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 Sciences
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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/122360
- author
- Fransson, Lars-Åke
LU
; Belting, Mattias
LU
; Cheng, Fang
LU
; Jönsson, M
; Mani, Katrin
LU
and Sandgren, Staffan
LU
- organization
- publishing date
- 2004
- 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 Sciences
- volume
- 61
- issue
- 9
- pages
- 1016 - 1024
- publisher
- Birkhäuser Verlag
- 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
- 2016-04-01 17:14:06
- date last changed
- 2023-10-17 13:12:10
@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}},
keywords = {{Caveolae; development; growth factors; heparan sulfate; nitric oxide; polyamines; S-nitrosylation}},
language = {{eng}},
number = {{9}},
pages = {{1016--1024}},
publisher = {{Birkhäuser Verlag}},
series = {{Cellular and Molecular Life Sciences}},
title = {{Novel aspects of glypican glycobiology.}},
url = {{http://dx.doi.org/10.1007/s00018-004-3445-0}},
doi = {{10.1007/s00018-004-3445-0}},
volume = {{61}},
year = {{2004}},
}