umu.sePublikationer
Ändra sökning
RefereraExporteraLänk till posten
Permanent länk

Direktlänk
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Annat format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annat språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf
Comprehensive analysis to explain reduced or increased SOD1 enzymatic activity in ALS patients and their relatives
Umeå universitet, Medicinska fakulteten, Institutionen för farmakologi och klinisk neurovetenskap, Klinisk neurovetenskap.
Umeå universitet, Medicinska fakulteten, Institutionen för farmakologi och klinisk neurovetenskap, Klinisk neurovetenskap.
Umeå universitet, Medicinska fakulteten, Institutionen för farmakologi och klinisk neurovetenskap, Klinisk neurovetenskap. Polish Academy of Sciences, Warsaw, Poland.
Umeå universitet, Medicinska fakulteten, Institutionen för medicinsk biovetenskap, Klinisk kemi.
Visa övriga samt affilieringar
2017 (Engelska)Ingår i: Amyotrophic Lateral Sclerosis and Frontotemporal Degeneration, ISSN 2167-8421, E-ISSN 2167-9223, Vol. 18, nr 5-6, s. 457-463Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Objective: To characterise stabilities in erythrocytes of mutant SOD1 proteins, compare SOD1 enzymatic activities between patients with different genetic causes of ALS and search for underlying causes of deviant SOD1 activities in individuals lacking SOD1 mutations.Methods: Blood samples from 4072 individuals, ALS patients with or without a SOD1 mutation, family members and controls were studied. Erythrocyte SOD1 enzymatic activities normalised to haemoglobin content were determined, and effects of haemoglobin disorders on dismutation assessed. Coding SOD1 sequences were analysed by Sanger sequencing, exon copy number variations by fragment length analysis and by TaqMan Assay.Results: Of the 44 SOD1 mutations found, 75% caused severe destabilisation of the mutant protein but in 25% it was physically stable. Mutations producing structural changes caused halved erythrocyte SOD1 activities. There were no differences in SOD1 activities between patients without a SOD1 mutation and control individuals or carriers of TBK1 mutations and C9orf72(HRE). In the low and high SOD1 activity groups no deviations were found in exon copy numbers and intron gross structures. Thalassemias and iron deficiency were associated with increased SOD1 activity/haemoglobin ratios.Conclusion: Adjunct erythrocyte SOD1 activity analysis reliably signals destabilising SOD1 mutations including intronic mutations that are missed by exon sequencing.

Ort, förlag, år, upplaga, sidor
TAYLOR & FRANCIS LTD , 2017. Vol. 18, nr 5-6, s. 457-463
Nyckelord [en]
Amyotrophic lateral sclerosis, superoxide dismutase, mutation, enzymatic activity
Nationell ämneskategori
Klinisk medicin
Identifikatorer
URN: urn:nbn:se:umu:diva-138241DOI: 10.1080/21678421.2017.1301481ISI: 000405584600019OAI: oai:DiVA.org:umu-138241DiVA, id: diva2:1133539
Tillgänglig från: 2017-08-16 Skapad: 2017-08-16 Senast uppdaterad: 2018-06-09Bibliografiskt granskad

Open Access i DiVA

Fulltext saknas i DiVA

Övriga länkar

Förlagets fulltext

Personposter BETA

Keskin, IsilBirve, AnnaHjertkvist, KarinRofougaran, RezaNilsson, Torbjörn K.Marklund, Stefan L.Andersen, Peter M.

Sök vidare i DiVA

Av författaren/redaktören
Keskin, IsilBirve, AnnaHjertkvist, KarinRofougaran, RezaNilsson, Torbjörn K.Marklund, Stefan L.Andersen, Peter M.
Av organisationen
Klinisk neurovetenskapKlinisk kemi
I samma tidskrift
Amyotrophic Lateral Sclerosis and Frontotemporal Degeneration
Klinisk medicin

Sök vidare utanför DiVA

GoogleGoogle Scholar

doi
urn-nbn

Altmetricpoäng

doi
urn-nbn
Totalt: 304 träffar
RefereraExporteraLänk till posten
Permanent länk

Direktlänk
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Annat format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annat språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf