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 physiological precursor low molecular weight kininogen.

5 lutionarily related to high-molecular-weight kininogen.

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

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

8 ase of bradykinin from high molecular weight kininogen.

9 age and consumption of high-molecular-weight kininogen.

10 ikrein and cleavage of high-molecular-weight kininogen.

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

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

13 ringle 3 domain, perhaps altering binding to kininogens.

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

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

16 ogen (PLG-HAE), angiopoietin 1 (ANGPT1-HAE), kininogen 1 genes (KNG1-HAE), or angioedema of unknown o

17 erum samples compared to controls, including kininogen-1 isoform 1, alpha-1-microglobulin/bikunen pre

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

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

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

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

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

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

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

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

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

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

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

29 ulation factor XII and high molecular weight kininogen and accelerate the activation of the system.

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

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

32 prekallikrein, cleaved high molecular weight kininogen and elevated plasma bradykinin.

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

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

35 Kininogens and their breakdown products also are antithr

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

37 hock proteins, cleaved high molecular weight kininogen, and adipokines.

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

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

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

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

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

43 Plasma kininogens are selective inhibitors of alpha-thrombin ac

44 genic in the context of human Plm when human kininogens are the substrates.

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

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

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

48 Human kininogen belongs to the plasma kallikreinkinin system.

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

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

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

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

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

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

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

56 smin also released bradykinin from wild-type kininogens but cleaved HK-Lys379 and LK-Lys379 after Lys

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

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

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

60 he kinin released from wild-type and variant kininogens by PKa is bradykinin.

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

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

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

64 Kininogen can thus serve as an important regulator of th

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

66 centrations of cleaved high-molecular-weight kininogen (cHK), vascular endothelial growth factors (VE

67 with PLC activity and cleaved high molecular kininogen (cHK).

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

69 High-molecular-weight kininogen cleavage protection at the 600 mg dose was att

70 spontaneously triggers high-molecular-weight kininogen cleavage.

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

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

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

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

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

76 ced in APAP-challenged high-molecular-weight kininogen-deficient (HK-/-) mice.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

112 C1INH to regulate it, high-molecular-weight kininogen (HK) cleavage, and bradykinin (BK) liberation.

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

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

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

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

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

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

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

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

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

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

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

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

125 form, PK-R371A cleaves high-molecular-weight kininogen (HK) to release bradykinin with a catalytic ef

126 likrein, which cleaves high molecular weight kininogen (HK) to release bradykinin.

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

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

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

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

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

132 rekallikrein (PK), and high-molecular-weight kininogen (HK), and has received increased interest as a

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

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

135 munoassays to quantify high molecular weight kininogen (HK), plasma prekallikrein and Factor XII clea

136 Kallikrein cleaves high-molecular-weight kininogen (HK), releasing the vasoactive peptide bradyki

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

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

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

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

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

142 eptide bradykinin from high-molecular-weight kininogen (HK).

143 ein (PK), and cofactor high-molecular-weight kininogen (HK).

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

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

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

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

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

149 Glu311 cleaves high and low molecular weight kininogens (HK and LK, respectively), releasing BK more

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

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

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

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

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

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

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

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

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

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

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

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

162 Kininogens inhibit thrombin binding to platelets and thu

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

164 Kininogen inhibited the binding of biotinylated thrombin

165 rekallikrein (PK), and high molecular weight kininogen interact with anionic surfaces-has been shown

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

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

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

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

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

171 Cleaved high molecular weight kininogen is antiangiogenic.

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

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

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

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

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

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

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

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

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

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

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

183 g1 gene encoding HK and low-molecular weight kininogen (LK) was identified recently in a family with

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

185 F activator (HGFAC) and low molecular weight kininogen (LK).

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

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

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

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

190 h has Glu311, did not liberate BK from human kininogens more rapidly than human Plg-Lys311.

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

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

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

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

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

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

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

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

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

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

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

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

203 ein-kinin system (KKS) and downregulation of kininogen prior to transplant were associated with survi

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

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

206 12.5 days) and blocked high molecular weight kininogen proteolysis in activated plasma in a dose- and

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

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

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

210 e-treated mice also showed reduced levels of kininogen, the precursor to the permeability mediator br

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

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

213 ctivity, which cleaves high-molecular-weight kininogen to generate the proinflammatory hormone bradyk

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

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

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

217 sma protease kallikrein (PKa), which cleaves kininogens to release bradykinin and converts the protea

218 ein, which cleaves HK (high-molecular-weight kininogen) to liberate bradykinin.

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

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

221 Kininogens were measured by particle concentration fluor

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