ID 83835
Author
Yao, Dengbing Division of Enzyme Chemistry, Institute for Enzyme Research, the University of Tokushima
Yao, Min Division of Enzyme Chemistry, Institute for Enzyme Research, the University of Tokushima
Yamaguchi, Miyoko Division of Enzyme Chemistry, Institute for Enzyme Research, the University of Tokushima
Chida, Junji Division of Enzyme Chemistry, Institute for Enzyme Research, the University of Tokushima Tokushima University Educator and Researcher Directory KAKEN Search Researchers
Kido, Hiroshi Division of Enzyme Chemistry, Institute for Enzyme Research, the University of Tokushima Tokushima University Educator and Researcher Directory KAKEN Search Researchers
Keywords
carnitine palmitoyltransferase-II
missense mutation
half-life
COS-7 cells
Content Type
Journal Article
Description
Background : In mammals, carnitine palmitoyltransferase (CPT) system is a pivotal
component of energy metabolism through mitochondrial fatty acid oxidation. The majority
of patients with fatal or handicapped influenza-associated encephalopathy exhibit
thermolabile compound homo/heterozygous mutations of CPT II. Objective : Compound
CPT II mutations, [c.647A G (p.Q216R)], [c.1102G A (p.V368I)], [c.1939A G (p.M647V)]
and [c.745delG (p.G249EfsX16)], were found in a patient with adenovirus-associated encephalopathy
and his family. The properties of these CPT II mutations were analyzed in
COS-7 cells. Methods : CPT II mutations in the patient and his family were expressed in
COS-7 cells and their molecular masses, enzyme activities, thermal instabilities and halflives
were analyzed. Results : We identified two novel CPT II mutations in the patient,
[c.647A G (p.Q216R)] and [c.745delG (p.G249EfsX16)]. The CPT II Q216R mutation showed
mild reduction of activity, thermal instability and short half-life but compound mutations
with Q216R+V368I+M647V showed further enhancement of these disabilities, although
mutations V368I and M647V had no such effects. CPT II mutation [c.745delG (p.G249
EfsX16)] abolished enzyme activity and showed short half-life. Conclusion : The thermal
instability and short half-life of the novel CPT II mutations, [c.647A G (p.Q216R)] and
[c.745delG (p.G249EfsX16)], could play important roles in energy crisis in the pathogenesis
of virus-associated encephalopathy.
Journal Title
The journal of medical investigation : JMI
ISSN
13431420
NCID
AA11166929
Volume
58
Issue
3-4
Start Page
210
End Page
218
Sort Key
210
Published Date
2011-08
Remark
The journal of medical investigation : http://medical.med.tokushima-u.ac.jp/jmi/index.html
EDB ID
FullText File
language
eng
departments
Institute of Advanced Medical Sciences