Cellular distribution of branched-chain amino acid aminotransferase isoenzymes among rat brain glial cells in culture

被引:69
作者
Bixel, MG
Hutson, SM
Hamprecht, B
机构
[1] UNIV TUBINGEN, INST PHYSIOL CHEM, D-72076 TUBINGEN, GERMANY
[2] WAKE FOREST UNIV, BOWMAN GRAY SCH MED, DEPT BIOCHEM, WINSTON SALEM, NC 27103 USA
关键词
astroglial cells; energy metabolism; immunocytochemistry; nitrogen metabolism; oligodendroglial cells; O2A progenitor cells;
D O I
10.1177/002215549704500506
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
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.
引用
收藏
页码:685 / 694
页数:10
相关论文
共 50 条
[1]   TRACING THE DEVELOPMENT OF OLIGODENDROCYTES FROM PRECURSOR CELLS USING MONOCLONAL-ANTIBODIES, FLUORESCENCE-ACTIVATED CELL SORTING, AND CELL-CULTURE [J].
ABNEY, ER ;
WILLIAMS, BP ;
RAFF, MC .
DEVELOPMENTAL BIOLOGY, 1983, 100 (01) :166-171
[2]   TRANSAMINASE OF BRANCHED CHAIN AMINO ACIDS .3. PURIFICATION AND PROPERTIES OF MITOCHONDRIAL ENZYME FROM HOG HEART AND COMPARISON WITH SUPERNATANT ENZYME [J].
AKI, K ;
OGAWA, K ;
SHIRAI, A ;
ICHIHARA, A .
JOURNAL OF BIOCHEMISTRY, 1967, 62 (05) :610-&
[3]   HIGH ACTIVITY OF CHOLINE-ACETYLTRANSFERASE INDUCED IN NEUROBLASTOMA - GLIA HYBRID CELLS [J].
AMANO, T ;
HAMPRECHT, B ;
KEMPER, W .
EXPERIMENTAL CELL RESEARCH, 1974, 85 (02) :399-408
[4]  
[Anonymous], ADV CELL NEUROBIOL
[5]   LOCATIONS OF AMINO-ACIDS IN BRAIN SLICES FROM RAT - TETRODOTOXIN-SENSITIVE RELEASE OF AMINO-ACIDS [J].
BENJAMIN, AM ;
QUASTEL, JH .
BIOCHEMICAL JOURNAL, 1972, 128 (03) :631-&
[6]  
BERL S, 1977, DYNAMIC PROPERTIES G, P143
[7]   LOCALIZATION OF GLIAL FIBRILLARY ACIDIC PROTEIN IN ASTROCYTES BY IMMUNOFLUORESCENCE [J].
BIGNAMI, A ;
ENG, LF ;
DAHL, D ;
UYEDA, CT .
BRAIN RESEARCH, 1972, 43 (02) :429-&
[8]  
Bixel M. G., 1995, Biological Chemistry Hoppe-Seyler, V376, pS86
[9]  
BIXEL MG, 1995, J NEUROCHEM, V65, P2450
[10]  
BIXEL MG, 1994, J NEUROCHEM, V63, pS62