A comparative account of cyst coat ontogeny in saprophytic and fish-lesion (pathogenic) isolates of the Saprolegnia diclina – parasitica complex

1983 ◽  
Vol 61 (2) ◽  
pp. 603-625 ◽  
Author(s):  
Gordon Beakes
Keyword(s):  
Endoplasmic Reticulum ◽  
Rough Endoplasmic Reticulum ◽  
Phylogenetic Significance ◽  
High Concentration ◽  
Protease Digestion

The ultrastructural development of encystment vesicles (formerly bar bodies) and the outer cyst coat has been examined in primary and secondary spores of a range of isolates of Saprolegnia, mostly from the S. diclina – parasitica complex, of both saprophytic and fish-lesion origin. The development of both primary encystment vesicles (PEVs) in zoosporangia and secondary encystment vesicles (SEVs) in primary cysts appears essentially similar. The vesicles are probably derived from the rough endoplasmic reticulum system. The tubular primary spines and solid secondary boathooks seem to form autonomously within the vesicle matrix. Upon settling all of the preformed encystment vesicles are liberated from the zoospores to give rise to an electron-dense, amorphous, outer cyst coat, in which the spines are embedded. Fish-lesion isolates of S. parasitica have longer tubules on their primary cysts than saprophytic isolates and have distinctive bundles of long (<10 μm) boathooks on their secondary cysts compared with the single short (< 1.0 μm) boathooks typical of the saprophytes. However, even in fish-lesion isolates considerable variation in SEV and boathook sizes was observed. Staining by the Thiéry procedure revealed a high concentration of polysaccharidelike material with both the encystment vesicle cortex layer and spines, although treatment with various glucanases and proteases failed to digest either component. Spherical fibrous vesicles also appear in primary cysts and their contents are partially removed by protease digestion. These appear morphologically similar to the glycoprotein adhesive vesicles described in other oomycetes and appear to be discharged by secondary zoospores. The complex encystment apparatus in Saprolegnia is compared with that described in other oomycete and chytridiomycete fungi and the possible phylogenetic significance discussed. The role of the long boathook spines in relation to the infection of fish is also considered.

The Role of Endoplasmic Reticulum in the Repair of Amoeba Nuclear Envelopes Damaged Microsurgically

1974 ◽  
Vol 14 (2) ◽  
pp. 421-437
Author(s):  
C. J. FLICKINGER
Keyword(s):  
Endoplasmic Reticulum ◽  
Nuclear Envelope ◽  
Rough Endoplasmic Reticulum ◽  
Repair Process ◽  
Nuclear Membranes ◽  
Normal Configuration ◽  
Layer Characteristic ◽  
The Relationship ◽  
Coated Slide

The nuclear envelopes of amoebae were damaged microsurgically, and the fate of the lesions was studied with the electron microscope. Amoebae were placed on the surface of an agar-coated slide. Using a glass probe, the nucleus was pushed from an amoeba, damaged with a chopping motion of the probe, and reinserted into the amoeba. Cells were prepared for electron microscopy at intervals of between 10 min and 4 days after the manipulation. Nuclear envelopes studied between 10 min and 1 h after the injury displayed extensive damage, including numerous holes in the nuclear membranes. Beginning 15 min after the manipulation, pieces of rough endoplasmic reticulum intruded into the holes in the nuclear membranes. These pieces of rough endoplasmic reticulum subsequently appeared to become connected to the nuclear membranes at the margins of the holes. By 1 day following the injury, many cells had died, but the nuclear membranes were intact in those cells that survived. The elaborate fibrous lamina or honeycomb layer characteristic of the amoeba nuclear envelope was resistant to early changes after the manipulation. Patches of disorganization of the fibrous lamina were present 5 h to 1 day after injury, but the altered parts showed evidence of progress toward a return to normal configuration by 4 days after the injury. It is proposed that the rough endoplasmic reticulum participates in the repair of injury to the nuclear membranes. The similarity of this repair process to reconstitution of the nuclear envelope in telophase of mitosis is noted, and the relationship between the nuclear envelope and the rough endoplasmic reticulum is discussed.

scholarly journals Localization of thyroglobulin antigenicity in rat thyroid sections using antibodies labled with peroxidase or (125)I-radioiodine

1977 ◽  
Vol 74 (3) ◽  
pp. 992-1015 ◽  
Author(s):  
J Paiement ◽  
CP Leblond
Keyword(s):  
Endoplasmic Reticulum ◽  
Rough Endoplasmic Reticulum ◽  
Follicular Cells ◽  
Lysosomal Degradation ◽  
High Concentration ◽  
Different Types ◽  
Apical Vesicles ◽  
Rat Thyroid ◽  
Silver Grains ◽  
Distinct Distribution

In the hope of localizing thyroglobulin within focullar cells of the thyroid gland, antibodies raised against rat thyroglobulin were labeled with the enzyme horseradish peroxidase or with (125)I-radioiodine. Sections of rat thyroids fixed in glutaraldehyde and embedded in glycol methacrylate or Araldite were placed in contact with the labeled antibodies. The sites of antibody binding were detected by diaminobenzidine staining in the case of peroxidase labeling, and radioautography in the case of 125(I) labeling. Peroxidase labeling revealed that the antibodies were bound by the luminal colloid of the thyroid follicles and, within focullar cells, by colloid droplets, condensing vacuoles, and apical vesicles. (125)I labeling confirmed these findings, and revealed some binding of antibodies within Golgi saccules and rough endoplasmic reticulum. This method provides a visually less distinct distribution than peroxidase labeling, but it allowed ready quantitation of the reactions by counts of silver grains in the radioautographs. The counts revealed that the concentration of label was similar in the luminal colloid of different follicles, but that it varied within the compartments of follicular cells. A moderate concentration was detected in rough endoplasmic reticulum and Golgi saccules, whereas a high concentration was found in condensing vacuoles, apical vesicles, and in the luminal colloid. Varying amounts of label were observed over the different types of colloid droplets, and this was attributed to various degrees of lysosomal degradation of thyroglobulin. It is concluded that the concentration of thyroglobulin antigenicity increases during transport from the ribosomal site of synthesis to the follicular colloid, and then decreases during the digestion of colloid droplets which leads to the release of the thyoid hormone.

The Role of Membrane Proteins and Phospholipids in the Interaction of Ribosomes with Endoplasmic Reticulum Membranes

1975 ◽  
Vol 53 (9) ◽  
pp. 1039-1045 ◽  
Author(s):  
Serge Jothy ◽  
Jean-Louis Bilodeau ◽  
Henry Simpkins
Keyword(s):  
Endoplasmic Reticulum ◽  
Membrane Proteins ◽  
Rat Liver ◽  
Rough Endoplasmic Reticulum ◽  
Binding Sites ◽  
Molecular Weights ◽  
Low Concentrations ◽  
Phospholipid Headgroups ◽  
Hydrolysis Of

Hydrolysis of the membrane proteins and phospholipid headgroups of rat liver rough endoplasmic reticulum membranes showed that the ribosomal binding sites involve membrane proteins susceptible to low concentrations of trypsin, chymotrypsin, and papain. Three membrane proteins having molecular weights of 120 000, 93 000 and 36 000 are found to be altered by trypsin and chymotrypsin treatment. Also the polar headgroup of phosphatidylinositol appears to play a role in the binding process.

Two different mutants blocked in synthesis of dolichol-phosphoryl-mannose do not add glycophospholipid anchors to membrane proteins: quantitative correction of the phenotype of a CHO cell mutant with tunicamycin

1991 ◽  
Vol 11 (1) ◽  
pp. 391-400
Author(s):  
N Singh ◽  
A M Tartakoff
Keyword(s):  
Alkaline Phosphatase ◽  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Membrane Proteins ◽  
Rough Endoplasmic Reticulum ◽  
Essential Role ◽  
Placental Alkaline Phosphatase ◽  
Cho Cell ◽  
Cell Mutant

The addition of glycophospholipid (GPL) anchors to certain membrane proteins occurs in the rough endoplasmic reticulum and is essential for transport of the proteins to the plasma membrane. Limited circumstantial evidence suggests that dolichol-phosphoryl-mannose (DPM) is a donor of mannose residues of these anchors. We here report studies of a CHO cell mutant (B421) transfected to express the GPL-anchored protein, placental alkaline phosphatase (AP). Only a few transfectants were found to express GPL-anchored AP on their surface, and these clones synthesized DPM. Moreover, and most strikingly, when surface AP-negative transfectants were treated with tunicamycin to cause accumulation of DPM, these cells expressed lipid-anchored AP. Fusion of a cloned surface AP-negative transfectant of B421 with the Thy-1-class E mutant thymoma, which is also deficient in DPM synthesis, produced hybrids that synthesized DPM and expressed AP and Thy-1. Thus, two mutations can interrupt DPM synthesis, and three sets of observations point to an essential role of DPM for addition of GPL anchors.

Role of glucocorticoids and progesterone in the development of rough endoplasmic reticulum involved in casein biosynthesis

Biochimie ◽  
1979 ◽  
Vol 61 (4) ◽  
pp. 453-461 ◽  
Author(s):  
Eve Devinoy ◽  
Louis-Marie Houdebine ◽  
Michèle Ollivier-Bousquet
Keyword(s):  
Endoplasmic Reticulum ◽  
Rough Endoplasmic Reticulum

scholarly journals Two different mutants blocked in synthesis of dolichol-phosphoryl-mannose do not add glycophospholipid anchors to membrane proteins: quantitative correction of the phenotype of a CHO cell mutant with tunicamycin.

1991 ◽  
Vol 11 (1) ◽  
pp. 391-400 ◽  
Author(s):  
N Singh ◽  
A M Tartakoff
Keyword(s):  
Alkaline Phosphatase ◽  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Membrane Proteins ◽  
Rough Endoplasmic Reticulum ◽  
Essential Role ◽  
Placental Alkaline Phosphatase ◽  
Cho Cell ◽  
Cell Mutant

The addition of glycophospholipid (GPL) anchors to certain membrane proteins occurs in the rough endoplasmic reticulum and is essential for transport of the proteins to the plasma membrane. Limited circumstantial evidence suggests that dolichol-phosphoryl-mannose (DPM) is a donor of mannose residues of these anchors. We here report studies of a CHO cell mutant (B421) transfected to express the GPL-anchored protein, placental alkaline phosphatase (AP). Only a few transfectants were found to express GPL-anchored AP on their surface, and these clones synthesized DPM. Moreover, and most strikingly, when surface AP-negative transfectants were treated with tunicamycin to cause accumulation of DPM, these cells expressed lipid-anchored AP. Fusion of a cloned surface AP-negative transfectant of B421 with the Thy-1-class E mutant thymoma, which is also deficient in DPM synthesis, produced hybrids that synthesized DPM and expressed AP and Thy-1. Thus, two mutations can interrupt DPM synthesis, and three sets of observations point to an essential role of DPM for addition of GPL anchors.

Modification of Pineal Ultrastructure by Exogenous Hormones

1967 ◽  
Vol 25 ◽  
pp. 170-171
Author(s):  
R. A. Turner ◽  
A. E. Rodin ◽  
D. K. Roberts
Keyword(s):  
Electron Microscopy ◽  
Endoplasmic Reticulum ◽  
Rough Endoplasmic Reticulum ◽  
Estradiol Benzoate ◽  
Female Rats ◽  
List Type ◽  
Type Number ◽  
Pregnant Rats ◽  
Gonadal Atrophy ◽  
Pineal Ultrastructure

There have been many reports which establish a relationship between the pineal and sexual structures, including gonadal hypertrophy after pinealectomy, and gonadal atrophy after injection of pineal homogenates or of melatonin. In order to further delineate this relationship the pineals from 5 groups of female rats were studied by electron microscopy:ControlsPregnant ratsAfter 4 weekly injections of 0.1 mg. estradiol benzoate.After 8 daily injections of 150 mcgm. melatonin (pineal hormone).After 8 daily injections of 3 mg. serotonin (melatonin precursor).No ultrastructural differences were evident between the control, and the pregnancy and melatonin groups. However, the estradiol injected animals exhibited a marked increase in the amount and size of rough endoplasmic reticulum within the pineal cells.

Membrane-associated microtubular areays induced in proximal myelinated processes of dorsal root ganglia by large doses of vitamin B6

1986 ◽  
Vol 44 ◽  
pp. 368-369
Author(s):  
V.J. Montpetit ◽  
S. Dancea ◽  
L. Tryphonas ◽  
D.F. Clapin
Keyword(s):  
Animal Model ◽  
Endoplasmic Reticulum ◽  
Dorsal Root Ganglia ◽  
Rough Endoplasmic Reticulum ◽  
Dorsal Root ◽  
Vitamin B6 ◽  
Morphological Changes ◽  
Model System ◽  
Sensory Nerves ◽  
Peripheral Sensory

Very large doses of pyridoxine (vitamin B6) are neurotoxic in humans, selectively affecting the peripheral sensory nerves. We have undertaken a study of the morphological and biochemical aspects of pyridoxine neurotoxicity in an animal model system. Early morphological changes in dorsal root ganglia (DRG) associated with pyridoxine megadoses include proliferation of neurofilaments, ribosomes, rough endoplasmic reticulum, and Golgi complexes. We present in this report evidence of the formation of unique aggregates of microtubules and membranes in the proximal processes of DRG which are induced by high levels of pyridoxine.

Localization of Intracisternal a Particle Antigens in Neoplastic Cells and Preimplantation Mouse Embryos

1980 ◽  
Vol 38 ◽  
pp. 696-697
Author(s):  
Thomas T.F. Huang ◽  
Patricia G. Calarco
Keyword(s):  
Endoplasmic Reticulum ◽  
Normal Development ◽  
Mouse Embryos ◽  
Neoplastic Cells ◽  
Large Numbers ◽  
Preimplantation Mouse Embryos ◽  
Preimplantation Mouse ◽  
Intracisternal A Particle ◽  
Normal Feature

The stage specific appearance of a retravirus, termed the Intracisternal A particle (IAP) is a normal feature of early preimplantation development. To date, all feral and laboratory strains of Mus musculus and even Asian species such as Mus cervicolor and Mus pahari express the particles during the 2-8 cell stages. IAP form by budding into the endoplasmic reticulum and appear singly or as groups of donut-shaped particles within the cisternae (fig. 1). IAP are also produced in large numbers in several neoplastic cells such as certain plasmacytomas and rhabdomyosarcomas. The role of IAP, either in normal development or in neoplastic behavior, is unknown.

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