Differentiation Processes of the Ocellar Retina of the Honeybee (Apis Mellifera L.)

1990 ◽  
Vol 48 (3) ◽  
pp. 430-431
Author(s):  
Maria Anna Pabst
Keyword(s):  
Apis Mellifera ◽  
Distal Part ◽  
Cell Layer ◽  
Single Layer ◽  
Photoreceptor Cells ◽  
Distal Segment ◽  
Compound Eyes ◽  
Thin Sections ◽  
Ultrastructural Studies ◽  
Adult Worker

In addition to the compound eyes, honeybees have three dorsal ocelli on the vertex of the head. Each ocellus has about 800 elongated photoreceptor cells. They are paired and the distal segment of each pair bears densely packed microvilli forming together a platelike fused rhabdom. Beneath a common cuticular lens a single layer of corneagenous cells is present.Ultrastructural studies were made of the retina of praepupae, different pupal stages and adult worker bees by thin sections and freeze-etch preparations. In praepupae the ocellar anlage consists of a conical group of epidermal cells that differentiate to photoreceptor cells, glial cells and corneagenous cells. Some photoreceptor cells are already paired and show disarrayed microvilli with circularly ordered filaments inside. In ocelli of 2-day-old pupae, when a retinogenous and a lentinogenous cell layer can be clearly distinguished, cell membranes of the distal part of two photoreceptor cells begin to interdigitate with each other and so start to form the definitive microvilli. At the beginning the microvilli often occupy the whole width of the developing rhabdom (Fig. 1).

Probing the ultrastructure of the mitotic and meiotic spindle in eggs: An expeditious approach based on semi-thin (0.25 μm) serial sections

1983 ◽  
Vol 41 ◽  
pp. 552-555
Author(s):  
Conly L. Rieder ◽  
S. Bowser ◽  
R. Nowogrodzki ◽  
K. Ross ◽  
G. Sluder
Keyword(s):  
Small Sample Size ◽  
Small Sample ◽  
Meiotic Spindle ◽  
Serial Sections ◽  
Mitotic Apparatus ◽  
Thin Sections ◽  
Cell Cycles ◽  
Ultrastructural Studies

Eggs have long been a favorite material for studying the mechanism of karyokinesis in-vivo and in-vitro. They can be obtained in great numbers and, when fertilized, divide synchronously over many cell cycles. However, they are not considered to be a practical system for ultrastructural studies on the mitotic apparatus (MA) for several reasons, the most obvious of which is that sectioning them is a formidable task: over 1000 ultra-thin sections need to be cut from a single 80-100 μm diameter egg and of these sections only a small percentage will contain the area or structure of interest. Thus it is difficult and time consuming to obtain reliable ultrastructural data concerning the MA of eggs; and when it is obtained it is necessarily based on a small sample size.We have recently developed a procedure which will facilitate many studies concerned with the ultrastructure of the MA in eggs. It is based on the availability of biological HVEM's and on the observation that 0.25 μm thick serial sections can be screened at high resolution for content (after mounting on slot grids and staining with uranyl and lead) by phase contrast light microscopy (LM; Figs 1-2).

scholarly journals Visualization of intracellular concanavalin A binding sites in retinal photoreceptors.

1978 ◽  
Vol 26 (10) ◽  
pp. 822-828 ◽  
Author(s):  
I Nir
Keyword(s):  
Concanavalin A ◽  
Binding Sites ◽  
Photoreceptor Cells ◽  
Con A ◽  
Thin Sections ◽  
Glycol Methacrylate ◽  
Outer Segments ◽  
Retinal Photoreceptors ◽  
Carbohydrate Components ◽  
The Relationship

Localization of carbohydrate components in retinal photoreceptor cells and membranes was studied. Frog and rat retinas were fixed with glutaraldehyde and embedded in glycol methacrylate or in a mixture of glycol methacrylate, glutaraldehyde and urea. Thin sections were incubated with ferritin-labeled concanavalin A (F-Con A) and stained with osmium vapors. Intensive binding was observed in both rod and cone outer segments. In the rod inner segment, differential binding of F-Con A was demonstrated. While numerous ferritin granules were observed in the myoid zone, only a few were seen in the ellipsoid zone, except for a local accumulation along the plasma membrane. In the rod outer segment, Con A binding sites were closely associated with the disk membranes. Ferritin granules were observed on both sides of the membranes. The relationship between the localization of Con A binding sites and the orientation of visual pigment molecules within the rod outer segments disk membranes was discussed.

An unusual cell surface modification: a double plasma membrane

1979 ◽  
Vol 39 (1) ◽  
pp. 355-372
Author(s):  
N.J. Lane ◽  
J.B. Harrison
Keyword(s):  
Plasma Membrane ◽  
Membrane Structure ◽  
Cell Layer ◽  
Peritrophic Membrane ◽  
Thin Sections ◽  
Double Membrane ◽  
Freeze Fracturing ◽  
Blood Sucking ◽  
Great Pressure ◽  
Insertion Sites

The occurrence of an unusual double plasma membrane structure is reported; it has been studied in conventional thin sections, after lanthanum-impregnation and with freeze-fracturing. This modification of the plasmalemma is found where the luminal cell membrane (I membrane) of gut microvilli in the haematophagous insect, Rhodnius prolixus, is surrounded by a second, outer membrane (O membrane), the 2 separated from one another by a highly regular I-O space of about 10 nm. Lanthanum impregnation reveals the presence of columns inclined at an angle, within this I-O space; as in the continuous junctions which link the lateral borders of these cells, these columns may maintain the very precise I-O distance. From the outer microvillar membranes radiate short spoke-like fibrils or sheets which encounter another more extensive system of myelin-like sheets. Freeze-fracturing reveals that the spoke-like sheets and the other ones which lie like a tube, around and parallel to the microvilli, contain linear ridges composed of particles, lying at random within layers of the myelin-like material which also extends into the lumen of the gut. The microvillar membanes, both O and I, fracture into faces containing rows of either PF particles or EF pits arranged as spiral ridges or grooves around the sides and across the tip of each microbillus. These could be the insertion sites of one or both of the I-O columns and spoke-like sheets while the sheets could represent a variant of peritrophic membrane. The double membrane may be a cellular device to increase the strength of the microvillar layer in these blood-sucking animals, since the cell layer must withstand great pressure owing to a sudden massive extension of the gut during a blood meal.

scholarly journals Transcriptional Control of Honey Bee (Apis mellifera) Major Royal Jelly Proteins by 20-Hydroxyecdysone

Insects ◽  
2018 ◽  
Vol 9 (3) ◽  
pp. 122 ◽  
Author(s):  
Paul Winkler ◽  
Frank Sieg ◽  
Anja Buttstedt
Keyword(s):  
Gene Expression ◽  
Apis Mellifera ◽  
Juvenile Hormone ◽  
Honey Bee ◽  
Honey Bees ◽  
Transcriptional Control ◽  
Royal Jelly ◽  
Adult Worker ◽  
Gene Expression Dynamics

One of the first tasks of worker honey bees (Apis mellifera) during their lifetime is to feed the larval offspring. In brief, young workers (nurse bees) secrete a special food jelly that contains a large amount of unique major royal jelly proteins (MRJPs). The regulation of mrjp gene expression is not well understood, but the large upregulation in well-fed nurse bees suggests a tight repression until, or a massive induction upon, hatching of the adult worker bees. The lipoprotein vitellogenin, the synthesis of which is regulated by the two systemic hormones 20-hydroxyecdysone and juvenile hormone, is thought to be a precursor for the production of MRJPs. Thus, the regulation of mrjp expression by the said systemic hormones is likely. This study focusses on the role of 20-hydroxyecdysone by elucidating its effect on mrjp gene expression dynamics. Specifically, we tested whether 20-hydroxyecdysone displayed differential effects on various mrjps. We found that the expression of the mrjps (mrjp1–3) that were finally secreted in large amounts into the food jelly, in particular, were down regulated by 20-hydroxyecdysone treatment, with mrjp3 showing the highest repression value.

Regional differences in potassium content of smooth muscle from opossum esophagus.

1978 ◽  
Vol 235 (6) ◽  
pp. E709
Author(s):  
K Schulze ◽  
J J Hajjar ◽  
J Christensen
Keyword(s):  
Smooth Muscle ◽  
Distal Part ◽  
Proximal Part ◽  
Distal Segment ◽  
Intracellular Concentration ◽  
Potassium Content ◽  
Intracellular Potassium ◽  
The Mean ◽  
Intracellular Potassium Concentration ◽  
Space Volume

Strips from the proximal part of the smooth muscle segment of opossum esophagus have a significantly higher potassium content (50 +/- 3 meq/kg) than those from the distal part (38 +/- 3 meq/kg). There are no significant differences between the two regions in content of sodium (65 +/- 4 meq/kg in proximal, 71 +/- 3 meq/kg in distal) or chloride (48 +/- 10 meq/kg in proximal, 42 +/- 5 meq/ kg in distal). The mean [14C]inulin uptake is 240 +/- 10 ml/kg in both proximal and distal strips. [14C]polyethylene glycol uptake is smaller and [14C]sucrose and [14C]mannitol uptake in both areas are larger than that of inulin. Intracellular potassium concentration (based on the inulin uptake as an estimate of the extracellular space volume) is significantly higher proximally (71 +/- 3 mM) than distally (52 +/- mM). Ouabain, 10(-4) M, increases the intracellular concentration of sodium and decreases the intracellular concentration of potassium in both the proximal and distal segment. The efflux of 86Rb, measured by a washout technique, is higher in the distal than in the proximal smooth muscle segment. A difference in membrane permeability to rubidium and hence, potassium between proximal and distal smooth muscle segments may account in part for the different intracellular potassium concentrations.

scholarly journals Morphological peculiarities of neuromuscular junctions among different fiber types: Effect of exercise

2017 ◽  
Vol 27 (3) ◽  
Author(s):  
Teet Seene ◽  
Maria Umnova ◽  
Priit Kaasik
Keyword(s):  
Axon Terminal ◽  
Neuromuscular Junctions ◽  
Muscle Fibers ◽  
Cross Sectional Area ◽  
Fiber Types ◽  
Sectional Area ◽  
Cross Sectional ◽  
Thin Sections ◽  
Axon Terminals ◽  
Ultrastructural Studies

The aim of our research was to examine whether there are differences in the morphology of neuromuscular junctions of different types of muscle fibers in rodents, and after their adaptation to six weeks endurance exercise training. After 5-day acclimation, Wistar rats were subjected to run with the speed 35 m/min during 6 week, 5 days per week and the training volume reached 60 min per day. Muscle samples for ultrastructural studies were fixed, dehydrated and embedded in Epon-812. Ultra-thin sections were cut from longitudinally and transversely oriented blocs, using 4 blocks from each animal. The area of axon terminals on fast- twitch fibers is 1.5 time large (p<0.001) and the perimeter of terminals is 1.7 time large in comparison with slow- twitch oxidative fibers (p<0.001) in control group. There are correlation between cross-sectional area of different muscle fibers and length of axon terminals (r=0.72), between cross-sectional area and with of axon terminal (r=-0.62), and between turnover rate of contractile proteins and length of axon terminal (r=0.75). Fast remodeling of synapse on oxidative and oxidative-glycolytic muscle fibers during endurance training seems to guarantees the intensive renewal of the structures of muscle fibers with higher oxidative capacity.

Organisation and ultrastructure of the regenerative crypts in the midgut of the adult worker honeybee (L. Apis mellifera)

1994 ◽  
Vol 26 (2) ◽  
pp. 231-238 ◽  
Author(s):  
H. Raes ◽  
M. Verbeke ◽  
W. Meulemans ◽  
W.De Coster
Keyword(s):  
Apis Mellifera ◽  
Adult Worker

scholarly journals Ultrastructural and molecular characteristics of crayfish photoreceptor membranes.

1976 ◽  
Vol 69 (3) ◽  
pp. 721-732 ◽  
Author(s):  
H R Fernandez ◽  
E E Nickel
Keyword(s):  
Freeze Fracture ◽  
Photoreceptor Cells ◽  
Molecular Characteristics ◽  
Thin Sections ◽  
Freeze Fracturing ◽  
Mean Diameter ◽  
Hexagonal Arrangement ◽  
Photoreceptor Membranes

The ultrastructure of photoreceptor cells of the crayfish (P. clarkii) has been examined by means of thin sections and freeze-fracturing. The study reveals that in the photoreceptor membranes there are particles associated primarily with the A faces of freeze-fracture preparations which have a mean diameter of 80-84 A and a density of 6,600 per per micrometer2. Treatment of the retina with digitonin (a substance capable of extracting visual photopigments) in Ringer's causes marked disruption of the hexagonal arrangement of the microvilli, breakdown of the microvilli into smaller segments, and gradual removal of the particles. The estimated photopigment concentration in the microvillus is 4,000 per micrometer. It is suggested that the observed particles represent the photopigment in situ.

scholarly journals Hereditary Suprabasilar Acantholytic Mechanobullous Dermatosis in Buffaloes (Bubalus bubalis)

1994 ◽  
Vol 31 (4) ◽  
pp. 450-454 ◽  
Author(s):  
F. Riet-Correa ◽  
S. S. Barros ◽  
M. C. Dame ◽  
P. V. Peixoto
Keyword(s):  
Autosomal Recessive ◽  
Cell Layer ◽  
Single Layer ◽  
Bubalus Bubalis ◽  
Recessive Trait ◽  
Intercellular Spaces ◽  
Outer Root Sheath ◽  
Root Sheath ◽  
Stratum Spinosum ◽  
Histologic Evaluation

A skin disease characterized by trauma-induced sloughing of haired skin, hooves, and horns is described in four calves from a herd of Murrah buffaloes ( Bubalus bubalis) in Brazil. Affected calves were detected shortly after birth by the presence of lesions affecting the distal extremities, the scapular and gluteal regions, and the tip of the tail. On histologic evaluation of affected skin, the lesions were characterized by suprabasilar vesicles and acantholysis affecting the epidermis and outer root sheath of the hair follicle infundibulum. The basal cell layer was intact and appeared as a single layer of cuboidal cells attached to the dermis. Ultrastructurally, the region between the stratum basale and the lower stratum spinosum had widened intercellular spaces with loss of desmosomal attachments, which led to the suprabasilar separation. The disease appears to be inherited as an autosomal recessive trait.

scholarly journals Immunocytochemical localization of opsin in outer segments and Golgi zones of frog photoreceptor cells. An electron microscope analysis of cross-linked albumin-embedded retinas

1978 ◽  
Vol 77 (1) ◽  
pp. 196-210 ◽  
Author(s):  
DS Papermaster ◽  
BG Schneider ◽  
MA Zorn ◽  
JP Kraehenbuhl
Keyword(s):  
Electron Microscope ◽  
Outer Segment ◽  
Specific Binding ◽  
Photoreceptor Cells ◽  
Indirect Detection ◽  
Thin Sections ◽  
Rods And Cones ◽  
Outer Segments ◽  
Cell Structures ◽  
Cone Photopigments

Adult vertebrate retinal cells (rod and cones) continuously synthesize membrane proteins and transport them to the organelle specialized for photon capture, the outer segment. The cell structures involved in the synthesis of opsin have been identified by means of immunocytochemistry at the electron microscope level. Two indirect detection systems were used: (a) rabbit antibodies to frog opsin were localized with ferritin conjugated F(ab')2 of sheep antibodies to rabbit F(ab')2 and (b) sheep antibodies to cattle opsin were coupled to biotin and visualized by means of avidin-ferritin conjugates (AvF). The reagents were applied directly to the surface of thin sections of frog retinal tissues embedded in glutaraldehyde cross-linked bovine serum albumin (BSA). Specific binding of anti-opsin antibodies indicates that opsin is localized in the disks of rod outer segments (ROS), as expected, and in the Golgi zone of the rod cell inner segments. In addition, we observed quantitatively different labeling patterns of outer segments of rods and cones with each of the sera employed. These reactions may indicate immunological homology of rod and cone photopigments. Because these quantitiative variations of labeling density extend along the entire length of the outer segment, they also serve to identify the cell which has shed its disks into adjacent pigment ipithelial cell phagosomes.

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