scholarly journals RADIOAUTOGRAPHIC VISUALIZATION OF THE INCORPORATION OF GALACTOSE-3H AND MANNOSE-3H BY RAT THYROIDS IN VITRO IN RELATION TO THE STAGES OF THYROGLOBULIN SYNTHESIS

1969 ◽  
Vol 43 (2) ◽  
pp. 289-311 ◽  
Author(s):  
P. Whur ◽  
Annette Herscovics ◽  
C. P. Leblond
Keyword(s):  
Endoplasmic Reticulum ◽  
Electron Microscope ◽  
Golgi Apparatus ◽  
Rough Endoplasmic Reticulum ◽  
Light Microscope ◽  
Detectable Effect ◽  
Apical Vesicles ◽  
Rat Thyroid

Rat thyroid lobes incubated with mannose-3H, galactose-3H, or leucine-3H, were studied by radioautography. With leucine-3H and mannose-3H, the grain reaction observed in the light microscope is distributed diffusely over the cells at 5 min, with no reaction over the colloid. Later, the grains are concentrated towards the apex, and colloid reactions begin to appear by 2 hr. With galactose-3H, the reaction at 5 min is again restricted to the cells but it consists of clumped grains next to the nucleus. Soon after, grains are concentrated at the cell apex and colloid reactions appear in some follicles as early as 30 min. Puromycin almost totally inhibits incorporation of leucine-3H and mannose-3H, but has no detectable effect on galactose-3H incorporation during the 1st hr. Quantitation of electron microscope radioautographs shows that mannose-3H label localizes initially in the rough endoplasmic reticulum, and by 1–2 hr much of this reaction is transferred to the Golgi apparatus. At 3 hr and subsequently, significant reactions are present over apical vesicles and colloid, while the Golgi reaction declines. Label associated with galactose-3H localizes initially in the Golgi apparatus and rapidly transfers to the apical vesicles, and then to the colloid. These findings indicate that mannose incorporation into thyroglobulin precursors occurs within the rough endoplasmic reticulum; these precursors then migrate to the Golgi apparatus, where galactose incorporation takes place. The glycoprotein thus formed migrates via the apical vesicles to the colloid.

Ultrastructure of the Genital Duct Epithelium of the Male Port Jackson Shark, Heterodontus-Portusjacksoni

1992 ◽  
Vol 40 (3) ◽  
pp. 257 ◽  
Author(s):  
RC Jones ◽  
M Lin
Keyword(s):  
Endoplasmic Reticulum ◽  
Epithelial Cells ◽  
Golgi Apparatus ◽  
Rough Endoplasmic Reticulum ◽  
Secretory Granules ◽  
Close Association ◽  
Ciliated Cells ◽  
Dense Bodies ◽  
Ductuli Efferentes ◽  
Apical Vesicles

The genital ducts of Heterodontus portusjacksoni are lined by a ciliated epithelium. In the ductuli efferentes the epithelium is low and contains numerous intraepithelial leucocytes which often contain large dense bodies. All epithelial cells are ciliated and are characterised by apical vesicles, vacuoles and glycogen granules, some rough endoplasmic reticulum, dense bodies and lipid droplets, and a Golgi apparatus. The initial segment of the ductus epididymidis is lined by a very tall epithelium of ciliated and non-ciliated cells. The non-ciliated cells contain numerous apical vesicles, a large Golgi apparatus and numerous mitochondria and secretory granules in close association with an extensive endoplasmic reticulum. The terminal segment of the ductus epididymidis is lined by a low columnar epithelium. A proximal region, occupying part of the head of the epididymis, is similar to the epithelium in the ductuli efferentes. Distally, all the epithelial cells are ciliated. They are characterised by considerable dilated endoplasmic reticulum, a Golgi apparatus, apical vesicles, and numerous mitochondria and secretory granules. The secretory tubules of Leydig's glands are lined by a very tall epithelium with non-ciliated cells containing extensive, dilated, rough endoplasmic reticulum, a large Golgi apparatus, and numerous mitochondria and secretory granules. The significance of the structural differentiation of the duct is discussed in relation to the evolution of the mammalian epididymis.

scholarly journals Ultrastructure of mononuclear phagocytes developing in liquid bone marrow cultures. A study on peroxidatic activity

1979 ◽  
Vol 149 (1) ◽  
pp. 17-26 ◽  
Author(s):  
JWM Van Der Meer ◽  
RHJ Beelen ◽  
DM Fluitsma ◽  
R Van Furth
Keyword(s):  
Bone Marrow ◽  
Endoplasmic Reticulum ◽  
Golgi Apparatus ◽  
Nuclear Envelope ◽  
Rough Endoplasmic Reticulum ◽  
Precursor Cells ◽  
Mononuclear Phagocytes ◽  
Peroxidatic Activity

Monoblasts, promonocytes, and macrophages in in vitro cultures of murine bone marrow were studied ultrastructurally, with special attention to peroxidatic activity. Monoblasts show peroxidatic activity in the rough endoplasmic reticulum and nuclear envelope as well as in the granules. The presence of peroxidatic activity in the Golgi apparatus could not be determined. Promonocytes have peroxidase-positive rough endoplasmic reticulum, Golgi apparatus, nuclear envelope, and granules, as previously reported. During culture, cells are formed with peroxidatic activity similar to that of monocytes or exudate macrophages (positive granules; negative Golgi apparatus, RER, and nuclear envelope); we call these cells early macrophages. In addition, transitional macrophages with both positive granules and positive RER, nuclear envelope, negative Golgi apparatus (as in exudate- resident macrophages in vivo), and mature macrophages with peroxidatic activity only in the RER and nuclear envelope (as in resident macrophages in vivo) were found. A considerable number of cells without detectable peroxidatic activity were also encountered. Our finding that macrophages with the peroxidatic pattern of monocytes (early macrophages), exudate-resident macrophages (transitional macrophages), and resident macrophages (mature macrophages), develop in vitro from proliferating precursor cells deriving from the bone marrow, demonstrates once again that resident macrophages in tissues originate from precursor cells in the bone marrow. Therefore, this conclusion can no longer be challenged on the basis of a cytochemical difference between monocytes and exudate macrophages on the one hand and resident macrophages on the other.

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.

scholarly journals IN VIVO INCORPORATION OF 3H-GALACTOSE BY THYROID FOLLICULAR CELLS OF THE RAT, AS SHOWN BY ELECTRON MICROSCOPIC RADIOAUTOGRAPHY

1972 ◽  
Vol 20 (3) ◽  
pp. 220-224 ◽  
Author(s):  
A. HADDAD
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Apparatus ◽  
Rough Endoplasmic Reticulum ◽  
Side Chains ◽  
Follicular Cells ◽  
Electron Microscopic ◽  
Thyroid Follicular Cells ◽  
Apical Vesicles ◽  
Electron Microscopic Radioautography

Radioactive galactose was injected intravenously into rats and localized in thyroid follicular cells by electron microscopic radioautography at intervals ranging from 2.5 to 30 min after injection. The galactose label was mostly present in the Golgi apparatus at 2.5 min, with some of it in the adjacent rough endoplasmic reticulum. By 30 min, the label was found in apical vesicles and colloid. It was concluded that galactose is added to the carbohydrate side chains of incomplete thyroglobulin molecules during their travel through the cisternae of the endoplasmic reticulum into the Golgi apparatus; the uptake begins as this organelle is approached, but predominates within it. The thyroglobulin molecule which has thus been labeled is transported by the apical vesicles to the colloid.

scholarly journals Polyribosomal attachment to rat liver and hepatoma endoplasmic reticulum in vitro. A method for its study

1971 ◽  
Vol 121 (2) ◽  
pp. 271-278 ◽  
Author(s):  
W. L. Ragland ◽  
T. K. Shires ◽  
H. C. Pitot
Keyword(s):  
Endoplasmic Reticulum ◽  
Electron Microscope ◽  
Citric Acid ◽  
Low Temperature ◽  
Rough Endoplasmic Reticulum ◽  
Half Life ◽  
Binding Capacity ◽  
Smooth Endoplasmic Reticulum ◽  
Quantitative Separation

A system for study and measurement of the attachment in vitro of exogenous polyribosomes to membranes has been presented. Its main features are use of low temperature, post-microsomal supernatant, pyrophosphate and citric acid to remove ribosomes from the surface of rough endoplasmic reticulum, and a method for quantitative separation of unattached from membrane-associated polyribosomes. The following were found. (1) Rough endoplasmic reticulum, from which ribosomes had been removed by treatment with pyrophosphate and citrate, bound over 50% of added polyribosomes, whereas the untreated (or control) rough and smooth endoplasmic reticulum and the smooth endoplasmic reticulum treated with pyrophosphate–citrate did not bind polyribosomes. (2) The polyribosome-binding capacity of rough endoplasmic reticulum stripped of its ribosomes decayed upon storage of the membranes at 0–4°C. The half-life of this decay was about 6 days whereas that of the polyribosome-binding capacity of hepatoma stripped rough endoplasmic reticulum was about 1.5 days. (3) Preparations of stripped rough endoplasmic reticulum after reassociation with polyribosomes in vitro were quite similar to preparations of native rough endoplasmic reticulum as viewed with the electron microscope. Evidence is presented to support the contention that association of polyribosomes with membranes was the result of polyribosomal reattachment to the membranes rather than trapping of the polyribosomes between vesicles of the membranes.

scholarly journals RADIOAUTOGRAPHIC STUDY OF IN VIVO AND IN VITRO INCORPORATION OF FUCOSE-3H INTO THYROGLOBULIN BY RAT THYROID FOLLICULAR CELLS

1971 ◽  
Vol 49 (3) ◽  
pp. 856-882 ◽  
Author(s):  
A. Haddad ◽  
Meredith D. Smith ◽  
Annette Herscovics ◽  
N. J. Nadler ◽  
C. P. Leblond
Keyword(s):  
Golgi Apparatus ◽  
Side Chains ◽  
Follicular Cells ◽  
Thyroid Follicular Cells ◽  
Apical Vesicles ◽  
Electron Microscopes ◽  
Rat Thyroid ◽  
Silver Grains

The incorporation of fucose-3H in rat thyroid follicles was studied by radioautography in the light and electron microscopes to determine the site of fucose incorporation into the carbohydrate side chains of thyroglobulin, and to follow the migration of thyroglobulin once it had been labeled with fucose-3H. Radioautographs were examined quantitatively in vivo at several times after injection of fucose-3H into rats, and in vitro following pulse-labeling of thyroid lobes in medium containing fucose-3H. At 3–5 min following fucose-3H administration in vivo, 85% of the silver grains were localized over the Golgi apparatus of thyroid follicular cells. By 20 min, silver grains appeared over apical vesicles, and by 1 hr over the colloid. At 4 hr, nearly all of the silver grains had migrated out of the cells into the colloid. Analysis of the changes in concentration of label with time showed that radioactivity over the Golgi apparatus increased for about 20 min and then decreased, while that over apical vesicles increased to reach a maximum at 35 min. Later, the concentration of label over the apical vesicles decreased, while that over the colloid increased. Similar results were obtained in vitro. It is concluded that fucose, which is located at the end of some of the carbohydrate side chains, is incorporated into thyroglobulin within the Golgi apparatus of thyroid follicular cells, thereby indicating that some of these side chains are completed there. Furthermore, the kinetic analysis demonstrates that apical vesicles are the secretion granules which transport thyroglobulin from the Golgi apparatus to the apex of the cell and release it into the colloid.

scholarly journals In vitro incorporation of (3H)threonine and (3H)glucose by the mucous and serous cells of the human bronchial submucosal gland. A quantitative electron microscope study.

1975 ◽  
Vol 67 (2) ◽  
pp. 320-344 ◽  
Author(s):  
B Meyrick ◽  
L Reid
Keyword(s):  
Endoplasmic Reticulum ◽  
Electron Microscope ◽  
Golgi Apparatus ◽  
Secretory Granules ◽  
Mucous Cell ◽  
Submucosal Gland ◽  
Electron Microscope Autoradiography ◽  
Serous Cell ◽  
Relationship Of

Incorporation of [3H]threonine and [3H]glucose by the mucous and serous cells of the human bronchial submucosal gland has been studied over 8 h using, for the first time in vitro pulse labeling and electron microscope autoradiography. In assessing the autoradiographs, two methods were compared, the circle analysis and the recently described hypothetical grain analysis. Preliminary studies showed formaldehyde to be the most suitable fixative. Chemical analysis of tissue revealed that [3H]threonine was incorporated into the polypeptide moiety of the bronchial gland product and that metabolites of [3H]-glucose were incorporated into the carbohydrate. Tritiated threonine was first localized in the endoplasmic reticulum of both mucous and serous cells and later migrated to the Golgi apparatus, while metabolites of [3H]glucose localized first mainly in the Golgi apparatus. From here, both radioactive precursors were next identified in vacuoles and, finally, in secretory granules. The mucous cell incorporated strikingly more of both radioactive precursors than the serous cell. Thus, it seems that oligosaccharides of mucous and serous cell glycoproteins are synthesized mainly in the Golgi apparatus and added there to the polypeptide core which is synthesized in the endoplasmic reticulum. The relationship of the mucous cell to the serous cell is discussed. It seems that under "normal" conditions each cell represents a different line but that injury may transform a serous cell into a mucous cell.

scholarly journals Cytological events involved in glycoprotein synthesis in cellular and syncytial trophoblast of human placenta. An electron microscope autoradiographic study of [3H]galactose incorporation.

1978 ◽  
Vol 76 (2) ◽  
pp. 418-429 ◽  
Author(s):  
D M Nelson ◽  
A C Enders ◽  
B F King
Keyword(s):  
Endoplasmic Reticulum ◽  
Electron Microscope ◽  
Rough Endoplasmic Reticulum ◽  
Autoradiographic Study ◽  
Leucine Incorporation ◽  
Electron Microscope Autoradiography ◽  
Glycoprotein Synthesis ◽  
Placental Villi ◽  
Syncytial Trophoblast

Electron microscope autoradiography was used to study glycoprotein synthesis in cellular trophoblast (cytotrophoblast) and syncytial trophoblast of term human placental villi incubated in vitro with D-[1-3H]galactose ([3H]gal). Autoradiographs were analyzed using the hypothetical grain analysis of Blackett and Parry (1973. J. Cell Biol. 57:9-15). The results of this study indicated that [3H]gal incorporation into term placental villi was predominantly localized to cytotrophoblast. Utilization of [3H]gal by term syncytial trophoblast was extremely low and yielded too few grains for a quantitative grain analysis. This result is in striking contrast to that found in the preceding study of [3H]leucine incorporation (Nelson, D. M., A. C. Enders, and B. F. King. 1978). Within cytotrophoblast, the rough endoplasmic reticulum incorporated the most [3H]gal into glycoprotein. The Golgi apparatus was another site of [3H]gal incorporation. The vast majority of the [3H]gal incorporated into cytotrophoblast during the pulse incubation remained intracellular through the duration of the experiment. There was little autoradiographic evidence for secretion of tritiated macromolecules. Cytotrophoblast incubated for the longest time period studied (4 h+) showed a substantial concentration of tritiated macromolecules in the Golgi complex and in the ground plasm but not in the rough endoplasmic reticulum.

scholarly journals ELECTRON MICROSCOPE STUDIES ON THE DICTYOSOMES AND ACROBLASTS IN THE MALE GERM CELLS OF THE CRICKET

1956 ◽  
Vol 2 (4) ◽  
pp. 123-128 ◽  
Author(s):  
H. W. Beams ◽  
T. N. Tahmisian ◽  
R. L. Devine ◽  
Everett Anderson
Keyword(s):  
Electron Microscope ◽  
Golgi Apparatus ◽  
Electron Micrographs ◽  
Germ Cells ◽  
Light Microscope ◽  
Golgi Body ◽  
Duplex Structure ◽  
Male Germ Cells ◽  
Secondary Spermatocyte ◽  
A Chain

The dictyosome (Golgi body) in the secondary spermatocyte of the cricket appears in electron micrographs as a duplex structure composed of (a) a group of parallel double-membraned lamellae and (b) a group of associated vacuoles arranged along the compact lamellae in a chain-like fashion. This arrangement of ultramicroscopic structure for the dictyosomes is strikingly comparable to that described for the Golgi apparatus of vertebrates. Accordingly, the two are considered homologous structures. Associated with the duplex structure of the dictyosomes is a differentiated region composed of small vacuoles. This is thought to represent the pro-acrosome region described in light microscope preparations. In the spermatid the dictyosomes fuse, giving rise to the acroblast. Like the dictyosomes, the acroblasts are made up of double-membraned lamellae and associated vacuoles. In addition, a differentiated acrosome region is present which, in some preparations, may display the acrosome vacuole and granule. Both the dictyosomes and acroblasts are distinct from mitochondria.

Sign in / Sign up

Export Citation Format

Share Document