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WFRF:(Glass D)
 

Sökning: WFRF:(Glass D) > Comprehensive analy...

LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00003296nam a2200325 4500
001oai:DiVA.org:umu-124955
003SwePub
008160831| | |||||||||||000 ||eng|
0247 a https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-1249552 URI
040 a (SwePub)umu
041 a engb eng
042 9 SwePub
072 7a vet2 swepub-contenttype
072 7a ovr2 swepub-publicationtype
1001 a Keskin, Isil,d 1987-u Umeå universitet,Klinisk neurovetenskap4 aut0 (Swepub:umu)iske0003
2451 0a Comprehensive analysis to explain reduced or increased SOD1 enzymatic activity in erythrocytes in ALS patients and their relatives
338 a print2 rdacarrier
520 a Our objective was to in blood samples from 3723 individuals including ALS patients without a coding SOD1 mutation and 372 control individuals characterize stabilities of mutant SOD1s, 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. Erythrocyte SOD1 enzymatic activities normalized to hemoglobin content were determined. Coding SOD1 sequences were analyzed by Sanger sequencing, copy number variations by fragment length analysis and by TaqMan Assay. Hemoglobin disorders were searched for. Of the 46 SOD1 mutations found, ¾ caused severe destabilization of the mutant protein but in ¼ SOD1 was essentially physically stable. Mutations producing structural changes all caused halved SOD activities. There were no differences in SOD1 activities between controls and patients without any detected SOD1 mutations or patients with C9ORF72HRE or TBK1 mutations. In the low and high SOD1 activity groups no deviations were found in exon copy numbers and intron gross structures. Also, no uncommon variants in exon-flanking sequences were detected. Thalassemias and iron deficiency anemia were associated with increased SOD1 activity/hemoglobin ratios. In conclusion, adjunct erythrocyte SOD activity analysis is of value to signal the presence of exon and splice-site-intron mutations that influence the SOD1 structure.
650 7a NATURVETENSKAPx Biologix Biokemi och molekylärbiologi0 (SwePub)106022 hsv//swe
650 7a NATURAL SCIENCESx Biological Sciencesx Biochemistry and Molecular Biology0 (SwePub)106022 hsv//eng
7001 a Birve, Annau Umeå universitet,Klinisk neurovetenskap4 aut0 (Swepub:umu)anbi0001
7001 a Berdynski, Mariuszu Umeå universitet,Klinisk neurovetenskap4 aut0 (Swepub:umu)mabe0489
7001 a Hjertkvist, Karinu Umeå universitet,Institutionen för medicinsk biovetenskap4 aut0 (Swepub:umu)kahj0001
7001 a Rofougaran, Rezau Umeå universitet,Klinisk neurovetenskap4 aut0 (Swepub:umu)rearon05
7001 a Nilsson, Torbjörn K.u Umeå universitet,Institutionen för medicinsk biovetenskap4 aut0 (Swepub:umu)toni0049
7001 a Glass, Jonathan D.4 aut
7001 a Marklund, Stefan L.u Umeå universitet,Institutionen för medicinsk biovetenskap4 aut0 (Swepub:umu)stma0003
7001 a Andersen, Peter M.u Umeå universitet,Klinisk neurovetenskap4 aut0 (Swepub:umu)pean0001
7102 a Umeå universitetb Klinisk neurovetenskap4 org
8564 8u https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-124955

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