| pubmed-article:12494998 | 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. | lld:pubmed |
