NDLI: Sea urchin arylsulfatase, an extracellular matrix component, is involved in gastrulation during embryogenesis

Content Provider	Springer Nature Link
Author	Mitsunaga Nakatsubo, Keiko Akimoto, Yoshihiro Kawakami, Hayato Akasaka, Koji
Copyright Year	2009
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 β-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.
Starting Page	281
Ending Page	288
Page Count	8
File Format	PDF
ISSN	0949944X
Journal	Development Genes and Evolution
Volume Number	219
Issue Number	6
e-ISSN	1432041X
Language	English
Publisher	Springer-Verlag
Publisher Date	2009-05-21
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Arylsulfatase Sea urchin Extracellular matrix Gastrulation Heparin-binding Animal Genetics and Genomics Neurosciences Biochemistry Cell Biology Developmental Biology
Content Type	Text
Resource Type	Article
Subject	Genetics Developmental Biology

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