ライフサイエンスコーパス: protease-nexin

1 e, we identify the serine protease inhibitor protease nexin 1 (PN1) as a negative regulator of Hh sig

2 Protease nexin 1 (PN1) in solution forms inhibitory comp

3 We have previously described thrombin (Th)-protease nexin 1 (PN1) inhibitory complex binding to cel

4 Protease nexin 1 (PN1) is a serine protease inhibitor (S

5 eptide, Pro47-Ile58, derived from the mature protease nexin 1 (PN1) sequence, that inhibited the low

6 dies we have made the novel observation that protease nexin 1 (PN1), a member of the serine protease

7 The results suggested that protease nexin 1 (PN1), a protease inhibitor, is overexp

8 the papers of Aymonnier et al on the use of protease nexin 1 and de Maat et al on the use of altered

9 ee sLRPs also bound lactoferrin and thrombin-protease nexin 1 complexes.

10 Protease nexin 1 mRNA was found only in the mesenchymal

11 , plasminogen activator inhibitor type 2 and protease nexin 1, in human hair follicles using in situ

12 tor binding protein 5, KIAA0179 protein, and protease nexin 1.

13 re that two genes identified by this screen, protease nexin-1 (Pn-1) and vanin-1 (Vnn1), exhibit male

14 a proteomic screen, we identified the serpin protease nexin-1 (PN-1) as a potential target of MMP-9.

15 Protease nexin-1 (PN-1) is a serine protease inhibitor b

16 Protease nexin-1 (PN-1) is a serpin that is barely detec

17 , revealed that a serine protease inhibitor, protease nexin-1 (PN-1), was significantly up-regulated

18 in inhibitor, expressed by platelets, called protease nexin-1 (PN-1).

19 Protease nexin-1 (PN1) is a specific and extremely effic

20 s (Ki) for S195A with serpins (antithrombin, protease nexin-1 and alpha1-antitrypsin with a P1 argini

21 r195; it increased the affinity of S195A for protease nexin-1 and antithrombin by 140-fold and 1000-f

22 we identified the secreted protein SerpinE2/protease nexin-1 as causative for the highly invasive po

23 Because protease nexin-1 expression has been shown to be regulat

24 Kinetic studies with antithrombin and protease nexin-1 in the presence of heparin indicated th

25 otentially important roles that thrombin and protease nexin-1 may play during skeletal muscle develop

26 n both genotypes, including uPA, tPA, PAI-1, protease nexin-1, and alpha2-antiplasmin.

27 Because another serpin, protease nexin-1, has been shown to promote the in vivo

28 , we have shown that the thrombin inhibitor, protease nexin-1, significantly prevents neuronal cell d

29 formed SDS-stable complexes with the serpin protease nexin-1.

30 ravasculature by an extracellular inhibitor, protease nexin-1.

31 Protease nexin 2 (PN2) is a Kunitz-type protease inhibit

32 This study demonstrates that "protease nexin 2 (PN2)," the secreted form of the kunitz

33 contain the Kunitz domain are also known as protease nexin 2 (PN2).

34 f a physiologically relevant FXIa inhibitor, protease nexin 2 (PN2).

35 Because APP/protease nexin 2 and mesotrypsin are coexpressed in a nu

36 APP containing this domain is also known as protease nexin 2 and potently inhibits serine proteases,

37 late the protease inhibitory function of APP/protease nexin 2 in vivo and may also modulate other act

38 substrates of mesotrypsin, we find that APP/protease nexin 2 is selectively cleaved by mesotrypsin w

39 nd may also modulate other activities of APP/protease nexin 2 that involve the Kunitz domain.

40 et surface protected FXIa from inhibition by protease nexin 2.

41 1.7-fold) and the Kunitz inhibitor domain of protease Nexin-2 (1.4-fold).

42 Protease nexin-2 (PN-2), a soluble form of amyloid beta-

43 he kunitz protease inhibitor (KPI) domain of protease nexin-2 (PN2) is a potent, highly specific inhi

44 cell-secreted proteinase inhibitor known as protease nexin-2 (PN2).

45 tes activated factor XI (FXIa) inhibition by protease nexin-2 by providing a template to which both p

46 ng a template for the assembly of factor XIa-protease nexin-2 complexes, and only heparin polymers co

47 e units potentiated factor XIa inhibition by protease nexin-2 in a size- and concentration-dependent

48 Previous kinetic studies have shown that protease nexin-2 is a potent, reversible, and competitiv

49 o provide a template to which factor XIa and protease nexin-2 molecules can bind simultaneously.

50 ar weight heparin potentiates the ability of protease nexin-2 to inhibit factor XIa with a parabolic

51 No effect on factor XIa inhibition by protease nexin-2 was observed with heparin preparations

52 ated enhancement of factor XIa inhibition by protease nexin-2 was partially abrogated by high molecul

53 in inhibitor, the Kunitz inhibitor domain of protease Nexin-2, and the first two inhibitor domains of

54 inhibitor of Factor IXa and Factor XIa (ie, protease nexin-2/ amyloid beta-protein precursor, A beta

55 For example, the Abeta parent molecule protease nexin-2/amyloid beta-protein precursor (PN-2/Ab

56 constructed representing most of the mature protease nexin I (PN1) sequence from the amino terminus

57 II (HCII), alpha2-macroglobulin (alpha2-M), protease nexin I, and plasminogen activator inhibitor-1

58 tor-2, antithrombin, alpha 2-antiplasmin and protease nexin I.

59 Inhibition of factor XIa by protease nexin II (K(i) approximately 450 pM) is potenti

60 -1 (TIMP-1), alpha1-antitrypsin (alpha1-AT), protease nexin II (PN-II), thrombospondin-1 and soluble

61 te constants for inhibition of factor XIa by protease nexin II [(3.35 +/- 0.35) x 10(6) M(-1) s(-1)]

62 ctions required for factor XIa inhibition by protease nexin II are localized to the catalytic domain

63 talytic domain of factor XIa is inhibited by protease nexin II with an inhibition constant of 437 +/-

64 Protease nexin II, a platelet-secreted protein containin

65 omain of factor XIa and the Kunitz domain of protease nexin II.