메뉴 건너뛰기




Volumn 7, Issue 7, 2009, Pages 1184-1191

New insights into the expression and role of platelet factor XIII-A

Author keywords

FXIII A; Platelet activation; Transglutaminase activity

Indexed keywords

BLOOD CLOTTING FACTOR 8A; DANSYLCADAVERINE; FIBRINOGEN; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; THROMBIN RECEPTOR ACTIVATING PEPTIDE;

EID: 67649460715     PISSN: 15387933     EISSN: 15387836     Source Type: Journal    
DOI: 10.1111/j.1538-7836.2009.03456.x     Document Type: Article
Times cited : (22)

References (30)
  • 1
    • 25144508676 scopus 로고    scopus 로고
    • Factor XIII and the clotting of fibrinogen: From basic research to medicine
    • Lorand L. Factor XIII and the clotting of fibrinogen: From basic research to medicine. J Thromb Haemost 2005; 3: 1337-48.
    • (2005) J Thromb Haemost , vol.3 , pp. 1337-1348
    • Lorand, L.1
  • 2
    • 0020316936 scopus 로고
    • The zymogen forms of blood coagulation factor.XIII bind specifically to fibrinogen
    • Greenberg CS, Shuman MA. The zymogen forms of blood coagulation factor.XIII bind specifically to fibrinogen. J Biol Chem 1982; 257: 6096-101.
    • (1982) J Biol Chem , vol.257 , pp. 6096-6101
    • Greenberg, C.S.1    Shuman, M.A.2
  • 3
    • 0029798238 scopus 로고    scopus 로고
    • Plasma factor.XIII binds specifically to fibrinogen molecules containing gamma chains
    • Siebenlist KR, Meh DA, Mosesson MW. Plasma factor.XIII binds specifically to fibrinogen molecules containing gamma chains. Biochemistry 1996; 35: 10448-53.
    • (1996) Biochemistry , vol.35 , pp. 10448-10453
    • Siebenlist, K.R.1    Meh, D.A.2    Mosesson, M.W.3
  • 4
    • 0025219629 scopus 로고
    • Non-proteolytic activation of cellular protransglutaminase (placenta macrophage factor XIII)
    • Polgar J, Hidasi V, Muszbek L. Non-proteolytic activation of cellular protransglutaminase (placenta macrophage factor XIII). Biochem J 1990; 267: 557-60.
    • (1990) Biochem J , vol.267 , pp. 557-560
    • Polgar, J.1    Hidasi, V.2    Muszbek, L.3
  • 5
    • 0027512006 scopus 로고
    • Platelet factor XIII becomes active without the release of activation peptide during platelet activation
    • Muszbek L, Polgar J, Boda Z. Platelet factor XIII becomes active without the release of activation peptide during platelet activation. Thromb Haemost 1993; 69: 282-5.
    • (1993) Thromb Haemost , vol.69 , pp. 282-285
    • Muszbek, L.1    Polgar, J.2    Boda, Z.3
  • 6
    • 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
  • 7
    • 0037317032 scopus 로고    scopus 로고
    • Transglutaminases: Crosslinking enzymes with pleiotropic functions
    • Lorand L, Graham RM. Transglutaminases: Crosslinking enzymes with pleiotropic functions. Nat Rev Mol Cell Biol 2003; 4: 140-56.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 140-156
    • Lorand, L.1    Graham, R.M.2
  • 8
    • 0037710318 scopus 로고    scopus 로고
    • Factor.XIII subunit. A as an intracellular transglutaminase
    • Adany R, Bardos H. Factor.XIII subunit. A as an intracellular transglutaminase. Cell Mol Life Sci 2003; 60: 1049-60.
    • (2003) Cell Mol Life Sci , vol.60 , pp. 1049-1060
    • Adany, R.1    Bardos, H.2
  • 9
    • 0022350303 scopus 로고
    • Catalytic properties of a calmodulin-regulated transglutaminase from human platelet and chicken gizzard
    • Puszkin EG, Raghuraman V. Catalytic properties of a calmodulin-regulated transglutaminase from human platelet and chicken gizzard. J Biol Chem 1985; 260: 16012-20.
    • (1985) J Biol Chem , vol.260 , pp. 16012-16020
    • Puszkin, E.G.1    Raghuraman, V.2
  • 10
    • 0028969515 scopus 로고
    • Transformation of cellular factor XIII into an active zymogen transglutaminase in thrombin-stimulated platelets
    • Muszbek L, Haramura G, Polgar J. Transformation of cellular factor XIII into an active zymogen transglutaminase in thrombin-stimulated platelets. Thromb Haemost 1995; 73: 702-5.
    • (1995) Thromb Haemost , vol.73 , pp. 702-705
    • Muszbek, L.1    Haramura, G.2    Polgar, J.3
  • 11
    • 0034924217 scopus 로고    scopus 로고
    • Physiopathology and regulation of factor XIII
    • Ichinose A. Physiopathology and regulation of factor XIII. Thromb Haemost 2001; 86: 57-65.
    • (2001) Thromb Haemost , vol.86 , pp. 57-65
    • Ichinose, A.1
  • 12
    • 0017174264 scopus 로고
    • Platelet aggregation in congenital factor XIII deficiency
    • Ozsoylu S, Hicsonmez G. Platelet aggregation in congenital factor XIII deficiency. Acta Haematol 1976; 56: 314-17.
    • (1976) Acta Haematol , vol.56 , pp. 314-317
    • Ozsoylu, S.1    Hicsonmez, G.2
  • 13
    • 0031055171 scopus 로고    scopus 로고
    • Molecular mechanism of a mild phenotype in coagulation factor.XIII (FXIII) deficiency: A splicing mutation permitting partial correct splicing of FXIII A-subunit mRNA
    • Mikkola H, Muszbek L, Laiho E, Syrjala M, Hamalainen E, Haramura G, Salmi T, Peltonen L, Palotie A. Molecular mechanism of a mild phenotype in coagulation factor.XIII (FXIII) deficiency: A splicing mutation permitting partial correct splicing of FXIII A-subunit mRNA. Blood 1997; 89: 1279-87.
    • (1997) Blood , vol.89 , pp. 1279-1287
    • Mikkola, H.1    Muszbek, L.2    Laiho, E.3    Syrjala, M.4    Hamalainen, E.5    Haramura, G.6    Salmi, T.7    Peltonen, L.8    Palotie, A.9
  • 14
    • 0008444519 scopus 로고
    • Bleeding complications in heterozygotes with congenital factor XIII deficiency
    • In: Mosesson M, Amrani D, Siebenlist K, Diorio J, eds. Amsterdam: Elsevier Science
    • Egbring R, Seitz R, Gürten M. Bleeding complications in heterozygotes with congenital factor XIII deficiency. In: Mosesson M, Amrani D, Siebenlist K, Diorio J, eds. Fibrinogen: Biochemistry, Biological Functions, Gene Regulation and Expression. Amsterdam: Elsevier Science, 1988: 341-6.
    • (1988) Fibrinogen: Biochemistry, Biological Functions, Gene Regulation and Expression , pp. 341-346
    • Egbring, R.1    Seitz, R.2    Gürten, M.3
  • 15
    • 33748749809 scopus 로고    scopus 로고
    • Thrombin induces GPIb-IX-mediated fibrin binding to aIIbb3 in a reconstituted Chinese hamster ovary cell model
    • Pabón D, Jayo A, Xie J, Lastres P, González-Manchón C. Thrombin induces GPIb-IX-mediated fibrin binding to aIIbb3 in a reconstituted Chinese hamster ovary cell model. J Thromb Haemost 2006; 4: 2238-47.
    • (2006) J Thromb Haemost , vol.4 , pp. 2238-2247
    • Pabón, D.1    Jayo, A.2    Xie, J.3    Lastres, P.4    González-Manchón, C.5
  • 17
    • 0029048415 scopus 로고
    • A point mutation in an invariant splice acceptor site results in a decreased mRNA level in a patient with severe coagulation factor XIII subunit. A deficiency
    • Vreken P, Niessen RW, Peters M, Schaap MC, Zuithoff-Rijntjes JG, Sturk A. A point mutation in an invariant splice acceptor site results in a decreased mRNA level in a patient with severe coagulation factor.XIII subunit. A deficiency. Thromb Haemost 1995; 74: 584-9.
    • (1995) Thromb Haemost , vol.74 , pp. 584-589
    • Vreken, P.1    Niessen, R.W.2    Peters, M.3    Schaap, M.C.4    Zuithoff-Rijntjes, J.G.5    Sturk, A.6
  • 19
    • 0025195103 scopus 로고
    • Labeling of epsilon-lysine crosslinking sites in proteins with peptide substrates of factor XIIIa and transglutaminase
    • Parameswaran KN, Velasco PT, Wilson J, Lorand L. Labeling of epsilon-lysine crosslinking sites in proteins with peptide substrates of factor XIIIa and transglutaminase. Proc Natl Acad Sci USA 1990; 87: 8472-5.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 8472-8475
    • Parameswaran, K.N.1    Velasco, P.T.2    Wilson, J.3    Lorand, L.4
  • 20
    • 0023946311 scopus 로고
    • Monocytes of patients congenitally deficient in plasma factor.XIII lack factor XIII subunit. A antigen and transglutaminase activity
    • Muszbek L, Adany R, Kavai M, Boda Z, Lopaciuk S. Monocytes of patients congenitally deficient in plasma factor XIII lack factor XIII subunit. A antigen and transglutaminase activity. Thromb Haemost 1988; 59: 231-5.
    • (1988) Thromb Haemost , vol.59 , pp. 231-235
    • Muszbek, L.1    Adany, R.2    Kavai, M.3    Boda, Z.4    Lopaciuk, S.5
  • 21
    • 0032523163 scopus 로고    scopus 로고
    • Molecular mechanisms of type.II factor XIII deficiency: Novel Gly562-Arg mutation and C-terminal truncation of the A.subunit cause factor XIII deficiency as characterized in a mammalian expression system
    • Takahashi N, Tsukamoto H, Umeyama H, Castaman G, Rodeghiero F, Ichinose A. Molecular mechanisms of type II factor XIII deficiency: Novel Gly562-Arg mutation and C-terminal truncation of the A.subunit cause factor.XIII deficiency as characterized in a mammalian expression system. Blood 1998; 91: 2830-8.
    • (1998) Blood , vol.91 , pp. 2830-2838
    • Takahashi, N.1    Tsukamoto, H.2    Umeyama, H.3    Castaman, G.4    Rodeghiero, F.5    Ichinose, A.6
  • 22
    • 33846934728 scopus 로고    scopus 로고
    • Single base-pair substitutions in exon-intron junctions of human genes: Nature, distribution, and consequences for mRNA splicing
    • Krawczak M, Thomas NS, Hundrieser B, Mort M, Wittig M, Hampe J, Cooper DN. Single base-pair substitutions in exon-intron junctions of human genes: Nature, distribution, and consequences for mRNA splicing. Hum Mutat 2007; 28: 150-8.
    • (2007) Hum Mutat , vol.28 , pp. 150-158
    • Krawczak, M.1    Thomas, N.S.2    Hundrieser, B.3    Mort, M.4    Wittig, M.5    Hampe, J.6    Cooper, D.N.7
  • 23
    • 0036724443 scopus 로고    scopus 로고
    • Order of intron removal influences multiple splice outcomes, including a two-exon skip, in a COL5A1 acceptor-site mutation that results in abnormal pro-alpha1(V) N-propeptides and Ehlers-Danlos syndrome type I
    • Takahara K, Schwarze U, Imamura Y, Hoffman GG, Toriello H, Smith LT, Byers PH, Greenspan DS. Order of intron removal influences multiple splice outcomes, including a two-exon skip, in a COL5A1 acceptor-site mutation that results in abnormal pro-alpha1(V) N-propeptides and Ehlers-Danlos syndrome type I. Am J Hum Genet 2002; 71: 451-65.
    • (2002) Am J Hum Genet , vol.71 , pp. 451-465
    • Takahara, K.1    Schwarze, U.2    Imamura, Y.3    Hoffman, G.G.4    Toriello, H.5    Smith, L.T.6    Byers, P.H.7    Greenspan, D.S.8
  • 24
    • 0037370902 scopus 로고    scopus 로고
    • Outcome of donor splice site mutations accounting for congenital afibrinogenemia reflects order of intron removal in the fibrinogen alpha gene (FGA)
    • Attanasio C, David A, Neerman-Arbez M. Outcome of donor splice site mutations accounting for congenital afibrinogenemia reflects order of intron removal in the fibrinogen alpha gene (FGA). Blood 2003; 101: 1851-6.
    • (2003) Blood , vol.101 , pp. 1851-1856
    • Attanasio, C.1    David, A.2    Neerman-Arbez, M.3
  • 26
    • 0036339654 scopus 로고    scopus 로고
    • Intracellular factor XIII crosslinks platelet cytoskeletal elements upon platelet activation
    • Serrano K, Devine DV. Intracellular factor XIII crosslinks platelet cytoskeletal elements upon platelet activation. Thromb Haemost 2002; 88: 315-20.
    • (2002) Thromb Haemost , vol.88 , pp. 315-320
    • Serrano, K.1    Devine, D.V.2
  • 27
    • 1242276192 scopus 로고    scopus 로고
    • Roles of G-protein-coupled receptor dimerization
    • Terrillon S, Bouvier M. Roles of G-protein-coupled receptor dimerization. EMBO Rep 2004; 5: 30-4.
    • (2004) EMBO Rep , vol.5 , pp. 30-34
    • Terrillon, S.1    Bouvier, M.2
  • 28
    • 7044274535 scopus 로고    scopus 로고
    • Factor XIIIA transglutaminase crosslinks AT1 receptor dimers of monocytes at the onset of atherosclerosis
    • AbdAlla S, Lother H, Langer A, el Faramawy Y, Quitterer U. Factor XIIIA transglutaminase crosslinks AT1 receptor dimers of monocytes at the onset of atherosclerosis. Cell 2004; 119: 343-54.
    • (2004) Cell , vol.119 , pp. 343-354
    • AbdAlla, S.1    Lother, H.2    Langer, A.3    el Faramawy, Y.4    Quitterer, U.5
  • 29
    • 3142674975 scopus 로고    scopus 로고
    • Platelet factor XIII and calpain negatively regulate integrin alphaIIbbeta3 adhesive function and thrombus growth
    • Kulkarni S, Jackson SP. Platelet factor XIII and calpain negatively regulate integrin alphaIIbbeta3 adhesive function and thrombus growth. J Biol Chem 2004; 279: 30697-706.
    • (2004) J Biol Chem , vol.279 , pp. 30697-30706
    • Kulkarni, S.1    Jackson, S.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.