ライフサイエンスコーパス: fibrinopeptide

1 time course of thrombin-catalyzed release of fibrinopeptides.

2 catalytic triads for cleavage of fibrinogen fibrinopeptides.

3 ch as complement anaphylatoxins, kinins, and fibrinopeptides.

4 merization and requires only cleavage of the fibrinopeptides.

5 We found that the variant fibrinopeptide A (F8Y 1-16) was cleaved by thrombin, in

6 ta-4 (Tbeta-4), fibrinopeptide B (FP-B), and fibrinopeptide A (FP-A).

7 T), prothrombin fragment 1 + 2 (F1 + 2), and fibrinopeptide A (FPA) as well as markers of fibrinolysi

8 ction of which requires different extents of fibrinopeptide A (FpA) cleavage from fibrinogen.

9 were obtained from 247 patients and urinary fibrinopeptide A (FPA) from 178 of the 247.

10 he thrombin-catalyzed cleavage of N-terminal fibrinopeptide A (FPA) from the two Aalpha-chains of fib

11 During cleavage of fibrinogen by thrombin, fibrinopeptide A (FpA) release precedes fibrinopeptide B

12 n platelet activation, formation of TAT, and fibrinopeptide A (FPA) release.

13 amples by immunoassay and immunoblotting for fibrinopeptide A (FPA), thrombin-antithrombin (TAT), fac

14 In addition, fibrinopeptide A (FPA), thrombin-antithrombin III (TAT)

15 plasma levels (at 0, 4, 12, and 24 hours) of fibrinopeptide A (FPA), which reflects thrombin action,

16 vo to fibrinogen and conducting an assay for fibrinopeptide A (FPA).

17 Respective values for plasma fibrinopeptide A (FPA, nmol/L) were 1.52, 1.35, and 1.15

18 (NaCl, ChCl, or NaF) and is -1.5 +/- 0.1 for fibrinopeptide A and -2.5 +/- 0.1 for fibrinopeptide B.

19 In contrast to thrombin, which releases fibrinopeptide A and B from the NH2-terminal domains of

20 Fibrinogen Longmont had normal fibrinopeptide A and B release and a functional polymeri

21 wo sets of two consecutive Glu residues, and fibrinopeptide A and fibrinopeptide B, with isolated aci

22 thrombin-catalyzed fibrinogen activation to fibrinopeptide A are most consistent with a two-proton b

23 T was polymerized with Ancrod, which cleaves fibrinopeptide A at the same rate from either fibrinogen

24 34Val peptide was released more slowly than fibrinopeptide A but more quickly than fibrinopeptide B

25 (2) Fibrinopeptide A cleavage further unmasks the NH2 and Ar

26 this structure with the crystal structure of fibrinopeptide A complexed with thrombin highlights seve

27 eparin reduced beta-thromboglobulin release; fibrinopeptide A concentrations were significantly highe

28 rminal portion (1ADSGE5) of unphosphorylated fibrinopeptide A does not interact with the surface of b

29 ragment of GPIb alpha reduced the release of fibrinopeptide A from fibrinogen by about 50% by a nonco

30 The k(cat)/K(m) for the release of fibrinopeptide A from fibrinogen was 4.5 +/- 0.5 microM(

31 Fibrinopeptide A generation showed threshold variability

32 vated partial thromboplastin time assays and fibrinopeptide A generation tests.

33 uch as argatroban, were the observation that fibrinopeptide A had antithrombotic properties and deter

34 he hypothesis given above, and indicate that fibrinopeptide A is also involved.

35 Neither treatment changed fibrinopeptide A or prothrombin fragment 1 and 2.

36 The rate of fibrinopeptide A release was decreased 27-fold, and the

37 Fibrinopeptide A release was normal, whereas fibrinopept

38 Fibrinopeptide A release was slower over the course of t

39 o its higher affinity interaction, selective fibrinopeptide A release, and prothrombotic properties.

40 n concentrations that equalized the rates of fibrinopeptide A release, BbetaA68T fibrinogen polymeriz

41 hrombin activation and fibrin formation with fibrinopeptide A release.

42 Ancrod-induced cleavage of fibrinopeptide A was not affected.

43 le the rate of thrombin-catalyzed release of fibrinopeptide A was similar, the release of fibrinopept

44 rhauser effect spectroscopy studies of bound fibrinopeptide A(1-16 Ser3P) indicate that phosphorylati

45 rd peptides such as YGGFLR, angiotensin III, fibrinopeptide A, and des-Arg1-bradykinin were dissociat

46 ivated factor XII, prothrombin fragment 1+2, fibrinopeptide A, and fibrinogen were measured in 1153 m

47 duced rates for TAT formation but equivalent fibrinopeptide A, and fV activation/inactivation.

48 peptide F1.2, thrombin-antithrombin complex, fibrinopeptide A, and soluble fibrin, combined with a co

49 tor VII, prothrombin fragment 1 + 2, urinary fibrinopeptide A, C-reactive protein, and interleukin-6

50 Here we present SID of leucine enkephalin, fibrinopeptide A, melittin, insulin chain-B, and a nonco

51 ges were observed with treatment in d-dimer, fibrinopeptide A, prothrombin fragment F1.2, factor VIIa

52 eu peptide was released at a similar rate as fibrinopeptide A, the 34Val peptide was released more sl

53 The systemic levels of fibrinopeptide A, thrombin-antithrombin complex, D-dimer

54 exposed by the thrombin-catalyzed removal of fibrinopeptide A, was found to reside in the gamma-chain

55 n for urothelial carcinoma was identified as fibrinopeptide A-a known biomarker of ovarian cancer and

56 ized A'beta fibrinogen, replacing FpB with a fibrinopeptide A-like peptide, FpA' (G14V).

57 ion, ITS accumulation, and the production of fibrinopeptide A.

58 cificity constant 280-fold lower than normal fibrinopeptide A.

59 -terminal neoepitope generated by release of fibrinopeptide A.

60 rmation seen in both factor XIII-(28-37) and fibrinopeptide A.

61 ogen, respectively, batroxobin only releases fibrinopeptide A.

62 depends on the release of the two N-terminal fibrinopeptides A (FPA) from fibrinogen, and its formati

63 h fibrinogen promotes sequential cleavage of fibrinopeptides A and B (fpA and fpB, respectively) from

64 Upon addition of thrombin, fibrinopeptides A and B are cleaved off from the N-termi

65 The release of fibrinopeptides A and B by the slow and fast forms of th

66 blood coagulation cascade, thrombin cleaves fibrinopeptides A and B from fibrinogen revealing sites

67 Thrombin cleaves fibrinopeptides A and B from the N-termini of the fibrin

68 -termini of Bbeta chains and that removal of fibrinopeptides A and B upon fibrin assembly results in

69 We found that the release of fibrinopeptides A and B was the same for these variants

70 haC-connector, bound to NDSK, which contains fibrinopeptides A and B, and less frequently to desA-NDS

71 of the alpha- and beta-chains, including the fibrinopeptides A and B, are also disordered.

72 ents of the alpha and beta chains, including fibrinopeptides A and B, are not visible in electron den

73 aining was detected using antibodies against fibrinopeptides A and B, as well as with the T2G1 monocl

74 ogen and fibrin I, leading to the release of fibrinopeptides A and B, is driven by electrostatic forc

75 -knobs, which are exposed by the cleavage of fibrinopeptides A and B, respectively, and between corre

76 late the two knobs exposed by the removal of fibrinopeptides A and B, respectively.

77 g to the knobs exposed by the release of the fibrinopeptides A and B.

78 Thrombin failed to release fibrinopeptide-A from fibrinogen(AEK) and failed to indu

79 e may serve as an anionic linker between the fibrinopeptide and the enzyme thrombin.

80 ble by thrombin, but the rates of release of fibrinopeptides and clotting times were delayed compared

81 he most common structural defect involve the fibrinopeptides and their cleavage sites, and the second

82 While the release of fibrinopeptides as a function of salt concentration was

83 led monolayers) released a smaller amount of fibrinopeptides, at a reduced rate relative to those of

84 (both are proteins), and 0.002% (w/v) human fibrinopeptide B (a peptide).

85 et basic protein, thymosin beta-4 (Tbeta-4), fibrinopeptide B (FP-B), and fibrinopeptide A (FP-A).

86 bin, fibrinopeptide A (FpA) release precedes fibrinopeptide B (FpB) release.

87 receded lysis of the Aalpha chain, such that fibrinopeptide B (FpB) was released prior to F8Y 1-16.

88 d decrease in the rate of thrombin-catalyzed fibrinopeptide B (FpB, Bbeta 1-14) release, whereas the

89 SdrG could recognize fibrinopeptide B (residues 1-14), but with a substantial

90 [Glu(1)]-Fibrinopeptide B and substance P were used to evaluate t

91 reported here indicate that IIa-cleavage of fibrinopeptide B enhances exposure of a heparin binding

92 than fibrinopeptide A but more quickly than fibrinopeptide B generation.

93 In rabbit arteries, fibrinopeptide B is reported to have both vasoconstricto

94 lease was decreased 27-fold, and the rate of fibrinopeptide B release was decreased 45-fold relative

95 Fibrinopeptide A release was normal, whereas fibrinopeptide B release was delayed approximately 3-fol

96 uced fibrinogen clotting by interfering with fibrinopeptide B release.

97 Injection of 25 fmol of [Glu1]-fibrinopeptide B using the new device produced a CE-ESI-

98 fibrinopeptide A was similar, the release of fibrinopeptide B was accelerated in STAT5-deficient plas

99 For angiotensin II and [Glu(1)]-fibrinopeptide B we achieved coefficients of determinati

100 e deuterium uptake of Leu-Enkephalin and Glu-Fibrinopeptide B, confirmed that this gas-phase HDX-MS a

101 haC-domains and the central E region through fibrinopeptide B, in agreement with the hypothesis given

102 ptides P294 and P326, a hydrophilic peptide, fibrinopeptide B, showed much weaker affinity for zwitte

103 clarifies the role played by the release of fibrinopeptide B, which leads to slightly thicker fibers

104 utive Glu residues, and fibrinopeptide A and fibrinopeptide B, with isolated acidic residues, also sh

105 tor affecting thrombin-triggered cleavage of fibrinopeptide B.

106 .1 for fibrinopeptide A and -2.5 +/- 0.1 for fibrinopeptide B.

107 suppression is demonstrated for LSIMS of Glu-fibrinopeptide B.

108 ith desAB-NDSK and (beta15-66)2 both lacking fibrinopeptide B.

109 er fragments by thrombin treatment to remove fibrinopeptides B, bound the recombinant VE-cadherin fra

110 o desA-NDSK and (Bbeta1-66)2 containing only fibrinopeptides B; it was poorly reactive with desAB-NDS

111 The rapidity of release of the fibrinopeptides by thrombin had been shown to depend on

112 inhibited in a dose-dependent manner, as was fibrinopeptide cleavage from fibrinogen.

113 ficantly affected the extent and kinetics of fibrinopeptide cleavage, and the conversion of adsorbed

114 hase of fibrin formation, thrombin-catalyzed fibrinopeptide cleavage, from adsorbed fibrinogen using

115 (osteonectin release), factor Va generation, fibrinopeptide (FP) A and FPB release, and factor XIII a

116 ture were attributable to delayed release of fibrinopeptide (FP) A from fibrinogen 2 by thrombin, whi

117 t structure due to delayed thrombin-mediated fibrinopeptide (FP) B release or impaired cross-linking

118 We have developed methods to quantitate fibrinopeptides (FPs) and soluble and insoluble Fg/Fn pr

119 We conclude that premature release of the fibrinopeptide from the N terminus of the beta chain doe

120 ed fibrinogen and the release of radioactive fibrinopeptides from formed clots was measured.

121 on of the protein that, after the removal of fibrinopeptides from the N-termini of its alpha chains b

122 We report here that fibrinopeptides had no vasoactive effects on saphenous v

123 exposed by the thrombin-mediated cleavage of fibrinopeptides in the central E region of the protein a

124 We conclude that the ordered release of fibrinopeptides is dictated by the specificity of thromb

125 The sequential mechanism for the release of fibrinopeptides originally proposed by Shafer was found

126 We examined thrombin-catalyzed fibrinopeptide release and found that the rate of FpB re

127 Fibrinopeptide release and insoluble clot formation were

128 Fibrinopeptide release by thrombin was normal in rate an

129 Analyses of fibrinopeptide release from A'beta fibrinogen showed tha

130 de release from the beta chain is similar to fibrinopeptide release from the alpha chain.

131 Thus, with A'beta fibrinogen, fibrinopeptide release from the beta chain is similar to

132 gen, and further demonstrate that sequential fibrinopeptide release has an important role in normal p

133 The ordered sequence of fibrinopeptide release is essential for the knob-hole in

134 Fibrinopeptide release was not significantly altered by

135 mined the kinetics of (1) thrombin-catalyzed fibrinopeptide release, (2) thrombin-catalyzed polymeriz

136 m and LPS-THP-1 the rates of TAT generation, fibrinopeptide release, and fV activation were almost do

137 of desAB fibrin monomers, which circumvents fibrinopeptide release, was the same for both fibrinogen

138 changes were not related to cross-linking or fibrinopeptide release.

139 The salt dependence of the release of fibrinopeptides shows a constant coefficient Gamma(salt)