No pathogenic mutations in the synphilin-1 gene in Parkinson's disease

Neurosci Lett. 2001 Jul 13;307(2):125-7. doi: 10.1016/s0304-3940(01)01935-8.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aged
  • Alleles
  • Carrier Proteins / genetics*
  • Exons / genetics
  • Female
  • Genetic Testing
  • Genotype
  • Humans
  • Introns / physiology
  • Lewy Bodies / genetics
  • Mutation / genetics
  • Mutation / physiology
  • Nerve Tissue Proteins / genetics*
  • Parkinson Disease / genetics*
  • Parkinson Disease / physiopathology
  • Polymorphism, Single-Stranded Conformational

Substances

  • Carrier Proteins
  • Nerve Tissue Proteins
  • SNCAIP protein, human