메뉴 건너뛰기




Volumn 41, Issue 6, 2009, Pages 566-571

Ser234Leu missense mutation in the A1 domain of factor v causing moderate factor v deficiency in a Chinese family

Author keywords

Coagulation factor V; Deficiency; Expression study; Gene mutation

Indexed keywords

ANTIGEN; BLOOD CLOTTING FACTOR 5; COMPLEMENTARY DNA; PROTHROMBIN; THROMBIN; THROMBOPLASTIN;

EID: 70350648028     PISSN: 00313025     EISSN: 14653931     Source Type: Journal    
DOI: 10.1080/00313020903072734     Document Type: Article
Times cited : (4)

References (23)
  • 1
    • 0242585716 scopus 로고    scopus 로고
    • Blood coagulation
    • Dahlback B. Blood coagulation. Lancet 2000; 355: 1627-1632
    • (2000) Lancet , vol.355 , pp. 1627-1632
    • Dahlback, B.1
  • 2
    • 0037220079 scopus 로고    scopus 로고
    • Factor V: A combination of Dr Jekyll and Mr Hyde
    • Mann KG, Kalafatis M. Factor V: a combination of Dr Jekyll and Mr Hyde. Blood 2003; 101: 20-30.
    • (2003) Blood , vol.101 , pp. 20-30
    • Mann, K.G.1    Kalafatis, M.2
  • 3
    • 0021046120 scopus 로고
    • The factor Xa-catalyzed activation of factor v
    • Foster WB, Nesheim ME, Mann KG. The factor Xa-catalyzed activation of factor V. J Biol Chem 1983; 258: 13970-13977
    • (1983) J Biol Chem , vol.258 , pp. 13970-13977
    • Foster, W.B.1    Nesheim, M.E.2    Mann, K.G.3
  • 4
    • 0020320628 scopus 로고
    • Thrombin-catalyzed activation of human coagulation factor v
    • Suzuki K, Dahlback B, Stenffo J. Thrombin-catalyzed activation of human coagulation factor V. J Biol Chem 1982; 257: 6556-6564
    • (1982) J Biol Chem , vol.257 , pp. 6556-6564
    • Suzuki, K.1    Dahlback, B.2    Stenffo, J.3
  • 5
    • 0028110027 scopus 로고
    • The mechanism of inactivation of human factor v and human factor Va by activated protein C
    • Kalafatis M, Rand MD, Mann KG. The mechanism of inactivation of human factor V and human factor Va by activated protein C. J Biol Chem 1994; 269: 31869-31880
    • (1994) J Biol Chem , vol.269 , pp. 31869-31880
    • Kalafatis, M.1    Rand, M.D.2    Mann, K.G.3
  • 6
    • 70350628467 scopus 로고
    • New factors concerned in the coagulation of blood
    • Owren PA. New factors concerned in the coagulation of blood. Bull Schweiz Akad Med Wiss 1947; 3: 163-177
    • (1947) Bull Schweiz Akad Med Wiss , vol.3 , pp. 163-177
    • Owren, P.A.1
  • 7
    • 0030698229 scopus 로고    scopus 로고
    • Phenotypic homozygous activated protein C resistance associated with compound heterozygosity for Arg506Gln (factor v Leiden) and His1299Arg substitutions in factor v
    • Castaman G, Lunghi B, Missiaglia E, et al. Phenotypic homozygous activated protein C resistance associated with compound heterozygosity for Arg506Gln (factor V Leiden) and His1299Arg substitutions in factor V. Br J Haematol 1997; 99: 257-261
    • (1997) Br J Haematol , vol.99 , pp. 257-261
    • Castaman, G.1    Lunghi, B.2    Missiaglia, E.3
  • 8
    • 0031058324 scopus 로고    scopus 로고
    • Molecular characterization of a type i quantitative factor v deficiency in a thrombosis patient that is 'pseudo homozygous' for activated protein C resistance
    • Guasch JF, Lensen RP, Bertina RM. Molecular characterization of a type I quantitative factor V deficiency in a thrombosis patient that is 'pseudo homozygous' for activated protein C resistance. Thromb Haemost 1997; 77: 252-257
    • (1997) Thromb Haemost , vol.77 , pp. 252-257
    • Guasch, J.F.1    Lensen, R.P.2    Bertina, R.M.3
  • 9
    • 0032529497 scopus 로고    scopus 로고
    • A novel factor v null mutation detected in a thrombophilia patient with pseudo homozygous APC-resistance and in an asymptomatic unrelated subject
    • Lunghi B, Castoldi E, Mingozzi F, et al. A novel factor V null mutation detected in a thrombophilia patient with pseudo homozygous APC-resistance and in an asymptomatic unrelated subject. Blood 1998; 92: 1463-1464
    • (1998) Blood , vol.92 , pp. 1463-1464
    • Lunghi, B.1    Castoldi, E.2    Mingozzi, F.3
  • 10
    • 0031757205 scopus 로고    scopus 로고
    • Molecular bases of pseudohomozygous APC resistance: The compound heterozygosity for FV R506Q and a FV null mutation results in the exclusive presence of FV Leiden molecules in plasma
    • Castoldi E, Kalafatis M, Lunghi B, et al. Molecular bases of pseudohomozygous APC resistance: the compound heterozygosity for FV R506Q and a FV null mutation results in the exclusive presence of FV Leiden molecules in plasma. Thromb Haemost 1998; 80: 403-406
    • (1998) Thromb Haemost , vol.80 , pp. 403-406
    • Castoldi, E.1    Kalafatis, M.2    Lunghi, B.3
  • 11
    • 0032847937 scopus 로고    scopus 로고
    • Familial coagulation factor v deficiency caused by a novel 4 base pair insertion in the factor v gene: Factor v Stanford
    • Zehnder JL, Hiraki DD, Jones CD, et al. Familial coagulation factor V deficiency caused by a novel 4 base pair insertion in the factor V gene: factor V Stanford. Thromb Haemost 1999; 82: 1097-1099
    • (1999) Thromb Haemost , vol.82 , pp. 1097-1099
    • Zehnder, J.L.1    Hiraki, D.D.2    Jones, C.D.3
  • 12
    • 0042738950 scopus 로고    scopus 로고
    • Factor v New Brunswick: Ala221Val associated with FV deficiency reproduced in vitro and functionally characterized
    • Steen M, Miteva M, Villoutreix BO, et al. Factor V New Brunswick: Ala221Val associated with FV deficiency reproduced in vitro and functionally characterized. Blood 2003; 102: 1316-1322
    • (2003) Blood , vol.102 , pp. 1316-1322
    • Steen, M.1    Miteva, M.2    Villoutreix, B.O.3
  • 13
    • 13244271981 scopus 로고    scopus 로고
    • Two novel mutations in EGF-like domains of human factor IX dramatically impair intracellular processing and secretion
    • Enjolras N, Plantier JL, Rodriguez MH, et al. Two novel mutations in EGF-like domains of human factor IX dramatically impair intracellular processing and secretion. J Thromb Haemost 2004; 2: 1143-1154
    • (2004) J Thromb Haemost , vol.2 , pp. 1143-1154
    • Enjolras, N.1    Plantier, J.L.2    Rodriguez, M.H.3
  • 14
    • 33644854287 scopus 로고    scopus 로고
    • Inherited defects of coagulation factory v : tthe hemorrhagic side
    • Asselta R, Tenchini ML, Duga S. Inherited defects of coagulation factory V : the hemorrhagic side. J Thromb Haemost 2006; 4: 26-34.
    • (2006) J Thromb Haemost , vol.4 , pp. 26-34
    • Asselta, R.1    Tenchini, M.L.2    Duga, S.3
  • 15
    • 29244450448 scopus 로고    scopus 로고
    • Molecular mechanisms of antithrombin deficiency in two Chinese families.One novel and one recurrent point mutation in the antithrombin gene causing venous thrombosis
    • Zhou RF, Fu QH, Wang WB, et al. Molecular mechanisms of antithrombin deficiency in two Chinese families. One novel and one recurrent point mutation in the antithrombin gene causing venous thrombosis. Thromb Haemost 2005; 94: 1172-1176
    • (2005) Thromb Haemost , vol.94 , pp. 1172-1176
    • Zhou, R.F.1    Fu, Q.H.2    Wang, W.B.3
  • 16
    • 15344350927 scopus 로고    scopus 로고
    • Gly392Cys missense mutation in the A2 domain of factor v causing severe factor v deficiency: Molecular characterization by expression of the recombinant protein
    • Chen TY, Lin TM, Chen HY, et al. Gly392Cys missense mutation in the A2 domain of factor V causing severe factor V deficiency: molecular characterization by expression of the recombinant protein. Thromb Haemost 2005; 93: 614-615
    • (2005) Thromb Haemost , vol.93 , pp. 614-615
    • Chen, T.Y.1    Lin, T.M.2    Chen, H.Y.3
  • 17
    • 0037220604 scopus 로고    scopus 로고
    • Arg2074Cys missense mutation in the C2-domain of factor v causing moderately severe factor v deficiency: Molecular characterization by expression of the recombinant protein
    • Duga S, Montefusco MC, Asselta R, et al. Arg2074Cys missense mutation in the C2-domain of factor V causing moderately severe factor V deficiency: molecular characterization by expression of the recombinant protein. Blood 2003; 101: 173-177
    • (2003) Blood , vol.101 , pp. 173-177
    • Duga, S.1    Montefusco, M.C.2    Asselta, R.3
  • 18
    • 0142183357 scopus 로고    scopus 로고
    • Clinical and molecular characterization of 6 patients a.ected by severe deficiency of coagulation factor V: Broadening of the mutational spectrum of factor v gene and in vitro analysis of the newly identified missense mutations
    • Montefusco MC, Duga S, Asselta R, et al. Clinical and molecular characterization of 6 patients a.ected by severe deficiency of coagulation factor V: Broadening of the mutational spectrum of factor V gene and in vitro analysis of the newly identified missense mutations. Blood 2003; 102: 3210-3216
    • (2003) Blood , vol.102 , pp. 3210-3216
    • Montefusco, M.C.1    Duga, S.2    Asselta, R.3
  • 19
    • 33645976142 scopus 로고    scopus 로고
    • A case of coagulation factor v deficiency caused by compound heterozygous mutations in the factor v gene
    • Yamakage N, Ikejiri M, Okumura K, et al. A case of coagulation factor V deficiency caused by compound heterozygous mutations in the factor V gene. Haemophilia 2006; 12: 172-178
    • (2006) Haemophilia , vol.12 , pp. 172-178
    • Yamakage, N.1    Ikejiri, M.2    Okumura, K.3
  • 20
    • 0347997285 scopus 로고    scopus 로고
    • De.ning the factor Xabinding site on factor Va by site-directed glycosylation
    • Steen M, Villoutreix BO, Norstrom EA, et al. De.ning the factor Xabinding site on factor Va by site-directed glycosylation. J Biol Chem 2002; 277: 50022-50029
    • (2002) J Biol Chem , vol.277 , pp. 50022-50029
    • Steen, M.1    Villoutreix, B.O.2    Norstrom, E.A.3
  • 21
    • 0029833850 scopus 로고    scopus 로고
    • Binding sites for blood coagulation factor Xa and protein S involving residues 493-506 in factor Va
    • Heeb MJ, Kojima Y, Hackeng TM, et al. Binding sites for blood coagulation factor Xa and protein S involving residues 493-506 in factor Va. Prot Sci 1996; 5: 1883-1889
    • (1996) Prot Sci , vol.5 , pp. 1883-1889
    • Heeb, M.J.1    Kojima, Y.2    Hackeng, T.M.3
  • 22
    • 0032511045 scopus 로고    scopus 로고
    • Binding site for blood coagulation factor Xa involving residues 311-325 in factor Va
    • Kojima Y, Heeb MJ, Gale AJ, et al. Binding site for blood coagulation factor Xa involving residues 311-325 in factor Va. J Biol Chem 1998; 273: 14900-14905
    • (1998) J Biol Chem , vol.273 , pp. 14900-14905
    • Kojima, Y.1    Heeb, M.J.2    Gale, A.J.3
  • 23
    • 0037159218 scopus 로고    scopus 로고
    • Identification of a binding site for blood coagulation factor Xa on the heavy chain of factor Va. Amino acid residues 323-331 of factor v represent an interactive site for activated factor X
    • Kalafatis M, Beck DO. Identification of a binding site for blood coagulation factor Xa on the heavy chain of factor Va. Amino acid residues 323-331 of factor V represent an interactive site for activated factor X. Biochemistry 2002; 41: 12715-12728
    • (2002) Biochemistry , vol.41 , pp. 12715-12728
    • Kalafatis, M.1    Beck, D.O.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.