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Volumn 99, Issue 4, 2008, Pages 668-674

Cleavage of factor XIII by human neutrophil elastase results in a novel active truncated form of factor XIII A subunit

Author keywords

Elastase; Factor XIII; Factor XIII A V34L polymorphism; Transglutaminase

Indexed keywords

AMINO ACID; BATROXOBIN; BATROXOBIN MOOJENI; BLOOD CLOTTING FACTOR 13A; BLOOD CLOTTING FACTOR 8; FIBRIN; LEUKOCYTE ELASTASE; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; THROMBIN; VALINE;

EID: 43749101177     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1160/TH07-09-0577     Document Type: Article
Times cited : (20)

References (43)
  • 1
    • 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: 271-305.
    • (1999) Thromb Res , vol.94 , pp. 271-305
    • Muszbek, L.1    Yee, V.C.2    Hevessy, Z.3
  • 3
    • 0033787010 scopus 로고    scopus 로고
    • Effect of Val34Leu polymorphism on the activation of the coagulation factor XIII-A
    • Wartiovaara U, Mikkola H, Szôke G, et al. Effect of Val34Leu polymorphism on the activation of the coagulation factor XIII-A. Thromb Haemost 2000; 84: 595-600.
    • (2000) Thromb Haemost , vol.84 , pp. 595-600
    • Wartiovaara, U.1    Mikkola, H.2    Szôke, G.3
  • 4
    • 0034254319 scopus 로고    scopus 로고
    • The factor XIII V34L polymorphism accelerates thrombin activation of factor XIII and affects cross-linked fibrin structure
    • Ariens RA, Philippou H, Nagaswami C, et al. The factor XIII V34L polymorphism accelerates thrombin activation of factor XIII and affects cross-linked fibrin structure. Blood 2000; 96: 988-995.
    • (2000) Blood , vol.96 , pp. 988-995
    • Ariens, R.A.1    Philippou, H.2    Nagaswami, C.3
  • 5
    • 0034307686 scopus 로고    scopus 로고
    • Val34Leu polymorphism of plasma FXIII: Biochemistry and epidemiology in familial thrombophilia
    • Balogh I, Szôke G, Kárpáti L, et al. Val34Leu polymorphism of plasma FXIII: biochemistry and epidemiology in familial thrombophilia. Blood 2000; 96: 2479-2486.
    • (2000) Blood , vol.96 , pp. 2479-2486
    • Balogh, I.1    Szôke, G.2    Kárpáti, L.3
  • 6
    • 0017724557 scopus 로고
    • The activation of plasma factor XIII with the snake venom enzymes ancrod and batroxobin marajoensis
    • Walter M, Nyman D, Krajnc V, et al. The activation of plasma factor XIII with the snake venom enzymes ancrod and batroxobin marajoensis. Thromb Haemost 1977; 38: 438-446.
    • (1977) Thromb Haemost , vol.38 , pp. 438-446
    • Walter, M.1    Nyman, D.2    Krajnc, V.3
  • 7
    • 0018646786 scopus 로고
    • Thrombocytin, a serine protease from Bothrops atrox venom. 2. Interaction with platelets and plasma-clotting factors
    • Niewiarowski S, Kirby EP, Brudzynski TM, et al. Thrombocytin, a serine protease from Bothrops atrox venom. 2. Interaction with platelets and plasma-clotting factors. Biochemistry 1979; 18: 3570-3577.
    • (1979) Biochemistry , vol.18 , pp. 3570-3577
    • Niewiarowski, S.1    Kirby, E.P.2    Brudzynski, T.M.3
  • 8
    • 0014549537 scopus 로고
    • The effect of proteolytic enzymes on fibrin stabilizing factor
    • Kopec M, Latallo ZS, Stahl M, et al. The effect of proteolytic enzymes on fibrin stabilizing factor. Biochim Biophys Acta 1969; 181: 437-445.
    • (1969) Biochim Biophys Acta , vol.181 , pp. 437-445
    • Kopec, M.1    Latallo, Z.S.2    Stahl, M.3
  • 9
    • 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, et al. 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: 1395-1407.
    • (1973) J Biol Chem , vol.248 , pp. 1395-1407
    • Schwartz, M.L.1    Pizzo, S.V.2    Hill, R.L.3
  • 10
    • 0016828167 scopus 로고
    • Alternative pathways for the activation of factor XIII
    • McDonagh J, McDonagh RP. Alternative pathways for the activation of factor XIII. Br J Haematol 1975; 30: 465-477.
    • (1975) Br J Haematol , vol.30 , pp. 465-477
    • McDonagh, J.1    McDonagh, R.P.2
  • 11
    • 0032711849 scopus 로고    scopus 로고
    • Elastase substrate specificity tailored through substrate-assisted catalysis and phage display
    • Dall'Acqua W, Halin C, Rodrigues ML, et al. Elastase substrate specificity tailored through substrate-assisted catalysis and phage display. Protein Eng 1999; 12: 981-987.
    • (1999) Protein Eng , vol.12 , pp. 981-987
    • Dall'Acqua, W.1    Halin, C.2    Rodrigues, M.L.3
  • 12
    • 0034608931 scopus 로고    scopus 로고
    • Rapid and general profiling of protease specificity by using combinatorial fluorogenic substrate libraries
    • Harris JL, Backes BJ, Leonetti F, et al. Rapid and general profiling of protease specificity by using combinatorial fluorogenic substrate libraries. Proc Natl Acad Sci USA 2000; 97: 7754-7759.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 7754-7759
    • Harris, J.L.1    Backes, B.J.2    Leonetti, F.3
  • 13
    • 0038306865 scopus 로고    scopus 로고
    • Compared action of neutrophil proteinase 3 and elastase on model substrates
    • Koehl C, Knight CG, Bieth JG. Compared action of neutrophil proteinase 3 and elastase on model substrates. J Biol Chem 2003; 278: 12609-12612.
    • (2003) J Biol Chem , vol.278 , pp. 12609-12612
    • Koehl, C.1    Knight, C.G.2    Bieth, J.G.3
  • 14
    • 0025767185 scopus 로고
    • ONO-5046, a novel inhibitor of human neutrophil elastase
    • Kawabata K, Suzuki M, Sugitani M, et al. ONO-5046, a novel inhibitor of human neutrophil elastase. Biochem Biophys Res Commun 1991; 177: 814-820.
    • (1991) Biochem Biophys Res Commun , vol.177 , pp. 814-820
    • Kawabata, K.1    Suzuki, M.2    Sugitani, M.3
  • 15
  • 16
    • 0025219629 scopus 로고
    • Non-proteolytic activation of cellular protransglutaminase (placental macrophage factor XIII)
    • Polgár J, Hidasi V, Muszbek L. Non-proteolytic activation of cellular protransglutaminase (placental macrophage factor XIII). Biochem J 1990; 267: 557-560.
    • (1990) Biochem J , vol.267 , pp. 557-560
    • Polgár, J.1    Hidasi, V.2    Muszbek, L.3
  • 17
    • 4444249428 scopus 로고    scopus 로고
    • Rapid detection of the factor XIII Val34Leu (163 G->T) polymorphism by real-time PCR using fluorescence resonance energy transfer detection and melting curve analysis
    • Shemirani AH, Muszbek L. Rapid detection of the factor XIII Val34Leu (163 G->T) polymorphism by real-time PCR using fluorescence resonance energy transfer detection and melting curve analysis. Clin Chem Lab Med 2004; 42: 877-879.
    • (2004) Clin Chem Lab Med , vol.42 , pp. 877-879
    • Shemirani, A.H.1    Muszbek, L.2
  • 18
    • 0033636292 scopus 로고    scopus 로고
    • A modified, optimized kinetic photometric assay for the determination of blood coagulation factor XIII activity in plasma
    • Kárpáti L, Penke B, Katona E, et al. A modified, optimized kinetic photometric assay for the determination of blood coagulation factor XIII activity in plasma. Clin Chem 2000; 46: 1946-1955.
    • (2000) Clin Chem , vol.46 , pp. 1946-1955
    • Kárpáti, L.1    Penke, B.2    Katona, E.3
  • 19
    • 0035159395 scopus 로고    scopus 로고
    • Protransglutaminase (Factor XIII) mediated crosslinking of fibrinogen and fibrin
    • Siebenlist KR, Meh DA, Mosesson MW. Protransglutaminase (Factor XIII) mediated crosslinking of fibrinogen and fibrin. Thromb Haemost 2001; 86: 1221-1228.
    • (2001) Thromb Haemost , vol.86 , pp. 1221-1228
    • Siebenlist, K.R.1    Meh, D.A.2    Mosesson, M.W.3
  • 21
    • 18744421735 scopus 로고    scopus 로고
    • Two non-proline cis peptide bonds may be important for factor XIII function
    • Weiss MS, Metzner HJ, Hilgenfeld R. Two non-proline cis peptide bonds may be important for factor XIII function. FEBS Letters 1998; 423: 291-296.
    • (1998) FEBS Letters , vol.423 , pp. 291-296
    • Weiss, M.S.1    Metzner, H.J.2    Hilgenfeld, R.3
  • 22
    • 0029878720 scopus 로고    scopus 로고
    • Humphrey W, Dalke A, Schulten K. VMD - Visual Molecular Dynamics. J Molec Graphics 1996; 14: 33-38.
    • Humphrey W, Dalke A, Schulten K. VMD - Visual Molecular Dynamics. J Molec Graphics 1996; 14: 33-38.
  • 23
    • 0025819769 scopus 로고
    • Role of calcium ion in the generation of factor XIII activity
    • Hornyak TJ, Shaffer JA. Role of calcium ion in the generation of factor XIII activity. Biochemistry 1991; 30: 6175-6182.
    • (1991) Biochemistry , vol.30 , pp. 6175-6182
    • Hornyak, T.J.1    Shaffer, J.A.2
  • 24
    • 0346374927 scopus 로고
    • Application of snake venom proteins in the diagnosis of hemostatic disorders
    • Stocker K ed, Boca Raton: CRC-Press
    • Stocker K. Application of snake venom proteins in the diagnosis of hemostatic disorders. In: Stocker K ed. Medical use of snake venom proteins. Boca Raton: CRC-Press, 1990: 213-252.
    • (1990) Medical use of snake venom proteins , pp. 213-252
    • Stocker, K.1
  • 25
    • 0017258208 scopus 로고
    • The thrombin-like enzyme from Bothrops atrox snake venom
    • Holleman WH, Weiss LJ. The thrombin-like enzyme from Bothrops atrox snake venom. J Biol Chem 1976; 251: 1663-1669.
    • (1976) J Biol Chem , vol.251 , pp. 1663-1669
    • Holleman, W.H.1    Weiss, L.J.2
  • 26
    • 0016724877 scopus 로고
    • Effect of elastase-like and chymotrpysin-like neutral proteases from human granulocytes on isolated clotting factors
    • Schmidt W, Egbring R, Havemann K. Effect of elastase-like and chymotrpysin-like neutral proteases from human granulocytes on isolated clotting factors. Thromb Res 1975; 5: 315-326.
    • (1975) Thromb Res , vol.5 , pp. 315-326
    • Schmidt, W.1    Egbring, R.2    Havemann, K.3
  • 27
    • 0020353188 scopus 로고
    • Degradation of human plasma fibrin stabilizing factor XIII subunits by human granulocytic proteinases
    • Klingemann HG, Egbring R, Holst F, et al. Degradation of human plasma fibrin stabilizing factor XIII subunits by human granulocytic proteinases. Thromb Res 1982; 25: 793-801.
    • (1982) Thromb Res , vol.25 , pp. 793-801
    • Klingemann, H.G.1    Egbring, R.2    Holst, F.3
  • 28
    • 0018848968 scopus 로고
    • Granulocyte elastase activation and degradation of factor XIII
    • Henriksson P, Nilsson IM, Ohlsson K, et al. Granulocyte elastase activation and degradation of factor XIII. Thromb Res 1980; 18: 343-351.
    • (1980) Thromb Res , vol.18 , pp. 343-351
    • Henriksson, P.1    Nilsson, I.M.2    Ohlsson, K.3
  • 29
    • 0027155343 scopus 로고
    • Association of A subunits of recombinant placental factor XIII with the native carrier B subunits from human plasma
    • Radek JT, Jeong JM, Wilson J, et al. Association of A subunits of recombinant placental factor XIII with the native carrier B subunits from human plasma. Biochemistry 1993; 32: 3527-3534.
    • (1993) Biochemistry , vol.32 , pp. 3527-3534
    • Radek, J.T.1    Jeong, J.M.2    Wilson, J.3
  • 30
    • 0027428185 scopus 로고
    • Human plasma factor XIII: Subunit interactions and activation of zymogen
    • Lorand L, Jeong JM, Radek JT, et al. Human plasma factor XIII: Subunit interactions and activation of zymogen. Methods Enzymol 1993; 222: 22-35.
    • (1993) Methods Enzymol , vol.222 , pp. 22-35
    • Lorand, L.1    Jeong, J.M.2    Radek, J.T.3
  • 31
    • 0029064315 scopus 로고
    • Structural evidence that the activation peptide is not released upon thrombin cleavage of factor XIII
    • Yee VC, Pedersen LC, Bishop PD, et al. Structural evidence that the activation peptide is not released upon thrombin cleavage of factor XIII. Thromb Res 1995; 78: 389-397.
    • (1995) Thromb Res , vol.78 , pp. 389-397
    • Yee, V.C.1    Pedersen, L.C.2    Bishop, P.D.3
  • 32
    • 34250679321 scopus 로고    scopus 로고
    • Factor XIII activation peptide is released into plasma upon cleavage by thrombin and shows a different structure compared to its bound form
    • Schroeder V, Vuissoz J, Caflisch A, et al. Factor XIII activation peptide is released into plasma upon cleavage by thrombin and shows a different structure compared to its bound form. Thromb Haemost 2007; 97: 890-898.
    • (2007) Thromb Haemost , vol.97 , pp. 890-898
    • Schroeder, V.1    Vuissoz, J.2    Caflisch, A.3
  • 33
    • 0030787645 scopus 로고    scopus 로고
    • Human neutrophil elastase activates human factor V but inactivates thrombin-activated human factor V
    • Samis JA, Garrett M, Manuel RP, et al. Human neutrophil elastase activates human factor V but inactivates thrombin-activated human factor V. Blood 1997; 90: 1065-1074.
    • (1997) Blood , vol.90 , pp. 1065-1074
    • Samis, J.A.1    Garrett, M.2    Manuel, R.P.3
  • 34
    • 0025398325 scopus 로고
    • The elastase-mediated pathway of fibrinolysis
    • Machovich R, Owen WG. The elastase-mediated pathway of fibrinolysis. Blood Coag Fibrinol 1990; 1: 79-90.
    • (1990) Blood Coag Fibrinol , vol.1 , pp. 79-90
    • Machovich, R.1    Owen, W.G.2
  • 36
    • 0029932045 scopus 로고    scopus 로고
    • Human eosinophils lack human leukocyte elastase
    • Wiedow O, Muehle K, Sreit V, et al. Human eosinophils lack human leukocyte elastase. Biochim Biophys Acta 1996; 1315: 185-187.
    • (1996) Biochim Biophys Acta , vol.1315 , pp. 185-187
    • Wiedow, O.1    Muehle, K.2    Sreit, V.3
  • 37
    • 0034672149 scopus 로고    scopus 로고
    • Polymorphonuclear leukocyte activation and hemostasis in patients with essential thrombocythemia and polycythemia vera
    • Falanga A, Marchetti M, Evangelista V, et al. Polymorphonuclear leukocyte activation and hemostasis in patients with essential thrombocythemia and polycythemia vera. Blood 2000; 96: 4261-4266.
    • (2000) Blood , vol.96 , pp. 4261-4266
    • Falanga, A.1    Marchetti, M.2    Evangelista, V.3
  • 38
    • 16244397365 scopus 로고    scopus 로고
    • Neutrophil serine proteases: Potential key regulators of cell signalling during inflammation
    • Wiedow O, Meyer-Hoffert U. Neutrophil serine proteases: potential key regulators of cell signalling during inflammation. J Int Med 2005; 257: 319-328.
    • (2005) J Int Med , vol.257 , pp. 319-328
    • Wiedow, O.1    Meyer-Hoffert, U.2
  • 40
    • 0031913016 scopus 로고    scopus 로고
    • Achyuthan KE. Characterization of the reciprocal binding sites on human α-thrombin and factor XIII A-chain. Mol Cel Biochem 1998; 178: 289-297.
    • Achyuthan KE. Characterization of the reciprocal binding sites on human α-thrombin and factor XIII A-chain. Mol Cel Biochem 1998; 178: 289-297.
  • 41
    • 34547880019 scopus 로고    scopus 로고
    • Down-regulation of activated factor XIII by polymorphonuclear granulocyte proteases within fibrin clot
    • Bagoly Z, Haramura G, Muszbek L. Down-regulation of activated factor XIII by polymorphonuclear granulocyte proteases within fibrin clot. Thromb Haemost 2007; 98: 359-367.
    • (2007) Thromb Haemost , vol.98 , pp. 359-367
    • Bagoly, Z.1    Haramura, G.2    Muszbek, L.3
  • 42
    • 1242306798 scopus 로고    scopus 로고
    • Role of human neutrophil peptides in lung inflammation associated with α1-antitrypsin deficiency
    • Spencer LT, Paone G, Krein PM, et al. Role of human neutrophil peptides in lung inflammation associated with α1-antitrypsin deficiency. Am J Physiol Lung Cell Mol Physiol 2004; 286: L514-520.
    • (2004) Am J Physiol Lung Cell Mol Physiol , vol.286
    • Spencer, L.T.1    Paone, G.2    Krein, P.M.3
  • 43
    • 25144444423 scopus 로고    scopus 로고
    • Factor XIII in bronchoalveolar lavage fluid from children with chronic bronchoalveolar inflammation
    • Katona É, Nagy B, Kappelmayer J, et al. Factor XIII in bronchoalveolar lavage fluid from children with chronic bronchoalveolar inflammation. J Throm Haemost 2005; 3: 1407-1413.
    • (2005) J Throm Haemost , vol.3 , pp. 1407-1413
    • Katona, E.1    Nagy, B.2    Kappelmayer, J.3


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