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Volumn 48, Issue 3, 2015, Pages 731-743

Tomoregulin (TMEFF2) Binds Alzheimer's Disease Amyloid-β (Aβ) Oligomer and AβPP and Protects Neurons from Aβ-Induced Toxicity

Author keywords

Alzheimer's disease; amyloid; binding; neuroprotection; neurotoxicity; tomoregulin

Indexed keywords

3 [(3 CHOLAMIDOPROPYL)DIMETHYLAMMONIO] 2 HYDROXY 1 PROPANESULFONIC ACID; ALPHA SECRETASE; AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; MEMBRANE PROTEIN; TOMOREGULIN; UNCLASSIFIED DRUG; RECOMBINANT PROTEIN; SECRETASE; TMEFF2 PROTEIN, HUMAN; TMEFF2 PROTEIN, MOUSE; TUMOR PROTEIN;

EID: 84943752604     PISSN: 13872877     EISSN: 18758908     Source Type: Journal    
DOI: 10.3233/JAD-150318     Document Type: Article
Times cited : (20)

References (46)
  • 1
    • 84879829589 scopus 로고    scopus 로고
    • Biochemistry of Amyloid beta-Protein and Amyloid Deposits in Alzheimer Disease
    • Masters CL, Selkoe DJ (2012) Biochemistry of Amyloid beta-Protein and Amyloid Deposits in Alzheimer Disease. Cold Spring Harb Perspect Med 2, a006262.
    • (2012) Cold Spring Harb Perspect Med , vol.2 , pp. a006262
    • Masters, C.L.1    Selkoe, D.J.2
  • 2
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • Caughey B, Lansbury PT (2003) Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders. Annu Rev Neurosci 26, 267-298.
    • (2003) Annu Rev Neurosci , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 3
    • 34249860495 scopus 로고    scopus 로고
    • Small molecule inhibitors of aggregation indicate that amyloid beta oligomerization and fibrillization pathways are independent and distinct
    • Necula M, Kayed R, Milton S, Glabe CG (2007) Small molecule inhibitors of aggregation indicate that amyloid beta oligomerization and fibrillization pathways are independent and distinct. J Biol Chem 282, 10311-10324.
    • (2007) J Biol Chem , vol.282 , pp. 10311-10324
    • Necula, M.1    Kayed, R.2    Milton, S.3    Glabe, C.G.4
  • 4
    • 57649148788 scopus 로고    scopus 로고
    • Structural classification of toxic amyloid oligomers
    • Glabe CG (2008) Structural classification of toxic amyloid oligomers. J Biol Chem 283, 29639-29643.
    • (2008) J Biol Chem , vol.283 , pp. 29639-29643
    • Glabe, C.G.1
  • 8
  • 9
    • 0037200117 scopus 로고    scopus 로고
    • Oligomeric and fibrillar species of amyloid-beta peptides differentially affect neuronal viability
    • Dahlgren KN, Manelli AM, Stine WB Jr, Baker LK, Krafft GA, LaDu MJ (2002) Oligomeric and fibrillar species of amyloid-beta peptides differentially affect neuronal viability. J Biol Chem 277, 32046-32053.
    • (2002) J Biol Chem , vol.277 , pp. 32046-32053
    • Dahlgren, K.N.1    Manelli, A.M.2    Stine, W.B.3    Baker, L.K.4    Krafft, G.A.5    LaDu, M.J.6
  • 11
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy J, Selkoe DJ (2002) The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics. Science 297, 353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 12
    • 0034609516 scopus 로고    scopus 로고
    • The oligomerization of amyloid beta-protein begins intracellularly in cells derived from human brain
    • Walsh DM, Tseng BP, Rydel RE, Podlisny MB, Selkoe DJ (2000) The oligomerization of amyloid beta-protein begins intracellularly in cells derived from human brain. Biochemistry 39, 10831-10839.
    • (2000) Biochemistry , vol.39 , pp. 10831-10839
    • Walsh, D.M.1    Tseng, B.P.2    Rydel, R.E.3    Podlisny, M.B.4    Selkoe, D.J.5
  • 13
    • 30344448543 scopus 로고    scopus 로고
    • A dynamic relationship between intracellular and extracellular pools of Abeta
    • Oddo S, Caccamo A, Smith IF, Green KN, LaFerlaFM(2006) A dynamic relationship between intracellular and extracellular pools of Abeta. Am J Pathol 168, 184-194.
    • (2006) Am J Pathol , vol.168 , pp. 184-194
    • Oddo, S.1    Caccamo, A.2    Smith, I.F.3    Green, K.N.4    LaFerla, F.M.5
  • 14
    • 0033590080 scopus 로고    scopus 로고
    • A novel epidermal growth factor-like molecule containing two follistatin modules stimulates tyrosine phosphorylation of erbB-4 in MKN28 gastric cancer cells
    • Uchida T, Wada K, Akamatsu T, Yonezawa M, Noguchi H, Mizoguchi A, Kasuga M, Sakamoto C (1999) A novel epidermal growth factor-like molecule containing two follistatin modules stimulates tyrosine phosphorylation of erbB-4 in MKN28 gastric cancer cells. Biochem Biophys Res Commun 266, 593-602.
    • (1999) Biochem Biophys Res Commun , vol.266 , pp. 593-602
    • Uchida, T.1    Wada, K.2    Akamatsu, T.3    Yonezawa, M.4    Noguchi, H.5    Mizoguchi, A.6    Kasuga, M.7    Sakamoto, C.8
  • 15
    • 38049186998 scopus 로고    scopus 로고
    • Phorbol ester-induced shedding of the prostate cancer marker transmembrane protein with epidermal growth factor and two follistatin motifs 2 is mediated by the disintegrin and metalloproteinase-17
    • Ali N, Knauper V (2007) Phorbol ester-induced shedding of the prostate cancer marker transmembrane protein with epidermal growth factor and two follistatin motifs 2 is mediated by the disintegrin and metalloproteinase-17. J Biol Chem 282, 37378-37388.
    • (2007) J Biol Chem , vol.282 , pp. 37378-37388
    • Ali, N.1    Knauper, V.2
  • 17
    • 33646489010 scopus 로고    scopus 로고
    • Expression profiling the developing mammalian enteric nervous system identifies marker and candidate Hirschsprung disease genes
    • Heanue TA, Pachnis V (2006) Expression profiling the developing mammalian enteric nervous system identifies marker and candidate Hirschsprung disease genes. Proc Natl Acad Sci U S A 103, 6919-6924.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 6919-6924
    • Heanue, T.A.1    Pachnis, V.2
  • 18
    • 77956368181 scopus 로고    scopus 로고
    • Tomoregulin internalization confers selective cytotoxicity of immunotoxins on prostate cancer cells
    • Zhao XY, Liu HL, Liu B, Willuda J, Siemeister G, Mahmoudi M, Dinter H (2008) Tomoregulin internalization confers selective cytotoxicity of immunotoxins on prostate cancer cells. Transl Oncol 1, 102-109.
    • (2008) Transl Oncol , vol.1 , pp. 102-109
    • Zhao, X.Y.1    Liu, H.L.2    Liu, B.3    Willuda, J.4    Siemeister, G.5    Mahmoudi, M.6    Dinter, H.7
  • 19
    • 0035977710 scopus 로고    scopus 로고
    • Expression of TMEFF1 mRNA in the mouse central nervous system: Precise examination and comparative studies of TMEFF1 and TMEFF2
    • Kanemoto N, Horie M, Omori K, Nishino N, Kondo M, Noguchi K, Tanigami A (2001) Expression of TMEFF1 mRNA in the mouse central nervous system: Precise examination and comparative studies of TMEFF1 and TMEFF2. Brain Res Mol Brain Res 86, 48-55.
    • (2001) Brain Res Mol Brain Res , vol.86 , pp. 48-55
    • Kanemoto, N.1    Horie, M.2    Omori, K.3    Nishino, N.4    Kondo, M.5    Noguchi, K.6    Tanigami, A.7
  • 22
    • 10644259516 scopus 로고    scopus 로고
    • Apolipoprotein e isoforms and apolipoprotein AI protect from amyloid precursor protein carboxy terminal fragment-associated cytotoxicity
    • Maezawa I, Jin LW, Woltjer RL, Maeda N, Martin GM, Montine TJ, Montine KS (2004) Apolipoprotein E isoforms and apolipoprotein AI protect from amyloid precursor protein carboxy terminal fragment-associated cytotoxicity. J Neurochem 91, 1312-1321.
    • (2004) J Neurochem , vol.91 , pp. 1312-1321
    • Maezawa, I.1    Jin, L.W.2    Woltjer, R.L.3    Maeda, N.4    Martin, G.M.5    Montine, T.J.6    Montine, K.S.7
  • 24
    • 1242316263 scopus 로고    scopus 로고
    • Intracellular accumulation of amyloidogenic fragments of amyloid-beta precursor protein in neurons with Niemann-Pick type C defects is associated with endosomal abnormalities
    • Jin LW, Shie FS, Maezawa I, Vincent I, Bird T (2004) Intracellular accumulation of amyloidogenic fragments of amyloid-beta precursor protein in neurons with Niemann-Pick type C defects is associated with endosomal abnormalities. Am J Pathol 164, 975-985.
    • (2004) Am J Pathol , vol.164 , pp. 975-985
    • Jin, L.W.1    Shie, F.S.2    Maezawa, I.3    Vincent, I.4    Bird, T.5
  • 25
    • 33749521100 scopus 로고    scopus 로고
    • Intraneuronal beta-amyloid aggregates, neurodegeneration, and neuron loss in transgenic mice with five familial Alzheimer's disease mutations: Potential factors in amyloid plaque formation
    • Oakley H, Cole SL, Logan S, Maus E, Shao P, Craft J, Guillozet-Bongaarts A, Ohno M, Disterhoft J, Van Eldik L, Berry R, Vassar R (2006) Intraneuronal beta-amyloid aggregates, neurodegeneration, and neuron loss in transgenic mice with five familial Alzheimer's disease mutations: Potential factors in amyloid plaque formation. J Neurosci 26, 10129-10140.
    • (2006) J Neurosci , vol.26 , pp. 10129-10140
    • Oakley, H.1    Cole, S.L.2    Logan, S.3    Maus, E.4    Shao, P.5    Craft, J.6    Guillozet-Bongaarts, A.7    Ohno, M.8    Disterhoft, J.9    Van Eldik, L.10    Berry, R.11    Vassar, R.12
  • 28
    • 42549169394 scopus 로고    scopus 로고
    • A broadly neuroprotective derivative of curcumin
    • Liu Y, Dargusch R, Maher P, Schubert D (2008) A broadly neuroprotective derivative of curcumin. J Neurochem 105, 1336-1345.
    • (2008) J Neurochem , vol.105 , pp. 1336-1345
    • Liu, Y.1    Dargusch, R.2    Maher, P.3    Schubert, D.4
  • 30
    • 84869493355 scopus 로고    scopus 로고
    • Intraneuronal Abeta accumulation and neurodegeneration: Lessons from transgenic models
    • Wirths O, Bayer TA(2012) Intraneuronal Abeta accumulation and neurodegeneration: Lessons from transgenic models. Life Sci 91, 1148-1152.
    • (2012) Life Sci , vol.91 , pp. 1148-1152
    • Wirths, O.1    Bayer, T.A.2
  • 31
    • 84869506753 scopus 로고    scopus 로고
    • Critical role of intraneuronal Abeta in Alzheimer's disease: Technical challenges in studying intracellular Abeta
    • Gouras GK, Willen K, Tampellini D (2012) Critical role of intraneuronal Abeta in Alzheimer's disease: Technical challenges in studying intracellular Abeta. Life Sci 91, 1153-1158.
    • (2012) Life Sci , vol.91 , pp. 1153-1158
    • Gouras, G.K.1    Willen, K.2    Tampellini, D.3
  • 32
    • 18844444191 scopus 로고    scopus 로고
    • Role of glutathione in intracellular amyloid-alpha precursor protein/carboxy-terminal fragment aggregation and associated cytotoxicity
    • Woltjer RL, Nghiem W, Maezawa I, Milatovic D, Vaisar T, Montine KS, Montine TJ (2005) Role of glutathione in intracellular amyloid-alpha precursor protein/carboxy-terminal fragment aggregation and associated cytotoxicity. J Neurochem 93, 1047-1056.
    • (2005) J Neurochem , vol.93 , pp. 1047-1056
    • Woltjer, R.L.1    Nghiem, W.2    Maezawa, I.3    Milatovic, D.4    Vaisar, T.5    Montine, K.S.6    Montine, T.J.7
  • 33
    • 33745107526 scopus 로고    scopus 로고
    • Tomoregulin-2 is found extensively in plaques in Alzheimer's disease brain
    • Siegel DA, Davies P, Dobrenis K, Huang M (2006) Tomoregulin-2 is found extensively in plaques in Alzheimer's disease brain. J Neurochem 98, 34-44.
    • (2006) J Neurochem , vol.98 , pp. 34-44
    • Siegel, D.A.1    Davies, P.2    Dobrenis, K.3    Huang, M.4
  • 34
    • 0035986904 scopus 로고    scopus 로고
    • Ectopic dendrite initiation:CNSpathogenesis as a model ofCNSdevelopment
    • Siegel DA, Huang MK, Becker SF (2002) Ectopic dendrite initiation:CNSpathogenesis as a model ofCNSdevelopment. Int J Dev Neurosci 20, 373-389.
    • (2002) Int J Dev Neurosci , vol.20 , pp. 373-389
    • Siegel, D.A.1    Huang, M.K.2    Becker, S.F.3
  • 37
    • 0033812585 scopus 로고    scopus 로고
    • Identifying conformational changes with site-directed spin labeling
    • Hubbell WL, Cafiso DS, Altenbach C (2000) Identifying conformational changes with site-directed spin labeling. Nat Struct Biol 7, 735-739.
    • (2000) Nat Struct Biol , vol.7 , pp. 735-739
    • Hubbell, W.L.1    Cafiso, D.S.2    Altenbach, C.3
  • 38
    • 1842326248 scopus 로고    scopus 로고
    • Conformation of T4 lysozyme in solution. Hinge-bending motion and the substrate-induced conformational transition studied by site-directed spin labeling
    • McHaourab HS, Oh KJ, Fang CJ, Hubbell WL (1997) Conformation of T4 lysozyme in solution. Hinge-bending motion and the substrate-induced conformational transition studied by site-directed spin labeling. Biochemistry 36, 307-316.
    • (1997) Biochemistry , vol.36 , pp. 307-316
    • McHaourab, H.S.1    Oh, K.J.2    Fang, C.J.3    Hubbell, W.L.4
  • 40
    • 0034006944 scopus 로고    scopus 로고
    • Beta-Amyloid(1-42) binds to alpha7 nicotinic acetylcholine receptor with high affinity. Implications for Alzheimer's disease pathology
    • Wang HY, Lee DH, D'Andrea MR, Peterson PA, Shank RP, Reitz AB (2000) beta-Amyloid(1-42) binds to alpha7 nicotinic acetylcholine receptor with high affinity. Implications for Alzheimer's disease pathology. J Biol Chem 275, 5626-5632.
    • (2000) J Biol Chem , vol.275 , pp. 5626-5632
    • Wang, H.Y.1    Lee, D.H.2    D'Andrea, M.R.3    Peterson, P.A.4    Shank, R.P.5    Reitz, A.B.6
  • 41
    • 61349201380 scopus 로고    scopus 로고
    • Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers
    • Lauren J, Gimbel DA, Nygaard HB, Gilbert JW, Strittmatter SM (2009) Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers. Nature 457, 1128-1132.
    • (2009) Nature , vol.457 , pp. 1128-1132
    • Lauren, J.1    Gimbel, D.A.2    Nygaard, H.B.3    Gilbert, J.W.4    Strittmatter, S.M.5
  • 44
    • 79955527735 scopus 로고    scopus 로고
    • The tumor suppressor activity of the transmembrane protein with epidermal growth factor and two follistatin motifs 2 (TMEFF2) correlates with its ability to modulate sarcosine levels
    • Chen X, Overcash R, Green T, Hoffman D, Asch AS, Ruiz-Echevarria MJ (2011) The tumor suppressor activity of the transmembrane protein with epidermal growth factor and two follistatin motifs 2 (TMEFF2) correlates with its ability to modulate sarcosine levels. J Biol Chem 286, 16091-16100.
    • (2011) J Biol Chem , vol.286 , pp. 16091-16100
    • Chen, X.1    Overcash, R.2    Green, T.3    Hoffman, D.4    Asch, A.S.5    Ruiz-Echevarria, M.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.