Linked Life Data

9425012

Source:http://linkedlifedata.com/resource/pubmed/id/9425012

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1998-2-3
pubmed:abstractText
The rapid re-uptake of extracellular glutamate mediated by a family of high-affinity glutamate transporter proteins is essential to continued glutamatergic signaling and neuronal viability, but the contributions of individual transporter subtypes toward cellular physiology are poorly understood. Because the physiology of glutamate transport in the salamander retina has been well described, we have examined the expression and function of glutamate transporter subtypes in this preparation. cDNAs encoding five distinct salamander excitatory amino acid transporter (sEAAT) subtypes were isolated, and their molecular properties and distributions of expression were compared. We report evidence that at least four distinct sEAAT subtypes are expressed in glial (Müller) cells. In addition, four of the five transporter subtypes are localized in neurons throughout the retina. The brightest immunostaining was seen in the synaptic regions of the inner and outer plexiform layers and in the outer nuclear layer. Using electrophysiological measurements in the Xenopus oocyte expression system, we also examined the pharmacology and ionic dependence of the four expressing transporter subtypes that make it possible to distinguish, on the basis of functional behavior, among the various subtypes. Although no simple correlation between transporter subtype and retinal cell physiology can be made, the diverse population of sEAAT transporter subtypes with unique localization and functional properties indicates that glutamate transporters play a wide variety of roles in retinal function and are likely to underlie both the uptake of glutamate by Müller cells and the glutamate-elicited chloride conductance involved in signal transduction by photoreceptors and bipolar cells.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0270-6474
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
18
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
698-712
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:9425012-ATP-Binding Cassette Transporters, pubmed-meshheading:9425012-Ambystoma, pubmed-meshheading:9425012-Amino Acid Sequence, pubmed-meshheading:9425012-Amino Acid Transport System X-AG, pubmed-meshheading:9425012-Animals, pubmed-meshheading:9425012-Base Sequence, pubmed-meshheading:9425012-Carrier Proteins, pubmed-meshheading:9425012-Chloride Channels, pubmed-meshheading:9425012-Excitatory Amino Acid Transporter 2, pubmed-meshheading:9425012-Eye Proteins, pubmed-meshheading:9425012-Gene Expression, pubmed-meshheading:9425012-Molecular Sequence Data, pubmed-meshheading:9425012-Oligonucleotides, Antisense, pubmed-meshheading:9425012-Receptors, Glutamate, pubmed-meshheading:9425012-Receptors, Neurotransmitter, pubmed-meshheading:9425012-Retina, pubmed-meshheading:9425012-Xenopus
pubmed:year
1998
pubmed:articleTitle
Excitatory amino acid transporters of the salamander retina: identification, localization, and function.
pubmed:affiliation
Vollum Institute, Oregon Health Sciences University, Portland, Oregon 97201, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't