ライフサイエンスコーパス: procathepsin

1 , we have followed the fate of pulse-labeled procathepsin B (ProB, a lysosomal proenyzme) after postp

2 TNFalpha], and IL-6), and catabolic enzymes (procathepsin B and neutrophil elastase) were measured in

3 Therefore, ARF1-dependent trafficking of procathepsin B and the maturation of autophagosomes resu

4 Furthermore, procathepsin B could interact with the annexin II tetram

5 Secretion of the cysteine protease procathepsin B from breast fibroblasts may have physiolo

6 We have confirmed that recombinant human procathepsin B interacts with p11 as well as with the an

7 d exocytosis in parallel with insulin, while procathepsin B is efficiently converted to the mature fo

8 We found that procathepsin B is enriched in Golgi-containing microsome

9 ation-dependent MPRs, the modest fraction of procathepsin B normally remaining within mature secretor

10 tetramer can serve as a binding protein for procathepsin B on the surface of tumor cells, an interac

11 (2), and beta(1) integrin subunits prevented procathepsin B secretion from fibroblasts grown on colla

12 In addition, procathepsin B secretion was induced when cells were pla

13 IL-1beta, TNFalpha, IL-6, procathepsin B, and neutrophil elastase concentrations i

14 sion and secretion of cathepsin B, primarily procathepsin B, was induced by growth on collagen I gels

15 caerulein treatment increased processing of procathepsin B, whereas a known ARF inhibitor brefeldin

16 as a significant export route for lysosomal procathepsin B.

17 screen for proteins that interact with human procathepsin B.

18 r distribution of the cathepsin B precursor, procathepsin B.

19 iminishing the stimulus-dependent release of procathepsin B.

20 rocathepsin K is similar to that observed in procathepsins B and L despite differences in length and

21 int of human cathepsin D was engineered into procathepsin D according to known specificity requiremen

22 oved 6 residues toward the amino terminus of procathepsin D and expressed in Escherichia coli.

23 r the previously described hypersecretion of procathepsin D induced by wortmannin.

24 ot analyses revealed that whereas the 51-kDa procathepsin D is recruited to phagosomes, it is not pro

25 Human procathepsin D was expressed in a baculovirus system to

26 mediated through coassociation of VKORC1v2, procathepsin D, and vIL-6 with components of the ER-asso

27 ER-transiting, preproteolytically processed procathepsin D.

28 and lysosomal targeting of newly synthesized procathepsin D.

29 Regulation of human and mouse procathepsin E gene expression was shown not to be influ

30 Thus the extent to which the procathepsin E gene is expressed in a particular cell ty

31 Quantitation of procathepsin E mRNA by LightCyclertrade mark technology

32 [Ser139,Ala163]Procathepsin K (containing mutation C139S,S163A) failed

33 We have determined the structure of human procathepsin K at 2.8 A resolution.

34 The structure of procathepsin K contributes to an understanding of the mo

35 [Ser139,Ala163]Procathepsin K could be fully processed to mature enzyme

36 yme by including one equivalent of wild-type procathepsin K in the activation mixture.

37 It is presumed that the activation of procathepsin K in vivo occurs in the bone resorption pit

38 The fold of the propeptide of procathepsin K is similar to that observed in procatheps

39 Although procathepsin K is stable and readily detected, the activ

40 structure of the mature enzyme domain within procathepsin K is virtually identical to that of mature

41 Spontaneous in vitro activation of procathepsin K occurred at pH 4 and was catalyzed by exo

42 ts indicated that in vitro activation of the procathepsin K was an autocatalytic process.

43 tures secreted mature cathepsin K as well as procathepsin K, and expressed active cathepsin K in cyto

44 ween the propeptide and the mature enzyme of procathepsin K.

45 tion of a C-terminal epitope tag sequence to procathepsin L also induced misfolding of the proenzyme,

46 at several locations on the surface of mouse procathepsin L and modeling oligosaccharide conformation

47 Whereas wild-type procathepsin L and mutants bearing carbohydrate at Asn-1

48 biting sequence near the N terminus of mouse procathepsin L can result in glycosylation of a normally

49 and transport kinetics of recombinant human procathepsin L containing one, two, or three glycosylati

50 refore conclude that the carboxy terminus of procathepsin L contains a sequence essential for its sec

51 gged protein did not compete with endogenous procathepsin L for targeting to lysosomes.

52 High-level transient expression of human procathepsin L in mouse NIH 3T3 cells results in the sec

53 At the same time, the endogenous mouse procathepsin L in these nontransformed cells is found in

54 uration was not associated with mutations in procathepsin L mRNA, was not complemented by procathepsi

55 But the procathepsin L mutant having phenylalanine in place of T

56 procathepsin L mRNA, was not complemented by procathepsin L overexpression, and did not affect the ma

57 After several hours, much procathepsin L remains as precursor in a compartment tha

58 may have identified a recognition domain in procathepsin L that is important for its interactions wi

59 Misfolded mutant mouse procathepsin L was not efficiently targeted to lysosomes

60 Similarly, epitope-tagged mouse procathepsin L was not targeted to lysosomes in homologo

61 Mutants of human procathepsin L with carboxy-terminus deletions involving

62 gnals (Asn-X-Ser/Thr) into the cDNA of human procathepsin L, a lysosomal acid protease.

63 amino acids Tyr-Asn allowed secretion of the procathepsin L, but the replacement of these two amino a

64 dent lysine-based phosphorylation signals on procathepsin L, which account for the low level of phosp

65 milar treatment did not affect processing of procathepsin L.

66 models, we have compared the itineraries of procathepsins L and B, two closely related members of th

67 TNF-alpha increased secretion of procathepsin S, but did not affect TIMP-1 and reduced TI

68 Recombinant procathepsin V is autocatalytically activated at acidic