Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1997-5-22
pubmed:abstractText
gamma-Aminobutyric acid (GABA) plasma membrane transporters (GATs) influence synaptic neurotransmission by high-affinity uptake and release of GABA. The distribution and cellular localization of GAT-1, GAT-2, and GAT-3 in the rat retina have been evaluated by using affinity-purified polyclonal antibodies directed to the C terminus of each of these GAT subtypes. Small GAT-1-immunoreactive cell bodies were located in the proximal inner nuclear layer (INL) and ganglion cell layer (GCL), and processes were distributed to all laminae of the interplexiform layer (IPL). Varicose processes were in the optic fiber layer (OFL) and the outer plexiform layer (OPL). Weak GAT-1 immunostaining surrounded cells in the INL and GCL, and it was found in the OFL and OPL and in numerous processes in the outer nuclear layer (ONL) that ended at the outer limiting membrane. GAT-1 is therefore strongly expressed by amacrine, displaced amacrine, and interplexiform cells and weakly expressed by Müller cells. GAT-2 immunostaining was observed in the retina pigment epithelium and the nonpigmented ciliary epithelium. GAT-3 immunoreactivity was distributed to the OFL, to all laminae of the IPL, GCL and INL, and to processes in the ONL that ended at the outer limiting membrane. Small GAT-3-immunoreactive cell bodies were in the proximal INL and GCL. GAT-3 is therefore strongly expressed by Müller cells, and by some amacrine and displaced amacrine cells. Together, these observations demonstrate a heterologous distribution of GATs in the retina. These transporters are likely to take up GABA from, and perhaps release GABA into, the synaptic cleft and extracellular space. This suggests that GATs regulate GABA levels in these areas and thus influence synaptic neurotransmission.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-9967
pubmed:author
pubmed:issnType
Print
pubmed:day
11
pubmed:volume
375
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
212-24
pubmed:dateRevised
2011-8-1
pubmed:meshHeading
pubmed-meshheading:8915826-Amino Acid Sequence, pubmed-meshheading:8915826-Animals, pubmed-meshheading:8915826-Carrier Proteins, pubmed-meshheading:8915826-Epithelium, pubmed-meshheading:8915826-Eye Proteins, pubmed-meshheading:8915826-Female, pubmed-meshheading:8915826-GABA Plasma Membrane Transport Proteins, pubmed-meshheading:8915826-Immunohistochemistry, pubmed-meshheading:8915826-Male, pubmed-meshheading:8915826-Membrane Proteins, pubmed-meshheading:8915826-Membrane Transport Proteins, pubmed-meshheading:8915826-Molecular Sequence Data, pubmed-meshheading:8915826-Nerve Tissue Proteins, pubmed-meshheading:8915826-Organic Anion Transporters, pubmed-meshheading:8915826-Pigment Epithelium of Eye, pubmed-meshheading:8915826-Rats, pubmed-meshheading:8915826-Rats, Sprague-Dawley, pubmed-meshheading:8915826-Retina, pubmed-meshheading:8915826-Sequence Homology, Amino Acid, pubmed-meshheading:8915826-gamma-Aminobutyric Acid
pubmed:year
1996
pubmed:articleTitle
Multiple gamma-Aminobutyric acid plasma membrane transporters (GAT-1, GAT-2, GAT-3) in the rat retina.
pubmed:affiliation
Department of Neurobiology, UCLA School of Medicine 90095, USA. juliette@ucla.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.