Organization of the human synphilin-1 gene, a candidate for Parkinson's disease

We have recently identified a protein we called synphilin-1, which interacts in vivo with alpha-synuclein. Mutations in alpha-synuclein cause familial Parkinson's disease (PD). Alpha-synuclein protein is present in the pathologic lesions of familial and sporadic PD, and diffuse Lewy body diseas...

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Bibliographic Details
Published in:Mammalian genome 2000-09, Vol.11 (9), p.763-766
Main Authors: Engelender, Simone, Wanner, Tracy, Kleiderlein, John J, Wakabayashi, Koichi, Tsuji, Shoji, Takahashi, Hitoshi, Ashworth, Roxann, Margolis, Russell L, Ross, Christopher A
Format: Article
Language:English
Subjects:
Base Sequence
brain
Brain - metabolism
Brain - pathology
Carrier Proteins - genetics
Carrier Proteins - metabolism
Chromosome Mapping
Chromosomes, Human, Pair 5 - genetics
DNA - chemistry
DNA - genetics
Exons
genes
Genes - genetics
Genetic Predisposition to Disease
Genetics
Humans
Hybrid Cells
Immunohistochemistry
Introns
loci
Molecular Sequence Data
mutation
Nerve Tissue Proteins - genetics
Nerve Tissue Proteins - metabolism
open reading frames
Parkinson disease
Parkinson Disease - genetics
Parkinson's disease
patients
Polymorphism, Genetic
Sequence Analysis, DNA
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Summary:We have recently identified a protein we called synphilin-1, which interacts in vivo with alpha-synuclein. Mutations in alpha-synuclein cause familial Parkinson's disease (PD). Alpha-synuclein protein is present in the pathologic lesions of familial and sporadic PD, and diffuse Lewy body disease, indicating an important pathogenic role for alpha-synuclein. Here we describe the structure of the human synphilin-1 gene (SNCAIP). The open reading frame of this gene is contained within ten exons. We have designed primers to amplify each SNCAIP exon, so these primers can now be used to screen for mutations or polymorphisms in patients with Parkinson's disease or related diseases. We found a highly polymorphic GT repeat within intron 5 of SNCAIP, suitable for linkage analysis of families with PD. We have mapped SNCAIP locus to Chromosome (Chr) 5q23.1-23.3 near markers WI-4673 and AFMB352XH5. In addition, using immunohistochemistry in human postmortem brain tissue, we found that synphilin-1 protein is present in neuropil, similar to alpha-synuclein protein. Because of its association with alpha-synuclein, synphilin-1 may be a candidate for involvement in Parkinson's disease or other related disorders.
ISSN:0938-8990
1432-1777
DOI:10.1007/s003350010123