ライフサイエンスコーパス: factor XIII

1 nt findings on the structure and function of factor XIII.

2 functional homologue, a catalytic subunit of factor XIII.

3 rization, and stability of blood coagulation factor XIII.

4 t, which is cross-linked to fibrin by active factor XIII.

5 antibodies to B beta chains, plasminogen, or factor XIII.

6 s the interplay of thrombin, fibrinogen, and Factor XIII.

7 s of coagulation, thrombin helps to activate Factor XIII.

8 om gamma'408 to 427L that binds thrombin and factor XIII.

9 ombin are necessary for direct activation of factor XIII.

10 (7-16), thrombin receptor PAR1 (38-60), and factor XIII (28-37).

11 onserved substrate conformation seen in both factor XIII-(28-37) and fibrinopeptide A.

12 ructure of human alpha-thrombin bound to the factor XIII-(28-37) decapeptide has been determined.

13 In the case of factor XIII-(28-37), the aryl binding site is shared by

14 t paradox between epidemiological studies of factor XIII 34Leu and reported in-vitro effects on fibri

15 h tighter clot structures in the presence of factor XIII 34Val alleles compared with those in the pre

16 nt of complement factor B (CFB), coagulation factor XIII A chain (F13A1), thrombospondin 1 (THBS1), a

17 n translocation to DRM rafts was impaired in factor XIII A subunit-deficient mouse platelets, which s

18 , such as production of the transglutaminase factor XIII A subunit.

19 Thrombin activates the Factor XIII a(2) dimer by cleaving the Factor XIII activ

20 method revealed changes in the structure of Factor XIII a(2) localized to different areas of the pro

21 ge experiments were conducted on recombinant Factor XIII a(2) using matrix-assisted laser desorption

22 r VIII, PAI-1, tissue plasminogen activator, factor XIII A-subunit and B-subunit, and von Willebrand

23 association between a common mutation in the factor XIII a-subunit gene, coding for an amino acid cha

24 Factor XIII(a) [FXIII(a)] stabilizes clots and increases

25 We assayed mRNA for factor XIII-A (FXIII-A) by using real-time PCR and measu

26 Factor XIII-A (FXIII-A) is present in the cytosol of pla

27 Recently, factor XIII-A (FXIII-A) was reported to be a good marker

28 Factor XIII-A deficiency causes a severe bleeding phenot

29 ight have implications for the management of factor XIII-A deficiency states.

30 Factor XIII-A enzyme activity was measured in plasma and

31 erated a mouse floxed in coding exon7 of the factor XIII-A gene (F13A1).

32 Coagulation factor XIII-A has a crucial role in thrombus stabilisati

33 ed wound healing, but the cellular origin of Factor XIII-A is unknown.

34 Cd11b mice showed no reduction in factor XIII-A mRNA in cardiac tissue and a 54.6% reducti

35 quantitative PCR was performed to determine factor XIII-A mRNA levels in aortic and cardiac tissue.

36 In a human stem-cell study, factor XIII-A mRNA transcription increased as common mye

37 A major decrease in factor XIII-A mRNA was observed in the aorta (91.6%) and

38 A 40% decrease in factor XIII-A plasma activity was observed in Cd11b mice

39 Factor XIII-A recombination was evaluated by quantitativ

40 Factor XIII-A transcripts were assayed in human umbilica

41 By contrast, plasma factor XIII-A was normal in Mpl mice.

42 ogen) (Glu396) involved in binding activated factor XIII-A(2) (FXIII-A(2)*); however, the functional

43 roteins, including kindlin-3 and coagulation factor XIII-A.

44 a-D-galactosaminidase (NAGA; P = .0002), and Factor XIII, A1 (F13A1; P = .0001).

45 d the x-ray crystal structure of recombinant factor XIII A2 in the presence of calcium, strontium, an

46 t of factor XIII since placental or platelet factor XIII (A2), which does not contain B subunits, elu

47 on (1.9 +/- 0.2 minutes), 840 +/- 280 pM for factor XIII activation and factor Va generation (2.2 +/-

48 gammaA/gamma' fibrinogen accelerates plasma factor XIII activation by a non-proteolytic mechanism.

49 s on the role of fibrinogen as a cofactor in factor XIII activation by thrombin.

50 gamma' fibrinogen also increases the rate of factor XIII activation in a non-proteolytic manner.

51 A revised model of factor XIII activation is presented below.

52 tailed atomic level interactions between the factor XIII activation peptide and thrombin and provides

53 f both a small chromogenic substrate and the factor XIII activation peptide are increased in the pres

54 the kinetic and NMR results suggest that the factor XIII activation peptide binds to thrombin in a ma

55 s the Factor XIII a(2) dimer by cleaving the Factor XIII activation peptide segment at the Arg(37)-Gl

56 By hydrolyzing the Factor XIII activation peptide segment at the R37-G38 pe

57 34)VVPR(37) and (34)LVPR(37) segments of the factor XIII activation peptide serve as the major anchor

58 esidues in recognition and hydrolysis of the Factor XIII activation peptide, mutations within thrombi

59 In the absence of fibrin, the Factor XIII activation peptide-(28-41) exhibits a 10-fol

60 Factor XIII activation peptide-(28-41), and Factor XIII activation peptide-(28-41) with a Val(34) to

61 mbin hydrolysis of fibrinogen Aalpha-(7-20), Factor XIII activation peptide-(28-41), and Factor XIII

62 r characterize interactions of thrombin with factor XIII activation peptides.

63 This enables enhanced factor XIII activation to be localized around the fibrin

64 involved in high specificity fibrin-enhanced factor XIII activation were identified as His-66, Tyr-71

65 these sites may prove useful in controlling factor XIII activation.

66 , fibrinopeptide (FP) A and FPB release, and factor XIII activation.

67 activities that lead to an increased rate of factor XIII activation.

68 ble clotting (4 +/- 0.2 min) coincident with factor XIII activation.

69 ts, thrombomodulin inhibited fibrin-enhanced factor XIII activation.

70 riking associations included SNP rs5985 with factor XIII activity (p = 2.6 x 10(-186)), rs10665 with

71 Using a substrate-based screening assay for factor XIII activity complemented by kinetic analysis of

72 Most factor XIII activity elutes in the second peak with a sm

73 II results in a single protein peak with all factor XIII activity emerging with the leading edge of t

74 Factor XIII activity showed higher (82%) and factor XIIa

75 ence after activation aids in maintenance of Factor XIII activity.

76 men who had at least 2 copies of the variant factor XIII alleles and were current estrogen users, the

77 Compared to women homozygous for both common factor XIII alleles, the Arg95 variant was associated wi

78 Factor XIII alone applied to the same DEAE column elutes

79 exes in equilibrium mixtures containing free factor XIII and 2:1 complexes suggests that this interac

80 ns between common variations in the genes of factor XIII and altered risk profiles for thrombosis.

81 of the structural and functional features of factor XIII and fibrin(ogen) have been elucidated by pro

82 in clot is dependent on interactions between factor XIII and fibrin.

83 Factor XIII and fibrinogen are unusual among clotting fa

84 tween coding polymorphisms in fibrinogen and factor XIII and fibrinogen concentrations that modify fi

85 te interactions between polymorphisms in the factor XIII and fibrinogen genes, fibrinogen concentrati

86 segments with colocalized immunostaining for factor XIII and GPIIIa (P = 0.02).

87 ally with antibodies to fibrin cross-linking factor XIII and platelet glycoprotein (GP)-IIIa to ident

88 ficant affinity for the B subunits of plasma factor XIII and that through this interaction fibrinogen

89 hat contained two domains: one recognized by factor XIII and the other by plasmin.

90 experiments employing activated recombinant factor XIII and the transglutaminase cross-linking site

91 ment included pro-coagulant (factor VIII and factor XIII) and anti-coagulant (protein C, protein S, a

92 of other hepatic proteins including albumin, factor XIII, and apolipoprotein A-I.

93 ate transglutaminase (TGP), the a-subunit of factor XIII, and band 4.2 protein from different human c

94 ndings of a relationship between fibrinogen, factor XIII, and cardiovascular or other thrombotic diso

95 studies of wild-type and mutant peptides of factor XIII AP (28-37) suggest residues P(4)-P(1) are mo

96 raction between peak 2 fibrinogen and plasma factor XIII appears to be through binding to the B subun

97 becomes cross-linked to fibrin by activated factor XIII approximately 13 times faster than native Me

98 n plus factor XIII or peak 2 fibrinogen plus factor XIII are applied to DEAE columns, the peak 1/fact

99 due that serves as a substrate for activated factor XIII becomes more efficient after removal of the

100 nce contains features that are important for factor XIII binding.

101 Factor XIII binds fibrinogen gamma(A)/gamma' approximate

102 Second, thrombin activates plasma factor XIII bound to fibrin polymers to produce the acti

103 factor that acts to approximate thrombin and factor XIII bound to separate and complementary domains

104 vWbp association with fibrinogen and factor XIII, but not fibronectin, required prothrombin a

105 proteolytically activates blood coagulation factor XIII by cleavage at residue Arg(37); factor XIII

106 lood coagulation, thrombin helps to activate factor XIII by cleaving the activation peptide at the R3

107 Factor XIII can be activated proteolytically by thrombin

108 Factor XIII catalyzes the formation of isopeptide bonds

109 A second factor XIII concentrate (Bio Products Laboratory, Elstre

110 propriately timed periodic infusions of such factor XIII concentrates are able to live normal lives,

111 Two plasma-derived, virus-inactivated factor XIII concentrates are currently in production.

112 With the development of safe and effective factor XIII concentrates, reliable prophylactic treatmen

113 s clot structure and properties by increased factor XIII cross-linking and formation of thicker fibri

114 amma chain, such as platelet aggregation and factor XIII cross-linking, were also disrupted, suggesti

115 significantly accelerates clot formation and factor XIII cross-linking, whereas exposure of fibrinoge

116 Factor XIII-cross-linked fragment D (double-D) from huma

117 crystal structure of fragment double-D from factor XIII-cross-linked lamprey fibrin has been determi

118 its mutant that was replaced by A398A399 at factor XIII crosslinking sites (Q398Q399) was inhibited.

119 However, platelets from patients with factor XIII deficiency had normal retention, and a pan-t

120 Factor XIII deficiency is a severe autosomal recessive b

121 Patients with factor XIII deficiency who receive appropriately timed p

122 the fibrin matrix at high concentration in a factor XIII-dependent manner.

123 study examines the contribution of activated factor XIII (factor XIIIa) to fibrinolytic resistance in

124 FN) are covalently cross-linked by activated factor XIII (factor XIIIa) to form pFN-fibrin multimers.

125 nhibitor, von Willebrand factor, fibrinogen, factor XIII), fibrinolysis (D-dimer, tissue-type plasmin

126 gnetic resonance imaging of transglutaminase factor XIII (FXIII) and myeloperoxidase (MPO) activity t

127 Human factor XIII (FXIII) and tissue transglutaminase (tTG) ar

128 ee of sequence identity (~30%) to both human Factor XIII (FXIII) and tissue transglutaminase 2 (hTG2)

129 The transglutaminase Factor XIII (FXIII) catalyzes the formation of covalent

130 Congenital factor XIII (FXIII) deficiency is a rare, autosomal-rece

131 Congenital factor XIII (FXIII) deficiency is associated with a tend

132 Coagulation transglutaminase factor XIII (FXIII) exists in circulation as heterotetra

133 Factor XIII (FXIII) generates fibrin-fibrin and fibrin-i

134 Coagulation factor XIII (FXIII) is a heterotetramer consisting of 2

135 Plasma coagulation factor XIII (FXIII) is a transglutaminase that promotes

136 Coagulation factor XIII (FXIII) is a transglutaminase with a well de

137 rmined that activity of the transglutaminase factor XIII (FXIII) is critical for rbc retention within

138 The transglutaminase coagulation factor XIII (FXIII) is critical for the stability and fu

139 Transglutaminase factor XIII (FXIII) is essential for hemostasis, wound h

140 Coagulation factor XIII (FXIII) is the main stabilizer of the fibrin

141 Coagulation Factor XIII (FXIII) plays an important role in wound hea

142 The activation and regulation of coagulation Factor XIII (FXIII) protein has been the subject of acti

143 Factor XIII (FXIII) stabilizes thrombi against fibrinoly

144 The structure of human coagulation factor XIII (FXIII), a heterotetrameric plasma protransg

145 esion depended on fibrinogen and coagulation factor XIII (FXIII), and supraphysiological FXIII improv

146 trate that the coagulation transglutaminase, factor XIII (fXIII), drives arthritis pathogenesis by pr

147 plasminogen activator inhibitor (PAI-1), and factor XIII (FXIII), NO in exhaled breath (FENO ), spiro

148 rphism, which occurs in a region involved in factor XIII (FXIII)-dependent cross-linking processes, i

149 fibrin cross-linking catalyzed by activated factor XIII (FXIII).

150 C plasma by the addition of exogenous active factor XIII (FXIII).

151 n-proteolytic transglutaminase activation of Factor XIII (FXIII).

152 TG) family have been identified, of which 8 [factor XIII (FXIII)A and TG1-TG7] catalyze post-translat

153 The activated form of coagulation factor XIII (FXIII-A2B2), FXIII-A*, is a hemostatic enzy

154 nked to fibrin when activated blood clotting factor XIII (FXIIIa) catalyzes the formation of an isope

155 Activated factor XIII (FXIIIa) catalyzes the formation of gamma-gl

156 during a transglutaminase reaction activated factor XIII (FXIIIa) covalently cross-links von Willebra

157 Activated coagulation factor XIII (FXIIIa) cross-links the gamma-chains of fib

158 Activated factor XIII (FXIIIa) mediates fibrinolytic resistance an

159 transglutaminases, tTG and the A subunit of factor XIII (FXIIIA), are expressed on the surface of mo

160 oss-linking action of fibrin-bound activated factor XIII (FXIIIa), we examined the persistence of FXI

161 asma transglutaminase, also termed activated factor XIII (FXIIIa).

162 by both TG2 and activated blood coagulation factor XIII (FXIIIa).

163 t ligation by the activated transglutaminase factor XIII (FXIIIa).

164 Polymorphisms in the fibrinogen and factor XIII genes are associated with atherothrombotic r

165 ausal women, we assessed the associations of factor XIII genotypes and their interactions with estrog

166 oding for fibrinogen, factor VII, PAI-1, and factor XIII have been reported to affect both protein co

167 gamma' sequence was found to associate with factor XIII in a 2:1 molar ratio and act as an efficient

168 factor XIII by cleavage at residue Arg(37); factor XIII in turn cross-links fibrin molecules and giv

169 experiments revealed that although activated factor XIII incorporates thymosin beta(4) into the isola

170 achment, including laminin, fibronectin, and Factor XIII, indicating that the presence of fibrin(ogen

171 ich is important for lateral aggregation and factor XIII-induced cross-linking of fibrin fibers.

172 Factor XIII is a transglutaminase essential for normal h

173 Factor XIII is activated by thrombin, and this reaction

174 ch fibrin y-chain cross-linking by activated Factor XIII is eliminated (FGG3X) and applied methods to

175 K9-DON, illustrating that cross-linking via factor XIII is not essential for this phenomenon and sug

176 Factor XIII is the terminal enzyme of the coagulation ca

177 Plasma factor XIII is the zymogen of the transglutaminase facto

178 The overall structure of ion-bound factor XIII is very similar to the previously determined

179 trong correlation with plasma fibrinogen and factor XIII level (r = 0.84 and 0.66, respectively).

180 The transamidase activity potential of factor XIII, measured by the incorporation of radioactiv

181 roups receiving TPA, selective inhibition of factor XIII-mediated alpha2-antiplasmin-fibrin cross-lin

182 ture elutes in two peaks, whereas the peak 2/factor XIII mixture elutes in the peak 2 fibrinogen posi

183 XIII are applied to DEAE columns, the peak 1/factor XIII mixture elutes in two peaks, whereas the pea

184 Gel sieving on Superose 6 of peak 1/factor XIII mixtures results in two protein peaks, the f

185 w of this functionally important part of the factor XIII molecule.

186 V34L and V29F factor XIII mutant peptides were designed to further cha

187 Factor XIII on activation by thrombin cross-links fibrin

188 lysis, possibly as a result of concentrating factor XIII on the clot.

189 When mixtures of peak 1 fibrinogen plus factor XIII or peak 2 fibrinogen plus factor XIII are ap

190 Neither factor XIII polymorphism alone significantly modified th

191 ession of either of 2 functional coagulation factor XIII polymorphisms, one within subunit A (Val34Le

192 y, immunohistochemical studies revealed that factor XIII protein expression colocalizes with Lp(a) ex

193 /gamma' form complexes with a 2 fibrinogen:1 factor XIII ratio.

194 ion of the transgenic milk with thrombin and factor XIII resulted in a cross-linked fibrin clot, indi

195 Gel sieving of mixtures of peak 2 and factor XIII results in a single protein peak with all fa

196 own that gamma chain binding to thrombin and factor XIII results in clots that are mechanically stiff

197 mploying pre-activation of recombinant human Factor XIII (rFXIII[A'2]) were developed to effectively

198 ase in k(cat)/K(m) relative to the wild-type Factor XIII sequence.

199 /gamma' fibrin clots made in the presence of factor XIII showed increased proteolytic resistance to b

200 rs to be through binding to the B subunit of factor XIII since placental or platelet factor XIII (A2)

201 Factor XIII stabilizes this clot by catalyzing the forma

202 missense variant in the F13A1 gene encoding factor XIII subunit A (FXIII-A), a transglutaminase invo

203 y analyses, however, there was a significant factor XIII subunit gene-gene interaction.

204 rin cross-linked to fibronectin by activated factor XIII than on surfaces coated with fibrin lacking

205 n but not y-chain cross-linking by activated Factor XIII to reduce thrombus size and burden, while ma

206 The more easily activated factor XIII V34L has been correlated with protection fro

207 As a result, the Factor XIII V34L is proposed to be susceptible to wastef

208 With the Factor XIII V34L mutation, decreases in K(m) and increas

209 e was no evidence for an interaction between factor XIII Val34Leu genotype and FV:Q506, prothrombin G

210 To investigate the possible role of factor XIII Val34Leu in the pathogenesis of venous throm

211 ncluded that possession of the Leu allele at factor XIII Val34Leu is protective against deep venous t

212 ino acids from the thrombin activation site (factor XIII Val34Leu) that may protect against myocardia

213 igate interactions between fibrin structure, factor XIII Val34Leu, fibrinogen Aalpha Thr312Ala, fibri

214 , methylenetetrahydrofolate reductase C677T, factor XIII Val34Leu, PAI-1 4G/5G, and factor V HR2) did

215 ative to estrogen nonusers with fewer than 2 factor XIII variant alleles (P value for interaction =.0

216 ndlin-3 was indirectly regulated by miR-223, factor XIII was a direct target and both proteins were a

217 However, when factor XIII was added, slower lysis was seen in gammaA/g

218 An antibody to factor XIII was isolated which, although recognizing the

219 In contrast, factor XIII was lower in AKI (increased bleeding tendenc

220 iological concentrations of fibrin(ogen) and factor XIII was significant with molar incorporation rat

221 to prothrombin, fibrinogen, fibronectin, and factor XIII, whereas Coa co-purified with prothrombin an

222 hem was detected in the absence of activated factor XIII, while in its presence thymosin beta(4) was

223 e characterized the solution interactions of factor XIII with two variants of fibrinogen, the soluble

224 When fibrinogen is purified from plasma, the factor XIII zymogen (A2B2) copurifies with it and is fou

225 Factor XIII zymogen activation is a complex series of ev

226 previously determined crystal structures of factor XIII zymogen, likely due to the constraints of th

227 altered gamma chain and is known to bind to factor XIII zymogen.