Recent findings on oogenesis of Drosophila melanogaster

Development ◽  
1977 ◽  
Vol 38 (1) ◽  
pp. 115-124
Author(s):  
F. Giorgi ◽  
J. Jacob
Keyword(s):  
Drosophila Melanogaster ◽  
Plasma Membrane ◽  
Early Stage ◽  
Dense Body ◽  
Superficial Layer ◽  
Coated Vesicles ◽  
Nurse Cells ◽  
External Limiting Membrane ◽  
Ring Canals

The ultrastructure of the developing ooplasm has been examined in 2–3–day-old flies of Drosophila melanogaster with a view to clarifying the origin of the yolk platelets. Previtellogenic ovarian chambers have been shown to exhibit a number of cytolysosomes; these are first formed in the nurse cells and are later brought to the ooplasm after having passed through the ring canals. Just prior to the beginning of vitellogenesis some of the cytolysosomes in the ooplasm acquire in places a yolk-like appearance. As vitellogenesis commences, in early stage-8 chambers, the central ooplasm comes to exhibit a number of inclusions which combine in themselves features of both yolk platelets and cytolysosomes. The onset of vitellogenesis at stage 8 is marked by the appearance of several structural entities on the plasma membrane of the oocyte. At this site, there appear a number of depressions or pits in between the microvilli. Deeper in the cortical ooplasm there are also present a number of coated vesicles and tubules. While the former exhibit a typical threelayered structure similar to that of the pits, the tubules lack the outer spiked layer. Mature yolk platelets appear to be made up of three major components. These are a central homogeneous dense body, an outer superficial layer with a number of small spherules and a rounded body therein, and an external limiting membrane. Instances of fusion between vesicles of sizes progressively larger have been observed with frequency. This observation is discussed in relation to the formation of yolk platelets by means of pinocytotic uptake. A contribution made by the nurse cells to the formation of the yolk platelets is also taken into account.

Exterior and Interior Events in Early Stage of Thrombin-induced Platelet Aggregation

1977 ◽  
Vol 38 (03) ◽  
pp. 0630-0639 ◽  
Author(s):  
Shuichi Hashimoto ◽  
Sachiko Shibata ◽  
Bonro Kobayashi
Keyword(s):  
Molecular Weight ◽  
Enzyme Activity ◽  
Plasma Membrane ◽  
Platelet Aggregation ◽  
Early Stage ◽  
Adenyl Cyclase ◽  
Cellular Component ◽  
Primary Event ◽  
Rabbit Platelets ◽  
Membrane Bound

SummaryTreatment of washed rabbit platelets with 1 u/ml of thrombin at 37° C resulted in a disappearance from platelets of a protein with 250,000 dalton molecular weight which was shown to be originated from plasma membrane. Parallel loss of adenyl cyclase was noted, and both reactions were complete within 30 sec. From the patterns of disc electrophoretograms, the importance of quick suppression of thrombin action in demonstrating the primary event was stressed.Thrombin induced an apparent activation of membrane bound phosphodiesterase. This reaction was also complete within 30 sec. The cellular component which contained the enzyme activity was distinct from plasma membrane. Soluble phosphodiesterase was not influenced by thrombin at all.These reactions required intact platelet cells to react with thrombin, and no reaction was detected when subcellular preparations were treated with thrombin.Possibility of collaboration of changes in externally located synthetic enzyme with those in internally located degrading enzyme in the early phase of thrombin action on platelets was suggested.

scholarly journals The polymerization of actin: II. how nonfilamentous actin becomes nonrandomly distributed in sperm: evidence for the association of this actin with membranes

1976 ◽  
Vol 69 (1) ◽  
pp. 51-72 ◽  
Author(s):  
LG Tilney
Keyword(s):  
Plasma Membrane ◽  
Nuclear Envelope ◽  
Thin Section ◽  
Actin Filaments ◽  
Early Stage ◽  
Mature Sperm ◽  
Vacuole Membrane ◽  
Other Substances ◽  
Associated Proteins ◽  
Basal Half

At an early stage in spermiogenesis the acrosomal vacuole and other organelles including ribosomes are located at the basal end of the cell. From here actin must be transported to its future location at the anterior end of the cell. At no stage in the accumulation of actin in the periacrosomal region is the actin sequestered in a membrane-bounded compartment such as a vacuole or vesicle. Since filaments are not present in the periacrosomal region during the accumulation of the actin even though the fixation of these cells is sufficiently good to distinguish actin filaments in thin section, the actin must accumulate in the nonfilamentous state. The membranes in the periacrosomal region, specifically a portion of the nuclear envelope and the basal half of the acrosomal vacuole membrane, become specialized morphologically in advance of the accumulation of actin in this region. My working hypothesis is that the actin in combination with other substances binds to these specialized membranes and to itself and thus can accumulate in the periacrosmoal region by being trapped on these specialized membranes. Diffusion would then be sufficient to move these substances to this region. In support of this hypothesis are experiments in which I treated mature sperm with detergents, glycols, and hypotonic media, which solubilize or lift away the plasma membrane. The actin and its associated proteins remain attached to these specialized membranes. Thus actin can be nonrandomly distributed in cells in a nonfilamentous state presumably by its association with specialized membranes.

scholarly journals A morphological study of plasma and phagosome membranes during endocytosis in Acanthamoeba.

1980 ◽  
Vol 84 (2) ◽  
pp. 246-260 ◽  
Author(s):  
B Bowers
Keyword(s):  
Plasma Membrane ◽  
Morphological Study ◽  
Direct Evidence ◽  
Particle Density ◽  
Early Stage ◽  
Chemical Analyses ◽  
Surface Separation ◽  
Phospholipid Ratio ◽  
Major Route ◽  
Particle Ingestion

Particle ingestion by Acanthamoeba is rapid. Within 40 s bound particles can be surrounded by pseudopods, brought into the cytoplasm, and released as phagosomes into the cytoplasmic stream. In electron micrographs the phagosome appears as a flasklike invagination of the surface. Separation from the surface occurs by fragmentation of the attenuated "neck+ of the invagination. The separated phagosome membrane has a three- to fourfold greater density of intramembrane particles than the plasma membrane from which it derives. This change is evident within 15 min of ingestion and is detectable while the membrane is still tightly apposed to the particle. There is no direct evidence for the mechanism of this increase; no increase in particle density was seen in the membrane at an early stage in the forming phagosomes still connected to the surface. These morphological observations are consistent with chemical analyses, to be reported in a separate communication, that show that the phagosome membrane has a higher protein to phospholipid ratio and a higher glycosphingolipid content than the plasma membrane. Enlarged phagosomes (presumptive phagolysosomes) show multiple small vesiculations of characteristic morphology. The small vesicles are postulated to be the major route of membrane return to the cell surface.

scholarly journals Very Cool Clathrin

2005 ◽  
Vol 13 (6) ◽  
pp. 3-7
Author(s):  
Stephen W. Carmichael
Keyword(s):  
Plasma Membrane ◽  
Coated Vesicles ◽  
Membrane Bilayer ◽  
Membrane Bound ◽  
Membranous Component

Clathrin-coated vesicles are the shuttle containers within cells. The vesicles carry lipids and proteins between membrane-bound compartments. Clathrin forms a cage-like structure around the membrane-bound vesicle that is pinched off from the plasma membrane (in endocytosis) or a membranous component of the cytoplasm. Clathrin recruits cargo that is within a vesicle through intermediary proteins known as adaptors that help select membrane-anchored protein and form an interface between the clathrin cage and the membrane bilayer.

Investigation of the role of microtubules in protein secretion from lactating mouse mammary epithelial cells

1992 ◽  
Vol 102 (2) ◽  
pp. 239-247 ◽  
Author(s):  
M.E. Rennison ◽  
S.E. Handel ◽  
C.J. Wilde ◽  
R.D. Burgoyne
Keyword(s):  
Plasma Membrane ◽  
Epithelial Cells ◽  
Protein Secretion ◽  
Secretory Pathway ◽  
Mammary Epithelial Cells ◽  
Early Stage ◽  
Major Effect ◽  
Vesicle Transport ◽  
Mammary Epithelial ◽  
Mammary Cells

Disruption of microtubules has been shown to reduce protein secretion from lactating mammary epithelial cells. To investigate the involvement of microtubules in the secretory pathway in these cells we have examined the effect of nocodazole on protein secretion from mammary epithelial cells derived from the lactating mouse. Mouse mammary cells have extensive microtubule networks and 85% of their tubulin was in a polymeric form. Treatment with 1 micrograms/ml nocodazole converted most of the tubulin into a soluble form. In a continuous labelling protocol it was found that nocodazole did not interfere with protein synthesis but over a 5 h period secretion was markedly inhibited. To determine whether the inhibition was at the level of early or late stages of the secretory pathway mammary cells were pulse-labelled for 1 h to label protein throughout the secretory pathway before nocodazole treatment. When secretion was subsequently assayed it was found to be slower and only partially inhibited. These findings suggest that the major effect of nocodazole is on an early stage of the secretory pathway and that microtubules normally facilitate vesicle transport to the plasma membrane. An involvement of microtubules in vesicle transport to the plasma membrane is consistent with an observed accumulation of casein vesicles in nocodazole-treated cells. Exocytosis stimulated by the calcium ionophore ionomycin was unaffected by nocodazole treatment. We conclude from these results that the major effect of nocodazole is at an early stage of the secretory pathway, one possible target being casein vesicle biogenesis in the trans-Golgi network.

scholarly journals Armadillo nuclear import is regulated by cytoplasmic anchor Axin and nuclear anchor dTCF/Pan

Development ◽  
2001 ◽  
Vol 128 (11) ◽  
pp. 2107-2117 ◽  
Author(s):  
Nicholas S. Tolwinski ◽  
Eric Wieschaus
Keyword(s):  
Drosophila Melanogaster ◽  
Plasma Membrane ◽  
Nuclear Import ◽  
Current Model ◽  
Cellular Distribution ◽  
Nuclear Retention ◽  
Binding Partners ◽  
Wingless Signaling ◽  
Anchoring System ◽  
Import And Export

Drosophila melanogaster Armadillo plays two distinct roles during development. It is a component of adherens junctions, and functions as a transcriptional activator in response to Wingless signaling. In the current model, Wingless signal causes stabilization of cytoplasmic Armadillo allowing it to enter the nucleus where it can activate transcription. However, the mechanism of nuclear import and export remains to be elucidated. In this study, we show that two gain-of-function alleles of Armadillo activate Wingless signaling by different mechanisms. The S10 allele was previously found to localize to the nucleus, where it activates transcription. In contrast, the ΔArm allele localizes to the plasma membrane, and forces endogenous Arm into the nucleus. Therefore, ΔArm is dependent on the presence of a functional endogenous allele of arm to activate transcription. We show that ΔArm may function by titrating Axin protein to the membrane, suggesting that it acts as a cytoplasmic anchor keeping Arm out of the nucleus. In axin mutants, Arm is localized to the nuclei. We find that nuclear retention is dependent on dTCF/Pangolin. This suggests that cellular distribution of Arm is controlled by an anchoring system, where various nuclear and cytoplasmic binding partners determine its localization.

scholarly journals ‘Exceptional sons’ from Drosophila melanogaster mothers carrying a balancer X chromosome

1990 ◽  
Vol 55 (3) ◽  
pp. 159-164 ◽  
Author(s):  
Pierre Hutter
Keyword(s):  
Drosophila Melanogaster ◽  
X Chromosome ◽  
Early Stage ◽  
Interspecific Crosses ◽  
Hybrid Progeny ◽  
Female Hybrid ◽  
Mitotic Event ◽  
Meiotic Event ◽  
Third Instar Larvae

SummaryThis study reports on exceptional males which are obtained by using Drosophila melanogaster mothers carrying the balancers In(l)FM6 or In(l)FM7 as one of their X chromosomes. The phenomenon was first observed in interspecific crosses between D. melanogaster females and males of its closest relatives which normally produce unisexual female hybrid progeny. Whereas hybrid sons from these crosses die as third instar larvae, the presence of the particular X balancers in the mother allows a low percentage of sons to survive. Similar sterile males are also observed among non- hybrid flies. Data are presented which suggest that the males thus generated could be hyperploid for part of their X chromosome as a result of a meiotic event in their mothers or else they could start life as female zygotes and change sex through a mitotic event at an early stage.

scholarly journals ATP- and Cytosol-dependent Release of Adaptor Proteins from Clathrin-coated Vesicles: A Dual Role for Hsc70

1998 ◽  
Vol 9 (8) ◽  
pp. 2217-2229 ◽  
Author(s):  
Lisa A. Hannan ◽  
Sherri L. Newmyer ◽  
Sandra L. Schmid
Keyword(s):  
Plasma Membrane ◽  
Protein Complexes ◽  
Adaptor Protein ◽  
Adaptor Proteins ◽  
Dual Role ◽  
Vesicular Trafficking ◽  
Coated Vesicles ◽  
Golgi Network ◽  
Cytosolic Factor

Clathrin-coated vesicles (CCV) mediate protein sorting and vesicular trafficking from the plasma membrane and the trans-Golgi network. Before delivery of the vesicle contents to the target organelles, the coat components, clathrin and adaptor protein complexes (APs), must be released. Previous work has established that hsc70/the uncoating ATPase mediates clathrin release in vitro without the release of APs. AP release has not been reconstituted in vitro, and nothing is known about the requirements for this reaction. We report a novel quantitative assay for the ATP- and cytosol- dependent release of APs from CCV. As expected, hsc70 is not sufficient for AP release; however, immunodepletion and reconstitution experiments establish that it is necessary. Interestingly, complete clathrin release is not a prerequisite for AP release, suggesting that hsc70 plays a dual role in recycling the constituents of the clathrin coat. This assay provides a functional basis for identification of the additional cytosolic factor(s) required for AP release.

The Drosophila fusome, a germline-specific organelle, contains membrane skeletal proteins and functions in cyst formation

Development ◽  
1994 ◽  
Vol 120 (4) ◽  
pp. 947-956 ◽  
Author(s):  
H. Lin ◽  
L. Yue ◽  
A.C. Spradling
Keyword(s):  
Cyst Formation ◽  
Nurse Cells ◽  
Germline Stem Cells ◽  
Cytoplasmic Structure ◽  
Ring Canals ◽  
Alpha Spectrin ◽  
Polarized Transport ◽  
Form Ring ◽  
Molecular Components ◽  
Number Of Cells

Oogenesis in Drosophila takes place within germline cysts that support polarized transport through ring canals interconnecting their 15 nurse cells and single oocyte. Developing cystocytes are spanned by a large cytoplasmic structure known as the fusome that has been postulated to help form ring canals and determine the pattern of nurse cell-oocyte interconnections. We identified the adducin-like hts product and alpha-spectrin as molecular components of fusomes, discovered a related structure in germline stem cells and documented regular associations between fusomes and cystocyte centrosomes. hts mutations completely eliminated fusomes, causing abnormal cysts containing a reduced number of cells to form. Our results imply that Drosophila fusomes are required for ovarian cyst formation and suggest that membrane skeletal proteins regulate cystocyte divisions.

Recent findings in oogenesis of Drosophila melanogaster

Development ◽  
1977 ◽  
Vol 39 (1) ◽  
pp. 45-57
Author(s):  
F. Giorgi ◽  
J. Jacob
Keyword(s):  
Drosophila Melanogaster ◽  
Acid Phosphatase ◽  
Ovarian Development ◽  
Superficial Layer ◽  
Blood Proteins ◽  
Selective Hydrolysis ◽  
Internal Lining ◽  
Hydrolysis Of ◽  
Zinc Iodide ◽  
Yolk Platelet

The role played by the vitellogenic oocytes of Drosophila melanogaster in relation to the elaboration of material taken from the haemolymph is examined by ultrastructural cytochemistry. As revealed by the Gomori procedure, acid phosphatase occurs widely over the forming yolk platelets of the cortical and central ooplasm. A number of Golgi apparatuses in thecortical ooplasm are also positively stained with lead precipitates. With the proceeding of the ovarian development it becomes progressively more difficult to demonstrate cytochemically the enzyme over the yolk platelets. In stage 9–10 chambers the acid phosphatase is restricted to the so-called associated body, while the rest of the yolk platelet appears devoid of lead deposits. By using a osmium zinc iodide (OZ1) complex as a preferential staining method for the Golgi apparatus, it has been shown that, apart from the apparatus itself, a number of OZI deposits occur over the superficial layer of the forming yolk platelets. When mature yolk platelets are formed at later stages, the OZI deposits in the yolk platelets come to be restricted to the cap-like region of the superficial layer which contains the associated body. In vitellogenic oocytes, both the internal lining of the limiting membrane of the forming yolk platelets and the associated body of the mature yolk platelets react positively, to cytochemical methods to demonstrate carbohydrates. The present findings are interpreted as indicating the involvement of lysosomal enzymes in the process of maturation of the yolk material. The suggestion is also made that such an involvement is required to accomplish a selective hydrolysis of those blood proteins which have been taken in by vitellogenic oocytes along with yolk precursors.

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