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Volumn 390, Issue 12, 2009, Pages 1279-1283

Coagulation factor XIII variants with altered thrombin activation rates

Author keywords

Enzyme activation; Factor XIII; Factor XIII activation peptide; Thrombin

Indexed keywords

BLOOD CLOTTING FACTOR 13; FIBRINOGEN; THROMBIN;

EID: 72949121067     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/BC.2009.142     Document Type: Article
Times cited : (9)

References (31)
  • 1
    • 0031913016 scopus 로고    scopus 로고
    • Characterization of the reciprocal binding sites on human alpha-thrombin and factor XIII A-chain
    • Achyuthan, K.E. (1998). Characterization of the reciprocal binding sites on human alpha-thrombin and factor XIII A-chain. Mol. Cell. Biochem. 178, 289-297.
    • (1998) Mol. Cell. Biochem. , vol.178 , pp. 289-297
    • Achyuthan, K.E.1
  • 3
    • 0034254319 scopus 로고    scopus 로고
    • The factor XIII V34L polymorphism accelerates thrombin activation of factor XIII and affects cross-linked fibrin structure
    • Arië ns, R.A.S., Philippou, H., Nagaswami, C., Weisel, J.W., Lane, D.A., and Grant, P.J. (2000). The factor XIII V34L polymorphism accelerates thrombin activation of factor XIII and affects cross-linked fibrin structure. Blood 96, 988-995.
    • (2000) Blood , vol.96 , pp. 988-995
    • Ariëns, R.A.S.1    Philippou, H.2    Nagaswami, C.3    Weisel, J.W.4    Lane, D.A.5    Grant, P.J.6
  • 4
    • 0036682920 scopus 로고    scopus 로고
    • Role of factor XIII in fibrin clot formation and effects of genetic polymorphisms
    • Arië ns, R.A., Lai, T.S., Weisel, J.W., Greenberg, C.S., and Grant, P.J. (2002). Role of factor XIII in fibrin clot formation and effects of genetic polymorphisms. Blood 100, 743-754.
    • (2002) Blood , vol.100 , pp. 743-754
    • Ariëns, R.A.1    Lai, T.S.2    Weisel, J.W.3    Greenberg, C.S.4    Grant, P.J.5
  • 8
    • 0034212430 scopus 로고    scopus 로고
    • Yield improvement of heterologous peptides expressed in yps1-disrupted Saccharomyces cerevisiae strains
    • Egel-Mitani, M., Andersen, A.S., Diers, I., Hach, M., Thim, L., Hastrup, S., and Vad, K. (2000). Yield improvement of heterologous peptides expressed in yps1-disrupted Saccharomyces cerevisiae strains. Enzyme Microb. Technol. 26, 671-677.
    • (2000) Enzyme Microb. Technol. , vol.26 , pp. 671-677
    • Egel-Mitani, M.1    Andersen, A.S.2    Diers, I.3    Hach, M.4    Thim, L.5    Hastrup, S.6    Vad, K.7
  • 10
    • 0023140632 scopus 로고
    • Factor XIIIa formation promoted by complexing of a-thrombin, fibrin, and plasma factor XIII
    • Greenberg, C.S., Achyuthan, K.E., and Fenton, J.W.D. (1987). Factor XIIIa formation promoted by complexing of a-thrombin, fibrin, and plasma factor XIII. Blood 69, 867-871.
    • (1987) Blood , vol.69 , pp. 867-871
    • Greenberg, C.S.1    Achyuthan, K.E.2    Fenton, J.W.D.3
  • 11
    • 0034608931 scopus 로고    scopus 로고
    • Rapid and general profiling of protease specificity by using combinatorial fluorogenic substrate libraries
    • Harris, J.L., Backes, B.J., Leonetti, F., Mahrus, S., Ellman, J.A., and Craik, C.S. (2000). Rapid and general profiling of protease specificity by using combinatorial fluorogenic substrate libraries. Proc. Natl. Acad. Sci. USA 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    Mahrus, S.4    Ellman, J.A.5    Craik, C.S.6
  • 12
    • 0024467299 scopus 로고
    • AThrombincatalyzed activation of human platelet factor XIII: Relationship between proteolysis and factor XIIIa activity
    • Hornyak, T.J., Bishop, P.D., and Shafer, J.A. (1989). aThrombincatalyzed activation of human platelet factor XIII: relationship between proteolysis and factor XIIIa activity. Biochemistry 28, 7326-7332.
    • (1989) Biochemistry , vol.28 , pp. 7326-7332
    • Hornyak, T.J.1    Bishop, P.D.2    Shafer, J.A.3
  • 13
    • 1842473356 scopus 로고    scopus 로고
    • Probing thrombin's ability to accommodate a V34F substitution within the factor XIII activation peptide segment (28-41)*
    • Isetti, G. and Maurer, M.C. (2004). Probing thrombin's ability to accommodate a V34F substitution within the factor XIII activation peptide segment (28-41)*. J. Pept. Res. 63, 241-252.
    • (2004) J. Pept. Res. , vol.63 , pp. 241-252
    • Isetti, G.1    Maurer, M.C.2
  • 14
    • 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., Toth, K., Karpati, L., and Muszbek, L. (2001). Enzyme-linked immunosorbent assay for the determination of blood coagulation factor XIII A-subunit in plasma and in cell lysates. J. Immunol. Methods 258, 127-135.
    • (2001) J. Immunol. Methods , vol.258 , pp. 127-135
    • Katona, E.E.1    Ajzner, E.2    Toth, K.3    Karpati, L.4    Muszbek, L.5
  • 15
    • 0031725574 scopus 로고    scopus 로고
    • A common coding polymorphism in the FXIII A-subunit gene (FXIIIVal34Leu) affects cross-linking activity
    • Kohler, H.P., Arië ns, R.A., Whitaker, P., and Grant, P.J. (1998). A common coding polymorphism in the FXIII A-subunit gene (FXIIIVal34Leu) affects cross-linking activity. Thromb. Haemost. 80, 704.
    • (1998) Thromb. Haemost. , vol.80 , pp. 704
    • Kohler, H.P.1    Ariëns, R.A.2    Whitaker, P.3    Grant, P.J.4
  • 16
    • 12244253723 scopus 로고    scopus 로고
    • Effects of Val34Leu and Val35Leu polymorphism on the enzyme activity of the coagulation factor XIII-A
    • Lee, I.H., Chung, S.I., and Lee, S.Y. (2002). Effects of Val34Leu and Val35Leu polymorphism on the enzyme activity of the coagulation factor XIII-A. Exp. Mol. Med. 34, 385-390.
    • (2002) Exp. Mol. Med. , vol.34 , pp. 385-390
    • Lee, I.H.1    Chung, S.I.2    Lee, S.Y.3
  • 17
    • 0242348804 scopus 로고    scopus 로고
    • Genetic regulation of fibrin structure and function: Complex gene-environment interactions may modulate vascular risk
    • Lim, B.C.B., Arië ns, R.A.S., Carter, A.M.,Weisel, J.W., and Grant, P.J. (2003). Genetic regulation of fibrin structure and function: complex gene-environment interactions may modulate vascular risk. Lancet 361, 1424-1431.
    • (2003) Lancet , vol.361 , pp. 1424-1431
    • Lim, B.C.B.1    Ariëns, R.A.S.2    Carter, A.M.3    Weisel, J.W.4    Grant, P.J.5
  • 18
    • 0042332086 scopus 로고    scopus 로고
    • Enhancement of fibrinolytic potential in vitro by anticoagulant drugs targeting activated factor X, but not by those inhibiting thrombin or tissue factor
    • Lisman, T., Adelmeijer, J., Nieuwenhuis, H.K., and de Groot, P.G. (2003). Enhancement of fibrinolytic potential in vitro by anticoagulant drugs targeting activated factor X, but not by those inhibiting thrombin or tissue factor. Blood Coagul. Fibrinol. 14, 557-562.
    • (2003) Blood Coagul. Fibrinol. , vol.14 , pp. 557-562
    • Lisman, T.1    Adelmeijer, J.2    Nieuwenhuis, H.K.3    De Groot, P.G.4
  • 19
    • 25144508676 scopus 로고    scopus 로고
    • Factor XIII and the clotting of fibrinogen: From basic research to medicine
    • Lorand, L. (2005). Factor XIII and the clotting of fibrinogen: from basic research to medicine. J. Thromb. Haemost. 3, 1337-1348.
    • (2005) J. Thromb. Haemost. , vol.3 , pp. 1337-1348
    • Lorand, L.1
  • 20
    • 0026657151 scopus 로고
    • The structure of residues 7-16 of the A a-chain of human fibrinogen bound to bovine thrombin at 2.3 Å resolution
    • Martin, P.D., Robertson, W., Turk, D., Huber, R., Bode, W., and Edwards, B.F. (1992). The structure of residues 7-16 of the A a-chain of human fibrinogen bound to bovine thrombin at 2.3 Å resolution. J. Biol. Chem. 267, 7911-7920.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7911-7920
    • Martin, P.D.1    Robertson, W.2    Turk, D.3    Huber, R.4    Bode, W.5    Edwards, B.F.6
  • 21
    • 0033152222 scopus 로고    scopus 로고
    • Blood coagulation factor XIII: Structure and function
    • Muszbek, L., Yee, V.C., and Hevessy, Z. (1999). Blood coagulation factor XIII: structure and function. Thromb. Res. 94, 271-305.
    • (1999) Thromb. Res. , vol.94 , pp. 271-305
    • Muszbek, L.1    Yee, V.C.2    Hevessy, Z.3
  • 22
    • 33845525449 scopus 로고    scopus 로고
    • Factor XIII: Recommended terms and abbreviations
    • Muszbek, L., Ariens, R.A., and Ichinose, A. (2007). Factor XIII: recommended terms and abbreviations. J. Thromb. Haemost. 5, 181-183.
    • (2007) J. Thromb. Haemost. , vol.5 , pp. 181-183
    • Muszbek, L.1    Ariens, R.A.2    Ichinose, A.3
  • 23
    • 57749176194 scopus 로고    scopus 로고
    • Modeling of factor XIII activation peptide (28-41) V34L mutant bound to thrombin
    • Nair, D.G., Sunilkumar, P.N., and Sadasivan, C. (2008). Modeling of factor XIII activation peptide (28-41) V34L mutant bound to thrombin. J. Biomol. Struct. Dynam. 26, 387-394.
    • (2008) J. Biomol. Struct. Dynam. , vol.26 , pp. 387-394
    • Nair, D.G.1    Sunilkumar, P.N.2    Sadasivan, C.3
  • 24
    • 0034711216 scopus 로고    scopus 로고
    • Interaction of the factor XIII activation peptide with a-thrombin. Crystal structure of its enzyme-substrate analog complex
    • Sadasivan, C. and Yee, V.C. (2000). Interaction of the factor XIII activation peptide with a-thrombin. Crystal structure of its enzyme-substrate analog complex. J. Biol. Chem. 275, 36942-36948.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36942-36948
    • Sadasivan, C.1    Yee, V.C.2
  • 25
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schechter, I. and Berger, A. (1967). On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 27, 157-162.
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 26
    • 0034617203 scopus 로고    scopus 로고
    • Examining thrombin hydrolysis of the factor XIII activation peptide segment leads to a proposal for explaining the cardioprotective effects observed with the factor XIII V34L mutation
    • Trumbo, T.A. and Maurer, M.C. (2000). Examining thrombin hydrolysis of the factor XIII activation peptide segment leads to a proposal for explaining the cardioprotective effects observed with the factor XIII V34L mutation. J. Biol. Chem. 275, 20627-20631.
    • (2000) J. Biol. Chem. , vol.275 , pp. 20627-20631
    • Trumbo, T.A.1    Maurer, M.C.2
  • 27
    • 0037176908 scopus 로고    scopus 로고
    • Thrombin hydrolysis of V29F and V34L mutants of factor XIII (28-41) reveals roles of the P9 and P4 positions in factor XIII activation
    • Trumbo, T.A. and Maurer, M.C. (2002). Thrombin hydrolysis of V29F and V34L mutants of factor XIII (28-41) reveals roles of the P9 and P4 positions in factor XIII activation. Biochemistry 41, 2859-2868.
    • (2002) Biochemistry , vol.41 , pp. 2859-2868
    • Trumbo, T.A.1    Maurer, M.C.2
  • 28
    • 0037393655 scopus 로고    scopus 로고
    • V34I and V34A substitutions within the factor XIII activation peptide segment (28-41) affect interactions with the thrombin active site
    • Trumbo, T.A. and Maurer, M.C. (2003). V34I and V34A substitutions within the factor XIII activation peptide segment (28-41) affect interactions with the thrombin active site. Thromb. Haemost. 89, 647-653.
    • (2003) Thromb. Haemost. , vol.89 , pp. 647-653
    • Trumbo, T.A.1    Maurer, M.C.2
  • 29
    • 33947330306 scopus 로고    scopus 로고
    • Factor XIII Val34Leu variant protects against coronary artery disease. A meta-analysis
    • Vokó , Z., Bereczky, Z., Katona, E., Adá ny, R., and Muszbek, L. (2007). Factor XIII Val34Leu variant protects against coronary artery disease. A meta-analysis. Thromb. Haemost. 97, 458-463.
    • (2007) Thromb. Haemost. , vol.97 , pp. 458-463
    • Vokó, Z.1    Bereczky, Z.2    Katona, E.3    Adány, R.4    Muszbek, L.5
  • 30
    • 33745631483 scopus 로고    scopus 로고
    • Factor XIII Val34Leu variant is protective against venous thromboembolism: A HuGE review and metaanalysis
    • Wells, P.S., Anderson, J.L., Scarvelis, D.K., Doucette, S.P., and Gagnon, F. (2006). Factor XIII Val34Leu variant is protective against venous thromboembolism: a HuGE review and metaanalysis. Am. J. Epidemiol. 164, 101-109.
    • (2006) Am. J. Epidemiol. , vol.164 , pp. 101-109
    • Wells, P.S.1    Anderson, J.L.2    Scarvelis, D.K.3    Doucette, S.P.4    Gagnon, F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.