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Sökning: onr:"swepub:oai:DiVA.org:umu-4749" > Superoxide dismutas...

Superoxide dismutase in CSF from amyotrophic lateral sclerosis patients with and without CuZn-superoxide dismutase mutations

Jacobsson, Johan (författare)
Umeå universitet,Klinisk neurovetenskap
Jonsson, P. Andreas (författare)
Umeå universitet,Institutionen för medicinsk biovetenskap
Andersen, Peter M. (författare)
Umeå universitet,Klinisk neurovetenskap
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Forsgren, Lars (författare)
Umeå universitet,Klinisk neurovetenskap
Marklund, Stefan L. (författare)
Umeå universitet,Klinisk kemi
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 (creator_code:org_t)
2001
2001
Engelska.
Ingår i: Brain. - 0006-8950 .- 1460-2156. ; 124:7, s. 1461-1466
  • Tidskriftsartikel (refereegranskat)
Abstract Ämnesord
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  • Mutations in CuZn-superoxide dismutase (CuZn-SOD) have been linked to familial amyotrophic lateral sclerosis (ALS), and motor neurone death is caused by the gain of a toxic property of the mutant protein. Here we determined amounts, activity and molecular forms of CuZn-SOD in CSF from ALS patients carrying the D90A and other CuZn-SOD mutations and patients without such mutations. There were no differences in amount of protein and enzymic activities of CuZn-SOD between 37 neurological controls, 54 sporadic and 12 familial ALS cases, and 10 cases homozygous for the D90A mutation. Three cases heterozygous for the A89V, S105L and G114A CuZn-SOD mutations showed low amounts of CuZn-SOD. There was no evidence for accumulation of inactive protein in any of the groups. Immunoblots showed no evidence for the presence of any precipitates or other molecular forms of CuZn-SOD with higher molecular weight in the groups. About 25% of the CuZn-SOD subunits in CSF from controls shows an N-terminal truncation. This truncated portion does not differ between controls and ALS groups not carrying CuZn-SOD mutations, but is 70% larger in samples from D90A homozygous ALS patients. The findings suggest an essentially normal amount and activity of D90A mutant CuZn-SOD in CNS tissues of ALS cases. The increased occurrence of N-terminally truncated mutant subunits may indicate a difference in degradation routes compared with the wild-type enzyme, resistance against subsequent proteolytic steps and/or a compromised downstream proteolytic machinery. Molecular fragments accumulated to a greater extent from the D90A mutant enzyme might contribute to the motor neurone degeneration. We also determined the other SOD isoenzymes: in the controls, CuZn-SOD contributed 75%, extracellular SOD 25% and Mn-SOD <5% of the total SOD activity. There was no difference in the amount of extracellular SOD between any of the groups.

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