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Glypicans.

Fransson, Lars-Åke LU (2003) In International Journal of Biochemistry & Cell Biology 35(2). p.125-129
Abstract
A family of lipid-linked heparan sulfate (HS) proteoglycans, later named glypicans, were identified some 15 years ago. The discoveries that mutations in genes involved in glypican assembly cause developmental defects have brought them into focus. Glypicans have a characteristic pattern of 14 conserved cysteine residues. There are also two–three attachment sites for HS side-chains near the membrane anchor. The HS side-chains consist of a repeating disaccharide back-bone that is regionally and variably modified by epimerization and different types of sulfations, creating a variety of binding sites for polycationic molecules, especially growth factors. Recycling forms of glypican-1 are potential vehicles for transport of cargo into and... (More)
A family of lipid-linked heparan sulfate (HS) proteoglycans, later named glypicans, were identified some 15 years ago. The discoveries that mutations in genes involved in glypican assembly cause developmental defects have brought them into focus. Glypicans have a characteristic pattern of 14 conserved cysteine residues. There are also two–three attachment sites for HS side-chains near the membrane anchor. The HS side-chains consist of a repeating disaccharide back-bone that is regionally and variably modified by epimerization and different types of sulfations, creating a variety of binding sites for polycationic molecules, especially growth factors. Recycling forms of glypican-1 are potential vehicles for transport of cargo into and through cells. The glypican-1 core protein is S-nitrosylated and nitric oxide released from these sites cleave the HS chains at glucosamine units lacking N-substitution. This processing is necessary for polyamine uptake. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Heparan sulfate, Nitric oxide, Xyloside, Polyamine
in
International Journal of Biochemistry & Cell Biology
volume
35
issue
2
pages
125 - 129
publisher
Elsevier
external identifiers
  • pmid:12479862
  • wos:000180583800003
  • scopus:0037290749
ISSN
1878-5875
DOI
language
English
LU publication?
yes
id
5da959e6-8d59-4cf7-a101-85e6afb2832f (old id 111396)
alternative location
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12479862&dopt=Abstract
date added to LUP
2007-06-26 09:51:43
date last changed
2018-05-29 11:18:04
@article{5da959e6-8d59-4cf7-a101-85e6afb2832f,
  abstract     = {A family of lipid-linked heparan sulfate (HS) proteoglycans, later named glypicans, were identified some 15 years ago. The discoveries that mutations in genes involved in glypican assembly cause developmental defects have brought them into focus. Glypicans have a characteristic pattern of 14 conserved cysteine residues. There are also two–three attachment sites for HS side-chains near the membrane anchor. The HS side-chains consist of a repeating disaccharide back-bone that is regionally and variably modified by epimerization and different types of sulfations, creating a variety of binding sites for polycationic molecules, especially growth factors. Recycling forms of glypican-1 are potential vehicles for transport of cargo into and through cells. The glypican-1 core protein is S-nitrosylated and nitric oxide released from these sites cleave the HS chains at glucosamine units lacking N-substitution. This processing is necessary for polyamine uptake.},
  author       = {Fransson, Lars-Åke},
  issn         = {1878-5875},
  keyword      = {Heparan sulfate,Nitric oxide,Xyloside,Polyamine},
  language     = {eng},
  number       = {2},
  pages        = {125--129},
  publisher    = {Elsevier},
  series       = {International Journal of Biochemistry & Cell Biology},
  title        = {Glypicans.},
  url          = {http://dx.doi.org/},
  volume       = {35},
  year         = {2003},
}