PAPST1 regulates sulfation of heparan sulfate proteoglycans in epithelial MDCK II cells.
Författare
Summary, in English
Proteoglycan (PG) sulfation depends on activated nucleotide sulfate, 3'-phosphoadenosine-5'-phosphosulfate (PAPS). Transporters in the Golgi membrane translocate PAPS from the cytoplasm into the organelle lumen where PG sulfation occurs. Silencing of PAPS transporter (PAPST) 1 in epithelial MDCK cells reduced PAPS uptake into Golgi vesicles. Surprisingly, at the same time sulfation of heparan sulfate (HS) was stimulated. The effect was pathway specific in polarized epithelial cells. Basolaterally secreted PGs displayed an altered HS sulfation pattern and increased growth factor binding capacity. In contrast, the sulfation pattern of apically secreted PGs was unchanged while the secretion was reduced. Regulation of PAPST1 allows epithelial cells to prioritize between PG sulfation in the apical and basolateral secretory routes at the level of the Golgi apparatus. This provides sulfation patterns that ensure PG functions at the extracellular level, such as growth factor binding.
Avdelning/ar
- Matrix Biology
Publiceringsår
2015
Språk
Engelska
Sidor
30-41
Publikation/Tidskrift/Serie
Glycobiology
Volym
25
Issue
1
Länkar
Dokumenttyp
Artikel i tidskrift
Förlag
Oxford University Press
Ämne
- Biochemistry and Molecular Biology
Status
Published
Forskningsgrupp
- Matrix Biology
ISBN/ISSN/Övrigt
- ISSN: 1460-2423