ライフサイエンスコーパス: tissue kallikrein

1 s an excellent inhibitory specificity toward tissue kallikrein.

2 nhibitor (serpin) that specifically inhibits tissue kallikrein.

3 2 cleft generated by Tyr(99) and Trp(219) of tissue kallikrein.

4 s at P3 display better binding activity with tissue kallikrein.

5 e the inhibitory activity of a serpin toward tissue kallikrein.

6 Asp(98J) and hydrogen bond with Gln(174) of tissue kallikrein.

7 say between serum KBP and (125)I-labeled rat tissue kallikrein.

8 was determined by its complex formation with tissue kallikrein.

9 o, independent of regulating the activity of tissue kallikrein.

10 Fabs against human tissue kallikrein 1 (hK1, KLK1 gene product) were discov

11 Over-expression of tissue kallikrein-1 and modulation of the KKS shows bene

12 chronic administration of recombinant human tissue kallikrein-1 protein (DM199) to non-obese diabeti

13 eveloped and tested DM199, recombinant human tissue kallikrein-1 protein (rhKLK-1), as a potential no

14 about the role of kallikreins, in particular tissue kallikrein-1, in type 1 diabetes mellitus (T1D).

15 esponses is well documented, but the role of tissue kallikrein-1, the protease that generates bradyki

16 allergic sheep was associated with increased tissue kallikrein activity (TK) and decreased alpha-1-pr

17 ontained immunoreactive BK and BK precursor, tissue kallikrein activity, and bradykinin-destroying en

18 eu display significant binding activity with tissue kallikrein among the P1 variants.

19 eparin-suppressed inhibitory activity toward tissue kallikrein and exhibited an inhibitory activity 2

20 onents, kallikrein-binding protein, binds to tissue kallikrein and inhibits its activity in vitro.

21 a serine proteinase inhibitor which binds to tissue kallikrein and inhibits its activity.

22 milar in sequence to neuropsin, trypsin, and tissue kallikrein and is predicted to have trypsin-like

23 the effect of porcine and human recombinant tissue kallikrein and plasma kallikrein on [Ca(2+)](i) m

24 ), (2) BAL levels of the inflammatory marker tissue kallikrein, and (3) numbers of inflammatory cells

25 nhibitory activities of these mutants toward tissue kallikrein are in the order of P2 Phe (wild type)

26 llikrein interaction through competition for tissue kallikrein binding.

27 site responsible for its heparin-suppressed tissue kallikrein binding.

28 accelerate the association of a serpin with tissue kallikrein by acting as a secondary binding site.

29 (serpin), which specifically inhibits human tissue kallikrein by forming a covalent complex.

30 ermining inhibitory specificity toward human tissue kallikrein by site-directed mutagenesis and molec

31 Paradoxically, tissue kallikreins decreased the [(3)H]BK binding to the

32 specific serine protease and a member of the tissue kallikrein family, is a zymogen composed of 228 a

33 It is a member of the tissue kallikrein family, some of the members of which a

34 nthetic peptide-based inhibitor specific for tissue kallikrein (FE999024) was used in our studies to

35 (KLK)4 is a recently described member of the tissue kallikrein gene family that is specifically expre

36 Adenovirus carrying the human tissue kallikrein gene was delivered locally into the he

37 , plasmin, urokinase, plasma kallikrein, and tissue kallikrein had no effect.

38 Tissue kallikrein has been isolated and purified from ra

39 The serine proteinase tissue kallikrein has been previously demonstrated in se

40 ancer cell line, MDA-MB-231, which expresses tissue kallikrein in culture.

41 hibitory activities of the P1 mutants toward tissue kallikrein in the order of P1 Arg > P1 Phe > P1 L

42 reabsorption by parathyroid hormones or the tissue kallikrein in vivo.

43 kallistatin bound to the reactive crevice of tissue kallikrein indicated that the P2 residue required

44 ix and C2 sheet of kallistatin is crucial in tissue kallikrein inhibition, and this functional loop c

45 role of the basic residues in this region in tissue kallikrein inhibition.

46 ng the importance of these basic residues in tissue kallikrein inhibition.

47 ypsin, a non-heparin-binding serpin and slow tissue kallikrein inhibitor as a scaffold to engineer ka

48 n (KBP), a member of the serpin family, is a tissue kallikrein inhibitor.

49 Our results indicate that tissue kallikrein is a specific target proteinase for ka

50 to milk, BK, together with its precursor and tissue kallikrein, is continuously released into the vas

51 inhibited human plasmin (Ki = 0.1 nM), human tissue kallikrein (Ki = 0.1 nM), human plasma kallikrein

52 Renal tissue kallikrein levels and plasma renin activity were

53 Our results indicate tissue kallikrein may participate in the invasion and me

54 +/- 59 pg BK equivalents ml(-1) and that of tissue kallikrein, measured as cleavage of D-Val.Leu.Arg

55 f the kallikrein-kinin system are plasma and tissue kallikreins, proteases that cleave high molecular

56 Our previous study has shown that human tissue kallikrein protected against ischemia/reperfusion

57 In other tissues, kallikrein synthesis is under the influence of

58 Phe displays a better selectivity for human tissue kallikrein than P1 Arg, since P1 Arg also inhibit

59 ing specific protease inhibitors showed that tissue kallikrein (TK) processed pro-EGF in response to

60 (HA), in vitro, binds and inactivates airway tissue kallikrein (TK), the enzyme responsible for kinin

61 eptidase M); however, receptor activation by tissue kallikrein, trypsin, or cathepsin G was not affec

62 atin, the binding activity of K187A/K188A to tissue kallikrein was blocked by heparin, whereas K307A/