Sea urchin arylsulfatase,an extracellular matrix component,is involved in gastrulation during embryogenesis |
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Authors: | Keiko Mitsunaga-Nakatsubo Yoshihiro Akimoto Hayato Kawakami Koji Akasaka |
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Institution: | (1) Department of Mathematical and Life Sciences, Graduate School of Science, Hiroshima University, Higashi-Hiroshima Hiroshima, 739-8526, Japan;(2) Department of Anatomy, Kyorin University School of Medicine, Mitaka, Tokyo 181-8611, Japan;(3) MMBS, Graduate School of Sciences, University of Tokyo, Miura, Kanagawa 238-0225, Japan |
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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. |
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Keywords: | Arylsulfatase Sea urchin Extracellular matrix Gastrulation Heparin-binding |
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