Mechanisms of programmed cell death during oogenesis in Drosophila virilis.
We describe the features of programmed cell death occurring in the egg chambers of Drosophila virilis during mid-oogenesis and late oogenesis. During mid-oogenesis, the spontaneously degenerating egg chambers exhibit typical characteristics of apoptotic cell death. As revealed by propidium iodide, rhodamine-conjugated phalloidin staining, and the TUNEL assay, respectively, the nurse cells contain condensed chromatin, altered actin cytoskeleton, and fragmented DNA. In vitro caspase activity assays and immunostaining procedures demonstrate that the atretic egg chambers possess high levels of caspase activity. Features of autophagic cell death are also observed during D. virilis mid-oogenesis, as shown by monodansylcadaverine staining, together with an ultrastructural examination by transmission electron microscopy. During the late stages of oogenesis in D. virilis, once again, the two mechanisms, viz., nurse cell cluster apoptosis and autophagy, operate together, manifesting features of cell death similar to those detailed above. Moreover, an altered form of cytochrome c seems to be released from the mitochondria in the nurse cells proximal to the oocyte. We propose that apoptosis and autophagy function synergistically during oogenesis in D. virilis in order to achieve a more efficient elimination of the degenerated nurse cells and abnormal egg chambers.
Velentzas
Athanassios D
AD
Faculty of Biology, Department of Cell Biology and Biophysics, University of Athens, Panepistimiopolis 15784, Athens, Greece.
Nezis
Ioannis P
IP
Stravopodis
Dimitrios J
DJ
Papassideri
Issidora S
IS
Margaritis
Lukas H
LH
D000199:Actins / Q000032:analysis / Q000378:metabolism; D000818:Animals; D017209:Apoptosis / Q000502:physiology*; D001343:Autophagy / Q000502:physiology*; D002103:Cadaverine / Q000031:analogs & derivatives / Q000737:chemistry; D020169:Caspases / Q000032:analysis / Q000378:metabolism; D056668:Cathepsin L; D002403:Cathepsins / Q000032:analysis; D002467:Cell Nucleus / Q000737:chemistry; D045304:Cytochromes c / Q000032:analysis / Q000378:metabolism; D003599:Cytoskeleton / Q000737:chemistry / Q000378:metabolism; D053938:DNA Fragmentation; D004330:Drosophila / Q000166:cytology / Q000502:physiology*; D029721:Drosophila Proteins / Q000378:metabolism; D004792:Enzyme Precursors / Q000032:analysis; D005260:Female; D006107:Granulosa Cells / Q000737:chemistry / Q000166:cytology / Q000378:metabolism; D020287:In Situ Nick-End Labeling; D008247:Lysosomes / Q000737:chemistry; D046529:Microscopy, Electron, Transmission; D008928:Mitochondria / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D008954:Models, Biological; D009866:Oogenesis / Q000502:physiology*; D006080:Ovarian Follicle / Q000737:chemistry / Q000166:cytology / Q000378:metabolism; D011419:Propidium / Q000737:chemistry
D000199:Actins; D029721:Drosophila Proteins; D004792:Enzyme Precursors; D011419:Propidium; D045304:Cytochromes c; D002403:Cathepsins; D020169:Caspases; C118731:dronc protein, Drosophila; C063905:procathepsin L; D056668:Cathepsin L; C008542:monodansylcadaverine; D002103:Cadaverine