Morphological and molecular modifications induced by heat shock in Drosophila melanogaster embryos.
The early embryo of Drosophila melanogaster did not survive treatment at 37 degrees C (heat shock) for 25 min. The histological analysis of eggs treated in this way showed that the heat shock caused disintegration of nuclei and of cytoplasmic islands, displacement and swelling of nuclei and blocked mitoses. These effects were not observed in embryos treated after blastoderm formation. After this stage, we noticed that development was slowed down. The heat shock proteins (hsp 83, 70 and 68) were, under shock, synthesized at all developmental stages. There was little or no synthesis of hsp 70 and 68 in unfertilized eggs, but synthesis increased in proportion to the number of nuclei present. Most probably, hsp 70 synthesis was directed by zygotic mRNA. DNA synthesis was not blocked by the heat shock though the overall incorporation of [3H]thymidine was substantially reduced, presumably because of the block of mitoses. We did not find a direct relation between survival pattern and hsp synthesis. We concluded that some, at least, of the heat shock genes can be activated at all developmental stages and that heat shock could be used for synchronizing mitoses.
D000818:Animals; D002467:Cell Nucleus; D002470:Cell Survival; D003593:Cytoplasm; D004331:Drosophila melanogaster / Q000196:embryology*; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D005775:Gastrula / Q000166:cytology / Q000378:metabolism; D006360:Heat-Shock Proteins / Q000378:metabolism; D006358:Hot Temperature; D008938:Mitosis; D010063:Ovum / Q000166:cytology* / Q000378:metabolism; D013936:Thymidine / Q000378:metabolism; D013997:Time Factors
D006360:Heat-Shock Proteins; D013936:Thymidine