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PAPST1 regulates sulfation of heparan sulfate proteoglycans in epithelial MDCK II cells.

På svenska

Author

  • Gunnar Dick
  • Linn Kristin Akslen-Hoel
  • Frøy Grøndahl
  • Ingrid Kjos
  • Marco Maccarana
  • Kristian Prydz

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.

Department/s

  • Matrix Biology

Publishing year

2015

Language

English

Pages

30-41

Publication/Series

Glycobiology

Volume

25

Issue

1

Document type

Journal article

Publisher

Oxford University Press

Topic

  • Biochemistry and Molecular Biology

Status

Published

Research group

  • Matrix Biology

ISBN/ISSN/Other

  • ISSN: 1460-2423