surface: correlation of uptake of fibrinogen and antithrombin III with thrombin generation by the exposed subendothelium. Am J Pathol. 1989;135:499-508.
    • (1989) Am J Pathol , vol.135 , pp. 499-508
    • Hatton, M.W.1    Moar, S.L.2    Richardson, M.3
  • 19
    • 0019944110 scopus 로고
    • Isolation and partial characterization of two distinct types of antithrombin III from rabbit
    • Carlson TH, Atencio AC. Isolation and partial characterization of two distinct types of antithrombin III from rabbit. Thromb Res. 1982;27:23-34.
    • (1982) Thromb Res , vol.27 , pp. 23-34
    • Carlson, T.H.1    Atencio, A.C.2
  • 20
    • 0021991632 scopus 로고
    • Isolation and characterization of an antithrombin III variant with reduced carbohydrate content and enhanced heparin binding
    • Peterson CB, Blackburn MN. Isolation and characterization of an antithrombin III variant with reduced carbohydrate content and enhanced heparin binding. J Biol Chem. 1985;260:610-615.
    • (1985) J Biol Chem , vol.260 , pp. 610-615
    • Peterson, C.B.1    Blackburn, M.N.2
  • 21
    • 0023666419 scopus 로고
    • Physiological variant of antithrombin-III lacks carbohydrate sidechain at Asn 135
    • Brennan SO, George PM, Jordan RE. Physiological variant of antithrombin-III lacks carbohydrate sidechain at Asn 135. FEBS Lett. 1987;219:431-436.
    • (1987) FEBS Lett , vol.219 , pp. 431-436
    • Brennan, S.O.1    George, P.M.2    Jordan, R.E.3
  • 22
    • 0017599989 scopus 로고
    • Antithrombin (heparin cofactor) assay with 'new' chromogenic substrates (S-2238 and chromozym TH)
    • Abildgaard U, Lie M, Ödegård OR. Antithrombin (heparin cofactor) assay with 'new' chromogenic substrates (S-2238 and chromozym TH). Thromb Res. 1977;11:549-553.
    • (1977) Thromb Res , vol.11 , pp. 549-553
    • Abildgaard, U.1    Lie, M.2    Ödegård, O.R.3
  • 23
    • 0017618237 scopus 로고
    • Crossed immunoelectrophoresis as applied to studies on complex formation: The binding of heparin to antithrombin III and the antithrombin III-thrombin complex
    • Andersson LO, Engman L, Henningsson E. Crossed immunoelectrophoresis as applied to studies on complex formation: the binding of heparin to antithrombin III and the antithrombin III-thrombin complex. J Immunol Methods. 1977;14:271-281.
    • (1977) J Immunol Methods , vol.14 , pp. 271-281
    • Andersson, L.O.1    Engman, L.2    Henningsson, E.3
  • 25
    • 0019131617 scopus 로고
    • Rapid radioimmunoassay of human fibrinopeptide A: Removal of cross-reacting fibrinogen with bentonite
    • Kockum C, Frebelius S. Rapid radioimmunoassay of human fibrinopeptide A: removal of cross-reacting fibrinogen with bentonite. Thromb Res. 1980;19:589-598.
    • (1980) Thromb Res , vol.19 , pp. 589-598
    • Kockum, C.1    Frebelius, S.2
  • 26
    • 0022374908 scopus 로고
    • Uptake and inactivation of thrombin on rabbit aortic endothelium studied with two different substrates
    • Swedenborg J, Dryjski M, Frebelius S, Olsson P. Uptake and inactivation of thrombin on rabbit aortic endothelium studied with two different substrates. Thromb Haemost. 1985;54:828-832.
    • (1985) Thromb Haemost , vol.54 , pp. 828-832
    • Swedenborg, J.1    Dryjski, M.2    Frebelius, S.3    Olsson, P.4
  • 29
    • 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 ST, Björk I. Predominant contribution of surface approximation to the mechanism of heparin acceleration of the antithrombin-thrombin reaction: elucidation from salt concentration effects. J Biol Chem. 1991;266:6353-6364.
    • (1991) J Biol Chem , vol.266 , pp. 6353-6364
    • Olson, S.T.1    Björk, I.2
  • 30
    • 0020060771 scopus 로고
    • Identification in vitro of an endothelial cell surface cofactor for antithrombin III: Parallel studies with isolated perfused rat hearts and microcarrier cultures of bovine endothelium
    • Busch C, Owen WG. Identification in vitro of an endothelial cell surface cofactor for antithrombin III: parallel studies with isolated perfused rat hearts and microcarrier cultures of bovine endothelium. J Clin Invest. 1982;69:726-729.
    • (1982) J Clin Invest , vol.69 , pp. 726-729
    • Busch, C.1    Owen, W.G.2
  • 31
    • 0020504339 scopus 로고
    • Properties of antithrombin-thrombin complex formed in the presence and in the absence of heparin
    • Danielsson A, Björk I. Properties of antithrombin-thrombin complex formed in the presence and in the absence of heparin. Biochem J. 1983;213:345-353.
    • (1983) Biochem J , vol.213 , pp. 345-353
    • Danielsson, A.1    Björk, I.2
  • 32
    • 0025477374 scopus 로고
    • Coagulant and noncoagulant thrombin enzymatic activity on the endothelium
    • Frebelius S, Nydahl S, Swedenborg J. Coagulant and noncoagulant thrombin enzymatic activity on the endothelium. Blood Coagul Fibrinolysis. 1990;1:285-292.
    • (1990) Blood Coagul Fibrinolysis , vol.1 , pp. 285-292
    • Frebelius, S.1    Nydahl, S.2    Swedenborg, J.3
  • 34
    • 0021325685 scopus 로고
    • Repair in arterial tissue: Demonstration of fibrinogen/fibrin in the normal and healing rabbit thoracic aorta by the indirect immunoperoxidase technique
    • Chemnitz J, Christensen BC. Repair in arterial tissue: demonstration of fibrinogen/fibrin in the normal and healing rabbit thoracic aorta by the indirect immunoperoxidase technique. Virchows Arch [A]. 1984;403:163-171.
    • (1984) Virchows Arch [A] , vol.403 , pp. 163-171
    • Chemnitz, J.1    Christensen, B.C.2
  • 35
    • 0023265740 scopus 로고
    • Immunochemical characterization of fibrinogen, fibrin I, and fibrin II in human thrombi and atherosclerotic lesions
    • Bini A, Fenoglio J, Sobel J, Owen J, Fejgl M, Kaplan KL. Immunochemical characterization of fibrinogen, fibrin I, and fibrin II in human thrombi and atherosclerotic lesions. Blood. 1987;69:1038-1045.
    • (1987) Blood , vol.69 , pp. 1038-1045
    • Bini, A.1    Fenoglio, J.2    Sobel, J.3    Owen, J.4    Fejgl, M.5    Kaplan, K.L.6
  • 36
    • 0024670167 scopus 로고
    • Fibrin monomer protects thrombin from inactivation by heparin-antithrcmbin III: Implications for heparin efficacy
    • Hogg PJ, Jackson CM. Fibrin monomer protects thrombin from inactivation by heparin-antithrcmbin III: implications for heparin efficacy. Proc Natl Acad Sci U S A. 1989;86:3619-3623.
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 3619-3623
    • Hogg, P.J.1    Jackson, C.M.2
  • 37
    • 0025146426 scopus 로고
    • Clot-bound thrombin is protected from inhibition by heparin-antithrombin III but is susceptible to inactivation by antithrombin III-independent inhibitors
    • Weitz JI, Hudoba M, Massel D, Maragonore J, Hirsh J. Clot-bound thrombin is protected from inhibition by heparin-antithrombin III but is susceptible to inactivation by antithrombin III-independent inhibitors. J Clin Invest. 1990;86:385-391.
    • (1990) J Clin Invest , vol.86 , pp. 385-391
    • Weitz, J.I.1    Hudoba, M.2    Massel, D.3    Maragonore, J.4    Hirsh, J.5
  • 39
    • 0027762134 scopus 로고
    • Evidence for thrombin binding to dermatan sulphate sites in the rabbit aorta subendothelium in vitro
    • Hatton MW. Evidence for thrombin binding to dermatan sulphate sites in the rabbit aorta subendothelium in vitro. Blood Coagul Fibrinolysis. 1993;4:927-933.
    • (1993) Blood Coagul Fibrinolysis , vol.4 , pp. 927-933
    • Hatton, M.W.1
  • 40
    • 0029093486 scopus 로고
    • Elimination of glycosylation heterogeneity affecting heparin affinity of recombinant human antithrombin III by expression of a b-like variant in baculovirus-infected insect cells
    • Ersdal-Badju E, Lu A, Peng X, Picard V, Zendehrouh P, Turk B, Björk I, Oison S, Bock SC. Elimination of glycosylation heterogeneity affecting heparin affinity of recombinant human antithrombin III by expression of a b-like variant in baculovirus-infected insect cells. Biochem J. 1995;310:323-330.
    • (1995) Biochem J , vol.310 , pp. 323-330
    • Ersdal-Badju, E.1    Lu, A.2    Peng, X.3    Picard, V.4    Zendehrouh, P.5    Turk, B.6    Björk, I.7    Oison, S.8    Bock, S.C.9
  • 41
    • 0025875294 scopus 로고
    • Antithrombin III-β associates more readily than antithrombin III-α with uninjured and de-endothelialized aortic wall in vitro and in vivo
    • Witmer MR, Hatton MW. Antithrombin III-β associates more readily than antithrombin III-α with uninjured and de-endothelialized aortic wall in vitro and in vivo. Arterioscler Thromb. 1991;11:530-539.
    • (1991) Arterioscler Thromb , vol.11 , pp. 530-539
    • Witmer, M.R.1    Hatton, M.W.2
  • 42
    • 0024467010 scopus 로고
    • Effect of heparin on the vascular distribution of *I-antithrombin III isoforms in rabbits
    • Carlson TH. Effect of heparin on the vascular distribution of *I-antithrombin III isoforms in rabbits. Thromb Res. 1989;55:471-480.
    • (1989) Thromb Res , vol.55 , pp. 471-480
    • Carlson, T.H.1
  • 43
    • 0023179111 scopus 로고
    • Distribution of antithrombin III in rabbits: Role of host and protein
    • Regoeczi E. Distribution of antithrombin III in rabbits: role of host and protein. Am J Physiol. 1987;252:457-461.
    • (1987) Am J Physiol , vol.252 , pp. 457-461
    • Regoeczi, E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.