Your browser doesn't support javascript.
loading
Reactive oxygen species and Udx1 during early sea urchin development.
Wong, Julian L; Wessel, Gary M.
Affiliation
  • Wong JL; Department of Molecular Biology, Cellular Biology, and Biochemistry, Box G-J4, Brown University, Providence, RI 02912, USA.
Dev Biol ; 288(2): 317-33, 2005 Dec 15.
Article in En | MEDLINE | ID: mdl-16336958
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.
Subject(s)
Search on Google
Collection: 01-internacional Database: MEDLINE Main subject: Reactive Oxygen Species / NADPH Oxidases / Lytechinus / Flavoproteins Limits: Animals Language: En Journal: Dev Biol Year: 2005 Document type: Article Affiliation country: United States Country of publication: United States
Search on Google
Collection: 01-internacional Database: MEDLINE Main subject: Reactive Oxygen Species / NADPH Oxidases / Lytechinus / Flavoproteins Limits: Animals Language: En Journal: Dev Biol Year: 2005 Document type: Article Affiliation country: United States Country of publication: United States