ライフサイエンスコーパス: PEPD

1 PEPD binds to the proline-rich domain in p53, which inhi

2 PEPD differs from all known EGFR ligands in that it does

3 PEPD mutations also increase resurgent currents, which i

4 PEPD mutations impair Nav1.7 fast inactivation and incre

5 PEPD mutations in the putative inactivation gate have be

6 The Nav1.7 PEPD mutations are located in regions of the channel sug

7 enotype with characteristics of both IEM and PEPD and show that this mutation renders DRG and trigemi

8 These observations indicate that IEM and PEPD mutants are part of a physiological continuum that

9 ges in channel function seen in both IEM and PEPD mutations: A1632E hyperpolarizes (-7 mV) the voltag

10 patient with overlapping symptoms of IEM and PEPD was reported, displaying a shift of both activation

11 al phenotype with characteristics of IEM and PEPD, with an alanine 1632 substitution by glutamate (A1

12 ynthesized as a transmembrane precursor, but PEPD binding to EGFR can be blocked by EGF.

13 disruption of the fast-inactivated state by PEPD mutations can be more moderate than previously indi

14 In conclusion, PEPD is a ligand of EGFR and presents a novel mechanism

15 (GIPR), caveolin 2 (CAV2), and peptidase D (PEPD) (P-interaction < 0.05).

16 Here, we show that peptidase D (PEPD) binds and suppresses over half of nuclear and cyto

17 known as Xaa-Pro dipeptidase or peptidase D (PEPD), is a ubiquitously expressed cytosolic enzyme that

18 Paroxysmal extreme pain disorder (PEPD) and inherited erythromelalgia (IEM) are inherited

19 ted that a paroxysmal extreme pain disorder (PEPD) mutation in the human peripheral neuronal sodium c

20 syndrome, paroxysmal extreme pain disorder (PEPD), characterized by rectal, periocular, and perimand

21 (IEM) and paroxysmal extreme pain disorder (PEPD), enhance Nav1.7 function via distinct mechanisms.

22 Paroxysmal extreme pain disorder (PEPD), previously known as familial rectal pain (FRP, OM

23 (IEM) and paroxysmal extreme pain disorder (PEPD).

24 (IEM) and paroxysmal extreme pain disorder (PEPD).

25 neuropathy paroxysmal extreme pain disorder (PEPD).

26 nherited "paroxysmal extreme pain disorder" (PEPD) differs in its clinical picture and affects proxim

27 al and pro-proliferation activities of EGFR, PEPD stimulates DNA synthesis.

28 Eliminating PEPD causes cell death and tumor regression due to p53 a

29 doxorubicin and H2O2 each must free p53 from PEPD in order to achieve robust p53 activation, which is

30 However, PEPD mutations in the S4-S5 linker of domain 3 (D3/S4-S5

31 nt non-PEPD mutation (V1300F) and the I1461T PEPD mutation, located in the putative inactivation gate

32 In contrast to the IEM/PEPD crossover mutation A1632E, A1632T failed to slow cu

33 d their effects on gating to an adjacent non-PEPD mutation (V1300F) and the I1461T PEPD mutation, loc

34 urgent currents induces symptoms of IEM, not PEPD, in the new Nav1.7 mutation, A1632T.

35 c nor dependent on the enzymatic activity of PEPD.

36 We speculated that selective attenuation of PEPD-enhanced resurgent currents might contribute to thi

37 tant implications for the pathophysiology of PEPD.

38 se, but this also renders cells dependent on PEPD for survival, as it suppresses p53.

39 whether a mutation in Nav1.7 leads to IEM or PEPD.

40 e viral IFN-I antagonist, NS5, to prolidase (PEPD), a cellular dipeptidase implicated in primary immu

41 nctionally characterized two of the D3/S4-S5 PEPD mutations (V1298F and V1299F) and compared their ef

42 leavage of procaspase-9 at the cleavage site PEPD(315) to yield the large (p35) and small (p12) caspa

43 present in the extracellular space, but that PEPD is released from injured cells and tissues and that

44 n this article, however, we demonstrate that PEPD directly binds to and activates epidermal growth fa

45 We further show that PEPD activates EGFR only when it is present in the extra

46 93 cells expressing wild-type Nav1.7 and the PEPD mutants T1464I and M1627K, we examined the effects

47 However, the PEPD-p53 complex is critical for p53 response to stress,

48 In addition to the PEPD site, caspase-9 contains a caspase-3 cleavage site

49 We observed a similar effect with the PEPD mutation I1461T.

50 Interestingly, while all three PEPD mutations increased persistent currents, the relati

51 Thus, PEPD stores p53 for the stress response, but this also r

52 s is a characteristic normally attributed to PEPD-causing mutations.

53 t with biophysical characteristics common to PEPD (impaired fast inactivation) and IEM (hyperpolarize

54 steady-state fast inactivation often lead to PEPD.

55 nce activation, whereas mutations leading to PEPD alter fast inactivation.

56 ing in persistent inward currents similar to PEPD mutations.

57 .7 function due to mutations associated with PEPD, but not IEM, are important in I(NaR) generation, s

58 Furthermore, pain associated with PEPD, but not IEM, is alleviated by the sodium channel i

59 Mutations associated with PEPD, but not IEM, result in destabilized inactivation o

60 haracteristics more commonly associated with PEPD.

61 ty and pain hypersensitivity associated with PEPD.

62 NaR) may play a role in pain associated with PEPD.