ArticleDevelopment genes and evolution2009
Sea urchin arylsulfatase, an extracellular matrix component, is involved in gastrulation during embryogenesis.
Article in Development genes and evolution, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed, 14 citations in OpenAlex.
- Sulfatase modifying factors control the timing of zebrafish convergence and extension morphogenesis.Nature communications · 2026Article
- Sulfatase modifying factors control the timing of zebrafish convergence and extension morphogenesis.bioRxiv : the preprint server for biology · 2025Article
- Hematopoiesis at the onset of metamorphosis: terminal differentiation and dissociation of the Drosophila lymph gland.Development genes and evolution · 2011Article
- HpSumf1 is involved in the activation of sulfatases responsible for regulation of skeletogenesis during sea urchin development.Development genes and evolution · 2011Article
- Transport of arylsulfatase A across the blood-brain barrier in vitro.The Journal of biological chemistry · 2011Article
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Arylsulfatases (Arses) have been regarded as lysosomal enzymes because of their hydrolytic activities on synthetic aromatic substrates and their lysosomal localization of their enzymatic activities. Using sea urchin embryos, we previously demonstrated that the bulk of Hemicentrotus Ars (HpArs) does not exhibit enzyme activity and is located on the apical surface of the epithelial cells co-localizing with sulfated polysaccharides. Here we show that HpArs strongly binds to sulfated polysaccharides and that repression of the synthesis by HpArs-morpholino results in retardation of gastrulation in the sea urchin embryo. Accumulation of HpArs protein and sulfated polysaccharides on the apical surface of the epithelial cells in sea urchin larvae is repressed by treatment with beta-aminopropionitrile (BAPN), suggesting that deposition of HpArs and sulfated polysaccharides is dependent on the crosslinking of proteins such as collagen-like molecules. We suggest that HpArs functions by binding to components of the extracellular matrix.
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