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

Rina Bandopadhyay, Rohan De Silva, Naheed Khan, Elizabeth Graham, Jenny Vaughan, Simone Engelender, Christopher A Ross, Huw Morris, Christopher Morris, Nicholas W. Wood, Susan Daniel, Andrew Lees

Research output: Contribution to journalArticle

Abstract

α-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 α-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.

Original languageEnglish (US)
Pages (from-to)125-127
Number of pages3
JournalNeuroscience Letters
Volume307
Issue number2
DOIs
StatePublished - Jul 13 2001

Fingerprint

Synucleins
Introns
Parkinson Disease
Lewy Bodies
Mutation
Genes
Neurites
Proteins

Keywords

  • Association study
  • Genetics
  • Intronic
  • Parkinson's disease
  • Polymorphism
  • Synphilin-1

ASJC Scopus subject areas

  • Neuroscience(all)

Cite this

Bandopadhyay, R., De Silva, R., Khan, N., Graham, E., Vaughan, J., Engelender, S., ... Lees, A. (2001). No pathogenic mutations in the synphilin-1 gene in Parkinson's disease. Neuroscience Letters, 307(2), 125-127. https://doi.org/10.1016/S0304-3940(01)01935-8

No pathogenic mutations in the synphilin-1 gene in Parkinson's disease. / Bandopadhyay, Rina; De Silva, Rohan; Khan, Naheed; Graham, Elizabeth; Vaughan, Jenny; Engelender, Simone; Ross, Christopher A; Morris, Huw; Morris, Christopher; Wood, Nicholas W.; Daniel, Susan; Lees, Andrew.

In: Neuroscience Letters, Vol. 307, No. 2, 13.07.2001, p. 125-127.

Research output: Contribution to journalArticle

Bandopadhyay, R, De Silva, R, Khan, N, Graham, E, Vaughan, J, Engelender, S, Ross, CA, Morris, H, Morris, C, Wood, NW, Daniel, S & Lees, A 2001, 'No pathogenic mutations in the synphilin-1 gene in Parkinson's disease', Neuroscience Letters, vol. 307, no. 2, pp. 125-127. https://doi.org/10.1016/S0304-3940(01)01935-8
Bandopadhyay R, De Silva R, Khan N, Graham E, Vaughan J, Engelender S et al. No pathogenic mutations in the synphilin-1 gene in Parkinson's disease. Neuroscience Letters. 2001 Jul 13;307(2):125-127. https://doi.org/10.1016/S0304-3940(01)01935-8
Bandopadhyay, Rina ; De Silva, Rohan ; Khan, Naheed ; Graham, Elizabeth ; Vaughan, Jenny ; Engelender, Simone ; Ross, Christopher A ; Morris, Huw ; Morris, Christopher ; Wood, Nicholas W. ; Daniel, Susan ; Lees, Andrew. / No pathogenic mutations in the synphilin-1 gene in Parkinson's disease. In: Neuroscience Letters. 2001 ; Vol. 307, No. 2. pp. 125-127.
@article{6b92343efc1d4324a3d2c5ee3531a352,
title = "No pathogenic mutations in the synphilin-1 gene in Parkinson's disease",
abstract = "α-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 α-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.",
keywords = "Association study, Genetics, Intronic, Parkinson's disease, Polymorphism, Synphilin-1",
author = "Rina Bandopadhyay and {De Silva}, Rohan and Naheed Khan and Elizabeth Graham and Jenny Vaughan and Simone Engelender and Ross, {Christopher A} and Huw Morris and Christopher Morris and Wood, {Nicholas W.} and Susan Daniel and Andrew Lees",
year = "2001",
month = "7",
day = "13",
doi = "10.1016/S0304-3940(01)01935-8",
language = "English (US)",
volume = "307",
pages = "125--127",
journal = "Neuroscience Letters",
issn = "0304-3940",
publisher = "Elsevier Ireland Ltd",
number = "2",

}

TY - JOUR

T1 - No pathogenic mutations in the synphilin-1 gene in Parkinson's disease

AU - Bandopadhyay, Rina

AU - De Silva, Rohan

AU - Khan, Naheed

AU - Graham, Elizabeth

AU - Vaughan, Jenny

AU - Engelender, Simone

AU - Ross, Christopher A

AU - Morris, Huw

AU - Morris, Christopher

AU - Wood, Nicholas W.

AU - Daniel, Susan

AU - Lees, Andrew

PY - 2001/7/13

Y1 - 2001/7/13

N2 - α-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 α-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.

AB - α-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 α-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.

KW - Association study

KW - Genetics

KW - Intronic

KW - Parkinson's disease

KW - Polymorphism

KW - Synphilin-1

UR - http://www.scopus.com/inward/record.url?scp=0035854630&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0035854630&partnerID=8YFLogxK

U2 - 10.1016/S0304-3940(01)01935-8

DO - 10.1016/S0304-3940(01)01935-8

M3 - Article

C2 - 11427316

AN - SCOPUS:0035854630

VL - 307

SP - 125

EP - 127

JO - Neuroscience Letters

JF - Neuroscience Letters

SN - 0304-3940

IS - 2

ER -