Abstract. The small RNP complexes of defined morphology
In Podarcis sicula specialized follicle cells send reserve materials to the previtellogenic oocyte via intercellular bridges. Immediately before the onset of vitellogenesis this transferring becomes particularly massive so that the cell volume significantly reduces, meanwhile in the nucleus the morphological alterations typical of apoptosis appear. To clarify why these follicle cells are not simply fully resorbed by the oocyte and to determine whether their DNA is discarded or recycled, we carried out a series of morphological and biochemical investigations. The finding that large macromolecular scaffolds are formed and that these are able to retain the DNA until it is extensively cut by two different endonucleases suggests that regression of the follicle cells is programmed and that the fate of their DNA is strictly controlled. Following its genetical neutralization via fragmentation, the DNA is apparently recycled by being transferred into the oocyte via the intercellular bridges, that, in fact, remain open until the very late stages of cell regression. The small DNA fragments reaching the oocyte cytoplasm would not interfere with meiosis completion but could significantly contribute to the stock of reserve materials to the advantage of the growing oocyte and/or developing embryo.
The prosomes, biochemically well characterized small RNA-protein complexes, found associated with mRNA in all eukaryotic cells tested, have been identified as maternal components in sea urchin and chick embryos. In this study, we investigated their presence and cytolocalization in the oocytes and embryos of Pleurodeles waltl by immunoblot analysis and immunofluorescence, using monoclonal antibodies prepared against duck prosome proteins. Of the four antibodies tested, three recognized the corresponding antigens in oocyte total protein extracts. Immunofluorescence analysis, using the three prosomal antibodies, demonstrated a drastic change in the localization of the prosome antigens, which changed from the cytoplasm to the nucleus during oogenesis. In the nucleus, in diplotene stages, prosomal antigens appeared to be associated with the lampbrush chromosomes and the nuclear matrix. During embryogenesis, the subcellular distribution of the prosome antigens was a function of development and differentiation: in the cleavage stages up to the mid-blastula they were localized in the cytoplasm and on the plasma membrane, while in the late blastula, gastrula and neurula they were in the nucleus. Interestingly, one of the prosome antigens, p31K, was found to be in a different location in certain cells in the animal pole of the mid-blastula and was absent in the neural tissue in the neurula. In still later stages, in the free-swimming larva, all three antigens were localized in the cytoplasm, specifically in certain cell types in the epidermal tissues. Furthermore, they were sectorially distributed in the cytoplasm. These data taken together indicate the possible presence of tissue-type-specific prosome antigens in Pleurodeles. Differentiation-dependent subcellular localization of the prosome antigens suggests a cell-compartment-related multiple function of prosomes.
Prosomes, ubiquitous ribonucleoprotein (RNP) particles of defined biochemical and morphological structure, first isolated as a subcomplex of the repressed globin mRNP in avian and mouse erythroblasts, were also found in the cytoplasm of other vertebrates associated with other mRNAs. Here we show that prosomes are also present in the cell nucleus and, furthermore, that the cytolocalization of specific prosomal peptides is a function of differentiation. Four monoclonal antibodies, raised against the duck prosomal proteins, p27K, p28K, p29K and p31K (K = 10(3) Mr) react to variable degree with prosomes of chicken, mouse, and human cells. Immunocytochemical and biochemical analyses show that all four antigens are present in both the cytoplasm and the nucleus of avian erythroblasts and avian erythroblastosis virus (AEV)-transformed erythroleukaemic cells. Interestingly, the prosomes disappear in the course of the terminal differentiation of erythroblasts to mature erythrocytes. Although all the four prosomal antigens tested are present in both the nuclear and cytoplasmic compartments, slight differences in the immunofluorescent patterns indicate that each antigen may have a particular cytological distribution that varies in the course of differentiation.
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