Linked Life Data

2148115

Source:http://linkedlifedata.com/resource/pubmed/id/2148115

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
35
pubmed:dateCreated
1991-2-7
pubmed:abstractText
When MDCK cells were incubated in the presence of the protein synthesis inhibitor puromycin or cycloheximide, there was a rapid and concentration-dependent inhibition in the incorporation of [2-3H]mannose into lipid-linked oligosaccharide and into protein. However, mannose incorporation into dolichyl-P-mannose was not affected. Interestingly, these inhibitors did block [6-3H]glucosamine incorporation into dolichyl-PP-GlcNAc as well as into lipid-linked oligosaccharides. Similar results were obtained when other cell lines were used and also when inhibitors of protein glycosylation such as beta-hydroxynorvaline and beta-fluoroasparagine were used. Cells incubated in puromycin did not show any changes in the levels of sugar nucleotides, GDP-mannose or UDP-GlcNAc, or in the in vitro activities of the glycosyltransferases that add mannose to the lipid-linked oligosaccharides. The inhibition of mannose incorporation into lipid-linked oligosaccharides could not be overcome by addition of dolichyl-P to the inhibited cells, even though the addition of dolichyl-P to control cells stimulated mannose incorporation into dolichyl-P-mannose, lipid-linked oligosaccharides, and protein from 3- to 5-fold. Thus, limitations in the levels of dolichyl-P do not appear to be a major factor in this inhibition. On the other hand, addition of the tripeptide acceptor N-acyl-Asn-Try-Thr did overcome the puromycin inhibition to some extent, suggesting that accumulation of some intermediate such as lipid-linked oligosaccharides might be involved in the inhibition.
pubmed:grant
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
4
pubmed:volume
29
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8077-84
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:2148115-Amino Acid Sequence, pubmed-meshheading:2148115-Animals, pubmed-meshheading:2148115-Carbohydrate Sequence, pubmed-meshheading:2148115-Cattle, pubmed-meshheading:2148115-Cell Line, pubmed-meshheading:2148115-Dolichol Monophosphate Mannose, pubmed-meshheading:2148115-Dolichol Phosphates, pubmed-meshheading:2148115-Fibroblasts, pubmed-meshheading:2148115-Glucosyltransferases, pubmed-meshheading:2148115-Glycolipids, pubmed-meshheading:2148115-Glycoproteins, pubmed-meshheading:2148115-Kidney, pubmed-meshheading:2148115-Mannose, pubmed-meshheading:2148115-Molecular Sequence Data, pubmed-meshheading:2148115-Oligosaccharides, pubmed-meshheading:2148115-Peptides, pubmed-meshheading:2148115-Polyisoprenyl Phosphate Sugars, pubmed-meshheading:2148115-Protein Processing, Post-Translational, pubmed-meshheading:2148115-Protein Synthesis Inhibitors
pubmed:year
1990
pubmed:articleTitle
Control of N-linked oligosaccharide synthesis: cellular levels of dolichyl phosphate are not the only regulatory factor.
pubmed:affiliation
Department of Biochemistry, University of Texas Health Science Center, San Antonio 78284.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't