Identification and characterization of amyloid-like substance in mouse oocytes and embryos

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.