No pathogenic mutations in the synphilin-1 gene in Parkinson's disease.
alpha-Synuclein is mutated in rare autosomal dominant forms of Parkinson's disease and is a major component of Lewy bodies and neurites. Synphilin-1, a novel protein interacts in vivo and co-localises with alpha-synuclein in Lewy bodies. We analysed the synphilin-1 gene in familial Parkinson's disease by single-strand conformation polymorphism (SSCP) and automated sequencing but found no coding mutations. However, we identified two novel intronic polymorphisms; an A/T polymorphism in intron 2, resulting in the introduction of an Alu1 site and a second G/T polymorphism in intron 4. We analysed the intron 2 polymorphism for allelic association as it was conducive to rapid screening but observed no changes in frequency between Parkinson's disease cases and controls.
Bandopadhyay
R
R
Reta Lila Weston Institute of Neurological Studies, Royal Free and University College Medical School, Windeyer Building, 46 Cleveland Street, W1T 4JF, London, UK.
de Silva
R
R
Khan
N
N
Graham
E
E
Vaughan
J
J
Engelender
S
S
Ross
C
C
Morris
H
H
Morris
C
C
Wood
N W
NW
Daniel
S
S
Lees
A
A
D000368:Aged; D000483:Alleles; D002352:Carrier Proteins / Q000235:genetics*; D005091:Exons / Q000235:genetics; D005260:Female; D005820:Genetic Testing; D005838:Genotype; D006801:Humans; D007438:Introns / Q000502:physiology; D016631:Lewy Bodies / Q000235:genetics; D009154:Mutation / Q000235:genetics / Q000502:physiology; D009419:Nerve Tissue Proteins / Q000235:genetics*; D010300:Parkinson Disease / Q000235:genetics* / Q000503:physiopathology; D018807:Polymorphism, Single-Stranded Conformational
D002352:Carrier Proteins; D009419:Nerve Tissue Proteins; C118958:SNCAIP protein, human