Accumulation of the proteolytic marker peptide ubiquitin in the trophoblast of mammalian blastocysts
Language English Country United States Media print
Document type Comparative Study, Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Biomarkers analysis MeSH
- Blastocyst metabolism MeSH
- Cells, Cultured MeSH
- Mice, Inbred ICR MeSH
- Mice MeSH
- Mammals embryology MeSH
- Cattle MeSH
- Trophoblasts metabolism MeSH
- Ubiquitin metabolism MeSH
- Animals MeSH
- Check Tag
- Mice MeSH
- Cattle MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Comparative Study MeSH
- Names of Substances
- Biomarkers MeSH
- Ubiquitin MeSH
Ubiquitination is a universal protein degradation pathway in which the molecules of 8.5-kDa proteolytic peptide ubiquitin are covalently attached to the epsilon-amino group of the substrate's lysine residues. Little is known about the importance of this highly conserved mechanism for protein recycling in mammalian gametogenesis and fertilization. The data obtained by the students and faculty of the international training course Window to the Zygote 2000 demonstrate the accumulation of ubiquitin-cross-reactive structures in the trophoblast, but not in the inner cell mass of the expanding bovine and mouse blastocysts. This observation suggests that a major burst of ubiquitin-dependent proteolysis occurs in the trophoblast of mammalian peri-implantation embryos. This event may be important for the success of blastocyst hatching, differentiation of embryonic stem cells into soma and germ line, and/or implantation in both naturally conceived and reconstructed mammalian embryos.
References provided by Crossref.org
The neglected part of early embryonic development: maternal protein degradation
Characterization of SCF-Complex during Bovine Preimplantation Development
