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

Dick, Gunnar ; Akslen-Hoel, Linn Kristin ; Grøndahl, Frøy ; Kjos, Ingrid ; Maccarana, Marco LU and Prydz, Kristian (2015) In Glycobiology 25(1). p.30-41
Abstract
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... (More)
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. (Less)
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author
; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Glycobiology
volume
25
issue
1
pages
30 - 41
publisher
Oxford University Press
external identifiers
  • pmid:25138304
  • wos:000347410500004
  • scopus:84924941678
  • pmid:25138304
ISSN
1460-2423
DOI
10.1093/glycob/cwu084
language
English
LU publication?
yes
id
6387ac4c-6771-45d1-b471-7a132dd67c67 (old id 4614311)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/25138304?dopt=Abstract
date added to LUP
2016-04-01 10:40:59
date last changed
2022-04-12 08:36:51
@article{6387ac4c-6771-45d1-b471-7a132dd67c67,
  abstract     = {{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.}},
  author       = {{Dick, Gunnar and Akslen-Hoel, Linn Kristin and Grøndahl, Frøy and Kjos, Ingrid and Maccarana, Marco and Prydz, Kristian}},
  issn         = {{1460-2423}},
  language     = {{eng}},
  number       = {{1}},
  pages        = {{30--41}},
  publisher    = {{Oxford University Press}},
  series       = {{Glycobiology}},
  title        = {{PAPST1 regulates sulfation of heparan sulfate proteoglycans in epithelial MDCK II cells.}},
  url          = {{http://dx.doi.org/10.1093/glycob/cwu084}},
  doi          = {{10.1093/glycob/cwu084}},
  volume       = {{25}},
  year         = {{2015}},
}