scholarly journals CYTOCHEMICAL LOCALIZATION OF ENDOGENOUS PEROXIDASE IN THYROID FOLLICULAR CELLS

1970 ◽  
Vol 44 (3) ◽  
pp. 655-666 ◽  
Author(s):  
Judy M. Strum ◽  
Morris J. Karnovsky
Keyword(s):  
Peroxidase Activity ◽  
Apical Cell ◽  
Thyroid Peroxidase ◽  
Follicular Cells ◽  
Cytochemical Localization ◽  
Thyroid Follicular Cells ◽  
Endogenous Peroxidase ◽  
Rat Thyroid ◽  
Vitro Effect

Endogenous peroxidase activity in rat thyroid follicular cells is demonstrated cytochemically. Following perfusion fixation of the thyroid gland, small blocks of tissue are incubated in a medium containing substrate for peroxidase, before being postfixed in osmium tetroxide, and processed for electron microscopy. Peroxidase activity is found in thyroid follicular cells in the following sites: (a) the perinuclear cisternae, (b) the cisternae of the endoplasmic reticulum, (c) the inner few lamellae of the Golgi complex, (d) within vesicles, particularly those found apically, and (e) associated with the external surfaces of the microvilli that project apically from the cell into the colloid. In keeping with the radioautographic evidence of others and the postulated role of thyroid peroxidase in iodination, it is suggested that the microvillous apical cell border is the major site where iodination occurs. However, that apical vesicles also play a role in iodination cannot be excluded. The in vitro effect of cyanide, aminotriazole, and thiourea is also discussed.

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 Rabbit thyroid extracellular matrix as a 3D bioscaffold for thyroid bioengineering: a preliminary in vitro study

2021 ◽  
Vol 20 (1) ◽  
Author(s):  
Jie Weng ◽  
Bi Chen ◽  
Mengying Xie ◽  
Xinlong Wan ◽  
Peng Wang ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
In Vitro Study ◽  
Biomechanical Properties ◽  
Space Structure ◽  
Thyroid Diseases ◽  
Human Thyroid ◽  
Thyroid Peroxidase ◽  
Follicular Cells ◽  
Thyroid Follicular Cells

Abstract Background Advances in regenerative medicine technologies have been strongly proposed in the management of thyroid diseases. Mechanistically, the adoption of thyroid bioengineering requires a scaffold that shares a similar three-dimensional (3D) space structure, biomechanical properties, protein component, and cytokines to the native extracellular matrix (ECM). Methods 24 male New Zealand white rabbits were used in this experimental study. The rabbit thyroid glands were decellularized by immersion/agitation decellularization protocol. The 3D thyroid decellularization scaffolds were tested with histological and immunostaining analyses, scanning electron microscopy, DNA quantification, mechanical properties test, cytokine assay and cytotoxicity assays. Meanwhile, the decellularization scaffold were seeded with human thyroid follicular cells, cell proliferation and thyroid peroxidase were determined to explore the biocompatibility in vitro. Results Notably, through the imaging studies, it was distinctly evident that our protocol intervention minimized cellular materials and maintained the 3D spatial structure, biomechanical properties, ECM composition, and biologic cytokine. Consequently, the decellularization scaffold was seeded with human thyroid follicular cells, thus strongly revealing its potential in reinforcing cell adhesion, proliferation, and preserve important protein expression. Conclusions The adoption of our protocol to generate a decellularized thyroid scaffold can potentially be utilized in transplantation to manage thyroid diseases through thyroid bioengineering.

scholarly journals Rabbit thyroid extracellular matrix as a 3D bioscaffold for thyroid bioengineering: a preliminary in vitro study

2021 ◽  
Author(s):  
Jie Weng ◽  
Bi Chen ◽  
Mengying Xie ◽  
Xinlong Wan ◽  
Wang Peng ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Three Dimensional ◽  
Biomechanical Properties ◽  
Space Structure ◽  
Thyroid Diseases ◽  
Human Thyroid ◽  
Thyroid Peroxidase ◽  
Follicular Cells ◽  
Thyroid Follicular Cells

Abstract Background: Advances in regenerative medicine technologies have been strongly proposed in the management of thyroid diseases. Mechanistically, the adoption of thyroid bioengineering requires a scaffold that shares a similar three dimensional (3D) space structure, biomechanical properties, protein component, and cytokines to the native extracellular matrix (ECM).Methods: 24 male New Zealand white rabbits were used in this experimental study. The rabbit thyroid glands were decellularized by immersion/agitation decellularization protocol. The 3D thyroid decellularization scaffolds were tested with histological and immunostaining analyses, scanning electron microscopy, DNA quantification, mechanical properties test, cytokine assay and cytotoxicity assays. Meanwhile, the decellularization scaffold were seeded with human thyroid follicular cells, cell proliferation and thyroid peroxidase were determined to explore the biocompatibility in vitro.Results: Notably, through the imaging studies, it was distinctly evident that our protocol intervention minimized cellular materials and maintained the 3D spatial structure, biomechanical properties, ECM composition, and biologic cytokine. Consequently, the decellularization scaffold was seeded with human thyroid follicular cells, thus strongly revealing its potential in reinforcing cell adhesion, proliferation, and preserve important protein expression.Conclusions: The adoption of our protocol to generate a decellularized thyroid scaffold can potentially be utilized in transplantation to manage thyroid diseases through thyroid bioengineering.

scholarly journals APPEARANCE AND FUNCTION OF ENDOGENOUS PEROXIDASE IN FETAL RAT THYROID

1971 ◽  
Vol 51 (1) ◽  
pp. 162-175 ◽  
Author(s):  
Judy M. Strum ◽  
Janice Wicken ◽  
John R. Stanbury ◽  
Morris J. Karnovsky
Keyword(s):  
Apical Cell ◽  
Thyroid Peroxidase ◽  
Follicular Cells ◽  
Thyroid Follicle ◽  
Apical Cell Membrane ◽  
Fetal Rat ◽  
Apical Vesicles ◽  
Rat Thyroid ◽  
And Function

Iodination within the thyroid follicle is intimately associated with a thyroid peroxidase. In order to locate the in vivo site of iodination, the initial cytochemical appearance of this enzyme has been determined in fetal rat thyroid and its presence correlated with the onset of iodinated thyroglobulin synthesis. Peroxidase first appears in follicular cells during the 18th day of gestation. It is seen first in the perinuclear cisternae, the cisternae of the endoplasmic reticulum, and within the inner few Golgi lamellae. These organelles presumably represent sites of peroxidase synthesis. During the 19th and 20th days of gestation, there is a tremendous increase in peroxidase activity. In addition to the stained sites described, there are now many peroxidase-positive apical vesicles in the follicular cells. Newly forming follicles stain most conspicuously for peroxidase, the reaction product being heavily concentrated at the external surfaces of apical microvilli and in the adjacent colloid. Iodinated thyroglobulin becomes biochemically detectable in thyroids during the 19th day of gestation and increases greatly during the 20th day. The parallel rise in peroxidase staining that just precedes, and overlaps, the rise in iodinated thyroglobulin, suggests that apical vesicles and the apical cell membrane are the major sites of iodination within the thyroid follicle.

Stimulation of Na(+)-K(+)-ATPase by thyrotropin in cultured thyroid follicular cells

1995 ◽  
Vol 268 (5) ◽  
pp. C1252-C1258 ◽  
Author(s):  
T. A. Pressley ◽  
S. C. Higham ◽  
L. A. Joson ◽  
D. W. Mercer
Keyword(s):  
Thyroid Stimulating Hormone ◽  
Follicular Cells ◽  
Hormone Synthesis ◽  
Metabolic Turnover ◽  
Striking Increase ◽  
Thyroid Follicular Cells ◽  
A Cell ◽  
Messenger System ◽  
Rat Thyroid ◽  
Stimulation Of

Thyroid-stimulating hormone (TSH; thyrotropin) produces a pleiotropic response in the thyroid gland, accelerating nearly every aspect of metabolic turnover within the follicular epithelia. We examined the effects of TSH on expression of Na(+)-K(+)-ATPase in FRTL-5 cells, a cell line derived from rat thyroid. TSH (10 mU/ml) produced a nearly twofold increase in abundance of the mRNA encoding the catalytic alpha 1-subunit within 6 h of treatment. With the four mRNAs encoding the beta 1-subunit, TSH produced a striking increase in abundance, but this regulation was discoordinate, and some species increased more than others. Similar increases in mRNA abundance were elicited by activators of the adenosine 3',5'-cyclic monophosphate second messenger system. In contrast to the alpha 1- and beta 1-mRNAs, the abundance of the mRNA encoding the beta 2-subunit was unchanged with TSH after 6 h, indicating that the effects of thyrotropin were not universal or indiscriminate. Thyrotropin also caused a 76% increase in Na(+)-K(+)-ATPase activity and a 46% increase in pump-mediated transport after 48 h. These studies suggest that the changes in metabolic turnover initiated by TSH during hormone synthesis include upregulation of the N(+)-K+ pump.

Rat Thyroid Peroxidase (Tpo) Biosynthesis in Vitro: Studies Using Antiserum to Porcine Tpo

1987 ◽  
Vol 13 (1) ◽  
pp. 15-29 ◽  
Author(s):  
David S. Cooper ◽  
Farahe Maloof ◽  
E. Chester Ridgway
Keyword(s):  
In Vitro Studies ◽  
Thyroid Peroxidase ◽  
Rat Thyroid
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