Linked Life Data

11384608

Source:http://linkedlifedata.com/resource/pubmed/id/11384608

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2001-5-31
pubmed:abstractText
One of the vitally important functions of glutathione (GSH) is to adequately protect cells against toxic chemicals, reactive oxygen metabolites and free radical species. The amino acid, cysteine, is the key rate-limiting substrate for the biosynthesis of GSH, and the maintenance of adequate intracellular GSH levels is dependent upon the extracellular availability and transport of cysteine into cells. In the present study, primary cultures of astrocytes and neurons were employed to characterize cysteine transport systems. Both astrocytes and neurons used Na(+)-dependent systems as the major route for cysteine uptake (80-90% of total), while Na(+)-independent uptake represented a minor component of total transport (10-20% of total). Among the Na(+)-dependent systems, X(AG(-)) was the major contributor (approx. 80-90%) for cysteine uptake in both neurons and astrocytes, with a minor contribution from the ASC transport system (Na(+)-dependent neutral amino acid transport system for alanine, serine, and cysteine). In the Na(+)-independent transport systems (10-20% of total cysteine transport), multifunctional ectoenzyme/amino acid transporter gamma-glutamyltranspeptidase (GGT), and the neutral amino acid L-system contributed approximately equally towards cysteine uptake, in both neurons and astrocytes. The present studies demonstrate that astrocytes and neurons accumulate cysteine by both Na(+)-dependent and Na(+)-independent uptake systems, with major uptake occurring through the X(AG(-)) system and minor uptake via the ASC, GGT and L-systems.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0006-8993
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
902
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
156-63
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:11384608-Amino Acid Transport System X-AG, pubmed-meshheading:11384608-Animals, pubmed-meshheading:11384608-Animals, Newborn, pubmed-meshheading:11384608-Astrocytes, pubmed-meshheading:11384608-Carrier Proteins, pubmed-meshheading:11384608-Cells, Cultured, pubmed-meshheading:11384608-Central Nervous System, pubmed-meshheading:11384608-Cysteine, pubmed-meshheading:11384608-Drug Interactions, pubmed-meshheading:11384608-Enzyme Inhibitors, pubmed-meshheading:11384608-Glutamate Plasma Membrane Transport Proteins, pubmed-meshheading:11384608-Glutathione, pubmed-meshheading:11384608-Neurons, pubmed-meshheading:11384608-Rats, pubmed-meshheading:11384608-Rats, Sprague-Dawley, pubmed-meshheading:11384608-Reactive Oxygen Species, pubmed-meshheading:11384608-Sodium, pubmed-meshheading:11384608-Sulfur Radioisotopes, pubmed-meshheading:11384608-Symporters
pubmed:year
2001
pubmed:articleTitle
The uptake of cysteine in cultured primary astrocytes and neurons.
pubmed:affiliation
Department of Physiology and Pharmacology, Wake Forest University School of Medicine, Medical Center Blvd., 27157-1083, Winston-Salem, NC, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.