Cited by 78Amino Acid Enzymes and MetabolismMetabolism and Genetic DisordersNeuroscience and Neuropharmacology Research

Cellular Distribution of Branched-chain Amino Acid Aminotransferase Isoenzymes Among Rat Brain Glial Cells in Culture

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Bixel, M. Gabriele, Hutson, Susan M., Hamprecht, Bernd·1997·Journal of Histochemistry & Cytochemistry

Abstract

The first step in the catabolism of branched-chain amino acids (BCAA), reversible transamination, is catalyzed by one of the two isoforms of branched-chain amino acid aminotransferase (BCAT). The mitochondrial isoenzyme (BCATm) is widely distributed among tissues, whereas the cytosolic isoenzyme (BCATc) is restricted to only a few organs. Remarkably, BCATc is the prominent isoenzyme found in brain. The physiological significance of the subcellular compartmentation of BCAT is still not understood. To contribute to the elucidation of the cellular distribution of the two isoenzymes in brain, we used cultured rat glial cells in an immunocytochemical study to determine the pattern of BCAT isoenzyme expression by glial cells. Antiserum against BCATm generated a punctate staining pattern of astroglial cells, confirming the mitochondrial location of this isoenzyme. In contrast, the cytosol of galactocerebroside-expressing oligodendroglial cells and O2A progenitor cells displayed intense staining only for BCATc. In addition, subpopulations of astroglial cells exhibited BCATc immunoreactivity. The presence of BCATm in astrocytes is consistent with the known ability of these cells to oxidize BCAA. Furthermore, our results on BCATc provide support for the hypothesis that BCATs are also involved in nitrogen transfer from astrocytes to neurons.

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Research works printed but not linked: 2

  1. Hamberger A, Cotman CW, Sellström A, Weiler CT (1977) Gluta- mine, glial cells and their relationship to transmitter glutamate. In Schoffeniels E, Frank G, Hertz L, Tower DB, eds. Dynamic Properties of Glia Cells. Oxford, Pergamon Press, 163-172
  2. Ichihara A (1985) Aminotransferases of branched-chain amino ac- ids. In Christen P, Metzler DE, eds. Transaminases. Vol 2. New York, John Wiley & Sons, 430-438

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Authors
Bixel, M. G., Hutson, S. M., & Hamprecht, B.
Affiliations
University of Tübingen (DE)
Venue
Journal of Histochemistry & Cytochemistry
Published
1997-05
Volume
45
Issue
5
Pages
685-694
ISSN
  • 0022-1554 (ISSN-L)
  • 1551-5044
OpenAlex
W2154403203
Cited by
78
References
46
Citations by year
2026: 1 · 2024: 1 · 2022: 2 · 2020: 4 · 2019: 1 · 2018: 3 · 2017: 4 · 2016: 2 · 2015: 3 · 2014: 3 · 2013: 3 · 2012: 3
FWCI
0.99
Type
journal article
Language
en
Open access
Locations
  • Journal of Histochemistry & Cytochemistry (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • Eberhard Karls Universität Tübingen
  • National Institutes of Health
  • National Institute of Diabetes and Digestive and Kidney Diseases (DK34738)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Metabolism and Genetic Disorders
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
Keywords
branched-chain amino acid aminotransferase, brain glial cells, astrocytes, oligodendrocytes, galactocerebroside, branched-chain amino acid catabolism, mitochondrial isoenzyme, cytosolic isoenzyme
MeSH terms
Amino Acids, Branched-Chain, Transaminases, Animals, Brain, Cells, Cultured, Galactosylceramides, Glial Fibrillary Acidic Protein, Isoenzymes, Neuroglia, Blotting, Western, Rats, Wistar, Rats

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