scholarly journals Immunoelectron microscopic demonstration of thyroglobulin and thyroid hormones in rat thyroid gland.

1987 ◽  
Vol 35 (10) ◽  
pp. 1095-1104 ◽  
Author(s):  
P K Ring ◽  
V Johanson
Keyword(s):  
Endoplasmic Reticulum ◽  
Thyroid Gland ◽  
Thyroid Hormones ◽  
Electron Microscopic ◽  
Cell Compartments ◽  
Lr White ◽  
Microscopic Demonstration ◽  
Rat Thyroid ◽  
Rat Thyroid Gland ◽  
Electron Microscopic Localization

We have developed a post-embedding immunogold technique for electron microscopic localization and quantitation of thyroglobulin (TG), thyroxine (T4), and triiodothyronine (T3) in rat thyroid. Labeling for TG was located on rough endoplasmic reticulum, Golgi apparatus, exocytotic vesicles, luminal colloid, colloid droplets, and lysosomes, whereas labeling for thyroid hormones was located on luminal colloid, colloid droplets, and lysosomes. We tested different procedures of fixation, dehydration, embedding, polymerization, and immunoincubation to optimize ultrastructural preservation and immunolabeling. Fixation with glutaraldehyde and osmium was possible with retained antigenicity. Dehydration temperature and the choice of embedding resin were the two crucial factors for good immunolabeling. Low-temperature dehydration greatly improved immunolabeling and could be combined with embedding in the methacrylate LR White or the epoxide Agar 100 (equivalent of Epon 812) polymerized at 40-60 degrees C, as the temperature during subsequent embedding and polymerization was of little importance for the immunoreactivity. Labeling on LR White sections was always higher than on Agar 100 sections. Various etching procedures were tested without improved specific labeling. Etching with hydrochloric acid gave nonspecific labeling of certain cell compartments.

scholarly journals Immunohistochemical localization of thyroid hormone in rat thyroid gland.

1978 ◽  
Vol 26 (12) ◽  
pp. 1121-1124 ◽  
Author(s):  
M Wilson ◽  
K R Hitchcock ◽  
R A DeLellis
Keyword(s):  
Thyroid Hormone ◽  
Thyroid Gland ◽  
Thyroid Hormones ◽  
Parathyroid Gland ◽  
Immunohistochemical Localization ◽  
Follicular Cells ◽  
Adult Rat ◽  
Apical Cytoplasm ◽  
Rat Thyroid ◽  
Rat Thyroid Gland

Direct and indirect immunofluorescence techniques were used to localize the thyroid hormones triidothyronine (T3) and thyroxine (T4) in adult rat thyroid gland. Optimum dilutions of the antisera were established and four tissue fixatives were investigated for usefulness in this technique. Use of antibodies specific for either T3 or T4 resulted in brilliant fluorescence in the colloid pools and apical cytoplasm of follicular cells. In all cases, the adjacent parathyroid gland was devoid of fluorescence. This report demonstrates that these dipeptide hormones can be localized by using immunofluorescence techniques.

scholarly journals Localization of thyroid peroxidase and the site of iodination in rat thyroid gland

1976 ◽  
Vol 158 (2) ◽  
pp. 477-479 ◽  
Author(s):  
H H Edwards ◽  
M Morrison
Keyword(s):  
Endoplasmic Reticulum ◽  
Thyroid Gland ◽  
Thyroid Tissue ◽  
Follicular Cell ◽  
Thyroid Peroxidase ◽  
Tissue Slices ◽  
Rat Thyroid ◽  
Rat Thyroid Gland

The iodinated protein was localized in thyroid tissue slices by using radioautography. In unfixed tissue, the labelled protein was localized in the colloid, whereas, in tissue that was fixed before the 125I addition, the label was within the follicular cell. This localizes thyroid peroxidase largely on the endoplasmic reticulum of the cell.

Organization of the thyroglobulin polysome, studied in Endoplasmic Reticulum surface views of rough endoplasmic reticulum in cultured rat thyroid cells

1990 ◽  
Vol 48 (3) ◽  
pp. 546-547
Author(s):  
A. Kent Christensen ◽  
Hayden G. Coon
Keyword(s):  
Endoplasmic Reticulum ◽  
Thyroid Gland ◽  
Thyroid Hormones ◽  
Cross Section ◽  
Electron Micrographs ◽  
Rough Endoplasmic Reticulum ◽  
Thyroid Cells ◽  
En Face ◽  
Face View ◽  
Rat Thyroid

Thyroglobulin is synthesized in the thyroid gland and is subsequently degraded to provide thyroid hormones. Rat thyroglobulin is made up of two identical 330 kD subunits, and the mRNA for each subunit contains about 8,500 nucleotides. Since polysomes have approximately one ribosome for each 90-100 nucleotides of mRNA, a polysome of about 85-95 ribosomes would be expected for thyroglobulin. We have been interested in how this very large polysomes is organized on the membranes of the rough endoplasmic reticulum (RER).It is well known that bound polysomes assume characteristic shapes on the surface of the RER, resembling beads on a string arranged in circles, spirals, loops, hairpins or other forms. These polysomal shapes can be observed in conventional electron micrographs when the membranes of the RER are seen in surface or en face view, rather than in the usual cross section. Clearcut surface views are infrequent, but the likelihood of seeing them is greatly improved when flattened cells in culture are sectioned in the plane of the cell, since the RER in a flattened cell tends to be oriented in that plane.

scholarly journals An Electron Microscopic Study on Follicular Formation and TSH Sensitivity of the Fetal Rat Thyroid Gland in Organ Culture.

1993 ◽  
Vol 55 (1) ◽  
pp. 157-160 ◽  
Author(s):  
Tatsuya TAKIZAWA ◽  
Masako YAMAMOTO ◽  
Kazuyoshi ARISHIMA ◽  
Masahiko KUSANAGI ◽  
Hiroaki SOMIYA ◽  
...  
Keyword(s):  
Thyroid Gland ◽  
Organ Culture ◽  
Microscopic Study ◽  
Electron Microscopic Study ◽  
Electron Microscopic ◽  
Fetal Rat ◽  
Rat Thyroid ◽  
Rat Thyroid Gland

COMPARISON OF THE EFFECTS OF VARIOUS GOITROGENS ON THE BIOSYNTHESIS OF THYROID HORMONES IN VITRO

1961 ◽  
Vol 36 (2) ◽  
pp. 212-220 ◽  
Author(s):  
Shiro Iino
Keyword(s):  
Thyroid Gland ◽  
Thyroid Hormones ◽  
Potent Inhibitor ◽  
Relative Activity ◽  
Antithyroid Drugs ◽  
Modes Of Action ◽  
Antithyroid Activity ◽  
Rat Thyroid ◽  
Rat Thyroid Gland

ABSTRACT The effect of various goitrogens on in vitro biosynthesis of thyroid horhomes was studied. The compounds in decreasing order of relative activity to completely inhibit DIT formation were 1-methyl-2-mercaptoimidazole (MIA), thiouracil (TU); propylthiouracil PTU) and goitrin; thiourea and methylthiouracil (MTU). Those in decreasing order of relative activity to completely inhibit MIT formation were MIA; PTU, MTU, TU and thiourea; goitrin. Of the compounds tested MIA was thus the most potent inhibitor of the rat thyroid gland in vitro. The conversion of monoiodotyrosine to diiodotyrosine was more sensitive to every goitrogen than the iodination of tyrosine to form monoiodotyrosine. The modes of action of these antithyroid drugs seemed to be approximately the same, except for goitrin, which showed very weak inhibition of MIT formation. Progoitrin, the precursor of goitrin, did not seem to possess any antithyroid activity.

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