ライフサイエンスコーパス: prohormone convertase

1 e mechanisms of proprotein processing by the prohormone convertases.

2 th the cleavage specificities of PC1 and PC2 prohormone convertases.

3 es, particularly fungal kexins and mammalian prohormone convertases.

4 nular pH and thereby inhibiting pH-sensitive prohormone convertases.

5 okaryotic and eukaryotic proteins, including prohormone-convertases.

6 A candidate endoprotease is prohormone convertase 1 (PC1) also known as PC3, a Ca2+-

7 two different prohormone-processing enzymes, prohormone convertase 1 (PC1) and carboxypeptidase E, ha

8 al inhibitory peptides for recombinant mouse prohormone convertase 1 (PC1) and PC2 and to provide inf

9 ion for the neuropeptide processing enzymes, prohormone convertase 1 (PC1) and PC2, were determined.

10 ro-TRH by the actions of the endopeptidases, prohormone convertase 1 (PC1) and PC2.

11 a product of proopiomelanocortin (POMC), and prohormone convertase 1 (PC1) in granules at the tips of

12 Prohormone convertase 1 (PC1) mutations lead to obesity

13 We have purified the mouse prohormone convertase 1 (PC1) pro-domain expressed in Es

14 ne distribution generally similar to that of prohormone convertase 1 (PC1), a peptide-processing endo

15 types may be linked to reduced expression of prohormone convertase 1 (PC1).

16 prohormone processing by the endopeptidase, prohormone convertase 1 (PC1).

17 Prohormone convertase 1 (PC1; also known as PC3) is beli

18 pressed in p-FLCs were neuroendocrine genes: prohormone convertase 1 (PCSK1); neurotensin; delta/notc

19 Purified proSAAS inhibits prohormone convertase 1 activity with an IC(50) of 590 n

20 They revealed that cholecystokinin and prohormone convertase 1 mRNA levels in cerebral cortex a

21 lve increased expression of cholecystokinin, prohormone convertase 1 or 5 mRNA.

22 had higher expression of cholecystokinin and prohormone convertase 1, 2, and 5 mRNA than male mice.

23 e ghrelin was produced by human furin, mouse prohormone convertase 1, and human prohormone convertase

24 rocesses PEN-LEN, an endogenous inhibitor of prohormone convertase 1, into products that do not inhib

25 AAS may represent an endogenous inhibitor of prohormone convertase 1.

26 have demonstrated that (a) in mouse stomach, prohormone convertase 1/3 (PC1/3) is the endoprotease re

27 growth factor 15, and unexpectedly Tgr5 and prohormone convertase 1/3 gene expression in the ileum.

28 been identified, thus far, no small-molecule prohormone convertase 1/3 or prohormone convertase 2 (PC

29 Prohormone convertases 1 (PC1) and 2 (PC2) are members o

30 te stimulating hormone, adrenocorticotropin, prohormone convertases 1 and 2 (PC1 and PC2) and the PC2

31 oproteolytically cleaved by enzymes known as prohormone convertases 1 and 2 (PC1 and PC2) to generate

32 y the action of two members of the family of prohormone convertases 1 and 2 (PC1 and PC2).

33 maturation requires proteolytic cleavage by prohormone convertases 1 and 2 (PC1 and PC2).

34 lisin-like serine endoproteases PC1 and PC2 (prohormone convertases 1 and 2), and furin.

35 evertheless, the POMC processing components, prohormone convertases 1, 2 and regulatory protein 7B2,

36 values for the related convertases PACE4 and prohormone convertase-1 (PC1) were 110 nm and 2.5 microm

37 ormone (pro-TRH) is initially cleaved by the prohormone convertase-1/3 (PC1/3) in the trans-Golgi net

38 mozygous for a deletion in the gene encoding prohormone convertase 2 (PC2) are generally healthy but

39 hermore, VHS-GAT-GFP-overexpression disrupts prohormone convertase 2 (PC2) autocatalytic cleavage, pr

40 og of the vertebrate neuroendocrine-specific Prohormone Convertase 2 (PC2) gene, and showed that amon

41 small-molecule prohormone convertase 1/3 or prohormone convertase 2 (PC2) inhibitors have been descr

42 Prohormone convertase 2 (PC2) is a member of the subtili

43 Prohormone convertase 2 (PC2) is a subtilisin-like prote

44 s two domains, a 21-kDa protein required for prohormone convertase 2 (PC2) maturation and a carboxyl-

45 Prohormone convertase 2 (PC2) plays an essential role in

46 ese enzymes are evolutionarily related, only prohormone convertase 2 (PC2) requires 7B2 for activatio

47 Here, gene-targeted mice producing defective prohormone convertase 2 (PC2) were used to examine the p

48 7B2 is required for the production of active prohormone convertase 2 (PC2), an enzyme involved in the

49 ein 7B2 has been implicated in activation of prohormone convertase 2 (PC2), an important neuroendocri

50 The serine protease prohormone convertase 2 (PC2), principally involved in t

51 involved in the biosynthesis and activity of prohormone convertase 2 (PC2).

52 educes secretogranin II (SgII) processing by prohormone convertase 2 (PC2).

53 The loss of prohormone convertase 2 alters CCK processing in specifi

54 nin levels in these brain regions shows that prohormone convertase 2 is important for cholecystokinin

55 Prohormone convertase 2 is widely co-localized with chol

56 ere measured in dissected brain regions from prohormone convertase 2 knock-out mice.

57 emale mice were more affected by the loss of prohormone convertase 2 than male mice.

58 In Drosophila melanogaster, the homolog of prohormone convertase 2, dPC2 (amontillado), is required

59 man prohormone convertase 7 but not by mouse prohormone convertase 2.

60 ith an IC(50) of 590 nM but does not inhibit prohormone convertase 2.

61 he cDNA revealed that it corresponded to the prohormone convertase-2 (PC2) gene, which is involved in

62 Prohormone convertase-2 (PC2) is the only convertase tha

63 rd CPA substrates, but after incubation with prohormone convertase 4 the resulting protein was able t

64 , whereas the latter also expresses mRNA for prohormone convertase 5, an enzyme that cleaves pro-NT i

65 in, mouse prohormone convertase 1, and human prohormone convertase 7 but not by mouse prohormone conv

66 due to an alteration in carboxypeptidase and prohormone convertase activities and that this may lead

67 t of a decrease in both carboxypeptidase and prohormone convertase activities.

68 sites cleaved by subtilisin-like proprotein/prohormone convertases and is shown to be specifically c

69 ly five contain consensus cleavage sites for prohormone convertases at both the C and N termini.

70 Prohormone convertases belonging to the subtilisin famil

71 elix or reorganize as recently proposed in a prohormone-convertase complex?

72 icity of proSAAS toward other members of the prohormone convertase family was determined.

73 y the recombinant subtilisin-like proprotein/prohormone convertase furin.

74 There is also the 5' exon of a prohormone convertase gene, possibly PACE4.

75 trate for PC5, thereby supporting a role for prohormone convertases in the activation of transforming

76 es are recognized and cleaved by one or more prohormone convertases in the first processing step to y

77 (proghrelin) into mature ghrelin in various prohormone convertase null mouse strains generated in ou

78 inal domains of PAM must undergo a series of prohormone convertase or alpha-secretase-mediated cleava

79 terized family of processing enzymes are the prohormone convertases or kexins, and these are responsi

80 protein that was previously found to inhibit prohormone convertase (PC) 1 and not PC2.

81 pointed to the subtilisin/kexin-like enzymes prohormone convertase (PC) 1, PC2, and PC5 as potential

82 icted alpha-helical loops and four potential prohormone convertase (PC) cleavage sites, was necessary

83 Among the members of the prohormone convertase (PC) family, PC2 has a unique matu

84 s complex, requiring sequential actions of a prohormone convertase (PC), carboxypeptidase H, and pept

85 Prohormone convertases (PC) 1 and 2, enzymes found prima

86 that require proteolytic processing by the "prohormone convertase" (PC) family of endoproteases.

87 nescient helix loop helix 2 (NHLH2) and the prohormone convertase PC1 (encoded by PCSK1) were reduce

88 he major precursor processing endoproteases, prohormone convertases PC1 and PC2 in Cpe(fat) mice.

89 vaccinia viruses were used to coexpress the prohormone convertases PC1, PC2, PACE4, PC5-B, furin, or

90 The prohormone convertases PC1/3 and PC2 are eukaryotic seri

91 ne alpha-amidating mono-oxygenase (PAM), the prohormone convertases PC1/3, PC2, PC5 and the PC2 chape

92 Endoproteolysis is performed by two prohormone convertases, PC1 and PC2.

93 The prohormone convertases PC2 (SPC2) and PC3/PC1 (SPC3) are

94 effect of FFAs on proinsulin processing and prohormone convertases PC2 and PC1/PC3 in MIN6 cells cul

95 for the neuroendocrine subtilisin/kexin-like prohormone convertases, PC2 (SPC2) and PC1/3 (SPC3).

96 PP was incubated (0.5-16 h) with recombinant prohormone convertases, PC2 or PC3 at appropriate condit

97 The prohormone convertases (PCs) are an evolutionarily ancie

98 Prohormone convertases (PCs) are endoproteases that proc

99 The prohormone convertases (PCs) are serine proteinases resp

100 The prohormone convertases (PCs) are synthesized as zymogens

101 The subtilisin-like prohormone convertases (PCs) contain an essential downst

102 ng enzymes: carboxypeptidase E (CPE) and the prohormone convertases (PCs) PC1/3 and PC2.

103 rent posttranslational modification enzymes, prohormone convertases (PCs), carboxypeptidase E, and pe

104 by members of the subtilisin-like family of prohormone convertases (PCs), which are either soluble o

105 f subtilisin-like endoproteases known as the prohormone convertases (PCs).

106 The prohormone convertases play important roles in the matur

107 is processed in parallel by subtilisin-like prohormone convertases prior to secretion.

108 The prohormone convertase SPC2 (PC2) participates in the pro

109 ) junction, catalyzed by the subtilisin-like prohormone convertases SPC3 (PC1/PC3) and SPC2 (PC2), re

110 lated secretory cells containing appropriate prohormone convertases, the hProCpepGFP construct underg

111 ity of S1P(983)-C differs from that of furin/prohormone convertases, two related proteases, in its mo

112 le catecholamines, and an optimal pH for the prohormone convertases which cleave hormone precursors.

113 e same cells express phc2, a neural specific prohormone convertase, which suggests that they form an

114 ibasic amino acid residues whose cleavage by prohormone convertases would give rise to additional pep