Literature DB >> 3187533

Ovothiol replaces glutathione peroxidase as a hydrogen peroxide scavenger in sea urchin eggs.

E Turner1, L J Hager, B M Shapiro.   

Abstract

Despite its potential toxicity, H2O2 is used as an extracellular oxidant by Stronglylocentrotus purpuratus eggs to cross-link their fertilization envelopes. These eggs contain 5 mM 1-methyl-N alpha,N alpha-dimethyl-4-mercaptohistidine (ovothiol C), which reacts with H2O2. In consuming H2O2 and being reduced by glutathione, ovothiol acts as a glutathione peroxidase and replaces the function of the enzyme in eggs. The ovothiol system is more effective than egg catalase in destroying H2O2 at concentrations produced during fertilization and constitutes a principal mechanism for preventing oxidative damage at fertilization.

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Year:  1988        PMID: 3187533     DOI: 10.1126/science.3187533

Source DB:  PubMed          Journal:  Science        ISSN: 0036-8075            Impact factor:   47.728


  14 in total

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4.  The chemical defensome: environmental sensing and response genes in the Strongylocentrotus purpuratus genome.

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5.  Use of a Tyrosine Analogue To Modulate the Two Activities of a Nonheme Iron Enzyme OvoA in Ovothiol Biosynthesis, Cysteine Oxidation versus Oxidative C-S Bond Formation.

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6.  Sulfur-containing histidine compounds inhibit γ-glutamyl transpeptidase activity in human cancer cells.

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Review 7.  Cell surface changes in the egg at fertilization.

Authors:  Gary M Wessel; Julian L Wong
Journal:  Mol Reprod Dev       Date:  2009-10       Impact factor: 2.609

8.  The orphan protein bis-γ-glutamylcystine reductase joins the pyridine nucleotide disulfide reductase family.

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9.  Shedding light on ovothiol biosynthesis in marine metazoans.

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10.  Ovothiol isolated from sea urchin oocytes induces autophagy in the Hep-G2 cell line.

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