抗VIAAT/SLC32A1/VGAT抗体 | Anti-VIAAT/SLC32A1/VGAT Antibody

• 価格
• Background

価格

目次に戻る

Background

Synaptic transmission involves the regulated exocytosis of vesicles containing neurotransmitters. The inhibitory neurotransmitter g-aminobutyric acid (GABA) is synthesized in the cytoplasm from L-glutamate by the enzyme glutamic acid decarboxylase (GAD) and loaded in synaptic vesicles for exocytosis. The vesicular GABA transporter (VGAT, also termed vesicular inhibitory amino acid transporter or VIAAT, 52-57 kDa) is responsible for the uptake of GABA into synaptic vesicles, following synthesis by GAD, or reuptake by plasma membrane GABA transporters (GATs). VGAT protein (55 kDa) contains ten transmembrane domains and belongs to a new family of vesicular neurotransmitter transporters. VGAT is highly conserved in mouse, rat and human (95-98% identity). VGAT uses both chemical and electrical components of the luminal protein gradient to mediate the accumulation of GABA into synaptic vesicles. VGAT is also responsible for glycine uptake in glycinergic neurons. VGAT is a homolog of the c. elegans unc -47 protein involved in GABA transport. Unc-47 is expressed in GABA neurons, localizes to synaptic vesicles and confers vesicular GABA transport in transfected cells. Mutants of c. elegans in which the unc-47 gene encoding VGAT is non-functional or absent, exhibit a complete loss of GABAergic function and elevated levels of GABA in the cytoplasm. VGAT is present in nerve endings of inhibitory neurons containing GABA, but also in glycinergic neurons in the brain and retina.1,4,5 At subcellular levels, VGAT specifically associates with synaptic vesicles. VGAT/VIAAT is also expressed in rat pancreatic islet cells.

目次に戻る