H55N polymorphism as a likely cause of variation in citrate synthase activity of mouse skeletal muscle

2.50
Hdl Handle:
http://hdl.handle.net/10547/296164
Title:
H55N polymorphism as a likely cause of variation in citrate synthase activity of mouse skeletal muscle
Authors:
Ratkevicius, Aivaras; Carroll, Andrew M.; Kilikevicius, Audrius; Venckunas, Tomas; McDermott, Kevin T.; Gray, Stuart R.; Wackerhage, Henning; Lionikas, Arimantas
Abstract:
The aim of this study was to investigate the mechanisms underlying low activity of citrate synthase (CS) in A/J mice compared with other inbred strains of mice. Enzyme activity, protein content, and mRNA levels of CS were studied in the quadriceps muscles of A/J, BALB/cByJ, C57BL/6J, C3H/HeJ, DBA/2J, and PWD/PhJ strains of mice. Cytochrome c protein content was also measured. The results of the study indicate that A/J mice have a 50–65% reduction in CS activity compared with other strains despite similar levels of Cs mRNA and lack of differences in CS and cytochrome c protein content. CS from A/J mice also showed lower Michaelis constant (Km) for both acetyl CoA and oxaloacetate compared with the other strains of mice.
Citation:
Ratkevicius, A., Carroll, A.M., Kilikevicius, A. et al. (2010) 'H55N polymorphism as a likely cause of variation in citrate synthase activity of mouse skeletal muscle', Physiological Genomics, 42A (2), pp.96-102
Publisher:
American Physiological Society
Journal:
Physiological Genomics
Issue Date:
2010
URI:
http://hdl.handle.net/10547/296164
DOI:
10.1152/physiolgenomics.00066.2010
Additional Links:
http://physiolgenomics.physiology.org/cgi/doi/10.1152/physiolgenomics.00066.2010
Type:
Article
Language:
en
ISSN:
1094-8341; 1531-2267
Appears in Collections:
Muscle Cellular and Molecular Physiology

Full metadata record

DC FieldValue Language
dc.contributor.authorRatkevicius, Aivarasen_GB
dc.contributor.authorCarroll, Andrew M.en_GB
dc.contributor.authorKilikevicius, Audriusen_GB
dc.contributor.authorVenckunas, Tomasen_GB
dc.contributor.authorMcDermott, Kevin T.en_GB
dc.contributor.authorGray, Stuart R.en_GB
dc.contributor.authorWackerhage, Henningen_GB
dc.contributor.authorLionikas, Arimantasen_GB
dc.date.accessioned2013-07-16T10:10:09Z-
dc.date.available2013-07-16T10:10:09Z-
dc.date.issued2010-
dc.identifier.citationRatkevicius, A., Carroll, A.M., Kilikevicius, A. et al. (2010) 'H55N polymorphism as a likely cause of variation in citrate synthase activity of mouse skeletal muscle', Physiological Genomics, 42A (2), pp.96-102en_GB
dc.identifier.issn1094-8341-
dc.identifier.issn1531-2267-
dc.identifier.doi10.1152/physiolgenomics.00066.2010-
dc.identifier.urihttp://hdl.handle.net/10547/296164-
dc.description.abstractThe aim of this study was to investigate the mechanisms underlying low activity of citrate synthase (CS) in A/J mice compared with other inbred strains of mice. Enzyme activity, protein content, and mRNA levels of CS were studied in the quadriceps muscles of A/J, BALB/cByJ, C57BL/6J, C3H/HeJ, DBA/2J, and PWD/PhJ strains of mice. Cytochrome c protein content was also measured. The results of the study indicate that A/J mice have a 50–65% reduction in CS activity compared with other strains despite similar levels of Cs mRNA and lack of differences in CS and cytochrome c protein content. CS from A/J mice also showed lower Michaelis constant (Km) for both acetyl CoA and oxaloacetate compared with the other strains of mice.en_GB
dc.language.isoenen
dc.publisherAmerican Physiological Societyen_GB
dc.relation.urlhttp://physiolgenomics.physiology.org/cgi/doi/10.1152/physiolgenomics.00066.2010en_GB
dc.rightsArchived with thanks to Physiological Genomicsen_GB
dc.subjectinbred strainsen_GB
dc.subjectoxidative phosphorylationen_GB
dc.subjectpolymorphismsen_GB
dc.titleH55N polymorphism as a likely cause of variation in citrate synthase activity of mouse skeletal muscleen
dc.typeArticleen
dc.identifier.journalPhysiological Genomicsen_GB
All Items in UOBREP are protected by copyright, with all rights reserved, unless otherwise indicated.