Abstract
α-Synuclein (α-syn) protein and a fragment of it, called NAC, have been found in association with the pathological lesions of a number of neurodegenerative diseases. Recently, mutations in the α-syn gene have been reported in families susceptible to an inherited form of Parkinson's disease. We have shown that human wild-type α-syn, mutant α-syn(Ala30Pro) and mutant α-syn(Ala53Thr) proteins can self-aggregate and form amyloid-like filaments. Here we report that aggregates of NAC and α-syn proteins induced apoptotic cell death in human neuroblastoma SH-SY5Y cells. These findings indicate that accumulation of α-syn and its degradation products may play a major role in the development of the pathogenesis of these neurodegenerative diseases. Copyright (C) 1998 Federation of European Biochemical Societies.
Original language | English |
---|---|
Pages (from-to) | 71-75 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 440 |
Issue number | 1-2 |
DOIs | |
Publication status | Published - 27 Nov 1998 |
Externally published | Yes |
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Keywords
- α-Synuclein
- Amyloid
- Lewy body
- Neurodegenerative disease
- Parkinson's disease
- Toxicity
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
Aggregates from mutant and wild-type α-synuclein proteins and NAC peptide induce apoptotic cell death in human neuroblastoma cells by formation of β-sheet and amyloid-like filaments. / Ali El-Agnaf, Omar; Jakes, Ross; Curran, Martin D.; Middleton, Derek; Ingenito, Raffaele; Bianchi, Elisabetta; Pessi, Antonello; Neill, David; Wallace, Andrew.
In: FEBS Letters, Vol. 440, No. 1-2, 27.11.1998, p. 71-75.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Aggregates from mutant and wild-type α-synuclein proteins and NAC peptide induce apoptotic cell death in human neuroblastoma cells by formation of β-sheet and amyloid-like filaments
AU - Ali El-Agnaf, Omar
AU - Jakes, Ross
AU - Curran, Martin D.
AU - Middleton, Derek
AU - Ingenito, Raffaele
AU - Bianchi, Elisabetta
AU - Pessi, Antonello
AU - Neill, David
AU - Wallace, Andrew
PY - 1998/11/27
Y1 - 1998/11/27
N2 - α-Synuclein (α-syn) protein and a fragment of it, called NAC, have been found in association with the pathological lesions of a number of neurodegenerative diseases. Recently, mutations in the α-syn gene have been reported in families susceptible to an inherited form of Parkinson's disease. We have shown that human wild-type α-syn, mutant α-syn(Ala30Pro) and mutant α-syn(Ala53Thr) proteins can self-aggregate and form amyloid-like filaments. Here we report that aggregates of NAC and α-syn proteins induced apoptotic cell death in human neuroblastoma SH-SY5Y cells. These findings indicate that accumulation of α-syn and its degradation products may play a major role in the development of the pathogenesis of these neurodegenerative diseases. Copyright (C) 1998 Federation of European Biochemical Societies.
AB - α-Synuclein (α-syn) protein and a fragment of it, called NAC, have been found in association with the pathological lesions of a number of neurodegenerative diseases. Recently, mutations in the α-syn gene have been reported in families susceptible to an inherited form of Parkinson's disease. We have shown that human wild-type α-syn, mutant α-syn(Ala30Pro) and mutant α-syn(Ala53Thr) proteins can self-aggregate and form amyloid-like filaments. Here we report that aggregates of NAC and α-syn proteins induced apoptotic cell death in human neuroblastoma SH-SY5Y cells. These findings indicate that accumulation of α-syn and its degradation products may play a major role in the development of the pathogenesis of these neurodegenerative diseases. Copyright (C) 1998 Federation of European Biochemical Societies.
KW - α-Synuclein
KW - Amyloid
KW - Lewy body
KW - Neurodegenerative disease
KW - Parkinson's disease
KW - Toxicity
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UR - http://www.scopus.com/inward/citedby.url?scp=0032573597&partnerID=8YFLogxK
U2 - 10.1016/S0014-5793(98)01418-5
DO - 10.1016/S0014-5793(98)01418-5
M3 - Article
C2 - 9862428
AN - SCOPUS:0032573597
VL - 440
SP - 71
EP - 75
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 1-2
ER -