ライフサイエンスコーパス: prekallikrein

1 cells possess the ability to activate plasma prekallikrein.

2 so corrected by reconstitution with purified prekallikrein.

3 with the identity of the Fletcher factor and prekallikrein.

4 contact phase proteins, factor XII, HK, and prekallikrein.

5 intrachain disulfide bond with Cys326 as in prekallikrein, a plasma protein that exists as a monomer

6 Replacing the A3 domain with the prekallikrein A3 domain increases K(m) for fIX cleavage

7 a template for a series of proteins in which prekallikrein A3 sequence was replaced with factor XI se

8 cells, factor XII activation is secondary to prekallikrein activation and amplifies it.

9 temic amyloidosis allow for plasma FXIIa and prekallikrein activation and increased formation of kall

10 Controlling prekallikrein activation by C1 inhibitor (C1Inh) represe

11 The fCS polysaccharides showed prekallikrein activation comparable with dextran sulfate

12 s the protein responsible for zinc-dependent prekallikrein activation in the presence of HK.

13 The immediate consequence of plasma prekallikrein activation is the cleavage of high molecul

14 Peptides GPV15 and PGG15 also blocked prekallikrein activation on endothelial cells.

15 at blocked HK binding to uPAR also inhibited prekallikrein activation on HUVEC.

16 iated HK is proteolyzed during the course of prekallikrein activation, releasing kallikrein from the

17 ial cells could augment release of Hsp90 and prekallikrein activation.

18 ogen on its multiprotein receptor allows for prekallikrein activation.

19 cal vein endothelial cell (HUVEC)-associated prekallikrein activator (PKA).

20 Homology scanning, using prekallikrein amino acid substitutions within the synthe

21 ne mapping of the heparin-binding site using prekallikrein analogue amino acid substitutions of the s

22 lement 1 inhibitor, neutralizing antibody to prekallikrein and bradykinin receptor antagonism.

23 of a surface, FXII-R353A and FXII-T activate prekallikrein and cleave the tripeptide S-2302, demonstr

24 proteins are normal except for an increased prekallikrein and decreased factor XI.

25 ide YHK9 also inhibits FXIIa's activation of prekallikrein and FXI on HUVECs.

26 cher factor-deficient plasma is deficient in prekallikrein and therefore generates no bradykinin upon

27 of the contact proteases factor XII (FXII), prekallikrein, and factor XI (FXI) can trigger coagulati

28 urfaces requiring interaction of factor XII, prekallikrein, and high M(r) kininogen (HK).

29 sine-sulfated hemostatic proteins-protein S, prekallikrein, and plasminogen-were identified.

30 a variety of known substrates such as plasma prekallikrein, bradykinin, angiotensins II and III, and

31 suggest that free HK, or HK in complex with prekallikrein but not in complex with factor XI, interac

32 lial cells possessed the ability to catalyze prekallikrein conversion to kallikrein, and activation d

33 system" factors (factor XI, factor XII, and prekallikrein) could not be identified.

34 However, homologous prekallikrein-derived peptides (encompassing Pro(45)-Gly

35 We have previously reported that prekallikrein expresses an active site when it is bound

36 presence of a physiological concentration of prekallikrein, factor XI abrogates HK binding to HUVEC i

37 ule with the A3 domain replaced with A3 from prekallikrein (FXI/PKA3) activated factor IX with a K(m)

38 We observed that the prekallikrein gene (Klkb1) is expressed highly in the ma

39 l, whereas the recombinant Apple 3 domain of prekallikrein had little effect.

40 Prekallikrein, high-molecular weight kininogen, factor X

41 When the prekallikrein-high molecular weight kininogen complex is

42 nt HK cleavage either by prekallikrein or by prekallikrein-HK autoactivation to generate kallikrein.

43 Zinc-dependent activation of the prekallikrein-HK complex also depended on addition of ei

44 lease of Hsp90 and augment activation of the prekallikrein-HK complex to generate kallikrein and brad

45 Augmented activation of the prekallikrein-HK complex to generate kallikrein was seen

46 results indicate that C1-INH stabilizes the prekallikrein-HK complex to prevent HK cleavage either b

47 Activation of the prekallikrein-HK complex was measured by using pro-phe-a

48 Addition of 0.1% factor XII relative to prekallikrein-HK leads to rapid formation of kallikrein;

49 We demonstrate that prekallikrein-HK will activate to kallikrein in phosphat

50 that streptococcal supernatants can activate prekallikrein, in addition to causing plasminogen activa

51 nogen complex is bound to endothelial cells, prekallikrein is stoichiometrically converted to kallikr

52 The plasma protease prekallikrein is structurally homologous to factor XI, b

53 factor XIa containing the Apple 3 domain of prekallikrein (Ki approximately 2.7 nM) competed with [1

54 Surprisingly, exposing VSMCs to prekallikrein leads to activation of the ERK1/2 mitogen-

55 precise mechanism for reduced thrombosis in prekallikrein null mice (Klkb1(-/-)) is unknown.

56 -HK complex to prevent HK cleavage either by prekallikrein or by prekallikrein-HK autoactivation to g

57 highly restricted in its ability to initiate prekallikrein or FXI activation.

58 tically active stimulus since neither C5 nor prekallikrein or inactivated kallikrein could enhance me

59 nM) but does not target either the zymogen (prekallikrein) or any other serine protease tested.

60 nti-gC1qR blocked both biotin-HK binding and prekallikrein (PK) activation on HUVECs with an inhibito

61 vein endothelial cells (HUVECs), is a plasma prekallikrein (PK) activator.

62 We measured the circulating levels of plasma prekallikrein (PK) activity, factor XII, and high-molecu

63 cells (HUVECs) results in the activation of prekallikrein (PK) and its dependent pathways.

64 When prekallikrein (PK) assembles on high molecular weight ki

65 The hypothesis that plasma prekallikrein (PK) is a risk factor for the development

66 ations determined the relative preference of prekallikrein (PK) or factor XI/XIa (FXI/FXIa) binding t

67 to be responsible for the binding of plasma prekallikrein (PK) or kallikrein.

68 n to encompass the binding domain for plasma prekallikrein (PK) within domain 6 of high molecular wei

69 the functional role of HK in the absence of prekallikrein (PK), the proenzyme of plasma kallikrein,

70 ng the FXI A4 domain with the A4 domain from prekallikrein (PK).

71 omologous but functionally distinct protease prekallikrein (PK).

72 n system (KKS) consists of serine proteases, prekallikrein (pKal) and factor XII (FXII), and a cofact

73 We demonstrate that selective reduction of prekallikrein (PKK), another member of the contact syste

74 We investigated the effects of tPA on plasma prekallikrein (PPK) activation and the role of PKal on c

75 The ability of prekallikrein to correct the coagulation, fibrinolytic,

76 h factor XII and C1-INH led to conversion of prekallikrein to kallikrein and cleavage of HK, as was s

77 heat shock protein 90 leads to conversion of prekallikrein to kallikrein in a zinc-dependent reaction

78 Prolylcarboxypeptidase (PRCP) activates prekallikrein to plasma kallikrein, leading to bradykini

79 Corn trypsin inhibitor binds to prekallikrein to prevent rPRCP activation, but it does n

80 s, the plasma proteins factor XII (FXII) and prekallikrein undergo reciprocal proteolytic conversion

81 amino acid sequence of the Apple 3 domain of prekallikrein was replaced with that of factor XI was as

82 e was associated with reduced factor XII and prekallikrein, whereas levels of factors VIII, IX, XI, a

83 ability to serve as an acquired receptor for prekallikrein, which, after its activation, may directly