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.

scholarly journals Immunocytochemical localization of cathepsins B, H, L, and T4 in follicular cells of rat thyroid gland.

1989 ◽  
Vol 37 (5) ◽  
pp. 691-696 ◽  
Author(s):  
Y Uchiyama ◽  
T Watanabe ◽  
M Watanabe ◽  
Y Ishii ◽  
H Matsuba ◽  
...  
Keyword(s):  
Thyroid Gland ◽  
Thyroid Tissue ◽  
Double Immunostaining ◽  
Follicular Cells ◽  
Thin Sections ◽  
Dense Granules ◽  
Dense Bodies ◽  
Rat Thyroid ◽  
Monospecific Antibodies ◽  
Rat Thyroid Gland

To localize cathepsins B, H, and L in follicular cells of rat thyroid gland, we applied immunocytochemistry to the thyroid tissue using their respective monospecific antibodies. On serial semi-thin sections, cathepsins B, H, and L were localized in granules of various sizes located throughout the cytoplasm, whereas T4 was detected in larger granules located in the apical and supranuclear regions. By electron microscopy, cathepsins B, H, and L were localized in large less-dense granules (so-called colloid droplets) and in dense bodies of various sizes, whereas T4 was localized more intensely in large less-dense granules than in smaller dense bodies. By double immunostaining using an immunogold method, cathepsins H and B or L were co-localized in the same cytoplasmic granules. Moreover, immunoblotting demonstrated that proteins similar to cathepsins B, H, and L in the liver are present in the thyroid gland. These results suggest that cathepsins B, H, and L participate not only in degradation of thyroglobulin but in maturation of thyroid hormones, although it remains unknown whether all of them participate in the maturation process.

scholarly journals Characterization of angiotensin II receptors (binding and mRNA) in the rat thyroid gland

1998 ◽  
Vol 20 (3) ◽  
pp. 299-304 ◽  
Author(s):  
M Montiel ◽  
E Jimenez
Keyword(s):  
Plasma Membrane ◽  
Angiotensin Ii ◽  
Thyroid Gland ◽  
Binding Sites ◽  
Thyroid Tissue ◽  
Receptor Subtype ◽  
Receptor Subtypes ◽  
Ang Ii ◽  
Rat Thyroid ◽  
Rat Thyroid Gland

In this study we showed, for the first time, the existence of a moderate density of specific angiotensin II (Ang II) binding sites (Kd=3.9+/-1.7 nM and Bmax=467.2 130.0 fmol/mg protein) in plasma membrane preparations from rat thyroid gland. Reverse transcriptase/polymerase chain reactions, using primers based on the cloned AT1 and AT2 receptor subtypes, and pharmacological characterization, using the Ang II receptor subtype antagonists Losartan and PD 123319, revealed that these Ang II binding sites match with the AT1 receptor subtypes. To obtain more information on the molecular structure of this Ang II receptor, immunoblotting analyses were carried out using a polyclonal rabbit anti-AT1 antiserum. Western analysis of fresh plasma membrane preparations from thyroid tissue showed three prominent bands of approximately 60, 45 and 40 kDa which appear to be related to different degrees of glycosylation of the receptor molecule. The functional significance of the Ang II receptors in thyroid gland is currently not known. Nevertheless, since Ang II receptors play a pivotal role in the co-ordinated actions of the renin-angiotensin system (RAS), our findings support a reciprocal regulation of thyroid function by the RAS.

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.

Effects of toxic doses of a novel histamine (H2) antagonist on the rat thyroid gland

1987 ◽  
Vol 25 (10) ◽  
pp. 787-794 ◽  
Author(s):  
C.G. Brown ◽  
R.F. Harland ◽  
I.R. Major ◽  
C.K. Atterwill
Keyword(s):  
Thyroid Gland ◽  
H2 Antagonist ◽  
Histamine H2 Antagonist ◽  
Rat Thyroid ◽  
Rat Thyroid Gland

CORRELATION OF IODIDE TRANSPORT WITH Na+, K+ -ATPase, HCO−3-ATPase AND CARBONIC ANHYDRASE ACTIVITIES IN DIFFERENT FUNCTIONAL STATES OF THE RAT THYROID GLAND

1982 ◽  
Vol 92 (3) ◽  
pp. 371-379 ◽  
Author(s):  
S.-Y. CHOW ◽  
J. W. KEMP ◽  
D. M. WOODBURY
Keyword(s):  
Thyroid Gland ◽  
Carbonic Anhydrase ◽  
Protein Content ◽  
Chronic Treatment ◽  
Cell Water ◽  
Iodide Uptake ◽  
G Cell ◽  
Functional States ◽  
Rat Thyroid ◽  
Rat Thyroid Gland

The effects of thyrotrophin, hypophysectomy, and chronic treatment with thyroxine and methimazole on radioiodide uptake (thyroid/plasma (T/P) 125I− ratio), protein and DNA contents and activities of Na+,K+ -ATPase, HCO−3-ATPase, and carbonic anhydrase (CA) of rat thyroid gland were evaluated. Thyrotrophin given to intact rats slightly increased thyroid iodide uptake, did not affect protein or DNA content, and slightly inhibited CA activity (units/g cell water). Hypophysectomy markedly decreased T/P 125I− ratio, increased protein content, decreased activity of Na+,K+-ATPase, and slightly increased HCO−3-ATPase (nmol/mg DNA per min) and CA (units/g cell water) activities. Thyro-trophin given to hypophysectomized rats (as compared with untreated hypophysectomized control animals) markedly increased T/P 125I− ratio, slightly decreased protein content and decreased Na+,K+-ATPase and CA activities. Chronic treatment with methimazole increased T/P 125I− ratio, decreased protein content, markedly increased Na+,K+-ATPase and HCO−3-ATPase activities, and decreased CA activity. Chronic treatment with thyroxine, in contrast, decreased T/P 125I− ratio, decreased Na+,K+-ATPase activity, and increased CA activity. There was a significant inverse correlation between T/P 125I− ratio and CA activity in follicular cells for the various induced functional states of the thyroid.

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