Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1991-5-28
pubmed:abstractText
N-linked sugar chains of rat 3Y1 cells and tumorigenic cells derived by transfection with activated c-myc gene were quantitatively released as oligosaccharides from membrane preparations by hydrazinolysis. Structural analyses revealed that cells of both types contain bi-, tri- and tetra-antennary complex-type oligosaccharides as well as high-mannose-type oligosaccharides. However, the c-myc-transfected cells showed an increase in tri- and tetra-antennary oligosaccharides having the GlcNAc beta 1----4Man alpha 1----and/or the GlcNAc beta 1----6Man alpha 1----linkages with a decrease in biantennary oligosaccharides compared to control 3Y1 cells. The data suggest that c-myc gene has a potential role in the regulation of cellular protein glycosylation and that an elevated expression of c-myc gene in the cells leads to increased branch formation of outer chains in N-linked oligosaccharides concomitant with the acquisition of tumorigenicity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0020-7136
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
48
pubmed:geneSymbol
c-myc
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
305-10
pubmed:dateRevised
2007-7-24
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Altered protein glycosylation of rat 3Y1 cells induced by activated c-myc gene.
pubmed:affiliation
Department of Biochemistry, University of Tokyo, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't