Lack of heat-shock response in preovulatory mouse oocytes.
The response to heat (hs response) of preovulatory mouse oocytes was compared with that of mouse granulosa cells and characterized in regard to in vitro resumption of meiosis, amino acid incorporation into total protein, and qualitative analysis of protein synthesized before and after the shock. Granulosa cells displayed a hs response typical of other mammalian systems. When incubated at 43 degrees C for 20-40 min, these cells maintained a normal level of amino acid incorporation into total protein, responded to stress by new synthesis of 33- and 68-kDa heat-shock proteins (hsps), and enhanced synthesis of 70-kDa heat-shock cognate protein (hsc70) and of 89- and 110-kDa hsps. In contrast to granulosa cells, preovulatory mouse oocytes were very sensitive to hyperthermia. Incubation at 43 degrees C for 20-40 min strongly inhibited oocyte resumption of meiosis and protein synthesis and did not induce a new or enhanced synthesis of hsps. Unstressed preovulatory mouse oocytes constitutively synthesized 70- and 89-kDa polypeptides resembling hsc70 and hsp89 of granulosa cells.
D000818:Animals; D005260:Female; D006107:Granulosa Cells / Q000166:cytology / Q000502:physiology*; D006360:Heat-Shock Proteins / Q000096:biosynthesis*; D006358:Hot Temperature; D007700:Kinetics; D008540:Meiosis; D051379:Mice; D009865:Oocytes / Q000166:cytology / Q000502:physiology*; D014176:Protein Biosynthesis
D006360:Heat-Shock Proteins