ライフサイエンスコーパス: PC5

1 of other furin-family PCs (rat PACE4, human PC5/6 and human PC7), showing that dicoumarol derivative

2 Herein, because furin and PC5/6 complete KOs are lethal, we used mice lacking furi

3 However, the lack of furin or PC5/6 in hepatocytes and complete PACE4 KO did not appre

4 showed that loss of the convertase furin or PC5/6 in hepatocytes results in a approximately 30% decr

5 Os are lethal, we used mice lacking furin or PC5/6 specifically in hepatocytes (hKO) or mice complete

6 The proprotein convertases (PCs) furin, PC5/6, and PACE4 exhibit unique and/or complementary fun

7 a proprotein convertase (PC), furin, and/or PC5/6, followed by the exposure of an N-terminal cross-n

8 from wild-type or hepatocyte-specific furin, PC5/6, or complete PACE4 knock-out mice suggested that t

9 prises nine members: PC1/3, PC2, furin, PC4, PC5/6, PACE4, PC7, SKI-1/S1P, and PCSK9.

10 Several PCs, including furin, PC5/6, paired basic amino acid-cleaving enzyme 4, and PC

11 sequence is susceptible to furin and also to PC5/6, PC7 and PACE4.

12 the relative efficiency of furin, PC2, PC4, PC5/6, PC7, and PACE4 in cleaving over 100 decapeptide s

13 st cleavage site is susceptible to furin and PC5/6, whereas the second sequence is susceptible to fur

14 convertases, such as PC1/3, PC4, PACE4, and PC5/6, with similar potency, whereas PC2, PC7, and tryps

15 C is first cleaved by the convertases furin, PC5/6A, and PACE4.

16 etermine whether RPTPmu cleavage depended on PC5 (a subtilisin/kexin like endoprotease present in end

17 These kex2/subtilisin-like enzymes, PC5 and furin, are members of the proprotein convertase

18 Coexpression of PC5 and MIS in transfected mammalian cells results in ef

19 bserved remarkably complementary patterns of PC5 and PACE4 expression.

20 These results suggest that both PC5 and PACE4 may be involved in neuropeptide precursor

21 rlapping expression patterns suggesting that PC5 and PACE4 may process distinct sets of proprotein su

22 ned that two recently identified PC members, PC5 and PACE4, are expressed prenatally in spatial and t

23 tive abundance of mRNA species encoding 7B2, PC5 and PAM were unchanged after treatment with omeprazo

24 PAM), the prohormone convertases PC1/3, PC2, PC5 and the PC2 chaperone 7B2 were localized to rat antr

25 (PC4), rotation of the peripapillary sclera (PC5), and forces through the peripapillary sclera (PC3).

26 ping nervous system, generally distinct from PC5, and including a uniquely high level of expression i

27 Widely expressed PCs (furin, PACE4, PC5, and PC7) all exhibited a similar expression profile

28 It is clear that PC1 and PC5 are extensively colocalized with CCK and could be pa

29 To evaluate whether PC1 and PC5 are possible candidates for the other enzymes involv

30 zymes prohormone convertase (PC) 1, PC2, and PC5 as potential candidates for these endoproteolytic cl

31 In GH4C1 cells, PC1, PC2, furin, PC5-B, and PACE4 produced both N-terminal and C-terminal

32 the prohormone convertases PC1, PC2, PACE4, PC5-B, furin, or control dynorphin together with rat pre

33 PC5, but not PACE4, cleaved RPTPmu, and RPTPmu cleavage

34 ormed RNA blot analysis to determine whether PC5 expression was affected by confluence in HUVEC.

35 re expressed in the heart and liver, whereas PC5 is expressed in the adrenal and kidney primordia.

36 These results indicate that PC5 may have an important role in mediating the cleavage

37 By midgestation (e13-e16), PC5 mRNA expression in the developing nervous system has

38 At e10, restricted PC5 mRNA expression is detected in the optic and otic ve

39 PC5 mRNA is first detected at e9 in highly restricted re

40 PC5 mRNA levels were upregulated by more than 30-fold wh

41 rocessing, the distribution of PC1, PC2, and PC5 mRNA was studied in rat brain.

42 PC1 and PC5 mRNA-positive cells were less abundant, but they wer

43 th expression plasmids coding for RPTPmu and PC5 or the closely related protease PACE4.

44 The proprotein convertases (PCs) furin, PC5, PACE4, and PC7 cleave secretory proteins after basi

45 primary hepatocytes from mice lacking furin, PC5, PACE4, or PC7 revealed that hepcidin, which limits

46 e cleaved by proprotein convertases, such as PC5, resulting in loss of activity.

47 sted OR 1.56, 95% CI 1.03-2.37), whereas the PC5 score, dominated by perfluorooctanoic acid (PFOA), w

48 In cells overexpressing PC5, the covalent homodimeric EL-EL appeared to be more

49 suggest that MIS is a natural substrate for PC5, thereby supporting a role for prohormone convertase

50 imarily in neuronal cells, whereas PACE4 and PC5 were limited to the glia of the retina and optic ner

51 with an expression plasmid encoding a mutant PC5 whose active-site serine had been mutated to alanine