메뉴 건너뛰기




Volumn 24, Issue 5, 2003, Pages 679-685

Humanin peptides block calcium influx of rat hippocampal neurons by altering fibrogenesis of Aβ1-40

Author keywords

A aggregation; Calcium influx; Electron microscopy; Humanin; Neurotoxicity

Indexed keywords

CALCIUM ANTAGONIST; HUMANIN; NEUROPROTECTIVE AGENT; PEPTIDE; UNCLASSIFIED DRUG;

EID: 0043207393     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0196-9781(03)00131-1     Document Type: Article
Times cited : (29)

References (22)
  • 1
    • 0027508926 scopus 로고
    • Alzheimer disease amyloid beta protein forms calcium channels in bilayer membranes: Blockade by tromethamine and aluminium
    • Arispe N., Rojas E., Pollard H.B. Alzheimer disease amyloid beta protein forms calcium channels in bilayer membranes: blockade by tromethamine and aluminium. Proc. Natl. Acad Sci. U.S.A. 90:1993;567-571.
    • (1993) Proc. Natl. Acad Sci. U.S.A. , vol.90 , pp. 567-571
    • Arispe, N.1    Rojas, E.2    Pollard, H.B.3
  • 2
    • 0030896414 scopus 로고    scopus 로고
    • Isolation and culture of adult rat hippocampal neurons
    • Brewer G.J. Isolation and culture of adult rat hippocampal neurons. J. Neurosci. Methods. 71:1997;143-155.
    • (1997) J. Neurosci. Methods , vol.71 , pp. 143-155
    • Brewer, G.J.1
  • 3
    • 0030841343 scopus 로고    scopus 로고
    • Conformational disease
    • Carrell R.W., Lomas D.A. Conformational disease. Lancet. 350:1997;134-138.
    • (1997) Lancet , vol.350 , pp. 134-138
    • Carrell, R.W.1    Lomas, D.A.2
  • 4
    • 0025232814 scopus 로고
    • Solid phase peptide synthesis utilizing 9-fluorenylmethoxy-carbonyl amino acids
    • Fields G.B., Noble R.L. Solid phase peptide synthesis utilizing 9-fluorenylmethoxy-carbonyl amino acids. Int. J. Pept. Protein Res. 35:1990;161-214.
    • (1990) Int. J. Pept. Protein Res. , vol.35 , pp. 161-214
    • Fields, G.B.1    Noble, R.L.2
  • 5
    • 0029664434 scopus 로고    scopus 로고
    • Aβ-peptide length and apolipoprotein E genotype in Alzheimer's disease
    • Gearing M., Mori H., Mira S. Aβ-peptide length and apolipoprotein E genotype in Alzheimer's disease. Ann. Neurol. 39:1996;395-399.
    • (1996) Ann. Neurol. , vol.39 , pp. 395-399
    • Gearing, M.1    Mori, H.2    Mira, S.3
  • 6
    • 0026597063 scopus 로고
    • Alzheimer's disease: The amyloid cascade hypothesis
    • Hardy J.A., Higgins G.A. Alzheimer's disease: the amyloid cascade hypothesis. Science. 256:1992;184-185.
    • (1992) Science , vol.256 , pp. 184-185
    • Hardy, J.A.1    Higgins, G.A.2
  • 7
    • 0030908095 scopus 로고    scopus 로고
    • Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
    • Harper J.D., Lansbury P.T. Jr. Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu. Rev. Biochem. 66:1997;385-407.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury P.T., Jr.2
  • 8
    • 0030614627 scopus 로고    scopus 로고
    • Observation of metastable Aβ amyloid protofibrils by atomic force microscopy
    • Harper J.D., Wong S.S., Lieber C.M., Lansbury P.T. Observation of metastable Aβ amyloid protofibrils by atomic force microscopy. Chem. Biol. 4:1997;119-125.
    • (1997) Chem. Biol. , vol.4 , pp. 119-125
    • Harper, J.D.1    Wong, S.S.2    Lieber, C.M.3    Lansbury, P.T.4
  • 10
    • 0035576106 scopus 로고    scopus 로고
    • Detailed characterization of neuroprotection by a resue factor humanin against various Alzheimer's disease-relevant insults
    • Hashimoto Y., Niikura T., Ito Y., Sudo H., Hata M., Arakawa E., Abe Y., Kita Y., Nishimoto I. Detailed characterization of neuroprotection by a resue factor humanin against various Alzheimer's disease-relevant insults. J. Neurosci. 21:2001;9235-9245.
    • (2001) J. Neurosci. , vol.21 , pp. 9235-9245
    • Hashimoto, Y.1    Niikura, T.2    Ito, Y.3    Sudo, H.4    Hata, M.5    Arakawa, E.6    Abe, Y.7    Kita, Y.8    Nishimoto, I.9
  • 12
    • 0028850087 scopus 로고
    • Suppression of mitochondrial succinate dehydrogenase, a primary target of beta-amyloid, and its derivative racemized at Ser residue
    • Kaneko I., Yamada N., Sakuraba Y., Kamenosono M., Tutumi S. Suppression of mitochondrial succinate dehydrogenase, a primary target of beta-amyloid, and its derivative racemized at Ser residue. J. Neurochem. 65:1995;2585-2593.
    • (1995) J. Neurochem. , vol.65 , pp. 2585-2593
    • Kaneko, I.1    Yamada, N.2    Sakuraba, Y.3    Kamenosono, M.4    Tutumi, S.5
  • 13
    • 0002580209 scopus 로고
    • The epidemiology of dementia and Alzheimer disease
    • Terry RD, Katzman R, Bick KL, editors. New York: Raven Press
    • Katzman R, Kawas C. The epidemiology of dementia and Alzheimer disease. In: Terry RD, Katzman R, Bick KL, editors. Alzheimer disease. New York: Raven Press; 1994. p. 105.
    • (1994) Alzheimer Disease , pp. 105
    • Katzman, R.1    Kawas, C.2
  • 14
    • 0034319190 scopus 로고    scopus 로고
    • Molecular mechanism of neurodegeneration induced by Alzheimer's β-amyloid protein: Channel formation and disruption of calcium homeostasis
    • Kawahara M., Kuroda Y. Molecular mechanism of neurodegeneration induced by Alzheimer's β-amyloid protein: channel formation and disruption of calcium homeostasis. Brain Res. Bull. 4:2000;389-397.
    • (2000) Brain Res. Bull. , vol.4 , pp. 389-397
    • Kawahara, M.1    Kuroda, Y.2
  • 15
    • 9044229145 scopus 로고    scopus 로고
    • On the nucleation and growth of amyloid β-protein fibrils: Detection of nuclei and quantitation of rate constants
    • Lomakin A., Chung D.S., Benedek G.B., Kirschner D.A., Teplow D.B. On the nucleation and growth of amyloid β-protein fibrils: detection of nuclei and quantitation of rate constants. Proc. Natl. Acad Sci. U.S.A. 93:1996;1125-1129.
    • (1996) Proc. Natl. Acad Sci. U.S.A. , vol.93 , pp. 1125-1129
    • Lomakin, A.1    Chung, D.S.2    Benedek, G.B.3    Kirschner, D.A.4    Teplow, D.B.5
  • 18
    • 0026570528 scopus 로고
    • β-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity
    • Mattson M.P., Cheng B., Davis D., Bryant K., Lieberburg I., Rydel R.E. β-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity. J. Neurosci. 12:1992;376-389.
    • (1992) J. Neurosci. , vol.12 , pp. 376-389
    • Mattson, M.P.1    Cheng, B.2    Davis, D.3    Bryant, K.4    Lieberburg, I.5    Rydel, R.E.6
  • 19
    • 0025753852 scopus 로고
    • The molecular pathology of Alzheimer's disease
    • Selkoe D.J. The molecular pathology of Alzheimer's disease. Neuron. 6:1991;487-498.
    • (1991) Neuron , vol.6 , pp. 487-498
    • Selkoe, D.J.1
  • 20
    • 0027459686 scopus 로고
    • Secretion of β-amyloid precursor protein cleaved at the amino terminus of the β-amyloid peptide
    • Seubert P., Oltersdorf T., Lee M.G., Barbour R., Blomquist C., Davis D.L.et al. Secretion of β-amyloid precursor protein cleaved at the amino terminus of the β-amyloid peptide. Nature. 361:1993;260-263.
    • (1993) Nature , vol.361 , pp. 260-263
    • Seubert, P.1    Oltersdorf, T.2    Lee, M.G.3    Barbour, R.4    Blomquist, C.5    Davis, D.L.6
  • 21
    • 0013615899 scopus 로고    scopus 로고
    • RAGE and amyloid-β peptide neurotoxicity in Alzheimer's disease
    • Yan S.D., Chen X., Fu J., Chen M., Zhu H., Roher A.et al. RAGE and amyloid-β peptide neurotoxicity in Alzheimer's disease. Nature. 382:1996;685-691.
    • (1996) Nature , vol.382 , pp. 685-691
    • Yan, S.D.1    Chen, X.2    Fu, J.3    Chen, M.4    Zhu, H.5    Roher, A.6
  • 22
    • 0032855482 scopus 로고    scopus 로고
    • Methodological and chemical factors affecting amyloid β peptide amyloidogenicity
    • Colowick SP, Kaplan NO, editors. New York: Academic Press
    • Zagorski MG, Yang J, Shao H, Ma K, Zeng H, Hong A. Methodological and chemical factors affecting amyloid β peptide amyloidogenicity. In: Colowick SP, Kaplan NO, editors. Methods in enzymology, vol. 309. New York: Academic Press; 1999. p. 189-204.
    • (1999) Methods in Enzymology , vol.309 , pp. 189-204
    • Zagorski, M.G.1    Yang, J.2    Shao, H.3    Ma, K.4    Zeng, H.5    Hong, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.