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.
Similar content being viewed by others
Author information
Authors and Affiliations
Corresponding author
Additional information
Received 27 November 2003; received after revision 8 January 2004; accepted 13 January 2004
Rights and permissions
About this article
Cite this article
Fransson, LÅ., Belting, M., Cheng, F. et al. Novel aspects of glypican glycobiology. CMLS, Cell. Mol. Life Sci. 61, 1016–1024 (2004). https://doi.org/10.1007/s00018-004-3445-0
Issue Date:
DOI: https://doi.org/10.1007/s00018-004-3445-0