ライフサイエンスコーパス: plasma kallikrein

1 ors that are selective either for or against plasma kallikrein.

2 dimensional views of the catalytic domain of plasma kallikrein.

3 tivity for factor Xa relative to trypsin and plasma kallikrein.

4 ient to meet target levels for inhibition of plasma kallikrein.

5 binant granzyme A, human thrombin, and human plasma kallikrein.

6 ls) for expression of the protease domain of plasma kallikrein, along with the purification and high

7 teases we identified two new HGF activators, plasma kallikrein and coagulation factor XIa (FXIa).

8 In conclusion, the ability of plasma kallikrein and FXIa to activate pro-HGF in vitro

9 the biochemical and enzymatic properties of plasma kallikrein and paves the way for structure-based

10 We find that HGFA, matriptase, hepsin, plasma kallikrein and trypsin are potently inhibited, an

11 ay inhibitor-2 (TFPI-2) inhibits factor XIa, plasma kallikrein, and factor VIIa/tissue factor; accord

12 is an important inhibitor of complement C1, plasma kallikrein, and factor XIIa, and as such is invol

13 shares high sequence identity with acrosin, plasma kallikrein, and hepsin.

14 oblotting revealed activation of factor XII, plasma kallikrein, and kininogen during the acute phase

15 from the cloned cDNA and inhibited trypsin, plasma kallikrein, and plasmin with IC50 values in the n

16 Thrombin, factor Xa, plasmin, urokinase, plasma kallikrein, and tissue kallikrein had no effect.

17 p-regulated the expression of kallikrein and plasma kallikrein B genes.

18 Plasma kallikrein bound to HK cleaves prourokinase to ur

19 min, trypsin, chymotrypsin, cathepsin G, and plasma kallikrein but not urokinase-type plasminogen act

20 thrombin and potentiating the inhibition of plasma kallikrein by antithrombin.

21 Inhibition of plasma kallikrein by EPI-KAL2 and 13G11 significantly su

22 MPO and HK on cells such that MPO masked the plasma kallikrein cleavage site on HK, and MPO-generated

23 In transfected HEK293 cells, we find that plasma kallikrein directly activates G protein-coupled p

24 ions at doses >/=400 mg q8 h met or exceeded plasma kallikrein EC50 values throughout the dosing inte

25 the only inhibitory domain, and it inhibits plasma kallikrein, factor XIa, and plasmin.

26 dy of serum scuPAR levels identified a human plasma kallikrein gene (KLKB1) promoter polymorphism (rs

27 sequence repeat polymorphisms for the human plasma kallikrein gene (KLKB1; previously known as KLK3)

28 Like the rat plasma kallikrein gene and the closely related human fac

29 ble swelling episodes caused by uncontrolled plasma kallikrein generation and excessive bradykinin re

30 The production of BK from HK by plasma kallikrein has been implicated in the pathogenesi

31 Although plasma kallikrein has been purified for 40 years, its st

32 bolytic zymogens plasminogen, urokinase, and plasma kallikrein have all been shown to cleave and acti

33 n or pharmacologic inhibition of factor XII, plasma kallikrein, high-molecular-weight kininogen, or t

34 on was found for plasmin (IC50 = 399 nm) and plasma kallikrein (IC50 = 686 nm).

35 A critical role for plasma kallikrein in the pathogenesis of autoantibody-in

36 ontact pathway: factor XIa, factor XIIa, and plasma kallikrein, in the presence and absence of high m

37 ntravenous human C1INH, with a Kunitz domain plasma kallikrein inhibitor (DX88), and with a bradykini

38 The role of plasma KKS was examined using a plasma kallikrein inhibitor (EPI-KAL2) and an antikallik

39 apse following treatment with ecallantide, a plasma kallikrein inhibitor approved for HAE attack trea

40 Using the selective plasma kallikrein inhibitor P8720, we investigate whethe

41 Avoralstat is a potent small-molecule oral plasma kallikrein inhibitor under development for treatm

42 Plasma kallikrein is a serine protease that has many imp

43 human tissue kallikrein (Ki = 0.1 nM), human plasma kallikrein (Ki = 0.3 nM) and human factor XIa (Ki

44 The plasma kallikrein-kinin system (KKS) consists of serine

45 ws that monoclonal antibody C11C1 attenuates plasma kallikrein-kinin system activation, local and sys

46 ctions between MPO and the components of the plasma kallikrein-kinin system resulted in decreased bra

47 ays an important role in the assembly of the plasma kallikrein-kinin system.

48 otein for the assembly of the vasoregulatory plasma kallikrein-kinin system; thus we explored whether

49 athway for thrombosis risk reduction via the plasma kallikrein/kinin and renin angiotensin systems.

50 r physiologic assembly and activation of the plasma kallikrein/kinin system and discusses its influen

51 The relevance and significance of the plasma kallikrein/kinin system as a risk factor for the

52 ypeptidase (PRCP) activates prekallikrein to plasma kallikrein, leading to bradykinin liberation, and

53 and human recombinant tissue kallikrein and plasma kallikrein on [Ca(2+)](i) mobilization and [(3)H]

54 ence of prekallikrein (PK), the proenzyme of plasma kallikrein, on vascular endothelial cells is not

55 WT, the KD1-L17R did not inhibit factor XIa, plasma kallikrein, or factor VIIa/tissue factor.

56 Plasma kallikrein (PK) cleaves high-molecular-weight kin

57 Plasma kallikrein (PK) has been identified in vitreous f

58 t this augmented expansion is ameliorated by plasma kallikrein (PK) inhibition or deficiency.

59 Intravitreal injections of autologous blood, plasma kallikrein (PK), bradykinin, and collagenase were

60 -affinity, high-specificity binders to human plasma kallikrein (pKAL) and human thrombin (THBN) can b

61 Although plasma kallikrein (PKal) has been implicated in contribu

62 Plasma kallikrein (pKal) proteolytically cleaves high mo

63 tissue-type plasminogen activator (tPA), and plasma kallikrein (PKal).

64 was demonstrated against the serine protease plasma kallikrein (Pkal).

65 In addition, formed plasma kallikrein promotes single-chain urokinase activa

66 or high-molecular-weight kininogen, but not plasma kallikrein, protected mice from prostasome-induce

67 Cleavage of HK by plasma kallikrein results in release of the nonapeptide

68 ecular-weight kininogen can be hydrolysed by plasma kallikrein to bradykinin and cleaved high-molecul

69 rine proteases (thrombin, tPA, FXa, plasmin, plasma kallikrein, trypsin, FVIIa).

70 Inhibition of plasma kallikrein was observed at all doses, and the deg

71 Activated factor XII generates plasma kallikrein, which proteolyzes kininogen, leading

72 e relatively open active site of plasmin and plasma kallikrein, while it is rejected from sterically

73 -triazole derivative 10 inhibits plasmin and plasma kallikrein with K(i) of 0.77 and 2.4 nM, respecti

74 ic inhibition of PRCP with Z-Pro-Prolinal or plasma kallikrein with soybean trypsin inhibitor, Pro-Ph