메뉴 건너뛰기




Volumn 10, Issue 1, 2009, Pages 94-100

Neprilysin gene expression requires binding of the amyloid precursor protein intracellular domain to its promoter: Implications for Alzheimer disease

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; GAMMA SECRETASE INHIBITOR; HISTONE DEACETYLASE INHIBITOR; L 685458; MEMBRANE METALLOENDOPEPTIDASE; TRICHOSTATIN A; UNCLASSIFIED DRUG; VALPROIC ACID;

EID: 58049089518     PISSN: 1469221X     EISSN: 14693178     Source Type: Journal    
DOI: 10.1038/embor.2008.222     Document Type: Article
Times cited : (144)

References (32)
  • 1
    • 35348948499 scopus 로고    scopus 로고
    • Lack of hepatocellular CD10 along bile canaliculi is physiologic in early childhood and persistent in Alagille syndrome
    • Byrne JA, Meara NJ, Rayner AC, Thompson RJ, Knisely AS (2007) Lack of hepatocellular CD10 along bile canaliculi is physiologic in early childhood and persistent in Alagille syndrome. Lab Invest 87 1138-1148
    • (2007) Lab Invest , vol.87 , pp. 1138-1148
    • Byrne, J.A.1    Meara, N.J.2    Rayner, A.C.3    Thompson, R.J.4    Knisely, A.S.5
  • 2
    • 0035816661 scopus 로고    scopus 로고
    • A transcriptionally active complex of APP with Fe65 and histone acetyltransferase Tip60
    • Cao X, Südhof TC (2001) A transcriptionally active complex of APP with Fe65 and histone acetyltransferase Tip60. Science 293: 115-120
    • (2001) Science , vol.293 , pp. 115-120
    • Cao, X.1    Südhof, T.C.2
  • 3
    • 0036077536 scopus 로고    scopus 로고
    • β-Amyloid catabolism: Roles for neprilysin (NEP) and other metallopeptidases?
    • Carson JA, Turner AJ (2002) β-Amyloid catabolism: Roles for neprilysin (NEP) and other metallopeptidases? J Neurochem 81: 1-8
    • (2002) J Neurochem , vol.81 , pp. 1-8
    • Carson, J.A.1    Turner, A.J.2
  • 4
    • 33846807664 scopus 로고    scopus 로고
    • Chen AC, Selkoe DJ (2007) Response to: Pardossi-Piquard et al, 'Presenilin-dependent transcriptional control of the Aβ-degrading enzyme neprilysin by intracellular domains of βAPP and APLP'. Neuron 53: 479-483
    • Chen AC, Selkoe DJ (2007) Response to: Pardossi-Piquard et al, 'Presenilin-dependent transcriptional control of the Aβ-degrading enzyme neprilysin by intracellular domains of βAPP and APLP'. Neuron 53: 479-483
  • 5
    • 34548515503 scopus 로고    scopus 로고
    • Gleevec increases levels of the amyloid precursor protein intracellular domain and of the amyloid-beta degrading enzyme neprilysin
    • Eisele YS, Baumann M, Klebl B, Nordhammer C, Jucker M, Kilger E (2007) Gleevec increases levels of the amyloid precursor protein intracellular domain and of the amyloid-beta degrading enzyme neprilysin. Mol Biol Cell 18: 3591-3600
    • (2007) Mol Biol Cell , vol.18 , pp. 3591-3600
    • Eisele, Y.S.1    Baumann, M.2    Klebl, B.3    Nordhammer, C.4    Jucker, M.5    Kilger, E.6
  • 6
    • 34248523169 scopus 로고    scopus 로고
    • Recovery of learning and memory is associated with chromatin remodelling
    • Fischer A, Sananbenesi F, Wang X, Dobbin M, Tsai LH (2007) Recovery of learning and memory is associated with chromatin remodelling. Nature 447: 178-182
    • (2007) Nature , vol.447 , pp. 178-182
    • Fischer, A.1    Sananbenesi, F.2    Wang, X.3    Dobbin, M.4    Tsai, L.H.5
  • 7
    • 34547240466 scopus 로고    scopus 로고
    • Effects of hypoxia and oxidative stress on expression of neprilysin in human neuroblastoma cells and rat cortical neurones and astrocytes
    • Fisk L, Nalivaeva NN, Boyle JP, Peers CS, Turner AJ (2007) Effects of hypoxia and oxidative stress on expression of neprilysin in human neuroblastoma cells and rat cortical neurones and astrocytes. Neurochem Res 32: 1741-1748
    • (2007) Neurochem Res , vol.32 , pp. 1741-1748
    • Fisk, L.1    Nalivaeva, N.N.2    Boyle, J.P.3    Peers, C.S.4    Turner, A.J.5
  • 9
    • 18244383806 scopus 로고    scopus 로고
    • Valproic acid defines a novel class of HDAC inhibitors inducing differentiation of transformed cells
    • Göttlicher M et al (2001) Valproic acid defines a novel class of HDAC inhibitors inducing differentiation of transformed cells. EMBO J 20: 6969-6978
    • (2001) EMBO J , vol.20 , pp. 6969-6978
    • Göttlicher, M.1
  • 10
    • 21844431659 scopus 로고    scopus 로고
    • Etiology of sporadic Alzheimer's disease: Somatostatin, neprilysin, and amyloid beta peptide
    • Hama E, Saido TC (2005) Etiology of sporadic Alzheimer's disease: somatostatin, neprilysin, and amyloid beta peptide. Med Hypotheses 65: 498-500
    • (2005) Med Hypotheses , vol.65 , pp. 498-500
    • Hama, E.1    Saido, T.C.2
  • 12
    • 42149188846 scopus 로고    scopus 로고
    • Neprilysin and amyloid β-peptide degradation
    • Hersh LB, Rodgers DW (2008) Neprilysin and amyloid β-peptide degradation. Curr Alzheimer Res 5: 225-231
    • (2008) Curr Alzheimer Res , vol.5 , pp. 225-231
    • Hersh, L.B.1    Rodgers, D.W.2
  • 13
    • 0029010556 scopus 로고
    • Analysis of the human CD10/neutral endopeptidase promoter region: Two separate regulatory elements
    • Ishimaru F, Shipp MA (1995) Analysis of the human CD10/neutral endopeptidase promoter region: Two separate regulatory elements. Blood 85: 3199-3207
    • (1995) Blood , vol.85 , pp. 3199-3207
    • Ishimaru, F.1    Shipp, M.A.2
  • 14
    • 47249142795 scopus 로고    scopus 로고
    • Enhanced clearance of Aβ in brain by sustaining the plasmin proteolysis cascade
    • Jacobsen JS et al (2008) Enhanced clearance of Aβ in brain by sustaining the plasmin proteolysis cascade. Proc Natl Acad Sci USA 105: 8754-8759
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 8754-8759
    • Jacobsen, J.S.1
  • 15
    • 0035955693 scopus 로고    scopus 로고
    • The intracellular domain of the β-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner
    • Kimberly WT, Zheng JB, Guénette SY, Selkoe DJ (2001) The intracellular domain of the β-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner. J Biol Chem 276: 40288-40292
    • (2001) J Biol Chem , vol.276 , pp. 40288-40292
    • Kimberly, W.T.1    Zheng, J.B.2    Guénette, S.Y.3    Selkoe, D.J.4
  • 17
    • 33645891431 scopus 로고    scopus 로고
    • APPε, the ε-secretase-derived N-terminal product of the β-amyloid precursor protein, behaves as a type I protein and undergoes α-, β-, and γ-secretase cleavages
    • Lefranc-Jullien S, Sunyach C, Checler F (2006) APPε, the ε-secretase-derived N-terminal product of the β-amyloid precursor protein, behaves as a type I protein and undergoes α-, β-, and γ-secretase cleavages. J Neurochem 97: 807-817
    • (2006) J Neurochem , vol.97 , pp. 807-817
    • Lefranc-Jullien, S.1    Sunyach, C.2    Checler, F.3
  • 18
    • 0028906255 scopus 로고
    • Tissue-specific expression of rat neutral endopeptidase (neprilysin) mRNAs
    • Li C, Booze RM, Hersh LB (1995) Tissue-specific expression of rat neutral endopeptidase (neprilysin) mRNAs. J Biol Chem 270: 5723-5728
    • (1995) J Biol Chem , vol.270 , pp. 5723-5728
    • Li, C.1    Booze, R.M.2    Hersh, L.B.3
  • 21
  • 22
    • 0031889217 scopus 로고    scopus 로고
    • Neutral endopeptidase 24.11 loss in metastatic human prostate cancer contributes to androgen-independent progression
    • Papandreou CN et al (1998) Neutral endopeptidase 24.11 loss in metastatic human prostate cancer contributes to androgen-independent progression. Nat Med 4: 50-57
    • (1998) Nat Med , vol.4 , pp. 50-57
    • Papandreou, C.N.1
  • 23
    • 20444398562 scopus 로고    scopus 로고
    • Presenilin-dependent transcriptional control of the Aβ-degrading enzyme neprilysin by intracellular domains of βAPP and APLP
    • Pardossi-Piquard R et al (2005) Presenilin-dependent transcriptional control of the Aβ-degrading enzyme neprilysin by intracellular domains of βAPP and APLP. Neuron 46: 541-554
    • (2005) Neuron , vol.46 , pp. 541-554
    • Pardossi-Piquard, R.1
  • 24
    • 27744487691 scopus 로고    scopus 로고
    • Valproate: A simple chemical with so much to offer
    • Peterson GM, Naunton M (2005) Valproate: A simple chemical with so much to offer. J Clin Pharm Ther 30: 417-421
    • (2005) J Clin Pharm Ther , vol.30 , pp. 417-421
    • Peterson, G.M.1    Naunton, M.2
  • 25
    • 37249048769 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase activity promotes invasion of human cancer cells through activation of urokinase plasminogen activator
    • Pulukuri SM, Gorantla B, Rao JS (2007) Inhibition of histone deacetylase activity promotes invasion of human cancer cells through activation of urokinase plasminogen activator. J Biol Chem 282: 35594-35603
    • (2007) J Biol Chem , vol.282 , pp. 35594-35603
    • Pulukuri, S.M.1    Gorantla, B.2    Rao, J.S.3
  • 26
    • 0035109068 scopus 로고    scopus 로고
    • Treatment of the agitation of late-life psychosis and Alzheimer's disease
    • Salzman C (2001) Treatment of the agitation of late-life psychosis and Alzheimer's disease. Eur Psychiatry 16: 25s-28s
    • (2001) Eur Psychiatry , vol.16
    • Salzman, C.1
  • 27
  • 29
    • 33745954388 scopus 로고    scopus 로고
    • Methylation of neutral endopeptidase 24.11 promoter in rat hepatocellular carcinoma
    • Uematsu F, Takahashi M, Yoshida M, Igarashi M, Nakae D (2006) Methylation of neutral endopeptidase 24.11 promoter in rat hepatocellular carcinoma. Cancer Sci 97: 611-617
    • (2006) Cancer Sci , vol.97 , pp. 611-617
    • Uematsu, F.1    Takahashi, M.2    Yoshida, M.3    Igarashi, M.4    Nakae, D.5
  • 31
    • 0033397841 scopus 로고    scopus 로고
    • Preparation and characterisation of the antibodies against acetylated isoforms of core histones
    • White D, Belyaev ND, Turner BM (1999) Preparation and characterisation of the antibodies against acetylated isoforms of core histones. Methods 19: 417-424
    • (1999) Methods , vol.19 , pp. 417-424
    • White, D.1    Belyaev, N.D.2    Turner, B.M.3
  • 32
    • 34347364706 scopus 로고    scopus 로고
    • Widespread disruption of repressor element-1 silencing transcription factor/neuron-restrictive silencer factor occupancy at its target genes in Huntington's disease
    • Zuccato C et al (2007) Widespread disruption of repressor element-1 silencing transcription factor/neuron-restrictive silencer factor occupancy at its target genes in Huntington's disease. J Neurosci 27: 6972-6983
    • (2007) J Neurosci , vol.27 , pp. 6972-6983
    • Zuccato, C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.