Linked Life Data

11514076

Source:http://linkedlifedata.com/resource/pubmed/id/11514076

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2001-8-21
pubmed:abstractText
Many structure-function studies of the glycine receptor (GlyR), and other ligand-gated ion channels, use somatic cell lines or Xenopus oocytes as expression systems. Using a polyethylenimine-based technique, we transfected GlyR cDNA into primary cultures of rat dorsal root ganglion (DRG) neurons. We then compared the functional properties of wildtype and a mutant GlyR expressed in DRG neurons with HEK 293 cells. The glycine sensitivity of the wildtype GlyR was nearly identical for the two cell types. The mutant GlyR has an arginine for glutamine substitution at position 271 (R271Q), which results in low glycine sensitivity relative to wildtype receptors expressed in HEK cells. This point mutation is associated with startle disease (hyperekplexia) in humans. Mutant GlyR expression in DRG neurons resulted in a significantly lower glycine sensitivity than was seen in HEK cells. This supports the idea that neuron-specific post-translational modifications may be important for determining receptor function.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0304-3940
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
309
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
202-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Expression of glycine receptors in rat sensory neurons vs. HEK293 cells yields different functional properties.
pubmed:affiliation
Department of Anesthesia & Critical Care, University of Chicago, 5841 S, Maryland Avenue, MC4028, Chicago, IL 60637, USA.
pubmed:publicationType
Journal Article, Comparative Study