Related Experiment Video
Updated: Jan 30, 2026

Cryopreservation of Preimplantation Embryos of Cattle, Sheep, and Goats
Published on: August 5, 2011
p66Shc is associated with hydrogen peroxide-induced oxidative stress in preimplantation sheep embryos
Tong Zhang1,2,3, Xiaofang Zhao1,3, Rihan Hai1,2
1Department of Animal Genetics, Breeding and Reproduction, College of Animal Science, Inner Mongolia Agricultural University, Hohhot, Inner Mongolia, China.
Abstract:
The low efficiency of in vitro embryo production is associated with oxidative stress induced by suboptimal culture conditions. p66Shc is a 66-kDa protein of the ShcA (Src homologous-collagen homolog) adaptor protein family, which is involved in signaling pathways involved in oxidative stress regulation, apoptosis induction, and aging. However, the functional role of p66Shc during the preimplantation development of sheep embryos is not understood. Our results showed that early-cleavage (≤28 hr) embryos had a higher developmental potential than late-cleavage (>28 hr) embryos. The poor quality of these late-cleavage embryos was associated with increased the transcripts and protein of p66Shc and decreased mitochondrial activity. In addition, exogenous hydrogen peroxide-induced oxidative stress significantly increased p66Shc protein abundance and suppressed embryonic development, which was ameliorated by antioxidant treatment. Notably, oxidative stress induced the nuclear localization of p66Shc and phosphorylated (Ser-36) p66Shc. Collectively, these observations suggest that p66Shc may be playing an important role in the regulation of oxidative stress during the preimplantation development of sheep embryos.
Related Concept Videos
Oxidation Numbers
Hydrogen Bonds
Hydrogen Bonds Control the World!
Because hydrogen has very weak electronegativity when it binds with a strongly electronegative atom, such as oxygen or nitrogen, electrons in the bond are unequally shared....
Hydrogen Bonds
Oxidation-Reduction Reactions
Cloning of Dolly the Sheep
Pyruvate Oxidation
First, the enzyme pyruvate dehydrogenase removes the carboxyl group from pyruvate and releases it as carbon dioxide. The stripped molecule is then oxidized and releases electrons, which are then picked up by NAD+...

