메뉴 건너뛰기




Volumn 124, Issue 26, 2014, Pages 3982-3990

Functional factor XIII-A is exposed on the stimulated platelet surface

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA 2 ANTIPLASMIN; BLOOD CLOTTING FACTOR 13A; COLLAGEN; FIBRIN; NEUTRALIZING ANTIBODY; PHOSPHATIDYLSERINE; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; THROMBIN; ANTIFIBRINOLYTIC AGENT; CROSS LINKING REAGENT;

EID: 84919476363     PISSN: 00064971     EISSN: 15280020     Source Type: Journal    
DOI: 10.1182/blood-2014-06-583070     Document Type: Article
Times cited : (102)

References (75)
  • 2
    • 0027993303 scopus 로고
    • Progressive cross-linking of fibrin gamma chains increases resistance to fibrinolysis
    • Siebenlist KR, Mosesson MW. Progressive cross-linking of fibrin gamma chains increases resistance to fibrinolysis. J Biol Chem. 1994;269(45):28414-28419.
    • (1994) J Biol Chem , vol.269 , Issue.45 , pp. 28414-28419
    • Siebenlist, K.R.1    Mosesson, M.W.2
  • 3
    • 0020077284 scopus 로고
    • Significance of cross-linking of alpha 2-plasmin inhibitor to fibrin in inhibition of fibrinolysis and in hemostasis
    • Sakata Y, Aoki N. Significance of cross-linking of alpha 2-plasmin inhibitor to fibrin in inhibition of fibrinolysis and in hemostasis. J Clin Invest. 1982;69(3):536-542.
    • (1982) J Clin Invest , vol.69 , Issue.3 , pp. 536-542
    • Sakata, Y.1    Aoki, N.2
  • 4
    • 0013932934 scopus 로고
    • Factor 13 deficiency with severe hemorrhagic diathesis
    • Fisher S, Rikover M, Naor S. Factor 13 deficiency with severe hemorrhagic diathesis. Blood. 1966;28(1):34-39.
    • (1966) Blood , vol.28 , Issue.1 , pp. 34-39
    • Fisher, S.1    Rikover, M.2    Naor, S.3
  • 5
    • 0042233483 scopus 로고    scopus 로고
    • Novel proangiogenic effect of factor XIII associated with suppression of thrombospondin 1 expression
    • Dardik R, Solomon A, Loscalzo J, et al. Novel proangiogenic effect of factor XIII associated with suppression of thrombospondin 1 expression. Arterioscler Thromb Vasc Biol. 2003;23(8):1472-1477.
    • (2003) Arterioscler Thromb Vasc Biol , vol.23 , Issue.8 , pp. 1472-1477
    • Dardik, R.1    Solomon, A.2    Loscalzo, J.3
  • 6
    • 0015367004 scopus 로고
    • Congenital deficiency of fibrin-stabilizing factor (factor XIII): A report of four cases (two families) and family members
    • Aziz MA, Siddigui AR. Congenital deficiency of fibrin-stabilizing factor (factor XIII): a report of four cases (two families) and family members. Blood. 1972;40(1):11-15.
    • (1972) Blood , vol.40 , Issue.1 , pp. 11-15
    • Aziz, M.A.1    Siddigui, A.R.2
  • 7
    • 0342847031 scopus 로고
    • Congenital deficiency of fibrin-stabilising factor; a report of three unrelated cases
    • Losowsky MS, Hall R, Goldie W. Congenital deficiency of fibrin-stabilising factor; a report of three unrelated cases. Lancet. 1965;1(7404):156-158.
    • (1965) Lancet , vol.1 , Issue.7404 , pp. 156-158
    • Losowsky, M.S.1    Hall, R.2    Goldie, W.3
  • 8
    • 84897516595 scopus 로고    scopus 로고
    • Interaction of factor XIII subunits
    • Katona E, Pénzes K, Csapó A, et al. Interaction of factor XIII subunits. Blood. 2014;123(11):1757-1763.
    • (2014) Blood , vol.123 , Issue.11 , pp. 1757-1763
    • Katona, E.1    Pénzes, K.2    Csapó, A.3
  • 9
    • 0002162129 scopus 로고
    • Activation of the Fibrin Stabilizing Factor of Plasma by Thrombin
    • Lorand L, Konishi K. Activation of the Fibrin Stabilizing Factor of Plasma by Thrombin. Arch Biochem Biophys. 1964;105:58-67.
    • (1964) Arch Biochem Biophys , vol.105 , pp. 58-67
    • Lorand, L.1    Konishi, K.2
  • 10
    • 0015935236 scopus 로고
    • Human Factor XIII from plasma and platelets. Molecular weights, subunit structures, proteolytic activation, and cross-linking of fibrinogen and fibrin
    • Schwartz ML, Pizzo SV, Hill RL, McKee PA. Human Factor XIII from plasma and platelets. Molecular weights, subunit structures, proteolytic activation, and cross-linking of fibrinogen and fibrin. J Biol Chem. 1973;248(4):1395-1407.
    • (1973) J Biol Chem , vol.248 , Issue.4 , pp. 1395-1407
    • Schwartz, M.L.1    Pizzo, S.V.2    Hill, R.L.3    McKee, P.A.4
  • 11
    • 0016198707 scopus 로고
    • Viscoelastic properties of ligation-inhibited fibrin clots
    • Mockros LF, Roberts WW, Lorand L. Viscoelastic properties of ligation-inhibited fibrin clots. Biophys Chem. 1974;2(2):164-169.
    • (1974) Biophys Chem , vol.2 , Issue.2 , pp. 164-169
    • Mockros, L.F.1    Roberts, W.W.2    Lorand, L.3
  • 12
    • 0020596436 scopus 로고
    • Contribution of fibrin stabilization to clot strength. Supplementation of factor XIII-deficient plasma with the purified zymogen
    • Shen L, Lorand L. Contribution of fibrin stabilization to clot strength. Supplementation of factor XIII-deficient plasma with the purified zymogen. J Clin Invest. 1983;71(5):1336-1341.
    • (1983) J Clin Invest , vol.71 , Issue.5 , pp. 1336-1341
    • Shen, L.1    Lorand, L.2
  • 13
    • 0014428478 scopus 로고
    • Cross-link in fibrin polymerized by factor 13: Epsilon-(gamma-glutamyl)lysine
    • Pisano JJ, Finlayson JS, Peyton MP. [Cross-link in fibrin polymerized by factor 13: epsilon-(gamma-glutamyl)lysine]. Science. 1968;160(3830):892-893.
    • (1968) Science , vol.160 , Issue.3830 , pp. 892-893
    • Pisano, J.J.1    Finlayson, J.S.2    Peyton, M.P.3
  • 14
    • 0014480824 scopus 로고
    • Chemical and enzymic detection of protein cross-links. Measurement of epsilon-(gamma-glutamyl)lysine in fibrin polymerized by factor XIII
    • Pisano JJ, Finlayson JS, Peyton MP. Chemical and enzymic detection of protein cross-links. Measurement of epsilon-(gamma-glutamyl)lysine in fibrin polymerized by factor XIII. Biochemistry. 1969;8(3):871-876.
    • (1969) Biochemistry , vol.8 , Issue.3 , pp. 871-876
    • Pisano, J.J.1    Finlayson, J.S.2    Peyton, M.P.3
  • 15
    • 0020625071 scopus 로고
    • Effects of crosslinking on the rigidity and proteolytic susceptibility of human fibrin clots
    • Gladner JA, Nossal R. Effects of crosslinking on the rigidity and proteolytic susceptibility of human fibrin clots. Thromb Res. 1983;30(3):273-288.
    • (1983) Thromb Res , vol.30 , Issue.3 , pp. 273-288
    • Gladner, J.A.1    Nossal, R.2
  • 16
    • 0014817348 scopus 로고
    • Subunit structure of human fibrinogen, soluble fibrin, and crosslinked insoluble fibrin
    • McKee PA, Mattock P, Hill RL. Subunit structure of human fibrinogen, soluble fibrin, and crosslinked insoluble fibrin. Proc Natl Acad Sci USA. 1970;66(3):738-744.
    • (1970) Proc Natl Acad Sci USA , vol.66 , Issue.3 , pp. 738-744
    • McKee, P.A.1    Mattock, P.2    Hill, R.L.3
  • 17
    • 0018864494 scopus 로고
    • Cross-linking of alpha 2-plasmin inhibitor to fibrin by fibrin-stabilizing factor
    • Sakata Y, Aoki N. Cross-linking of alpha 2-plasmin inhibitor to fibrin by fibrin-stabilizing factor. J Clin Invest. 1980;65(2):290-297.
    • (1980) J Clin Invest , vol.65 , Issue.2 , pp. 290-297
    • Sakata, Y.1    Aoki, N.2
  • 18
    • 0032538447 scopus 로고    scopus 로고
    • Human procarboxypeptidase U, or thrombin-activable fibrinolysis inhibitor, is a substrate for transglutaminases. Evidence for transglutaminase-catalyzed cross-linking to fibrin
    • Valnickova Z, Enghild JJ. Human procarboxypeptidase U, or thrombin-activable fibrinolysis inhibitor, is a substrate for transglutaminases. Evidence for transglutaminase-catalyzed cross-linking to fibrin. J Biol Chem. 1998;273(42):27220-27224.
    • (1998) J Biol Chem , vol.273 , Issue.42 , pp. 27220-27224
    • Valnickova, Z.1    Enghild, J.J.2
  • 19
    • 0032892173 scopus 로고    scopus 로고
    • Monocyte plasminogen activator inhibitor 2 (PAI-2) inhibits u-PA-mediated fibrin clot lysis and is cross-linked to fibrin
    • Ritchie H, Robbie LA, Kinghorn S, Exley R, Booth NA. Monocyte plasminogen activator inhibitor 2 (PAI-2) inhibits u-PA-mediated fibrin clot lysis and is cross-linked to fibrin. Thromb Haemost. 1999;81(1):96-103.
    • (1999) Thromb Haemost , vol.81 , Issue.1 , pp. 96-103
    • Ritchie, H.1    Robbie, L.A.2    Kinghorn, S.3    Exley, R.4    Booth, N.A.5
  • 20
    • 0017102105 scopus 로고
    • Isolation and characterization of alpha2-plasmin inhibitor from human plasma. A novel proteinase inhibitor which inhibits activator-induced clot lysis
    • Moroi M, Aoki N. Isolation and characterization of alpha2-plasmin inhibitor from human plasma. A novel proteinase inhibitor which inhibits activator-induced clot lysis. J Biol Chem. 1976;251(19):5956-5965.
    • (1976) J Biol Chem , vol.251 , Issue.19 , pp. 5956-5965
    • Moroi, M.1    Aoki, N.2
  • 21
    • 0021361211 scopus 로고
    • Histidinerich glycoprotein and alpha 2-plasmin inhibitor in inhibition of plasminogen binding to fibrin
    • Ichinose A, Mimuro J, Koide T, Aoki N. Histidinerich glycoprotein and alpha 2-plasmin inhibitor in inhibition of plasminogen binding to fibrin. Thromb Res. 1984;33(4):401-407.
    • (1984) Thromb Res , vol.33 , Issue.4 , pp. 401-407
    • Ichinose, A.1    Mimuro, J.2    Koide, T.3    Aoki, N.4
  • 22
    • 0022979474 scopus 로고
    • Cross-linking site in fibrinogen for alpha 2-plasmin inhibitor
    • Kimura S, Aoki N. Cross-linking site in fibrinogen for alpha 2-plasmin inhibitor. J Biol Chem. 1986;261(33):15591-15595.
    • (1986) J Biol Chem , vol.261 , Issue.33 , pp. 15591-15595
    • Kimura, S.1    Aoki, N.2
  • 23
    • 84886602742 scopus 로고
    • Subcellular distribution of fibrinogen and factor XIII in human blood platelets
    • Lopaciuk S, Lovette KM, McDonagh J, Chuang HY, McDonagh RP. Subcellular distribution of fibrinogen and factor XIII in human blood platelets. Thromb Res. 1976;8(4):453-465.
    • (1976) Thromb Res , vol.8 , Issue.4 , pp. 453-465
    • Lopaciuk, S.1    Lovette, K.M.2    McDonagh, J.3    Chuang, H.Y.4    McDonagh, R.P.5
  • 24
    • 0021191788 scopus 로고
    • Immunocytochemical localization of albumin and factor XIII in thin cryo sections of human blood platelets
    • Sixma JJ, van den Berg A, Schiphorst M, Geuze HJ, McDonagh J. Immunocytochemical localization of albumin and factor XIII in thin cryo sections of human blood platelets. Thromb Haemost. 1984;51(3):388-391.
    • (1984) Thromb Haemost , vol.51 , Issue.3 , pp. 388-391
    • Sixma, J.J.1    Van Den Berg, A.2    Schiphorst, M.3    Geuze, H.J.4    McDonagh, J.5
  • 25
    • 0020060360 scopus 로고
    • Specific protein and glycoprotein deficiencies in platelets isolated from two patients with the gray platelet syndrome
    • Nurden AT, Kunicki TJ, Dupuis D, Soria C, Caen JP. Specific protein and glycoprotein deficiencies in platelets isolated from two patients with the gray platelet syndrome. Blood. 1982;59(4):709-718.
    • (1982) Blood , vol.59 , Issue.4 , pp. 709-718
    • Nurden, A.T.1    Kunicki, T.J.2    Dupuis, D.3    Soria, C.4    Caen, J.P.5
  • 26
    • 0027989599 scopus 로고
    • Specific binding of the transglutaminase, platelet factor XIII, to HSP27
    • Zhu Y, Tassi L, Lane W, Mendelsohn ME. Specific binding of the transglutaminase, platelet factor XIII, to HSP27. J Biol Chem. 1994;269(35):22379-22384.
    • (1994) J Biol Chem , vol.269 , Issue.35 , pp. 22379-22384
    • Zhu, Y.1    Tassi, L.2    Lane, W.3    Mendelsohn, M.E.4
  • 27
    • 0015240197 scopus 로고
    • The subunit structures of human plasma and platelet factor XIII (fibrin-stabilizing factor)
    • Schwartz ML, Pizzo SV, Hill RL, McKee PA. The subunit structures of human plasma and platelet factor XIII (fibrin-stabilizing factor). J Biol Chem. 1971;246(18):5851-5854.
    • (1971) J Biol Chem , vol.246 , Issue.18 , pp. 5851-5854
    • Schwartz, M.L.1    Pizzo, S.V.2    Hill, R.L.3    McKee, P.A.4
  • 28
    • 0035545750 scopus 로고    scopus 로고
    • Enzyme-linked immunosorbent assay for the determination of blood coagulation factor XIII A-subunit in plasma and in cell lysates
    • Katona E E, Ajzner E, Tóth K, Kárpáti L, Muszbek L. Enzyme-linked immunosorbent assay for the determination of blood coagulation factor XIII A-subunit in plasma and in cell lysates. J Immunol Methods. 2001;258(1-2):127-135.
    • (2001) J Immunol Methods , vol.258 , Issue.1-2 , pp. 127-135
    • Katona, E.E.1    Ajzner, E.2    Tóth, K.3    Kárpáti, L.4    Muszbek, L.5
  • 29
    • 0033152222 scopus 로고    scopus 로고
    • Blood coagulation factor XIII: Structure and function
    • Muszbek L, Yee VC, Hevessy Z. Blood coagulation factor XIII: structure and function. Thromb Res. 1999;94(5):271-305.
    • (1999) Thromb Res , vol.94 , Issue.5 , pp. 271-305
    • Muszbek, L.1    Yee, V.C.2    Hevessy, Z.3
  • 30
    • 33845525449 scopus 로고    scopus 로고
    • Factor XIII: Recommended terms and abbreviations
    • Muszbek L, Ariëns RA, Ichinose A; ISTH SSC SUBCOMMITTEE ON FACTOR XIII. Factor XIII: recommended terms and abbreviations. J Thromb Haemost. 2007;5(1):181-183.
    • (2007) J Thromb Haemost , vol.5 , Issue.1 , pp. 181-183
    • Muszbek, L.1    Ariëns, R.A.2    Ichinose, A.3
  • 31
    • 0027512006 scopus 로고
    • Platelet factor XIII becomes active without the release of activation peptide during platelet activation
    • Muszbek L, Polgár J, Boda Z. Platelet factor XIII becomes active without the release of activation peptide during platelet activation. Thromb Haemost. 1993;69(3):282-285.
    • (1993) Thromb Haemost , vol.69 , Issue.3 , pp. 282-285
    • Muszbek, L.1    Polgár, J.2    Boda, Z.3
  • 32
    • 0024560892 scopus 로고
    • Differential sensitivity of erythrocyte-rich and platelet-rich arterial thrombi to lysis with recombinant tissue-type plasminogen activator. A possible explanation for resistance to coronary thrombolysis
    • Jang IK, Gold HK, Ziskind AA, et al. Differential sensitivity of erythrocyte-rich and platelet-rich arterial thrombi to lysis with recombinant tissue-type plasminogen activator. A possible explanation for resistance to coronary thrombolysis. Circulation. 1989;79(4):920-928.
    • (1989) Circulation , vol.79 , Issue.4 , pp. 920-928
    • Jang, I.K.1    Gold, H.K.2    Ziskind, A.A.3
  • 33
    • 0026361547 scopus 로고
    • Fibrin-fibrin and alpha 2-antiplasmin-fibrin cross-linking by platelet factor XIII increases the resistance of platelet clots to fibrinolysis
    • Reed GL, Matsueda GR, Haber E. Fibrin-fibrin and alpha 2-antiplasmin-fibrin cross-linking by platelet factor XIII increases the resistance of platelet clots to fibrinolysis. Trans Assoc Am Physicians. 1991;104:21-28.
    • (1991) Trans Assoc Am Physicians , vol.104 , pp. 21-28
    • Reed, G.L.1    Matsueda, G.R.2    Haber, E.3
  • 34
    • 0026806596 scopus 로고
    • Platelet factor XIII increases the fibrinolytic resistance of platelet-rich clots by accelerating the crosslinking of alpha 2-antiplasmin to fibrin
    • Reed GL, Matsueda GR, Haber E. Platelet factor XIII increases the fibrinolytic resistance of platelet-rich clots by accelerating the crosslinking of alpha 2-antiplasmin to fibrin. Thromb Haemost. 1992;68(3):315-320.
    • (1992) Thromb Haemost , vol.68 , Issue.3 , pp. 315-320
    • Reed, G.L.1    Matsueda, G.R.2    Haber, E.3
  • 35
    • 0030070041 scopus 로고    scopus 로고
    • Promotion of the crosslinking of fibrin and alpha 2-antiplasmin by platelets
    • Hevessy Z, Haramura G, Boda Z, Udvardy M, Muszbek L. Promotion of the crosslinking of fibrin and alpha 2-antiplasmin by platelets. Thromb Haemost. 1996;75(1):161-167.
    • (1996) Thromb Haemost , vol.75 , Issue.1 , pp. 161-167
    • Hevessy, Z.1    Haramura, G.2    Boda, Z.3    Udvardy, M.4    Muszbek, L.5
  • 36
    • 0023584366 scopus 로고
    • Rapid formation of large molecular weight alpha-polymers in cross-linked fibrin induced by high factor XIII concentrations. Role of platelet factor XIII
    • Francis CW, Marder VJ. Rapid formation of large molecular weight alpha-polymers in cross-linked fibrin induced by high factor XIII concentrations. Role of platelet factor XIII. J Clin Invest. 1987; 80(5):1459-1465.
    • (1987) J Clin Invest , vol.80 , Issue.5 , pp. 1459-1465
    • Francis, C.W.1    Marder, V.J.2
  • 37
    • 0015860697 scopus 로고
    • Retention of platelet fibrin stabilizing factor during the platelet release reaction and clot retraction
    • Joist JH, Niewiarowski S. Retention of platelet fibrin stabilizing factor during the platelet release reaction and clot retraction. Thromb Diath Haemorrh. 1973;29(3):679-683.
    • (1973) Thromb Diath Haemorrh , vol.29 , Issue.3 , pp. 679-683
    • Joist, J.H.1    Niewiarowski, S.2
  • 38
    • 77949395187 scopus 로고    scopus 로고
    • Association of coagulation factor XIII-A with Golgi proteins within monocyte-macrophages: Implications for subcellular trafficking and secretion
    • Cordell PA, Kile BT, Standeven KF, Josefsson EC, Pease RJ, Grant PJ. Association of coagulation factor XIII-A with Golgi proteins within monocyte-macrophages: implications for subcellular trafficking and secretion. Blood. 2010;115(13):2674-2681.
    • (2010) Blood , vol.115 , Issue.13 , pp. 2674-2681
    • Cordell, P.A.1    Kile, B.T.2    Standeven, K.F.3    Josefsson, E.C.4    Pease, R.J.5    Grant, P.J.6
  • 39
    • 77956485373 scopus 로고    scopus 로고
    • Model thrombi formed under flow reveal the role of factor XIII-mediated cross-linking in resistance to fibrinolysis
    • Mutch NJ, Koikkalainen JS, Fraser SR, et al. Model thrombi formed under flow reveal the role of factor XIII-mediated cross-linking in resistance to fibrinolysis. J Thromb Haemost. 2010;8(9):2017-2024.
    • (2010) J Thromb Haemost , vol.8 , Issue.9 , pp. 2017-2024
    • Mutch, N.J.1    Koikkalainen, J.S.2    Fraser, S.R.3
  • 41
    • 77954490706 scopus 로고    scopus 로고
    • Activation of single-chain urokinase-type plasminogen activator by platelet-associated plasminogen: A mechanism for stimulation of fibrinolysis by platelets
    • Baeten KM, Richard MC, Kanse SM, Mutch NJ, Degen JL, Booth NA. Activation of single-chain urokinase-type plasminogen activator by platelet-associated plasminogen: a mechanism for stimulation of fibrinolysis by platelets. J Thromb Haemost. 2010;8(6):1313-1322.
    • (2010) J Thromb Haemost , vol.8 , Issue.6 , pp. 1313-1322
    • Baeten, K.M.1    Richard, M.C.2    Kanse, S.M.3    Mutch, N.J.4    Degen, J.L.5    Booth, N.A.6
  • 42
    • 34548104845 scopus 로고    scopus 로고
    • A collaborative study to establish the 1st International Standard for factor XIII plasma
    • Raut S, Merton RE, Rigsby P, et al; ISTH/SSC Factor XIII Subcommittee and the Factor XIII Standardization Working Party. A collaborative study to establish the 1st International Standard for factor XIII plasma. J Thromb Haemost. 2007;5(9):1923-1929.
    • (2007) J Thromb Haemost , vol.5 , Issue.9 , pp. 1923-1929
    • Raut, S.1    Merton, R.E.2    Rigsby, P.3
  • 43
    • 0027935343 scopus 로고
    • Transglutaminase inhibition by 2-[(2-oxopropyl)thio]imidazolium derivatives: Mechanism of factor XIIIa inactivation
    • Freund KF, Doshi KP, Gaul SL, et al. Transglutaminase inhibition by 2-[(2-oxopropyl)thio]imidazolium derivatives: mechanism of factor XIIIa inactivation. Biochemistry. 1994;33(33):10109-10119.
    • (1994) Biochemistry , vol.33 , Issue.33 , pp. 10109-10119
    • Freund, K.F.1    Doshi, K.P.2    Gaul, S.L.3
  • 46
    • 0023720668 scopus 로고
    • Cytofluorometric identification of plasmin-sensitive factor XIIIa binding to platelets
    • Kreager JA, Devine DV, Greenberg CS. Cytofluorometric identification of plasmin-sensitive factor XIIIa binding to platelets. Thromb Haemost. 1988;60(1):88-93.
    • (1988) Thromb Haemost , vol.60 , Issue.1 , pp. 88-93
    • Kreager, J.A.1    Devine, D.V.2    Greenberg, C.S.3
  • 47
    • 67749139590 scopus 로고    scopus 로고
    • Binding of plasma factor XIII to thrombin-receptor activated human platelets
    • Nagy B Jr, Simon Z, Bagoly Z, Muszbek L, Kappelmayer J. Binding of plasma factor XIII to thrombin-receptor activated human platelets. Thromb Haemost. 2009;102(1):83-89.
    • (2009) Thromb Haemost , vol.102 , Issue.1 , pp. 83-89
    • Nagy, B.1    Simon, Z.2    Bagoly, Z.3    Muszbek, L.4    Kappelmayer, J.5
  • 48
    • 0030845821 scopus 로고    scopus 로고
    • Collagen but not fibrinogen surfaces induce bleb formation, exposure of phosphatidylserine, and procoagulant activity of adherent platelets: Evidence for regulation by protein tyrosine kinase-dependent Ca2+ responses
    • Heemskerk JW, Vuist WM, Feijge MA, Reutelingsperger CP, Lindhout T. Collagen but not fibrinogen surfaces induce bleb formation, exposure of phosphatidylserine, and procoagulant activity of adherent platelets: evidence for regulation by protein tyrosine kinase-dependent Ca2+ responses. Blood. 1997;90(7):2615-2625.
    • (1997) Blood , vol.90 , Issue.7 , pp. 2615-2625
    • Heemskerk, J.W.1    Vuist, W.M.2    Feijge, M.A.3    Reutelingsperger, C.P.4    Lindhout, T.5
  • 49
    • 0034161567 scopus 로고    scopus 로고
    • Surface expression and functional characterization of alpha-granule factor V in human platelets: Effects of ionophore A23187, thrombin, collagen, and convulxin
    • Alberio L, Safa O, Clemetson KJ, Esmon CT, Dale GL. Surface expression and functional characterization of alpha-granule factor V in human platelets: effects of ionophore A23187, thrombin, collagen, and convulxin. Blood. 2000;95(5):1694-1702.
    • (2000) Blood , vol.95 , Issue.5 , pp. 1694-1702
    • Alberio, L.1    Safa, O.2    Clemetson, K.J.3    Esmon, C.T.4    Dale, G.L.5
  • 50
    • 28444436585 scopus 로고    scopus 로고
    • Coated-platelets: An emerging component of the procoagulant response
    • Dale GL. Coated-platelets: an emerging component of the procoagulant response. J Thromb Haemost. 2005;3(10):2185-2192.
    • (2005) J Thromb Haemost , vol.3 , Issue.10 , pp. 2185-2192
    • Dale, G.L.1
  • 51
    • 0037050027 scopus 로고    scopus 로고
    • Stimulated platelets use serotonin to enhance their retention of procoagulant proteins on the cell surface
    • Dale GL, Friese P, Batar P, et al. Stimulated platelets use serotonin to enhance their retention of procoagulant proteins on the cell surface. Nature. 2002;415(6868):175-179.
    • (2002) Nature , vol.415 , Issue.6868 , pp. 175-179
    • Dale, G.L.1    Friese, P.2    Batar, P.3
  • 52
    • 28844461139 scopus 로고    scopus 로고
    • Role of FcRgamma and factor XIIIA in coated platelet formation
    • Jobe SM, Leo L, Eastvold JS, et al. Role of FcRgamma and factor XIIIA in coated platelet formation. Blood. 2005;106(13):4146-4151.
    • (2005) Blood , vol.106 , Issue.13 , pp. 4146-4151
    • Jobe, S.M.1    Leo, L.2    Eastvold, J.S.3
  • 53
    • 84885579102 scopus 로고    scopus 로고
    • Procoagulant platelets form an α-granule protein-covered "cap" on their surface that promotes their attachment to aggregates
    • Abaeva AA, Canault M, Kotova YN, et al. Procoagulant platelets form an α-granule protein-covered "cap" on their surface that promotes their attachment to aggregates. J Biol Chem. 2013;288(41):29621-29632.
    • (2013) J Biol Chem , vol.288 , Issue.41 , pp. 29621-29632
    • Abaeva, A.A.1    Canault, M.2    Kotova, Y.N.3
  • 54
    • 0027250293 scopus 로고
    • Packaging zinc, fibrinogen, and factor XIII in platelet alpha-granules
    • Marx G, Korner G, Mou X, Gorodetsky R. Packaging zinc, fibrinogen, and factor XIII in platelet alpha-granules. J Cell Physiol. 1993;156(3):437-442.
    • (1993) J Cell Physiol , vol.156 , Issue.3 , pp. 437-442
    • Marx, G.1    Korner, G.2    Mou, X.3    Gorodetsky, R.4
  • 55
    • 84929315350 scopus 로고    scopus 로고
    • Platelet factor XIIIa release during platelet aggregation and plasma clot strength measured by thrombelastography in patients with coronary artery disease treated with clopidogrel
    • [published online ahead of print May 15, 2014].
    • Kreutz RP, Owens J, Lu D, et al. Platelet factor XIIIa release during platelet aggregation and plasma clot strength measured by thrombelastography in patients with coronary artery disease treated with clopidogrel [published online ahead of print May 15, 2014]. Platelets. doi: 10.3109/09537104.2014.916793.
    • Platelets
    • Kreutz, R.P.1    Owens, J.2    Lu, D.3
  • 56
    • 0034609554 scopus 로고    scopus 로고
    • Catalytic life of activated factor XIII in thrombi. Implications for fibrinolytic resistance and thrombus aging
    • Robinson BR, Houng AK, Reed GL. Catalytic life of activated factor XIII in thrombi. Implications for fibrinolytic resistance and thrombus aging. Circulation. 2000;102(10):1151-1157.
    • (2000) Circulation , vol.102 , Issue.10 , pp. 1151-1157
    • Robinson, B.R.1    Houng, A.K.2    Reed, G.L.3
  • 57
    • 0023939414 scopus 로고
    • Increased resistance to plasmic degradation of fibrin with highly crosslinked alpha-polymer chains formed at high factor XIII concentrations
    • Francis CW, Marder VJ. Increased resistance to plasmic degradation of fibrin with highly crosslinked alpha-polymer chains formed at high factor XIII concentrations. Blood. 1988;71(5):1361-1365.
    • (1988) Blood , vol.71 , Issue.5 , pp. 1361-1365
    • Francis, C.W.1    Marder, V.J.2
  • 58
    • 34147136729 scopus 로고    scopus 로고
    • TAFIa, PAI-1 and alpha-antiplasmin: Complementary roles in regulating lysis of thrombi and plasma clots
    • Mutch NJ, Thomas L, Moore NR, Lisiak KM, Booth NA. TAFIa, PAI-1 and alpha-antiplasmin: complementary roles in regulating lysis of thrombi and plasma clots. J Thromb Haemost. 2007;5(4):812-817.
    • (2007) J Thromb Haemost , vol.5 , Issue.4 , pp. 812-817
    • Mutch, N.J.1    Thomas, L.2    Moore, N.R.3    Lisiak, K.M.4    Booth, N.A.5
  • 59
    • 84888266721 scopus 로고    scopus 로고
    • Clot retraction is mediated by factor XIII-dependent fibrin-aIIbb3-myosin axis in platelet sphingomyelin-rich membrane rafts
    • Kasahara K, Kaneda M, Miki T, et al. Clot retraction is mediated by factor XIII-dependent fibrin-aIIbb3-myosin axis in platelet sphingomyelin-rich membrane rafts. Blood. 2013;122(19):3340-3348.
    • (2013) Blood , vol.122 , Issue.19 , pp. 3340-3348
    • Kasahara, K.1    Kaneda, M.2    Miki, T.3
  • 60
    • 33847397992 scopus 로고    scopus 로고
    • Active tissue factor pathway inhibitor is expressed on the surface of coated platelets
    • Maroney SA, Haberichter SL, Friese P, et al. Active tissue factor pathway inhibitor is expressed on the surface of coated platelets. Blood. 2007;109(5):1931-1937.
    • (2007) Blood , vol.109 , Issue.5 , pp. 1931-1937
    • Maroney, S.A.1    Haberichter, S.L.2    Friese, P.3
  • 61
    • 0033485648 scopus 로고    scopus 로고
    • Activated platelets release two types of membrane vesicles: Microvesicles by surface shedding and exosomes derived from exocytosis of multivesicular bodies and alpha-granules
    • Heijnen HF, Schiel AE, Fijnheer R, Geuze HJ, Sixma JJ. Activated platelets release two types of membrane vesicles: microvesicles by surface shedding and exosomes derived from exocytosis of multivesicular bodies and alpha-granules. Blood. 1999;94(11):3791-3799.
    • (1999) Blood , vol.94 , Issue.11 , pp. 3791-3799
    • Heijnen, H.F.1    Schiel, A.E.2    Fijnheer, R.3    Geuze, H.J.4    Sixma, J.J.5
  • 62
    • 0027369521 scopus 로고
    • The difference between platelet and plasma FXIII used to study the mechanism of platelet microvesicle formation
    • Holme PA, Brosstad F, Solum NO. The difference between platelet and plasma FXIII used to study the mechanism of platelet microvesicle formation. Thromb Haemost. 1993;70(4):681-686.
    • (1993) Thromb Haemost , vol.70 , Issue.4 , pp. 681-686
    • Holme, P.A.1    Brosstad, F.2    Solum, N.O.3
  • 63
    • 0037040831 scopus 로고    scopus 로고
    • A structural and dynamic investigation of the facilitating effect of glycoprotein IIb/IIIa inhibitors in dissolving platelet-rich clots
    • Collet JP, Montalescot G, Lesty C, Weisel JW. A structural and dynamic investigation of the facilitating effect of glycoprotein IIb/IIIa inhibitors in dissolving platelet-rich clots. Circ Res. 2002;90(4):428-434.
    • (2002) Circ Res , vol.90 , Issue.4 , pp. 428-434
    • Collet, J.P.1    Montalescot, G.2    Lesty, C.3    Weisel, J.W.4
  • 64
    • 14344270942 scopus 로고    scopus 로고
    • Effects of Abciximab on the architecture of platelet-rich clots in patients with acute myocardial infarction undergoing primary coronary intervention
    • Collet JP, Montalescot G, Lesty C, et al. Effects of Abciximab on the architecture of platelet-rich clots in patients with acute myocardial infarction undergoing primary coronary intervention. Circulation. 2001;103(19):2328-2331.
    • (2001) Circulation , vol.103 , Issue.19 , pp. 2328-2331
    • Collet, J.P.1    Montalescot, G.2    Lesty, C.3
  • 65
    • 0035162774 scopus 로고    scopus 로고
    • Disaggregation of in vitro preformed platelet-rich clots by abciximab increases fibrin exposure and promotes fibrinolysis
    • Collet JP, Montalescot G, Lesty C, et al. Disaggregation of in vitro preformed platelet-rich clots by abciximab increases fibrin exposure and promotes fibrinolysis. Arterioscler Thromb Vasc Biol. 2001;21(1):142-148.
    • (2001) Arterioscler Thromb Vasc Biol , vol.21 , Issue.1 , pp. 142-148
    • Collet, J.P.1    Montalescot, G.2    Lesty, C.3
  • 66
    • 84894223979 scopus 로고    scopus 로고
    • In vitro evaluation of clot quality and stability in a model of severe thrombocytopenia: Effect of fibrinogen, factor XIII and thrombin-activatable fibrinolysis inhibitor
    • Shenkman B, Einav Y, Livnat T, Budnik I, Martinowitz U. In vitro evaluation of clot quality and stability in a model of severe thrombocytopenia: effect of fibrinogen, factor XIII and thrombin-activatable fibrinolysis inhibitor. Blood Transfus. 2014;12(1):78-84.
    • (2014) Blood Transfus , vol.12 , Issue.1 , pp. 78-84
    • Shenkman, B.1    Einav, Y.2    Livnat, T.3    Budnik, I.4    Martinowitz, U.5
  • 67
    • 0016165963 scopus 로고
    • The effect of major surgical procedures on plasma and platelet levels of Factor XIII
    • Letheby BA, Davis RB, Larsen AE. The effect of major surgical procedures on plasma and platelet levels of Factor XIII. Thromb Diath Haemorrh. 1974;31(1):20-29.
    • (1974) Thromb Diath Haemorrh , vol.31 , Issue.1 , pp. 20-29
    • Letheby, B.A.1    Davis, R.B.2    Larsen, A.E.3
  • 68
    • 84888403866 scopus 로고    scopus 로고
    • Relevant bleeding diathesis due to acquired factor XIII deficiency
    • Janning M, Holstein K, Spath B, et al. Relevant bleeding diathesis due to acquired factor XIII deficiency. Hamostaseologie. 2013;33(Suppl 1):S50-S54.
    • (2013) Hamostaseologie , vol.33 , pp. S50-S54
    • Janning, M.1    Holstein, K.2    Spath, B.3
  • 69
    • 0025217734 scopus 로고
    • A familial factor XIII subunit B deficiency
    • Saito M, Asakura H, Yoshida T, et al. A familial factor XIII subunit B deficiency. Br J Haematol. 1990;74(3):290-294.
    • (1990) Br J Haematol , vol.74 , Issue.3 , pp. 290-294
    • Saito, M.1    Asakura, H.2    Yoshida, T.3
  • 70
    • 0029947440 scopus 로고    scopus 로고
    • Type I factor XIII deficiency is caused by a genetic defect of its b subunit: Insertion of triplet AAC in exon III leads to premature termination in the second Sushi domain
    • Izumi T, Hashiguchi T, Castaman G, et al. Type I factor XIII deficiency is caused by a genetic defect of its b subunit: insertion of triplet AAC in exon III leads to premature termination in the second Sushi domain. Blood. 1996;87(7):2769-2774.
    • (1996) Blood , vol.87 , Issue.7 , pp. 2769-2774
    • Izumi, T.1    Hashiguchi, T.2    Castaman, G.3
  • 71
    • 0035353185 scopus 로고    scopus 로고
    • Truncated mutant B subunit for factor XIII causes its deficiency due to impaired intracellular transportation
    • Koseki S, Souri M, Koga S, et al. Truncated mutant B subunit for factor XIII causes its deficiency due to impaired intracellular transportation. Blood. 2001;97(9):2667-2672.
    • (2001) Blood , vol.97 , Issue.9 , pp. 2667-2672
    • Koseki, S.1    Souri, M.2    Koga, S.3
  • 72
    • 60249088087 scopus 로고    scopus 로고
    • Severe bleeding complications caused by an autoantibody against the B subunit of plasma factor XIII: A novel form of acquired factor XIII deficiency
    • Ajzner E, Schlammadinger A, Kerényi A, et al. Severe bleeding complications caused by an autoantibody against the B subunit of plasma factor XIII: a novel form of acquired factor XIII deficiency. Blood. 2009;113(3):723-725.
    • (2009) Blood , vol.113 , Issue.3 , pp. 723-725
    • Ajzner, E.1    Schlammadinger, A.2    Kerényi, A.3
  • 73
    • 41849131483 scopus 로고    scopus 로고
    • Administration of factor XIII B subunit increased plasma factor XIII A subunit levels in factor XIII B subunit knock-out mice
    • Souri M, Koseki-Kuno S, Takeda N, Degen JL, Ichinose A. Administration of factor XIII B subunit increased plasma factor XIII A subunit levels in factor XIII B subunit knock-out mice. Int J Hematol. 2008;87(1):60-68.
    • (2008) Int J Hematol , vol.87 , Issue.1 , pp. 60-68
    • Souri, M.1    Koseki-Kuno, S.2    Takeda, N.3    Degen, J.L.4    Ichinose, A.5
  • 74
    • 0025008716 scopus 로고
    • Activation of endothelial cells induces platelet thrombus formation on their matrix. Studies of new in vitro thrombosis model with low molecular weight heparin as anticoagulant
    • Zwaginga JJ, Sixma JJ, de Groot PG. Activation of endothelial cells induces platelet thrombus formation on their matrix. Studies of new in vitro thrombosis model with low molecular weight heparin as anticoagulant. Arteriosclerosis. 1990;10(1):49-61.
    • (1990) Arteriosclerosis , vol.10 , Issue.1 , pp. 49-61
    • Zwaginga, J.J.1    Sixma, J.J.2    De Groot, P.G.3
  • 75
    • 0026013003 scopus 로고
    • Quantification of fibrin deposition in flowing blood with peroxidase-labeled fibrinogen. High shear rates induce decreased fibrin deposition and appearance of fibrin monomers
    • Tijburg PN, Ijsseldijk MJ, Sixma JJ, de Groot PG. Quantification of fibrin deposition in flowing blood with peroxidase-labeled fibrinogen. High shear rates induce decreased fibrin deposition and appearance of fibrin monomers. Arterioscler Thromb. 1991;11(2):211-220.
    • (1991) Arterioscler Thromb , vol.11 , Issue.2 , pp. 211-220
    • Tijburg, P.N.1    Ijsseldijk, M.J.2    Sixma, J.J.3    De Groot, P.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.