Reactive oxygen species and Udx1 during early sea urchin development

• Published in: Developmental biology Vol. 288; no. 2; pp. 317 - 333
• Main Authors: Wong, Julian L., Wessel, Gary M.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 15.12.2005
• Subjects: Animals; Blastomeres - enzymology; Blastomeres - metabolism; Calcium - metabolism; Cleavage; Dual oxidase; Egg; Embryo; Flavoproteins - antagonists & inhibitors; Flavoproteins - genetics; Flavoproteins - metabolism; Hydrogen peroxide; Hydrogen Peroxide - metabolism; Hydrogen Peroxide - pharmacology; Lytechinus - embryology; Lytechinus - enzymology; Lytechinus - metabolism; Mitosis; NADPH Oxidases - antagonists & inhibitors; NADPH Oxidases - genetics; NADPH Oxidases - metabolism; Reactive oxygen species; Reactive Oxygen Species - metabolism; Udx1; Embryo; Reactive oxygen species; Hydrogen peroxide; Egg; Mitosis; TSH; H2DCFDA; H2O2; MAPK; IP3; PTP; S6K1; duox; Dual oxidase; ROS; Cleavage; DPI; IPD
• ISSN: 0012-1606; 1095-564X
• DOI: 10.1016/j.ydbio.2005.07.004

Sea urchin fertilization is marked by a massive conversion of molecular oxygen to hydrogen peroxide by a sea urchin dual oxidase, Udx1. This enzyme is essential for completing the physical block to polyspermy. Yet, its expression is maintained during development, as indicated by the presence of both Udx1 mRNA and Udx1 protein enriched at the surface of all non-mesenchymal blastomeres. When hydrogen peroxide synthesis by Udx1 is inhibited, either pharmacologically or by specific antibody injection, cleavage is delayed. Application of exogenous hydrogen peroxide, however, partially rescues a fraction of these defective embryos. We also report an unequal distribution of reactive oxygen species between sister blastomeres during early cleavage stages, suggesting a functional role for Udx1 in intracellular signaling.