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Cold-stress response in the amphibian oocyte: changes in synthesis and nucleocytoplasmic distribution of some proteins

Biology of the Cell
Wiley Blackwell (Blackwell Publishing)
Publication Date
  • Oocyte
  • Nuclear Proteins
  • β And γ-Actins
  • Cold Shock Proteins
  • Nucleocytoplasmic Exchanges
  • Biology


Abstract In vivo cold stress was found to induce characteristic changes in the protein synthesis pattern of Pleurodeles waltl oocytes, as analyzed by two-dimensional gel electrophoresis. The nature of the response varied with the duration and intensity of stress. After a short period of cold stress (12 h at 8°C), synthesis and intracellular distribution of polypeptides were dramatically disturbed. There occured: 1) a reduction in synthesis of several polypeptides, including two major polypeptides (54-kDa and 47-kDa); 2) changes in distribution of polypeptides in oocyte, ie some polypeptides (185- and 96-kDa) were blocked in the cytoplasm, while other polypeptides (82-, 74-, 72- and 68-kDa, actin and nucleoplasmin) continued to enter the nucleus, but were quantitatively reduced; 3) no changes in the distribution of two nuclear polypeptides (53- and 43-kDa); 4) changes in the relative quantities of β- and γ-actin and preferential migration of γ-actin towards the nucleus. After a long period of in vivo cold stress (5 days at 8°C), we noted a partial recuperation of synthesis and nuclear migration (except for a 96-kDa polypeptide), but a persistent perturbation at the level of actin. For more drastic stress conditions (4°C), such a recuperation of protein synthesis was never observed.

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