Linked Life Data

8068242

Source:http://linkedlifedata.com/resource/pubmed/id/8068242

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1994-9-29
pubmed:abstractText
Most membrane glycoproteins contain either N-linked or O-linked oligosaccharides, which play important roles in correct folding, stability, and intracellular transport. Some glycoproteins, however, contain both the N- and O-linked sugars. To study the roles of the two types of glycosylation in intracellular transport we have used as a model the glycoprotein gC-1 of herpes simplex virus type 1 (HSV-1), which contains both N- and O-linked oligosaccharides. Cloned gene of gC-1 was expressed constitutively in mammalian cells to produce the gC-1 glycoprotein containing both types of glycosylation. Only a fraction of the gC-1 glycoprotein was secreted into the medium. Addition of tunicamycin blocked N-glycosylation and the gC-1 protein of reduced size containing only O-linked sugars was formed. This O-glycosylated gC-1 protein was transported to the cell surface and secreted into the medium, indicating that glycoprotein transport to and across the cell surface occurs in the absence of N-glycans. The data suggest either that O-glycans may contribute to this process or that transport can occur in the absence of both N- and O-glycans.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0829-8211
pubmed:author
pubmed:issnType
Print
pubmed:volume
72
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
20-5
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
Effect of tunicamycin and monensin on the transport to the cell surface and secretion of a viral membrane glycoprotein containing both N- and O-linked sugars.
pubmed:affiliation
McMaster University, Department of Biochemistry, Hamilton, ON, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't