Morphogenèse de l'épiderme imaginal de l'abdomen de Calliphora erythrocephala (Insecte, Diptère)

Development ◽  
1978 ◽  
Vol 43 (1) ◽  
pp. 247-261
Author(s):  
Par Anne-Marie Bautz
Keyword(s):  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Rough Endoplasmic Reticulum ◽  
Cellular Proliferation ◽  
Epidermal Cells ◽  
Sensory Cells ◽  
Calliphora Erythrocephala ◽  
Abdominal Surface ◽  
Intense Activity

The morphogenesis of the abdominal epidermis in Calliphora erythrocephala begins by a cellular proliferation which proceeds slowly in larvae and rapidly in pupae. This allows histoblasts to glide and invade the whole abdominal surface. As soon as the new epidermal sheet has become continuous, differentiation begins. Generalized epidermal cells show an intense activity which leads to the deposition of imaginal cuticle from the 6th day after pupation onwards. After cuticle deposition they darken and become inactive although they remain alive, even after emergence. Trichogen and tormogen cells are even more active than generalized epidermal cells, especially the trichogen cell in which polyribosomes and microtubules are abundant. The former are possibly involved in microtubule synthesis. After cuticle deposition the trichogen and tormogen cells undergo degeneration. Their nuclei contract, rough endoplasmic reticulum breaks down and cytoplasm breaks up into fragments through infoldings which proliferate from the plasma membrane. Finally only generalized epidermal cells and sensory cells remain alive in the adult.

scholarly journals Cytochemical demonstration of extraperoxisomal catalase. I. Sheep liver.

1976 ◽  
Vol 24 (6) ◽  
pp. 713-724 ◽  
Author(s):  
F Roels
Keyword(s):  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Golgi Apparatus ◽  
Rough Endoplasmic Reticulum ◽  
Catalase Activity ◽  
Nonparenchymal Cells ◽  
Sheep Liver ◽  
Heat Stable ◽  
Cytochemical Demonstration ◽  
Electron Microscopes

In sheep hepatocytes catalase activity was demonstrated both within peroxisomes and within the cytosol. In the cytosol the catalase reaction product is contiguous to the plasma membrane and surrounds the nuclei, rough endoplasmic reticulum, cisternae, mitochondria and Golgi apparatus. This is the first cytochemical demonstration of guine extraperoxisomal catalase. No catalase reaction product was seen in the cytosol of nonparenchymal cells. To demonstrate catalase, both glutaraldehyde and formaldehyde fixation were used, followed by a diaminobenzidine technique modified from Novikoff and Goldfischer. Control reactions were performed to distinguish catalase reaction product from adsorption of oxidized diaminobenzidine and from precipitate due to oxidase-, peroxidase- or heat-stable peroxidatic activities. The results were evaluated in the light and electron microscopes.

Development of the lateral palatal brush in larvae of Aedes aegypti (L.) (Diptera: Culicidae)

1990 ◽  
Vol 68 (7) ◽  
pp. 1454-1467 ◽  
Author(s):  
K. M. Fry ◽  
S. B. McIver
Keyword(s):  
Electron Microscopy ◽  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Golgi Apparatus ◽  
Aedes Aegypti ◽  
Rough Endoplasmic Reticulum ◽  
Light And Electron Microscopy ◽  
Fourth Instar ◽  
Muscle Fibres ◽  
Final Length

Light and electron microscopy were used to observe development of the lateral palatal brush in Aedes aegypti (L.) larvae. Development was sampled at 4-h intervals from second- to third-instar ecdyses. Immediately after second-instar ecdysis, the epidermis apolyses from newly deposited cuticle in the lateral palatal pennicular area to form an extensive extracellular cavity into which the fourth-instar lateral palatal brush filaments grow as cytoplasmic extensions. On reaching their final length, the filaments deposit cuticulin, inner epicuticle, and procuticle sequentially on their outer surfaces. The lateral palatal crossbars, on which the lateral palatal brush filaments insert, form after filament development is complete. At the beginning of development, the organelles involved in plasma membrane and cuticle production are located at the base and middle of the cells. As the filament rudiments grow, most rough endoplasmic reticulum, mitochondria, and Golgi apparatus move to the apex of the epidermal cells and into the filament rudiments. After formation of the lateral palatal brush filaments and lateral palatal crossbars, extensive organelle breakdown occurs. Lateral palatal brush formation is unusual in that no digestion and resorption of old endocuticle occurs prior to deposition of new cuticle. No mucopolysaccharide secretion by the lateral palatal brush epidermis was observed, nor were muscle fibres observed to attach to the lateral palatal crossbars, as has been suggested by other workers.

Freeze-Fracture Replication of Rough Endoplasmic Reticulum of Mouse Liver Cells

1972 ◽  
Vol 11 (2) ◽  
pp. 477-489
Author(s):  
A. S. BREATHNACH ◽  
C. STOLINSKI ◽  
M. GROSS
Keyword(s):  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Rough Endoplasmic Reticulum ◽  
Nuclear Membrane ◽  
Mouse Liver ◽  
Freeze Fracture ◽  
The Other ◽  
Fracture Face ◽  
Mitochondrial Membranes ◽  
En Face

Fresh, chemically unfixed, glycerinated specimens of mouse liver were examined by the technique of freeze-fracture replication without sublimation (i.e. they were not ‘etched’). Where extensive areas of fractured lamellar membranes of the rough endoplasmic reticulum are revealed en face, 2 types of fracture face are distinguishable. One of these fracture faces (A) is directed towards the cytoplasm, and the other (B) towards the cisternal cavity. A characteristic mosaic, or patchwork pattern of flat areas circumscribed by particles, is evident on both faces, and more clearly so on face B, due to a greater number of more prominent particles. Similar mosaic patterns are revealed on convex faces of the nuclear membrane, and on concave fracture faces of mitochondrial membranes, but are not evident on fracture faces of the plasma membrane. Uncertainty in establishing the exact plane of fracture of membranes in this material, since glycerol is virtually non-sublimable, makes it difficult to assess the significance of these mosaic patterns. The fact that ribosomes are not identifiable on either face of fractured endoplasmic reticulum membranes, gives no certain indication of the plane of fracture.

scholarly journals Effect of microtubule assembly status on the intracellular processing and surface expression of an integral protein of the plasma membrane.

1984 ◽  
Vol 99 (3) ◽  
pp. 1101-1109 ◽  
Author(s):  
A A Rogalski ◽  
J E Bergmann ◽  
S J Singer
Keyword(s):  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Golgi Apparatus ◽  
G Protein ◽  
Rough Endoplasmic Reticulum ◽  
Intracellular Transport ◽  
Temperature Shift ◽  
Surface Expression ◽  
Microtubule Assembly ◽  
In Cells

We studied the effects of changes in microtubule assembly status upon the intracellular transport of an integral membrane protein from the rough endoplasmic reticulum to the plasma membrane. The protein was the G glycoprotein of vesicular stomatitis virus in cells infected with the Orsay-45 temperature-sensitive mutant of the virus; the synchronous intracellular transport of the G protein could be initiated by a temperature shift-down protocol. The intracellular and surface-expressed G protein were separately detected and localized in the same cells at different times after the temperature shift, by double-immunofluorescence microscopic measurements, and the extent of sialylation of the G protein at different times was quantitated by immunoprecipitation and SDS PAGE of [35S]methionine-labeled cell extracts. Neither complete disassembly of the cytoplasmic microtubules by nocodazole treatment, nor the radical reorganization of microtubules upon taxol treatment, led to any perceptible changes in the rate or extent of G protein sialylation, nor to any marked changes in the rate or extent of surface appearance of the G protein. However, whereas in control cells the surface expression of G was polarized, at membrane regions in juxtaposition to the perinuclear compact Golgi apparatus, in cells with disassembled microtubules the surface expression of the G protein was uniform, corresponding to the intracellular dispersal of the elements of the Golgi apparatus. The mechanisms of transfer of integral proteins from the rough endoplasmic reticulum to the Golgi apparatus, and from the Golgi apparatus to the plasma membrane, are discussed in the light of these observations, and compared with earlier studies of the intracellular transport of secretory proteins.

scholarly journals Sch proteins are localized on endoplasmic reticulum membranes and are redistributed after tyrosine kinase receptor activation.

1996 ◽  
Vol 16 (5) ◽  
pp. 1946-1954 ◽  
Author(s):  
L V Lotti ◽  
L Lanfrancone ◽  
E Migliaccio ◽  
C Zompetta ◽  
G Pelicci ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Tyrosine Kinase ◽  
Rough Endoplasmic Reticulum ◽  
Receptor Tyrosine Kinase ◽  
Receptor Activation ◽  
Kinase Activation ◽  
Epidermal Growth

The intracellular localization of Shc proteins was analyzed by immunofluorescence and immunoelectron microscopy in normal cells and cells expressing the epidermal growth factor receptor or the EGFR/erbB2 chimera. In unstimulated cells, the immunolabeling was localized in the central perinuclear area of the cell and mostly associated with the cytosolic side of rough endoplasmic reticulum membranes. Upon epidermal growth factor treatment and receptor tyrosine kinase activation, the immunolabeling became peripheral and was found to be associated with the cytosolic surface of the plasma membrane and endocytic structures, such as coated pits and endosomes, and with the peripheral cytosol. Receptor activation in cells expressing phosphorylation-defective mutants of Shc and erbB-2 kinase showed that receptor autophosphorylation, but not Shc phosphorylation, is required for redistribution of Shc proteins. The rough endoplasmic reticulum localization of Shc proteins in unstimulated cells and their massive recruitment to the plasma membrane, endocytic structures, and peripheral cytosol following receptor tyrosine kinase activation could account for multiple putative functions of the adaptor protein.

scholarly journals Temporal and spatial distribution of V-ATPase and its mRNA in the midgut of moulting Manduca sexta.

1996 ◽  
Vol 199 (5) ◽  
pp. 1019-1027
Author(s):  
D Jäger ◽  
F J Novak ◽  
W R Harvey ◽  
H Wieczorek ◽  
U Klein
Keyword(s):  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Manduca Sexta ◽  
Rough Endoplasmic Reticulum ◽  
Larval Instar ◽  
Goblet Cells ◽  
Apical Plasma Membrane ◽  
Tissue Preparation ◽  
Temporal And Spatial Distribution ◽  
Columnar Cells

The spatial and temporal distribution of the plasma membrane V-ATPase and its encoding mRNA in the midgut of Manduca sexta were investigated during the moult from the fourth to the fifth larval instar. Digoxigenin-labelled RNA probes were used for in situ hybridization of V-ATPase mRNA of both peripheral and integrated subunits; monoclonal antibodies to subunits of the peripheral sector of the purified plasma membrane V-ATPase were used for immunocytochemistry. Extensive mRNA labelling was found in both mature columnar and goblet cells of intermoult and moulting larvae. Hybridization screening in several tissues suggested that only cells with increased V-ATPase biosynthesis were labelled by our hybridization method. Mature goblet cells contain a large amount of V-ATPase in the apical plasma membrane and were therefore expected to contain V-ATPase mRNA. The intense mRNA signal found in mature columnar cells was unexpected. However, after refining the techniques of tissue preparation, immunolabelling in apical blebs of columnar cells was demonstrated. Since this immunoreactivity did not appear to be membrane-associated, it suggested a cytosolic localization of peripheral V1 subunits. The mRNA encoding subunit A of the peripheral V1 sector was distributed unevenly in columnar cells with a strong apical preference, whereas the mRNA for the proteolipid of the integral V0 sector was evenly distributed in the cytosol. This spatial pattern reflected the distribution of free ribosomes and rough endoplasmic reticulum in the cell, supporting the view that V1 subunits are synthesized at free ribosomes, whereas the V0 subunits are synthesized at the rough endoplasmic reticulum. All undifferentiated cells exhibited intense mRNA signals for V-ATPase subunits of both holoenzyme sectors from the start of proliferation and thus precursors of columnar and goblet cells could not be distinguished.

Sign in / Sign up

Export Citation Format

Share Document