Linked Life Data

12494998

Source:http://linkedlifedata.com/resource/pubmed/id/12494998

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2002-12-23
pubmed:abstractText
The TGN-localised, type I integral membrane protein TGN38 has previously been suggested to play a role as a cargo transporter within mammalian cells. We have undertaken a series of experiments designed to address this hypothesis, and, in so doing, have partially characterised the glycosylation status of the lumenal domain of TGN38. We find that elevated expression of different regions of the lumenal domain of TGN38 has no reproducible effect on secretion from stably transfected NRK cells expressing the different lumenal domain constructs; neither does it affect the gross morphology of organelles of the secretory and endocytic pathways. However, we observed that, whilst elevated expression of full-length TGN38 in stably transfected NRK cells does not have any significant effect on the morphology of organelles of the secretory and endocytic pathways, it does lead to a change in the pattern of protein secretion from these cells. In particular, elevated expression of full-length TGN38 led to increased secretion of a 48-kDa glycoprotein identified as plasminogen activator inhibitor-1.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0171-9335
pubmed:author
pubmed:issnType
Print
pubmed:volume
81
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
609-21
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Characterisation of the lumenal domain of TGN38 and effects of elevated expression of TGN38 on glycoprotein secretion.
pubmed:affiliation
Department of Biochemistry, University of Bristol, Bristol, BS8 1TD, UK.
pubmed:publicationType
Journal Article, Comparative Study