ライフサイエンスコーパス: kininogen

1 nd domains 2 and 3 of the Family 3 cystatin, kininogen).

2 rat (1 encoding K-kininogen and 2 encoding T-kininogen).

3 lting from cleavage of high-molecular-weight kininogen.

4 eight kininogen (HK) or low molecular weight kininogen.

5 scribed to domain 5 of high-molecular-weight kininogen.

6 with identity to residues 421-436 of human H-kininogen.

7 ase of bradykinin from high molecular weight kininogen.

8 ined to have detectable low-molecular-weight kininogen.

9 physiological precursor low molecular weight kininogen.

10 lutionarily related to high-molecular-weight kininogen.

11 aldosterone concentrations (SNP rs5030062 in kininogen 1 [KNG1]: P=0.001 for plasma renin, P=0.024 fo

12 We identified 2 genetic loci (kininogen 1 and kallikrein B) influencing key components

13 In myocardium, kininogen (10 micrograms/mL) and captopril, enalaprilat,

14 mplement C3, SHC-transforming protein 1, and kininogen 2.

15 that, unlike its effect on normal platelets, kininogen (2 micromol/L) did not inhibit the thrombin-in

16 the presence of either high molecular weight kininogen (45 nm) and ZnCl(2) (25 micrometer) or prothro

17 om) is able to replace high molecular weight kininogen (45 nm) as a cofactor for the specific binding

18 m) are able to replace high molecular weight kininogen (45 nm) or prothrombin (1 microm) as cofactors

19 In the presence of high molecular weight kininogen (45 nm), Zn(2+) and Ca(2+) ions, thrombin acti

20 The effect of kininogen adsorption on neutrophil adhesion, the surface

21 On PU, NR(4), and SO(3), kininogen adsorption reached 80% of monolayer coverage w

22 The NR(4) surface adsorbed the most kininogen along with a high exposure of D(3) and D(5H).

23 ene, 3 copies exist in the rat (1 encoding K-kininogen and 2 encoding T-kininogen).

24 cy reduced cleavage of high-molecular-weight kininogen and attacks of angioedema.

25 en is the precursor for two-chain kinin-free kininogen and bradykinin.

26 ain in the presence of high molecular weight kininogen and Zn2+ or prothrombin and Ca2+.

27 ed the alpha-thrombin inhibitory sequence of kininogens and describe its mechanism of action.

28 Kininogens and their breakdown products also are antithr

29 thrombin (and Ca2+) or high molecular weight kininogen (and Zn2+), which are required for factor XI b

30 asma levels of cleaved high-molecular-weight kininogen, and efficacy was assessed by the rate of atta

31 ng1, is responsible for production of plasma kininogen, and that plasma HK contributes to induced art

32 dhesion, the surface density of the adsorbed kininogen, and the exposure of HK domains 3 and 5 (D(3)

33 Kinins cleaved from kininogen are agonists of the B2R and must be processed

34 shown that both high and low molecular mass kininogens are able to inhibit the thrombin-induced aggr

35 Plasma kininogens are selective inhibitors of alpha-thrombin ac

36 The unexpected identification of H-kininogen as a ferritin-binding protein may link ferriti

37 he experiments described here, we identify H-kininogen as a ferritin-binding protein.

38 hil adhesion even in the absence of adsorbed kininogens because of its phosphorylcholine moiety.

39 Human kininogen belongs to the plasma kallikreinkinin system.

40 both H and L recombinant ferritins possess H-kininogen binding activity.

41 A kininogen binding protein(s), a putative receptor, was i

42 entify a new function for cytokeratin 1 as a kininogen binding protein.

43 d SZ 2, can inhibit 125I-high molecular mass kininogen binding to platelets.

44 These results indicated that kininogen binds to the GP Ib-IX-V complex modulating thr

45 or near the site where high molecular weight kininogen binds.

46 r plates, biotinylated high molecular weight kininogen (biotin-HK) or biotin-FXI binding to HUVEC mon

47 Further, HK and low molecular mass kininogen, but not factor XII, blocked biotin-HK binding

48 in factor XI or XII or high-molecular-weight kininogen, but not plasma kallikrein, protected mice fro

49 n (BK) and kallidin (Lys-BK), liberated from kininogens by kallikreins, are ligands of the BK B(2) re

50 monoclonal antibody to high-molecular weight kininogen, C11C1, blocked its binding to endothelial cel

51 to the light chain of high molecular weight kininogen, C11C1, to inhibit tumor growth compared to is

52 High-molecular-weight kininogen can be hydrolysed by plasma kallikrein to brad

53 Kininogen can thus serve as an important regulator of th

54 ritin binding domain to the light chain of H-kininogen chain, and revealed that both H and L recombin

55 In vitro studies showed a decreased rate of kininogen cleavage in Buffalo plasma.

56 When the prekallikrein-high molecular weight kininogen complex is bound to endothelial cells, prekall

57 No evidence for a thrombin-kininogen complex was found, and neither HK nor its deri

58 With higher high molecular weight kininogen concentrations (360 nm), the rate of thrombin-

59 Conversely, kininogen could block the binding of biotinylated TM-60

60 showed that nonsurvivors had increased total kininogen; decreased total cathepsin-L1, vascular cell a

61 tigating the cardiac radiation response in a kininogen-deficient Brown Norway Katholiek (BN/Ka) rat m

62 binding could not be detected in plasma from kininogen-deficient individuals.

63 Using monoclonal antibodies (Mabs) to kininogen domain 3, the propositus, family members, and

64 mHK-D5, a novel kininogen isoform that lacks kininogen domain 5.

65 vation of factor XII, plasma kallikrein, and kininogen during the acute phase of anaphylaxis but not

66 blot analysis confirmed the up-regulation of kininogen expression by FXR agonists.

67 A more robust induction of kininogen expression was observed in HepG2 cells, where

68 Prekallikrein, high-molecular weight kininogen, factor XI, and factor XII were decreased in t

69 es tested, does not effectively compete with kininogen for kallikrein binding (kd = 100 micromol/L).

70 peptide and additional high molecular weight kininogen fragments containing the antimicrobial peptide

71 In this study we show that the human kininogen gene is strongly up-regulated by agonists of t

72 bined results indicate that mutations in the kininogen gene may differentially affect biosynthesis, p

73 e human genome contains a single copy of the kininogen gene, 3 copies exist in the rat (1 encoding K-

74 cient in kinins because of a mutation in the kininogen gene, and their wild-type control (Brown Norwa

75 eavy chain coded for by exons 7, 8, and 9 of kininogen gene.

76 OG induced cleavage of high molecular weight kininogen, generating the proinflammatory bradykinin pep

77 that the mouse genome contains 2 homologous kininogen genes, mKng1 and mKng2, and demonstrate that t

78 A titration with high molecular weight kininogen had no effect on FXIa binding to platelets, bu

79 The cleaved form of high-molecular-weight kininogen has recently been demonstrated to exhibit anti

80 has been shown that the two-chain kinin-free kininogen has the properties of anti-adhesion, anti-plat

81 clonal antibody to the high molecular weight kininogen heavy chain or to an unrelated plasma protein.

82 ECs in the presence of high molecular weight kininogen (HK) (apparent Kd of 23 +/- 11 nmol/L, Bmax of

83 was isolated by a biotin-high molecular mass kininogen (HK) affinity column that, on aminoterminal se

84 High molecular weight kininogen (HK) also stimulates the expression of cell su

85 te when it is bound to high-molecular-weight kininogen (HK) and can digest HK to produce bradykinin.

86 binding site for both high molecular weight kininogen (HK) and factor XII (FXII).

87 High molecular weight kininogen (HK) and factor XII are known to bind to human

88 High molecular weight kininogen (HK) and its cleaved form (HKa) have been show

89 omplex formation between high-molecular-mass kininogen (HK) and plasminogen (Plg) which prevented Plg

90 n-mediated cleavage of high molecular-weight kininogen (HK) and release of proinflammatory bradykinin

91 ined binding sites for high molecular weight kininogen (HK) and thrombin in the Apple 1 (A1) domain o

92 ll, K(D) = 12 nm) when high molecular weight kininogen (HK) and zinc are present.

93 High molecular weight kininogen (HK) and Zn2+ ions exert opposite effects on t

94 to induce cleavage of high-molecular-weight kininogen (HK) at sites of inflammation.

95 have demonstrated that high molecular weight kininogen (HK) binds specifically on endothelial cells t

96 was recognized to have high-molecular-weight kininogen (HK) deficiency.

97 and derived from human high molecular weight kininogen (HK) domain 5 were inserted into GST (between

98 of the light chain of high molecular weight kininogen (HK) has previously been shown to be responsib

99 ned a binding site for high molecular weight kininogen (HK) in the A1 domain of factor XI (FXI).

100 ve previously reported high molecular weight kininogen (HK) inhibition of thrombin-induced platelet a

101 nonenzymatic cofactor high molecular weight kininogen (HK) is a precursor of bradykinin (BK).

102 High-molecular-weight kininogen (HK) is an abundant plasma protein that plays

103 High molecular weight kininogen (HK) is an endogenous protein that is proteoly

104 Factor XII (FXII) and high molecular weight kininogen (HK) mutually block each other's binding to th

105 by either single-chain high molecular weight kininogen (HK) or low molecular weight kininogen.

106 High-molecular-weight kininogen (HK) plays an important role in the assembly o

107 plored whether MPO and high molecular weight kininogen (HK) reside on CK1 together or whether they co

108 on the interaction of high molecular weight kininogen (HK) with endothelial cells have reported a la

109 ion is the cleavage of high molecular weight kininogen (HK) with liberation of bradykinin.

110 Proteolysis of plasma high molecular weight kininogen (HK) yielding bradykinin and cleaved HK (HKa)

111 Cleavage of high-molecular-weight kininogen (HK), a marker for activation of the inflammat

112 resence and absence of high molecular weight kininogen (HK), an important cofactor in this pathway.

113 uding the known ligand high-molecular-weight kininogen (HK), as well as the extracellular matrix prot

114 factor (f)XII, fXI, or high-molecular-weight kininogen (HK), key components of the contact pathway, o

115 tor (uPAR), and gC1qR, high-molecular-weight kininogen (HK)-binding proteins on endothelial cells, wa

116 es and is able to bind high molecular weight kininogen (HK).

117 PK) within domain 6 of high molecular weight kininogen (HK).

118 d factor XII (FXII), and a cofactor, high-MW kininogen (HK).

119 with the glycoprotein high molecular weight kininogen (HK).

120 vates PK when bound to high-molecular-weight kininogen (HK).

121 soluble uPAR (suPAR) and high molecular mass kininogen (HK).

122 of factor XII, prekallikrein, and high M(r) kininogen (HK).

123 ate in the presence of high molecular weight kininogen (HK, 45 nM), ZnCl2 (25 microM), and CaCl2 (2 m

124 ct cleavage of high and low molecular weight kininogens (HK and LK), the parent molecules of bradykin

125 ino acids derived from high molecular weight kininogen (HK31-mer) can also bind to factor XI.

126 Cleaved high molecular weight kininogen (HKa) has been shown to inhibit in vivo neovas

127 onstrated that cleaved high-molecular-weight kininogen (HKa) induces endothelial apoptosis and inhibi

128 e binding of two-chain high molecular weight kininogen (HKa) to endothelial cells may occur through i

129 bradykinin and cleaved high-molecular-weight kininogen (HKa).

130 leaving behind cleaved high-molecular-weight kininogen (HKa).

131 h a protein is cleaved high molecular weight kininogen (HKa).

132 aerosol challenge with high-molecular-weight kininogen (HMWK), a substrate of TK.

133 mg reduced cleavage of high-molecular-weight kininogen in plasma from patients with hereditary angioe

134 ivity, factor XII, and high-molecular weight kininogen in the plasma of 636 type 1 diabetic patients

135 ficant increases or decreases in the cleaved kininogen index (CKI), an index of HK proteolytic activa

136 ins prekalli-krein and high-molecular-weight kininogen indicated activation of the plasma contact sys

137 Kininogens inhibit thrombin binding to platelets and thu

138 The molecular mechanism by which kininogens inhibit thrombin-induced aggregation of plate

139 Kininogen inhibited the binding of biotinylated thrombin

140 lack the GP Ib-IX-V complex, suggesting that kininogen interacts either directly or indirectly with t

141 MASP-1 was shown to cleave high m.w. kininogen into bradykinin; therefore, we hypothesized th

142 To determine whether kininogen is a direct target of FXR, we examined the seq

143 H-kininogen is a multifunctional protein: it inhibits cyst

144 We conclude that kininogen is a novel and direct target of FXR, and bile

145 Cleaved high molecular weight kininogen is antiangiogenic.

146 We reported that high-molecular weight kininogen is proangiogenic by releasing bradykinin and t

147 have shown that human high molecular weight kininogen is proangiogenic due to release of bradykinin.

148 High molecular weight kininogen is the precursor for two-chain kinin-free kini

149 HKa (cleaved high molecular weight kininogen) is an endogenous inhibitor of angiogenesis fo

150 inogen (LK), as well as DeltamHK-D5, a novel kininogen isoform that lacks kininogen domain 5.

151 Kallikrein-kininogen-kinin systems are now topics of widespread int

152 High-molecular-weight kininogen (KNG) is a central constituent of the contact-

153 show trans associations for proteins (uPAR, kininogen) known to be cleaved by kallikrein and with NT

154 nerates plasma kallikrein, which proteolyzes kininogen, leading to the liberation of bradykinin.

155 ion only when bound to high molecular weight kininogen linked to microtiter plates.

156 formation between Plg and low-molecular-mass kininogen (LK) and between LK and HK with Plg cleaved wi

157 ut lacked plasma HK and low-molecular-weight kininogen (LK), as well as DeltamHK-D5, a novel kininoge

158 ceptor; thus, on the NR(4) surface, adsorbed kininogens lost their antiadhesive property, which resul

159 e L271-A277 derived from high molecular mass kininogen lower thrombin binding to platelets in a manne

160 nogen, suggesting that high molecular weight kininogen may play a role in regulating factor XIa activ

161 the complex chain of interactions by which H-kininogen mediates its multiple effects in contact activ

162 xpression was observed in HepG2 cells, where kininogen mRNA was increased by chenodeoxycholate or GW4

163 e and synthetic FXR agonist GW4064 increased kininogen mRNA with a maximum induction of 8-10-fold.

164 or of angiogenesis formed by the cleavage of kininogen on endothelial cells.

165 rein (PK) assembles on high molecular weight kininogen on HUVEC, PK is activated to kallikrein.

166 icate that assembly of high molecular weight kininogen on its multiprotein receptor allows for prekal

167 me inhibitor enalaprilat and the addition of kininogen or kallikrein enhanced norepinephrine exocytos

168 Thus, both SO(3) coupled with kininogen (or kininogen peptides) and GPC have the poten

169 II, plasma kallikrein, high-molecular-weight kininogen, or the bradykinin B2 receptor, but not the B1

170 the contact proteins, high molecular weight kininogen (P<0.03), and factor XI (P<0.04) in group II v

171 Thus, both SO(3) coupled with kininogen (or kininogen peptides) and GPC have the potential to marked

172 y demonstrating that commercially purified H-kininogen possessed ferritin binding activity and that f

173 more, peptide RPPGF or high-molecular-weight kininogen prevented alpha-thrombin from cleaving the thr

174 verted repeat, IR-1) in the proximity of the kininogen promoter (-66/-54).

175 rget of FXR, we examined the sequence of the kininogen promoter and identified a highly conserved FXR

176 12.5 days) and blocked high molecular weight kininogen proteolysis in activated plasma in a dose- and

177 Knowledge of the critical sequence of kininogen should allow design of compounds that can modu

178 partially abrogated by high molecular weight kininogen, suggesting that high molecular weight kininog

179 In coronary microvessels, kininogen (the precursor of kinin; 10 micrograms/mL) and

180 ntly blocks binding of high molecular weight kininogen to endothelial cells in a concentration-depend

181 roteolytically cleaves high molecular weight kininogen to generate the potent vasodilator and the pro

182 proteases that cleave high molecular weight kininogen to produce bradykinin.

183 allikrein (PK) cleaves high-molecular-weight kininogen to release bradykinin (BK) and is a key consti

184 The ability of kininogens to modulate thrombin-induced aggregation of h

185 T-kininogen was increased in the disease-untreated group w

186 tors VIII, IX, XI, and high molecular weight kininogen were elevated.

187 Kininogens were measured by particle concentration fluor

188 a series of reactions leading to cleavage of kininogens with subsequent release of bradykinin.