Glypicans.
(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:
https://lup.lub.lu.se/record/111396
- author
- Fransson, Lars-Åke LU
- organization
- publishing date
- 2003
- 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
- 10.1016/S1357-2725(02)00095-X
- 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
- 2016-04-01 17:13:56
- date last changed
- 2025-04-04 14:14:26
@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}},
keywords = {{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/10.1016/S1357-2725(02)00095-X}},
doi = {{10.1016/S1357-2725(02)00095-X}},
volume = {{35}},
year = {{2003}},
}