Linked Life Data

9422381

Source:http://linkedlifedata.com/resource/pubmed/id/9422381

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1998-2-2
pubmed:abstractText
The alpha7 subunit of the neuronal nicotinic acetylcholine receptor, when expressed in Xenopus oocytes, forms homooligomeric ligand-gated ion channels that are blocked by a snake toxin, alpha-bungarotoxin. The amino-terminal extracellular domain of the alpha7 sequence has three consensus sites for asparagine-linked glycosylation (N46DS, N90MS, and N133AS). In this study, we show that alpha7 expressed either in vivo or in vitro is a glycoprotein of 57 kDa. In addition, we demonstrate by site-directed mutagenesis that all three consensus sites are used for glycosylation. To elucidate the role(s) of asparagine-linked glycosylation in the formation and function of the alpha7 receptor, wild-type and glycosylation-deficient alpha7 subunits were expressed in COS cells and oocytes. We examined biochemical and physiological properties of expressed receptors and found that alpha7 glycosylation mutations do not affect homooligomerization and surface protein expression of the alpha7 receptor but do affect surface expression of alpha-bungarotoxin binding sites and the function of the receptor. Our data indicate that asparagine-linked glycosylation is required for the expression of a functional alpha7 receptor in oocytes.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0022-3042
pubmed:author
pubmed:issnType
Print
pubmed:volume
70
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
349-57
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Contributions of N-linked glycosylation to the expression of a functional alpha7-nicotinic receptor in Xenopus oocytes.
pubmed:affiliation
Division of Neuroscience, Baylor College of Medicine, Houston, Texas 77030, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.