Low alpha-synuclein 126 mRNA levels in dementia with Lewy bodies and Alzheimer disease

被引:41
作者
Beyer, Katrin [1 ]
Humbert, Jordi
Ferrer, Anna
Lao, Jose I.
Carrato, Cristina
Lopez, Dolores
Ferrer, Isidro
Ariza, Aurelio
机构
[1] Univ Autonoma Barcelona, Hosp Univ Germans Trias & Pujol, Dept Pathol, Badalona 08916, Barcelona, Spain
[2] Lab Dr Echevarne, Dept Genet & Mol Med, Barcelona, Spain
[3] Univ Barcelona, Neurol Tissue Bank, Barcelona, Spain
[4] Bellvitge Hosp, Inst Neuropathol, L Hosp Llogbtea, Spain
关键词
alpha-synuclein isoforms; Alzheimer's disease; competimer technology; dementia with Lewy bodies; differential isoform expression; mRNA expression;
D O I
10.1097/01.wnr.0000224773.66904.e7
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
Alpha-synuclein, a main component of Lewy bodies in synucleinopathies and senile plaques in Alzheimer disease, is centrally involved in neurodegeneration. Three different isoforms (alpha-synuclein 112, 126, and 140) resulting from alternative splicing have been described so far. The present study explores alpha-synuclein 126 mRNA expression levels in the prefrontal cortex of six patients with dementia with Lewy bodies, eight patients with Lewy body variant of Alzheimer disease, eight patients with Alzheimer disease, and 10 controls. Relative alpha-synuclein 126 expression levels were determined by real-time polymerase chain reaction with competimer technology. Alpha-synuclein 126 mRNA expression was markedly decreased in the three dementias in comparison with controls, suggesting an important role of this alpha-synuclein isoform in the normal brain.
引用
收藏
页码:1327 / 1330
页数:4
相关论文
共 24 条
[1]   Differential expression of α-synuclein isoforms in dementia with Lewy bodies [J].
Beyer, K ;
Lao, JI ;
Carrato, C ;
Mate, JL ;
López, D ;
Ferrer, I ;
Ariza, A .
NEUROPATHOLOGY AND APPLIED NEUROBIOLOGY, 2004, 30 (06) :601-607
[2]  
BISAGLIA M, BIOPOLYMERS
[3]   Lewy body dementia [J].
Brown, DF .
ANNALS OF MEDICINE, 1999, 31 (03) :188-196
[4]   Effects of Parkinson's disease-linked mutations on the structure of lipid-associated α-synuclein [J].
Bussell, R ;
Eliezer, D .
BIOCHEMISTRY, 2004, 43 (16) :4810-4818
[5]   THE NACP/SYNUCLEIN GENE - CHROMOSOMAL ASSIGNMENT AND SCREENING FOR ALTERATIONS IN ALZHEIMER-DISEASE [J].
CAMPION, D ;
MARTIN, C ;
HEILIG, R ;
CHARBONNIER, F ;
MOREAU, V ;
FLAMAN, JM ;
PETIT, JL ;
HANNEQUIN, D ;
BRICE, A ;
FREBOURG, T .
GENOMICS, 1995, 26 (02) :254-257
[6]   A broken α-helix in folded α-synuclein [J].
Chandra, S ;
Chen, XC ;
Rizo, J ;
Jahn, R ;
Südhof, TC .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (17) :15313-15318
[7]   Abnormal α-synuclein interactions with rab proteins in α-synuclein A30P transgenic mice [J].
Dalfó, E ;
Gómez-Isla, T ;
Rosa, JL ;
Bodelón, MN ;
Tejedor, MC ;
Barrachina, M ;
Ambrosio, S ;
Ferrer, I .
JOURNAL OF NEUROPATHOLOGY AND EXPERIMENTAL NEUROLOGY, 2004, 63 (04) :302-313
[8]   Stabilization of α-synuclein secondary structure upon binding to synthetic membranes [J].
Davidson, WS ;
Jonas, A ;
Clayton, DF ;
George, JM .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (16) :9443-9449
[9]   Mutant and wild type human α-synucleins assemble into elongated filaments with distinct morphologies in vitro [J].
Giasson, BI ;
Uryu, K ;
Trojanowski, JQ ;
Lee, VMY .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (12) :7619-7622
[10]   A hydrophobic stretch of 12 amino acid residues in the middle of α-synuclein is essential for filament assembly [J].
Giasson, BI ;
Murray, IVJ ;
Trojanowski, JQ ;
Lee, VMY .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (04) :2380-2386