메뉴 건너뛰기




Volumn 7, Issue 4, 2009, Pages 627-633

Molecular mechanism of the interaction between activated factor XIII and its glutamine donor peptide substrate

Author keywords

A2 plasmin inhibitor; Factor XIII; Factor XIII substrate peptides; STD NMR; Transglutaminase

Indexed keywords

ALANINE; AMINO ACID; ASPARAGINE; BLOOD CLOTTING FACTOR 8; FIBRIN; GLUTAMINE; LEUCINE; PEPTIDE DERIVATIVE;

EID: 63049121121     PISSN: 15387933     EISSN: 15387836     Source Type: Journal    
DOI: 10.1111/j.1538-7836.2009.03291.x     Document Type: Article
Times cited : (16)

References (35)
  • 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
    • 0035159395 scopus 로고    scopus 로고
    • Protransglutaminase (factor XIII) mediated cross linking of fibrinogen and fibrin
    • Siebenlist KR, Meh D, Mosesson MW. Protransglutaminase (factor XIII) mediated cross linking of fibrinogen and fibrin. Thromb Haemost 2001; 86: 1221-8.
    • (2001) Thromb Haemost , vol.86 , pp. 1221-1228
    • Siebenlist, K.R.1    Meh, D.2    Mosesson, M.W.3
  • 4
    • 49849101064 scopus 로고    scopus 로고
    • Evidence that γ2-antiplasmin becomes covalently ligated to plasma fibrinogen in the circulation: A new role for plasma factor XIII in fibrinolysis regulation
    • Mosesson MW, Siebenlist KR, Hernandez I, Lee KN, Christiansen VJ, McKee PA. Evidence that γ2-antiplasmin becomes covalently ligated to plasma fibrinogen in the circulation: A new role for plasma factor XIII in fibrinolysis regulation. J Thromb Haemost 2008; 6: 1565-70.
    • (2008) J Thromb Haemost , vol.6 , pp. 1565-1570
    • Mosesson, M.W.1    Siebenlist, K.R.2    Hernandez, I.3    Lee, K.N.4    Christiansen, V.J.5    McKee, P.A.6
  • 5
    • 0028177839 scopus 로고
    • Different NH2-terminal form with 12 additional residues of alpha 2-plasmin inhibitor from human plasma and culture media of Hep G2 cells
    • Koyama T, Koike Y, Toyota S, Miyagi F, Suzuki N, Aoki N. Different NH2-terminal form with 12 additional residues of alpha 2-plasmin inhibitor from human plasma and culture media of Hep G2 cells. Biochem Biophys Res Commun 1994; 200: 417-22.
    • (1994) Biochem Biophys Res Commun , vol.200 , pp. 417-422
    • Koyama, T.1    Koike, Y.2    Toyota, S.3    Miyagi, F.4    Suzuki, N.5    Aoki, N.6
  • 6
    • 2342447229 scopus 로고    scopus 로고
    • A novel plasma proteinase potentiates alpha2-antiplasmin inhibition of fibrin digestion
    • Lee KN, Jackson KW, Christiansen VJ, Chung KH, McKee PA. A novel plasma proteinase potentiates alpha2-antiplasmin inhibition of fibrin digestion. Blood 2004; 103: 3783-8.
    • (2004) Blood , vol.103 , pp. 3783-3788
    • Lee, K.N.1    Jackson, K.W.2    Christiansen, V.J.3    Chung, K.H.4    McKee, P.A.5
  • 7
    • 0024423657 scopus 로고
    • Expression and characterization of pro alpha 2-plasmin inhibitor
    • Sumi Y, Ichikawa Y, Nakamura Y, Miura O, Aoki N. Expression and characterization of pro alpha 2-plasmin inhibitor. J Biochem 1989; 106: 703-7.
    • (1989) J Biochem , vol.106 , pp. 703-707
    • Sumi, Y.1    Ichikawa, Y.2    Nakamura, Y.3    Miura, O.4    Aoki, N.5
  • 8
    • 0027315990 scopus 로고
    • Different N-terminal forms of alpha 2-plasmin inhibitor in human plasma
    • Bangert K, Johnsen AH, Christensen U, Thorsen S. Different N-terminal forms of alpha 2-plasmin inhibitor in human plasma. Biochem J 1993; 291: 623-5.
    • (1993) Biochem J , vol.291 , pp. 623-625
    • Bangert, K.1    Johnsen, A.H.2    Christensen, U.3    Thorsen, S.4
  • 9
    • 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: 15591-5.
    • (1986) J Biol Chem , vol.261 , pp. 15591-15595
    • Kimura, S.1    Aoki, N.2
  • 10
    • 0018859015 scopus 로고
    • Structural features of glutamine substrates for human plasma factor XIIIa (activated blood coagulation factor XIII)
    • Gorman JJ, Folk JE. Structural features of glutamine substrates for human plasma factor XIIIa (activated blood coagulation factor XIII). J Biol Chem 1980; 255: 419-27.
    • (1980) J Biol Chem , vol.255 , pp. 419-427
    • Gorman, J.J.1    Folk, J.E.2
  • 11
    • 0025907703 scopus 로고
    • A photometric assay for blood coagulation factor XIII
    • Fickenscher K, Aab A, Stüber W. A photometric assay for blood coagulation factor XIII. Thromb Haemost 1991; 65: 535-40.
    • (1991) Thromb Haemost , vol.65 , pp. 535-540
    • Fickenscher, K.1    Aab, A.2    Stüber, W.3
  • 12
    • 33947290263 scopus 로고
    • Y-Y cross-linking sites in human and bovine fibrin
    • Chen R, Doolittle RF. Y-Y cross-linking sites in human and bovine fibrin. Biochemistry 1971; 10: 4486-91.
    • (1971) Biochemistry , vol.10 , pp. 4486-4491
    • Chen, R.1    Doolittle, R.F.2
  • 13
    • 0029932912 scopus 로고    scopus 로고
    • Factor XIIIa-catalyzed cross-linking of recombinant alpha C fragments of human fibrinogen
    • Matsuka Y, Medved L, Migliorini M, Inghan K. Factor XIIIa-catalyzed cross-linking of recombinant alpha C fragments of human fibrinogen. Biochemistry 1996; 35: 5810-16.
    • (1996) Biochemistry , vol.35 , pp. 5810-5816
    • Matsuka, Y.1    Medved, L.2    Migliorini, M.3    Inghan, K.4
  • 14
    • 0018567763 scopus 로고
    • Amino acid sequence studies on the alpha chain of human fibrinogen. Exact location of cross-linking acceptor sites
    • Cotrell BA, Strong DD, Watt KWK, Doolittle RF. Amino acid sequence studies on the alpha chain of human fibrinogen. Exact location of cross-linking acceptor sites. Biochemistry 1979; 18: 5405-10.
    • (1979) Biochemistry , vol.18 , pp. 5405-5410
    • Cotrell, B.A.1    Strong, D.D.2    Watt, K.W.K.3    Doolittle, R.F.4
  • 16
    • 0025213864 scopus 로고
    • Sequence location of a putative transglutaminase cross-linking site in human vitronectin
    • Skorstengaard K, Halkier T, Hojrup P, Mosher DF. Sequence location of a putative transglutaminase cross-linking site in human vitronectin. FEBS Lett 1990; 262: 269-74.
    • (1990) FEBS Lett , vol.262 , pp. 269-274
    • Skorstengaard, K.1    Halkier, T.2    Hojrup, P.3    Mosher, D.F.4
  • 17
    • 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: 27220-4.
    • (1998) J Biol Chem , vol.273 , pp. 27220-27224
    • Valnickova, Z.1    Enghild, J.J.2
  • 18
    • 4644237859 scopus 로고    scopus 로고
    • Identification of factor XIIIA-reactive glutamine acceptor and lysine donor sites within fibronectin-binding protein (FnbA) from Staphylococcus aureus
    • Anderson ET, Fletcher L, Severin A, Murphy E, Baker SM, Matsuka YV. Identification of factor XIIIA-reactive glutamine acceptor and lysine donor sites within fibronectin-binding protein (FnbA) from Staphylococcus aureus. Biochemistry 2004; 43: 11842-52.
    • (2004) Biochemistry , vol.43 , pp. 11842-11852
    • Anderson, E.T.1    Fletcher, L.2    Severin, A.3    Murphy, E.4    Baker, S.M.5    Matsuka, Y.V.6
  • 19
    • 0021142637 scopus 로고
    • Structural features of glutamine substrates for transglutaminases. Role of extended interactions in the specificity of human plasma factor XIIIa and of the guinea pig liver enzyme
    • Gorman JJ, Folk JE. Structural features of glutamine substrates for transglutaminases. Role of extended interactions in the specificity of human plasma factor XIIIa and of the guinea pig liver enzyme. J Biol Chem 1984; 259: 9007-10.
    • (1984) J Biol Chem , vol.259 , pp. 9007-9010
    • Gorman, J.J.1    Folk, J.E.2
  • 20
    • 0036399286 scopus 로고    scopus 로고
    • Structural features associated with the binding of glutamine-containing peptides to factor XIII
    • Marinescu A, Cleary DB, Littlefield TR, Maurer MC. Structural features associated with the binding of glutamine-containing peptides to factor XIII. Arch Biochem Biophys 2002; 406: 9-20.
    • (2002) Arch Biochem Biophys , vol.406 , pp. 9-20
    • Marinescu, A.1    Cleary, D.B.2    Littlefield, T.R.3    Maurer, M.C.4
  • 21
    • 33746040431 scopus 로고    scopus 로고
    • Characterizing the specificity of activated factor XIII for glutamine-containing substrate peptides
    • Cleary DB, Maurer MC. Characterizing the specificity of activated factor.XIII for glutamine-containing substrate peptides. Biochim Biophys Acta 2006; 1764: 1207-17.
    • (2006) Biochim Biophys Acta , vol.1764 , pp. 1207-1217
    • Cleary, D.B.1    Maurer, M.C.2
  • 23
    • 0015739824 scopus 로고
    • Simultaneous purification of bovine prothrombin and factor X. Activation of prothrombin by trypsin-activated factor X
    • Bajaj SP, Mann KG. Simultaneous purification of bovine prothrombin and factor X. Activation of prothrombin by trypsin-activated factor X. J Biol Chem 1973; 248: 7729-41.
    • (1973) J Biol Chem , vol.248 , pp. 7729-7741
    • Bajaj, S.P.1    Mann, K.G.2
  • 24
    • 0017843408 scopus 로고
    • On the preparation of bovine alpha-thrombin
    • Workman EF Jr, Lundblad RL. On the preparation of bovine alpha-thrombin. Thromb Haemost 1978; 39: 193-200.
    • (1978) Thromb Haemost , vol.39 , pp. 193-200
    • Workman Jr., E.F.1    Lundblad, R.L.2
  • 25
    • 0022699646 scopus 로고
    • Solid phase synthesis
    • Merrifield B. Solid phase synthesis. Science 1986; 232: 341-7.
    • (1986) Science , vol.232 , pp. 341-347
    • Merrifield, B.1
  • 26
    • 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 É, Balogh I, Vámosi G, Muszbek L. A modified, optimized kinetic photometric assay for the determination of blood coagulation factor XIII activity in plasma. Clin Chem 2000; 46: 1946-55.
    • (2000) Clin Chem , vol.46 , pp. 1946-1955
    • Kárpáti, L.1    Penke, B.2    Katona, É.3    Balogh, I.4    Vámosi, G.5    Muszbek, L.6
  • 27
    • 0031264537 scopus 로고    scopus 로고
    • ROESY with water flip back for high-field NMR of biomolecules
    • Fulton DB, Ni F. ROESY with water flip back for high-field NMR of biomolecules. J Magn Reson 1997; 129: 93-7.
    • (1997) J Magn Reson , vol.129 , pp. 93-97
    • Fulton, D.B.1    Ni, F.2
  • 28
    • 0034823890 scopus 로고    scopus 로고
    • Group epitope mapping by saturation transfer difference NMR to identify segments of a ligand in direct contact with a protein receptor
    • Mayer M, Meyer B. Group epitope mapping by saturation transfer difference NMR to identify segments of a ligand in direct contact with a protein receptor. J Am Chem Soc 2001; 123: 6108-17.
    • (2001) J Am Chem Soc , vol.123 , pp. 6108-6117
    • Mayer, M.1    Meyer, B.2
  • 30
    • 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: 536-42.
    • (1982) J Clin Invest , vol.69 , pp. 536-542
    • Sakata, Y.1    Aoki, N.2
  • 31
    • 0020351368 scopus 로고
    • Cross-linking of alpha 2-plasmin inhibitor to fibrin catalyzed by activated fibrin-stabilizing factor
    • Tamaki T, Aoki N. Cross-linking of alpha 2-plasmin inhibitor to fibrin catalyzed by activated fibrin-stabilizing factor. J Biol Chem 1982; 257: 14767-72.
    • (1982) J Biol Chem , vol.257 , pp. 14767-14772
    • Tamaki, T.1    Aoki, N.2
  • 32
    • 0034531162 scopus 로고    scopus 로고
    • Cross-linking of wild-type and mutant alpha 2-antiplasmins to fibrin by activated factor XIII and by a tissue transglutaminase
    • Lee KN, Lee CS, Tae WC, Jackson KW, Christiansen VJ, McKee PA. Cross-linking of wild-type and mutant alpha 2-antiplasmins to fibrin by activated factor XIII and by a tissue transglutaminase. J Biol Chem 2000; 275: 37382-9.
    • (2000) J Biol Chem , vol.275 , pp. 37382-37389
    • Lee, K.N.1    Lee, C.S.2    Tae, W.C.3    Jackson, K.W.4    Christiansen, V.J.5    McKee, P.A.6
  • 33
    • 0023277723 scopus 로고
    • Characterization of recombinant human alpha 2-antiplasmin and of mutants obtained by site-directed mutagenesis of the reactive site
    • Holmes WE, Lijnen HR, Collen D. Characterization of recombinant human alpha 2-antiplasmin and of mutants obtained by site-directed mutagenesis of the reactive site. Biochemistry 1987; 26: 5133-40.
    • (1987) Biochemistry , vol.26 , pp. 5133-5140
    • Holmes, W.E.1    Lijnen, H.R.2    Collen, D.3
  • 34
    • 0020575314 scopus 로고
    • Factor XIII-mediated cross-linking of NH2-terminal peptide of alpha 2-plasmin inhibitor to fibrin
    • Ichinose A, Tamaki T, Aoki N. Factor XIII-mediated cross-linking of NH2-terminal peptide of alpha 2-plasmin inhibitor to fibrin. FEBS Lett 1983; 153: 369-71.
    • (1983) FEBS Lett , vol.153 , pp. 369-371
    • Ichinose, A.1    Tamaki, T.2    Aoki, N.3
  • 35
    • 33745846379 scopus 로고    scopus 로고
    • Screening for the preferred substrate sequence of transglutaminase using a phage-displayed peptide library: Identification of peptide substrates for TGASE 2 and factor XIIIA
    • Sugimura Y, Hosono M, Wada F, Yoshimura T, Maki M, Hitomi K. Screening for the preferred substrate sequence of transglutaminase using a phage-displayed peptide library: Identification of peptide substrates for TGASE 2 and factor XIIIA. J Biol Chem 2006; 281: 17699-706.
    • (2006) J Biol Chem , vol.281 , pp. 17699-17706
    • Sugimura, Y.1    Hosono, M.2    Wada, F.3    Yoshimura, T.4    Maki, M.5    Hitomi, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.