메뉴 건너뛰기




Volumn 483, Issue 1, 2009, Pages 120-126

The sea urchin embryo: A model to study Alzheimer's beta amyloid induced toxicity

Author keywords

Amyloid beta; Animal model; Apoptosis; Fibrillar aggregates; Oligomers; Paracentrotus lividus

Indexed keywords

AMYLOID BETA PROTEIN;

EID: 60049092466     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2008.12.006     Document Type: Article
Times cited : (16)

References (43)
  • 1
    • 0021256895 scopus 로고
    • Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner G., and Wong C.W. Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem. Biophys. Res. Commun. 120 (1984) 885-890
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , pp. 885-890
    • Glenner, G.1    Wong, C.W.2
  • 3
    • 0033600274 scopus 로고    scopus 로고
    • Translating cell biology into therapeutic advances in Alzheimer's disease
    • Selkoe D.J. Translating cell biology into therapeutic advances in Alzheimer's disease. Nature 399 (1999) 23-31
    • (1999) Nature , vol.399 , pp. 23-31
    • Selkoe, D.J.1
  • 4
    • 4043088415 scopus 로고    scopus 로고
    • The role of beta amyloid in Alzheimer's disease: still a cause of everything or the only one who got caught?
    • Verdile G., Fuller S., Atwood C.S., Laws S.M., Gandy S.E., and Martins R.N. The role of beta amyloid in Alzheimer's disease: still a cause of everything or the only one who got caught?. Pharmacol. Res. 50 (2004) 397-409
    • (2004) Pharmacol. Res. , vol.50 , pp. 397-409
    • Verdile, G.1    Fuller, S.2    Atwood, C.S.3    Laws, S.M.4    Gandy, S.E.5    Martins, R.N.6
  • 5
    • 4043137921 scopus 로고    scopus 로고
    • Neurodegenerative diseases caused by protein aggregation: a phenomenon at the borderline between molecular evolution and ageing
    • Stoppini M., Andreola A., Foresti G., and Bellotti V. Neurodegenerative diseases caused by protein aggregation: a phenomenon at the borderline between molecular evolution and ageing. Pharmacol. Res. 50 (2004) 419-431
    • (2004) Pharmacol. Res. , vol.50 , pp. 419-431
    • Stoppini, M.1    Andreola, A.2    Foresti, G.3    Bellotti, V.4
  • 6
    • 24044518189 scopus 로고    scopus 로고
    • Protofibril formation of amyloid beta-protein at low pH via a non-cooperative elongation mechanism
    • Carrotta R., Manno M., Bulone D., Martorana V., and San Biagio P.L. Protofibril formation of amyloid beta-protein at low pH via a non-cooperative elongation mechanism. J. Biol. Chem. 280 (2005) 30001-30008
    • (2005) J. Biol. Chem. , vol.280 , pp. 30001-30008
    • Carrotta, R.1    Manno, M.2    Bulone, D.3    Martorana, V.4    San Biagio, P.L.5
  • 7
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh D.M., Klyubin I., Fadeeva J.V., Cullen W.K., Anwyl R., Wolfe M.S., Rowan M.J., and Selkoe D.J. Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416 (2002) 535-539
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5    Wolfe, M.S.6    Rowan, M.J.7    Selkoe, D.J.8
  • 9
    • 2542427690 scopus 로고    scopus 로고
    • Oligomers on the brain: the emerging role of soluble protein aggregates in neurodegeneration
    • Walsh D.M., and Selkoe D.J. Oligomers on the brain: the emerging role of soluble protein aggregates in neurodegeneration. Protein Pept. Lett. 11 (2004) 213-228
    • (2004) Protein Pept. Lett. , vol.11 , pp. 213-228
    • Walsh, D.M.1    Selkoe, D.J.2
  • 10
    • 34248190279 scopus 로고    scopus 로고
    • A beta oligomers-a decade of discovery
    • Walsh D.M., and Selkoe D.J. A beta oligomers-a decade of discovery. J. Neurochem. 101 (2007) 1172-1184
    • (2007) J. Neurochem. , vol.101 , pp. 1172-1184
    • Walsh, D.M.1    Selkoe, D.J.2
  • 11
    • 0031871740 scopus 로고    scopus 로고
    • Detection of single amyloid beta-protein aggregates in the cerebrospinal fluid of Alzheimer's patients by fluorescence correlation spectroscopy
    • Pitschke M., Prior R., Haupt M., and Riesner D. Detection of single amyloid beta-protein aggregates in the cerebrospinal fluid of Alzheimer's patients by fluorescence correlation spectroscopy. Nat. Med. 4 (1998) 832-834
    • (1998) Nat. Med. , vol.4 , pp. 832-834
    • Pitschke, M.1    Prior, R.2    Haupt, M.3    Riesner, D.4
  • 13
    • 0012194808 scopus 로고
    • A Drosophila gene encoding a protein resembling the human beta-amyloid protein precursor
    • Rosen D.R., Martin-Morris L., Luo L.Q., and White K. A Drosophila gene encoding a protein resembling the human beta-amyloid protein precursor. Proc. Natl. Acad. Sci. USA 86 (1989) 2478-2482
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 2478-2482
    • Rosen, D.R.1    Martin-Morris, L.2    Luo, L.Q.3    White, K.4
  • 14
    • 0027333449 scopus 로고
    • Apl-1, a Caenorhabditis elegans gene encoding a protein related to the human beta-amyloid protein precursor
    • Daigle I., and Li C. Apl-1, a Caenorhabditis elegans gene encoding a protein related to the human beta-amyloid protein precursor. Proc. Natl. Acad. Sci. USA 90 (1993) 12045-12049
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 12045-12049
    • Daigle, I.1    Li, C.2
  • 15
    • 0033972608 scopus 로고    scopus 로고
    • What the evolution of the amyloid protein precursor supergene family tells us about its function
    • Coulson E.J., Paliga K., Beyreuther K., and Masters C.L. What the evolution of the amyloid protein precursor supergene family tells us about its function. Neurochem. Int. 36 (2000) 175-184
    • (2000) Neurochem. Int. , vol.36 , pp. 175-184
    • Coulson, E.J.1    Paliga, K.2    Beyreuther, K.3    Masters, C.L.4
  • 16
    • 33845566340 scopus 로고    scopus 로고
    • Toxicity of recombinant beta-amyloid prefibrillar oligomers on the morphogenesis of the sea urchin Paracentrotus lividus
    • Carrotta R., Di Carlo M., Manno M., Montana G., Picone P., Romancino D., and San Biagio P.L. Toxicity of recombinant beta-amyloid prefibrillar oligomers on the morphogenesis of the sea urchin Paracentrotus lividus. FASEB J. 20 (2006) 1916-1927
    • (2006) FASEB J. , vol.20 , pp. 1916-1927
    • Carrotta, R.1    Di Carlo, M.2    Manno, M.3    Montana, G.4    Picone, P.5    Romancino, D.6    San Biagio, P.L.7
  • 18
    • 1542473801 scopus 로고    scopus 로고
    • Divergent patterns of neural development in larval echinoids and asteroids
    • Nakajima Y., Kaneko H., Murray G., and Burke R.D. Divergent patterns of neural development in larval echinoids and asteroids. Evol. Dev. 6 (2004) 95-104
    • (2004) Evol. Dev. , vol.6 , pp. 95-104
    • Nakajima, Y.1    Kaneko, H.2    Murray, G.3    Burke, R.D.4
  • 19
    • 85047693458 scopus 로고    scopus 로고
    • Apoptotic mechanisms in Alzheimer neurofibrillary degeneration: cause or effect?
    • Dickson D.W. Apoptotic mechanisms in Alzheimer neurofibrillary degeneration: cause or effect?. J. Clin. Invest. 114 (2004) 121-130
    • (2004) J. Clin. Invest. , vol.114 , pp. 121-130
    • Dickson, D.W.1
  • 20
    • 0033973361 scopus 로고    scopus 로고
    • Calpain and caspase: can you tell the difference?
    • Wang K.K. Calpain and caspase: can you tell the difference?. Trends Neurosci. 23 (2000) 59
    • (2000) Trends Neurosci. , vol.23 , pp. 59
    • Wang, K.K.1
  • 21
    • 33846910826 scopus 로고    scopus 로고
    • Apoptosis in early development of the sea urchin, Strongylocentrotus purpuratus
    • Vega Thurber R., and Epel D. Apoptosis in early development of the sea urchin, Strongylocentrotus purpuratus. Dev. Biol. 303 (2007) 336-346
    • (2007) Dev. Biol. , vol.303 , pp. 336-346
    • Vega Thurber, R.1    Epel, D.2
  • 22
    • 0015383455 scopus 로고
    • Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr J.F., Wyllie A.H., and Currie A.R. Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br. J. Cancer 26 (1972) 239-257
    • (1972) Br. J. Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.1    Wyllie, A.H.2    Currie, A.R.3
  • 23
    • 0034644836 scopus 로고    scopus 로고
    • Regulation of APP cleavage by alpha-, beta- and gamma-secretases
    • Nunan J., and Small D.H. Regulation of APP cleavage by alpha-, beta- and gamma-secretases. FEBS Lett. 483 (2000) 6-10
    • (2000) FEBS Lett. , vol.483 , pp. 6-10
    • Nunan, J.1    Small, D.H.2
  • 24
    • 0038056193 scopus 로고    scopus 로고
    • Proteolytic processing of the amyloid-beta protein precursor of Alzheimer's disease
    • Nunan J., and Small D.H. Proteolytic processing of the amyloid-beta protein precursor of Alzheimer's disease. Essays Biochem. 38 (2002) 37-49
    • (2002) Essays Biochem. , vol.38 , pp. 37-49
    • Nunan, J.1    Small, D.H.2
  • 26
    • 0042838303 scopus 로고    scopus 로고
    • Alzheimer's disease-affected brain: presence of oligomeric A beta ligands (ADDLs) suggests a molecular basis for reversible memory loss
    • Gong Y., Chang L., Viola K.L., Lacor P.N., Lambert M.P., Finch C.E., Krafft G.A., and Klein W.L. Alzheimer's disease-affected brain: presence of oligomeric A beta ligands (ADDLs) suggests a molecular basis for reversible memory loss. Proc. Natl. Acad. Sci. USA 100 (2003) 10417-10422
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 10417-10422
    • Gong, Y.1    Chang, L.2    Viola, K.L.3    Lacor, P.N.4    Lambert, M.P.5    Finch, C.E.6    Krafft, G.A.7    Klein, W.L.8
  • 28
    • 0035149528 scopus 로고    scopus 로고
    • Apoptosis in sea urchin oocytes, eggs, and early embryos
    • Voronina E.W., and Wessel G.M. Apoptosis in sea urchin oocytes, eggs, and early embryos. Mol. Reprod. Dev. 60 (2001) 553-561
    • (2001) Mol. Reprod. Dev. , vol.60 , pp. 553-561
    • Voronina, E.W.1    Wessel, G.M.2
  • 30
    • 0344584508 scopus 로고    scopus 로고
    • Exposure to ultraviolet radiation causes apoptosis in developing sea urchin embryos
    • Lesser M.P., Kruse V.A., and Barry T.M. Exposure to ultraviolet radiation causes apoptosis in developing sea urchin embryos. J. Exp. Biol. 206 (2003) 4097-4103
    • (2003) J. Exp. Biol. , vol.206 , pp. 4097-4103
    • Lesser, M.P.1    Kruse, V.A.2    Barry, T.M.3
  • 33
    • 20444441575 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and Alzheimer's disease: role of amyloid-beta peptide alcohol dehydrogenase (ABAD)
    • Yan S.D., and Stern D.M. Mitochondrial dysfunction and Alzheimer's disease: role of amyloid-beta peptide alcohol dehydrogenase (ABAD). Int. J. Exp. Pathol. 86 (2005) 161-171
    • (2005) Int. J. Exp. Pathol. , vol.86 , pp. 161-171
    • Yan, S.D.1    Stern, D.M.2
  • 34
    • 0036438914 scopus 로고    scopus 로고
    • Solution structure of the Alzheimer amyloid beta-peptide (1-42) in an apolar microenvironment. Similarity with a virus fusion domain
    • Crescenzi O., Tomaselli S., Guerrini R., Salvatori S., D'Ursi A.M., Temussi P.A., and Picone D. Solution structure of the Alzheimer amyloid beta-peptide (1-42) in an apolar microenvironment. Similarity with a virus fusion domain. Eur. J. Biochem. 269 (2002) 5642-5648
    • (2002) Eur. J. Biochem. , vol.269 , pp. 5642-5648
    • Crescenzi, O.1    Tomaselli, S.2    Guerrini, R.3    Salvatori, S.4    D'Ursi, A.M.5    Temussi, P.A.6    Picone, D.7
  • 35
    • 37249062072 scopus 로고    scopus 로고
    • Internalization of beta-amyloid peptide by primary neurons in the absence of apolipoprotein E
    • Saavedra L., Mohamed A., Ma V., Kar S., and de Chaves E.P. Internalization of beta-amyloid peptide by primary neurons in the absence of apolipoprotein E. J. Biol. Chem. 282 (2007) 35722-35732
    • (2007) J. Biol. Chem. , vol.282 , pp. 35722-35732
    • Saavedra, L.1    Mohamed, A.2    Ma, V.3    Kar, S.4    de Chaves, E.P.5
  • 36
    • 2342495787 scopus 로고    scopus 로고
    • Amyloid beta-peptide interactions with neuronal and glial cell plasma membrane: binding sites and implications for Alzheimer's disease
    • Verdier Y., Zarándi M., and Penke B. Amyloid beta-peptide interactions with neuronal and glial cell plasma membrane: binding sites and implications for Alzheimer's disease. J. Pept. Sci. 10 (2004) 229-248
    • (2004) J. Pept. Sci. , vol.10 , pp. 229-248
    • Verdier, Y.1    Zarándi, M.2    Penke, B.3
  • 37
    • 0028972292 scopus 로고
    • Specificity in recognition of amyloid-beta peptide by the serpin-enzyme complex receptor in hepatoma cells and neuronal cells
    • Boland K., Manias K., and Perlmutter D.H. Specificity in recognition of amyloid-beta peptide by the serpin-enzyme complex receptor in hepatoma cells and neuronal cells. J. Biol. Chem. 270 (1995) 28022-28028
    • (1995) J. Biol. Chem. , vol.270 , pp. 28022-28028
    • Boland, K.1    Manias, K.2    Perlmutter, D.H.3
  • 39
  • 40
    • 3242809725 scopus 로고    scopus 로고
    • A model for studying Alzheimer's Abeta42-induced toxicity in Drosophila melanogaster
    • Finelli A., Kelkar A., Song H.J., Yang H., and Konsolaki M. A model for studying Alzheimer's Abeta42-induced toxicity in Drosophila melanogaster. Mol. Cell Neurosci. 26 (2004) 365-375
    • (2004) Mol. Cell Neurosci. , vol.26 , pp. 365-375
    • Finelli, A.1    Kelkar, A.2    Song, H.J.3    Yang, H.4    Konsolaki, M.5
  • 41
    • 0028981288 scopus 로고
    • Expression of human beta-amyloid peptide in transgenic Caenorhabditis elegans
    • Link C.D. Expression of human beta-amyloid peptide in transgenic Caenorhabditis elegans. Proc. Natl. Acad. Sci. USA 92 (1995) 9368-9372
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9368-9372
    • Link, C.D.1
  • 43
    • 33847049400 scopus 로고    scopus 로고
    • Alzheimer disease: amyloidogenesis, the presenilins and animal models
    • Newman M., Musgrave I.F., and Lardelli M. Alzheimer disease: amyloidogenesis, the presenilins and animal models. Biochim. Biophys. Acta 1772 (2007) 285-297
    • (2007) Biochim. Biophys. Acta , vol.1772 , pp. 285-297
    • Newman, M.1    Musgrave, I.F.2    Lardelli, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.