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Novel aspects of glypican glycobiology.

Fransson, Lars-Åke LU ; Belting, Mattias LU ; Cheng, Fang LU ; Jönsson, M; Mani, Katrin LU and Sandgren, Staffan LU (2004) In Cellular and Molecular Life Sciences1997-01-01+01:00 61(9). p.1016-1024
Abstract
Mutations in glypican genes cause dysmorphic and overgrowth syndromes in men and mice, abnormal development in flies and worms, and defective gastrulation in zebrafish and ascidians. All glypican core proteins share a characteristic pattern of 14 conserved cysteine residues. Upstream from the C-terminal membrane anchorage are 3–4 heparan sulfate attachment sites. Cysteines in glypican-1 can become nitrosylated by nitric oxide in a copper-dependent reaction. When glypican-1 is exposed to ascorbate, nitric oxide is released and participates in deaminative cleavage of heparan sulfate at sites where the glucosamines have a free amino group. This process takes place while glypican-1 recycles via a nonclassical, caveolin-1-associated route.... (More)
Mutations in glypican genes cause dysmorphic and overgrowth syndromes in men and mice, abnormal development in flies and worms, and defective gastrulation in zebrafish and ascidians. All glypican core proteins share a characteristic pattern of 14 conserved cysteine residues. Upstream from the C-terminal membrane anchorage are 3–4 heparan sulfate attachment sites. Cysteines in glypican-1 can become nitrosylated by nitric oxide in a copper-dependent reaction. When glypican-1 is exposed to ascorbate, nitric oxide is released and participates in deaminative cleavage of heparan sulfate at sites where the glucosamines have a free amino group. This process takes place while glypican-1 recycles via a nonclassical, caveolin-1-associated route. Glypicans are involved in growth factor signalling and transport, e.g. of polyamines. Cargo can be unloaded from heparan sulfate by nitric oxide-dependent degradation. How glypican and its degradation products and the cargo exit from the recycling route is an enigma. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Caveolae, development, growth factors, heparan sulfate, nitric oxide, polyamines, S-nitrosylation
in
Cellular and Molecular Life Sciences1997-01-01+01:00
volume
61
issue
9
pages
1016 - 1024
publisher
Birkhaüser
external identifiers
  • wos:000221056600002
  • pmid:15112050
  • scopus:2442656740
ISSN
1420-9071
DOI
10.1007/s00018-004-3445-0
language
English
LU publication?
yes
id
aa87a8a5-ddeb-48f6-b188-7fb0d160cd83 (old id 122360)
date added to LUP
2007-07-12 10:49:39
date last changed
2017-12-03 03:46:01
@article{aa87a8a5-ddeb-48f6-b188-7fb0d160cd83,
  abstract     = {Mutations in glypican genes cause dysmorphic and overgrowth syndromes in men and mice, abnormal development in flies and worms, and defective gastrulation in zebrafish and ascidians. All glypican core proteins share a characteristic pattern of 14 conserved cysteine residues. Upstream from the C-terminal membrane anchorage are 3–4 heparan sulfate attachment sites. Cysteines in glypican-1 can become nitrosylated by nitric oxide in a copper-dependent reaction. When glypican-1 is exposed to ascorbate, nitric oxide is released and participates in deaminative cleavage of heparan sulfate at sites where the glucosamines have a free amino group. This process takes place while glypican-1 recycles via a nonclassical, caveolin-1-associated route. Glypicans are involved in growth factor signalling and transport, e.g. of polyamines. Cargo can be unloaded from heparan sulfate by nitric oxide-dependent degradation. How glypican and its degradation products and the cargo exit from the recycling route is an enigma.},
  author       = {Fransson, Lars-Åke and Belting, Mattias and Cheng, Fang and Jönsson, M and Mani, Katrin and Sandgren, Staffan},
  issn         = {1420-9071},
  keyword      = {Caveolae,development,growth factors,heparan sulfate,nitric oxide,polyamines,S-nitrosylation},
  language     = {eng},
  number       = {9},
  pages        = {1016--1024},
  publisher    = {Birkhaüser},
  series       = {Cellular and Molecular Life Sciences1997-01-01+01:00},
  title        = {Novel aspects of glypican glycobiology.},
  url          = {http://dx.doi.org/10.1007/s00018-004-3445-0},
  volume       = {61},
  year         = {2004},
}