High-resolution mapping of SNCA encoding α-synuclein, the non-Aβ component of Alzheimer’s disease amyloid precursor, to human chromosome 4q21.3→q22 by fluorescence in situ hybridization

Shibasaki, Y.; Baillie, D.A.M.; Clair, David St; Brookes, Anthony J.

doi:10.1159/000134061

Cited by 48 publications

(27 citation statements)

References 4 publications

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“…The ␣-, ␤-, and ␥-synuclein genes (SNCA, SNCB, and SNCG) map to chromosome 4q21.3-q22 (Campion et al 195;Chen et al 1995;Shibasaki et al 1995;Lavedan et al 1998a), 5q35, (Spillantini et al 1995; C. Lavedan, E. Leroy, R. Torres, A. Dehejia, S. Buchholtz, A. Dutra, R.L. Nussbaum, and M.H.…”

Section: The Human Synuclein Genesmentioning

confidence: 99%

The Synuclein Family

Lavedan¹

1998

Genome Res.

305

243

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The synuclein gene family recently came into the spotlight, when one of its members, α-synuclein, was found to be mutated in several families with autosomal dominant Parkinson’s disease (PD). A peptide of the α-synuclein protein had been characterized previously as a major component of amyloid plaques in brains of patients with Alzheimer’s disease (AD). The mechanism by which this presynaptic protein is involved in the two most common neurodegenerative disorders, AD and PD, remains unclear. Remarkably, another member of this gene family, γ-synuclein, has been shown to be overexpressed in breast carcinomas and may also be overexpressed in ovarian cancer. The possible involvement of the synuclein proteins in the etiology of common human diseases has raised exciting questions and is the subject of intense investigation. Details of the properties of any member of the synuclein family may provide useful information for understanding the characteristics and function of other family members. The present review offers a synopsis of the current state of knowledge of all synuclein family members in different species.

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Section: The Human Synuclein Genesmentioning

confidence: 99%

The Synuclein Family

Lavedan¹

1998

Genome Res.

305

243

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“…Human b-synuclein also was identified, and it is a 134 amino acid long protein with homologies to human a-synuclein (Jakes et al, 1994;Goedert, 1997). However, human a-and b-synucleins are encoded by different genes located on chromosomes 4 (4q21) and 5 (5q35), respectively (Campion et al, 1995;Chen et al, 1995;Shibashi et al, 1995;Spillantini et al, 1995). Further, the bovine homologue of human b-synuclein has been characterized and it is known as phosphoneuronoprotein 14 or PNP14 (Nakajo et al, 1990;Shibayama-Imazu et al, 1993), while the song bird homologue of human synuclein is known as synelfin, and anti-synelfin antibodies crossreact with mammalian synucleins Irizarry et al, 1996;Withers et al, 1997).…”

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confidence: 99%

Fatal attractions: abnormal protein aggregation and neuron death in Parkinson's disease and Lewy body dementia

et al. 1998

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The abnormal aggregation of proteins into fibrillar lesions is a neuropathological hallmark of several sporadic and hereditary neurodegenerative diseases. For example, Lewy bodies (LBs) are intracytoplasmic filamentous inclusions that accumulate primarily in subcortical neurons of patients with Parkinson's disease (PD), or predominantly in neocortical neurons in a subtype of Alzheimer's disease (AD) known as the LB variant of AD (LBVAD) and in dementia with LBs (DLB). Aggregated neurofilament subunits and a-synuclein are major protein components of LBs, and these inclusions may contribute mechanistically to the degeneration of neurons in PD, DLB and LBVAD. Here we review recent studies of the protein building blocks of LBs, as well as the role LBs play in the onset and progression of PD, DLB and LBVAD. Increased understanding of the protein composition and pathological significance of LBs may provide insight into mechanisms of neuron dysfunction and death in other neurodegenerative disorders characterized by brain lesions containing massive deposits of proteinacious fibrils.

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“…The gene for alpha synuclein maps to chromosome position 4q21.3-22 (Chen et al, 1995;Shibasaki et al, 1995;Spillantini et al, 1995). This region has been associated with drug abuse through a genome-wide SNP genome scan (Uhl et al, 2001).…”

Section: Discussionmentioning

confidence: 99%

Alpha synuclein protein levels are increased in serum from recently abstinent cocaine abusers

Mash

Adi

Duque

et al. 2008

Drug and Alcohol Dependence

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Alpha synuclein is increased in dopamine neurons of cocaine abusers and in rats whose alcohol preference is inbred. Recent studies have shown increased alpha-synuclein protein expression in serum of alcoholic patients that is linked with severity of alcohol craving. The aim of this study was to analyze the serum levels of alpha synuclein in healthy subjects and in recently abstinent cocaine abusers. Alpha synuclein protein expression was measured by enzyme-linked immunosorbent assay in serum specimens obtained from 38 recently abstinent cocaine dependent patients and 14 control subjects. The presence of cocaine dependence disorder was based on the Structured Clinical Interview (DSM-IV). Drug severity was assessed by the Addiction Severity Index ratings and composite measures. Scores of the intensity and frequency of cocaine craving episodes were obtained from the Minnesota Cocaine Craving Questionnaire. The serum concentrations of alpha synuclein in cocaine dependent patients were significantly higher as compared with age-matched drug-free controls (p < 0.001). Alpha synuclein levels in blood were significantly correlated with the intensity (r = 0.60, p < 0.001) and frequency (r = 0.64. p < 0.001) of cocaine craving and with thirty days of cocaine use in the prior month before entry to treatment (r = 0.56, p < 0.005). However, there was no correlation between the serum protein levels of alpha synuclein and age in either group. This report is the first demonstration of altered alpha synuclein levels in peripheral blood from cocaine abusers. These data agree with previous reports in postmortem brain of cocaine abusers and provide support for an association between alpha synuclein and cocaine dependence.

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High-resolution mapping of SNCA encoding α-synuclein, the non-Aβ component of Alzheimer’s disease amyloid precursor, to human chromosome 4q21.3→q22 by fluorescence in situ hybridization

Abstract: The human α-synuclein gene (SNCA) was previously identified as the non-Aβ component of Alzheimer’s disease amyloid precursor (NACP). A cosmid clone containing this gene has been isolated and mapped by FISH and high-resolution fluorescence banding to human chromosome 4q21.3→q22.

Cited by 48 publications

References 4 publications

The Synuclein Family

The Synuclein Family

Fatal attractions: abnormal protein aggregation and neuron death in Parkinson's disease and Lewy body dementia

Alpha synuclein protein levels are increased in serum from recently abstinent cocaine abusers

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