EAAC1 is the major high-affinity L-glutamate transporter and expression is upregulated during differentiation of neonatal porcine enterocytes

被引:0
作者
Fan, MZ
Matthews, JC
Burrin, DG
Lackeyram, D
机构
[1] Univ Guelph, Guelph, ON N1G 2W1, Canada
[2] Univ Kentucky, Lexington, KY USA
[3] Baylor Coll Med, Dept Pediat, USDA ARS, Childrens Nutr Res Ctr, Houston, TX 77030 USA
关键词
D O I
暂无
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
引用
收藏
页码:A305 / A305
页数:1
相关论文
共 27 条
[21]   EFFECTS OF VARIATIONS IN IONIC CONCENTRATIONS ON HIGH-AFFINITY UPTAKE OF L-GLUTAMATE IN NON-GLUTAMATERGIC NEURONS AND NONNEURONAL CELLS CULTURED FROM NEONATAL RAT CORTEX [J].
BALCAR, VJ .
NEUROCHEMISTRY INTERNATIONAL, 1991, 18 (01) :43-49
[22]   Changes of high-affinity choline transporter CHT1 mRNA expression during degeneration and regeneration of hypoglossal nerves in mice [J].
Oshima, S ;
Yamada, K ;
Shirakawa, T ;
Watanabe, M .
NEUROSCIENCE LETTERS, 2004, 365 (02) :97-101
[23]   Complementary neuronal and glial expression of two high-affinity Glutamate transporter GLT1/EAAT2 forms in rat cerebral cortex [J].
Kugler, P ;
Schmitt, A .
HISTOCHEMISTRY AND CELL BIOLOGY, 2003, 119 (06) :425-435
[24]   Complementary neuronal and glial expression of two high-affinity glutamate transporter GLT1/EAAT2 forms in rat cerebral cortex [J].
Peter Kugler ;
Angelika Schmitt .
Histochemistry and Cell Biology, 2003, 119 :425-435
[25]   High-affinity glutamate transporter GLAST/EAAT1 regulates cell surface expression of glutamine/neutral amino acid transporter ASCT2 in human fetal astrocytes [J].
Gegelashvili, M ;
Rodriguez-Kern, A ;
Pirozhkova, I ;
Zhang, J ;
Sung, L ;
Gegelashvili, G .
NEUROCHEMISTRY INTERNATIONAL, 2006, 48 (6-7) :611-615
[26]   Human high affinity, Na+-dependent L-glutamate/L-aspartate transporter GLAST-1 (EAAT-1): Gene structure and localization to chromosome 5p11-p12 [J].
Stoffel, W ;
Sasse, J ;
Duker, M ;
Muller, R ;
Hofmann, K ;
Fink, T ;
Lichter, P .
FEBS LETTERS, 1996, 386 (2-3) :189-193
[27]   3-((+/-)2-CARBOXYPIPERAZIN-4-YL)PROPYL-1-PHOSPHONIC ACID (CPP) MORE POTENTLY ANTAGONIZES THE HIGH-AFFINITY MG2+ BINDING-SITE ON THE N-METHYL-D-ASPARTATE PHENCYCLIDINE RECEPTOR ION CHANNEL COMPLEX THAN THE L-GLUTAMATE RECOGNITION SITE [J].
HATTA, K ;
YAMAMOTO, T ;
HORI, T ;
OKUWA, M ;
MOROJI, T .
NEUROSCIENCE LETTERS, 1991, 124 (02) :229-231