Sea urchin arylsulfatase, an extracellular matrix component, is involved in gastrulation during embryogenesis.
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.
Mitsunaga-Nakatsubo
Keiko
K
Department of Mathematical and Life Sciences, Graduate School of Science, Hiroshima University, Higashi-Hiroshima, Hiroshima, Japan.
Akimoto
Yoshihiro
Y
Kawakami
Hayato
H
Akasaka
Koji
K
D000629:Aminopropionitrile / Q000494:pharmacology; D000818:Animals; D001192:Arylsulfatases / Q000235:genetics / Q000378:metabolism*; D004625:Embryo, Nonmammalian / Q000378:metabolism*; D004791:Enzyme Inhibitors / Q000494:pharmacology; D005109:Extracellular Matrix / Q000737:chemistry; D005643:Fucose / Q000378:metabolism; D054262:Gastrulation; D006493:Heparin / Q000378:metabolism; D008249:Protein-Lysine 6-Oxidase / Q000037:antagonists & inhibitors; D012617:Sea Urchins / Q000196:embryology* / Q000201:enzymology*
D004791:Enzyme Inhibitors; D000629:Aminopropionitrile; D005643:Fucose; D006493:Heparin; D008249:Protein-Lysine 6-Oxidase; D001192:Arylsulfatases