Linked Life Data

8998501

Source:http://linkedlifedata.com/resource/pubmed/id/8998501

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1997-1-23
pubmed:abstractText
The role of N-glycans in the secretion of glycoproteins by suspension-cultured sycamore cells was studied. The transport of glycoproteins to the extracellular compartment was investigated in the presence of a glycan-processing inhibitor, castanospermine. Castanospermine has been selected because it inhibits homogeneously glycan maturation in sycamore cells and leads to the accumulation of a single immature N-glycan. The structure of this glycan has been identified as Glc3Man7GlcNAc2 by labeling experiments, affinity chromatography on concanavalin A-Sepharose and proton NMR. In contrast with previous results showing that N-glycosylation is a prerequisite for secretion of N-linked glycoproteins, this secretion is not affected by the presence of castanospermine. As a consequence, the presence of this unprocessed glycan is sufficient for an efficient secretion of glycoproteins in the extracellular compartment of suspension-cultured sycamore cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0960-7412
pubmed:author
pubmed:issnType
Print
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
713-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
N-linked oligosaccharide processing is not necessary for glycoprotein secretion in plants.
pubmed:affiliation
Centre Régional Universitaire de Spectroscopie, CNRS-URA 464, Mont Saint Aignan, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't