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Low levels of citrin (SLC25A13) expression in adult mouse brain restricted to neuronal clusters
Journal of neuroscience research, 2010-04, Vol.88 (5), p.1009-1016
Contreras, Laura
Urbieta, Almudena
Kobayashi, Keiko
Saheki, Takeyori
Satrústegui, Jorgina
2010
Volltextzugriff (PDF)
Details
Autor(en) / Beteiligte
Contreras, Laura
Urbieta, Almudena
Kobayashi, Keiko
Saheki, Takeyori
Satrústegui, Jorgina
Titel
Low levels of citrin (SLC25A13) expression in adult mouse brain restricted to neuronal clusters
Ist Teil von
Journal of neuroscience research, 2010-04, Vol.88 (5), p.1009-1016
Ort / Verlag
Hoboken: Wiley Subscription Services, Inc., A Wiley Company
Erscheinungsjahr
2010
Quelle
MEDLINE
Beschreibungen/Notizen
The mitochondrial aspartate‐glutamate carriers (AGC) aralar (SLC25A12) and citrin (SLC25A13) are components of the malate aspartate shuttle (MAS), a major intracellular pathway to transfer reducing equivalents from NADH to the mitochondrial matrix. Aralar is the main AGC isoform present in the adult brain, and it is expressed mainly in neurons. To search for the other AGC isoform, citrin, in brain glial cells, we used a citrin knockout mouse in which the lacZ gene was inserted into the citrin locus as reporter gene. In agreement with the low citrin levels known to be present in the adult mouse brain, β‐galactosidase expression was very low. Surprisingly, unlike the case with astroglial cultures that express citrin, no β‐galactosidase was found in brain glial cells. It was confined to neuronal cells within discrete neuronal clusters. Double‐immunolabelling experiments showed that β‐galactosidase colocalized not with glial cell markers but with the pan‐neuronal marker NeuN. The deep cerebellar nuclei and a few midbrain nuclei (reticular tegmental pontine nuclei; magnocellular red nuclei) were the regions where β‐galactosidase expression was highest, and it was up‐regulated in fasted mice, as was also the case for liver β‐galactosidase. The results support the notion that glial cells have much lower AGC levels and MAS activity than neurons. © 2009 Wiley‐Liss, Inc.
Sprache
Englisch
Identifikatoren
ISSN: 0360-4012, 1097-4547
eISSN: 1097-4547
DOI: 10.1002/jnr.22283
Titel-ID: cdi_proquest_miscellaneous_883014909
Format
–
Schlagworte
Animals
,
aralar
,
Aspartic Acid - metabolism
,
beta-Galactosidase - analysis
,
beta-Galactosidase - genetics
,
beta-Galactosidase - metabolism
,
Biomarkers - analysis
,
Biomarkers - metabolism
,
Brain - cytology
,
Brain - metabolism
,
Brain Mapping - methods
,
Calcium-Binding Proteins - analysis
,
Calcium-Binding Proteins - genetics
,
Calcium-Binding Proteins - metabolism
,
cerebellum
,
citrin
,
fasting
,
Food Deprivation - physiology
,
Genes, Reporter - physiology
,
Immunohistochemistry
,
Lac Operon - physiology
,
Liver - metabolism
,
Malates - metabolism
,
Metabolic Networks and Pathways - physiology
,
Mice
,
Mice, Knockout
,
mitochondrial aspartate-glutamate carrier
,
Nerve Tissue Proteins - metabolism
,
Neuroglia - cytology
,
Neuroglia - metabolism
,
neuron
,
Neurons - cytology
,
Neurons - metabolism
,
Nuclear Proteins - metabolism
,
OmniBank
,
Organic Anion Transporters - analysis
,
Organic Anion Transporters - genetics
,
Organic Anion Transporters - metabolism
,
redox shuttle
,
Staining and Labeling
,
Up-Regulation - physiology
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