Abstract:
:Intense glucose-based energy metabolism and glutamate synthesis by astrocytes require malate-aspartate-shuttle (MAS) activity to regenerate NAD⁺ from NADH formed during glycolysis, since brain lacks significant glycerophosphate shuttle activity. Aralar is a necessary aspartate/glutamate exchanger for MAS function in brain. Based on cytochemical immunoassays the absence of aralar in adult astrocytes was repeatedly reported. This would mean that adult astrocytes must regenerate NAD⁺ by producing lactate from pyruvate, eliminating its use by oxidative and biosynthetic pathways. We alternatively used astrocytes and neurons from adult brain, freshly isolated by fluorescence-activated cell sorting, to determine aralar protein by a specific antibody and its mRNA by real-time PCR. Both protein and mRNA expressions were identical in adult neurons and astrocytes and similar to whole brain levels. The same level of aralar expression was reached in well-differentiated astrocyte cultures, but not until late development, coinciding with the late-maturing brain capability for glutamate formation and degradation.
journal_name
Neurochem Intjournal_title
Neurochemistry internationalauthors
Li B,Hertz L,Peng Ldoi
10.1016/j.neuint.2012.09.009subject
Has Abstractpub_date
2012-12-01 00:00:00pages
1325-32issue
8eissn
0197-0186issn
1872-9754pii
S0197-0186(12)00294-Xjournal_volume
61pub_type
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