Abstract
Mammalian oocytes are unique among germ cells in that they age precociously. The cellular and molecular mechanisms driving oocyte aging remain poorly understood. During meiosis in yeast, an RNA-binding protein, with a predicted prion domain, assumes an amyloid-like configuration to translationally repress cyclins and ensure homologous chromosome segregation. These findings suggest that prion domains enable formation of amyloid-like effectors in diverse settings. Since amyloid-like molecules can accelerate aging in long-lived, post mitotic cells, such as neurons, we sought to identify and characterize amyloid-like substance in oocytes, cleavage stage embryos, and blastocysts, using a murine model.
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