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Titolo:
THE VESICULAR GABA TRANSPORTER, VGAT, LOCALIZES TO SYNAPTIC VESICLES IN SETS OF GLYCINERGIC AS WELL AS GABAERGIC NEURONS
Autore:
CHAUDHRY FA; REIMER RJ; BELLOCCHIO EE; DANBOLT NC; OSEN KK; EDWARDS RH; STORMMATHISEN J;
Indirizzi:
UNIV OSLO,INST ANAT,POB 1105 BLINDERN N-0317 OSLO NORWAY UNIV OSLO,INST BASIC MED SCI,DEPT ANAT N-0317 OSLO NORWAY UNIV CALIF SAN FRANCISCO,SCH MED,DEPT NEUROL SAN FRANCISCO CA 94143 UNIV CALIF SAN FRANCISCO,SCH MED,DEPT PHYSIOL SAN FRANCISCO CA 94143
Titolo Testata:
The Journal of neuroscience
fascicolo: 23, volume: 18, anno: 1998,
pagine: 9733 - 9750
SICI:
0270-6474(1998)18:23<9733:TVGTVL>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
GAMMA-AMINOBUTYRIC ACID; ELECTRON-MICROSCOPIC IMMUNOCYTOCHEMISTRY; SUPERIOR OLIVARY COMPLEX; NEUROACTIVE AMINO-ACIDS; CAT SPINAL MOTONEURONS; RAT HIPPOCAMPAL REGION; GLUTAMATE-DECARBOXYLASE; GUINEA-PIG; VISUAL-CORTEX; IMMUNOREACTIVE TERMINALS;
Keywords:
NEUROTRANSMITTER TRANSPORT; SYNAPTIC VESICLES; GABA; GLYCINE; ANTIBODIES; IMMUNOGOLD; MICROSCOPY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
86
Recensione:
Indirizzi per estratti:
Citazione:
F.A. Chaudhry et al., "THE VESICULAR GABA TRANSPORTER, VGAT, LOCALIZES TO SYNAPTIC VESICLES IN SETS OF GLYCINERGIC AS WELL AS GABAERGIC NEURONS", The Journal of neuroscience, 18(23), 1998, pp. 9733-9750

Abstract

A transporter thought to mediate accumulation of GABA into synaptic vesicles has recently been cloned (McIntire et al., 1997). This vesicular GABA transporter (VGAT), the first vesicular amino acid transporterto be molecularly identified, differs in structure from previously cloned vesicular neurotransmitter transporters and defines a novel gene family. Here we use antibodies specific for N- and C-terminal epitopesof VGAT to localize the protein in the rat CNS. VGAT is highly concentrated in the nerve endings of GABAergic neurons in the brain and spinal cord but also in glycinergic nerve endings. In contrast, hippocampal mossy fiber boutons, which although glutamatergic are known to contain GABA, lack VGAT immunoreactivity. Post-embedding immunogold quantification shows that the protein specifically associates with synaptic vesicles. Triple labeling for VGAT, GABA, and glycine in the lateral oliva superior revealed a higher expression of VGAT in nerve endings rich in GABA, with or without glycine, than in others rich in glycine only. Although the great majority of nerve terminals containing GABA or glycine are immunopositive for VGAT, subpopulations of nerve endings rich in GABA or glycine appear to lack the protein. Additional vesiculartransporters or alternative modes of release may therefore contributeto the inhibitory neurotransmission mediated by these two amino acids.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/09/20 alle ore 05:50:19