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 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.

Autoradiographic Localization of Slow-Turnover Iodocompounds Within the Follicular Cells of the Rat Thyroid Gland

Endocrinology ◽  
1975 ◽  
Vol 97 (4) ◽  
pp. 978-984 ◽  
Author(s):  
A. HAEBERLI ◽  
H. STUDER ◽  
H. KOHLER ◽  
H. BüRGI ◽  
H. ENGLER
Keyword(s):  
Thyroid Gland ◽  
Follicular Cells ◽  
Rat Thyroid ◽  
Rat Thyroid Gland ◽  
Slow Turnover

scholarly journals CORRELATED LIGHT AND ELECTRON MICROSCOPE OBSERVATIONS ON GLYCOPROTEIN-CONTAINING GLOBULES IN THE FOLLICULAR CELLS OF THE THYROID GLAND OF THE RAT

1965 ◽  
Vol 13 (4) ◽  
pp. 286-295 ◽  
Author(s):  
HUBERTA E. VAN HEYNINGEN
Keyword(s):  
Electron Microscope ◽  
Thyroid Gland ◽  
Toluidine Blue ◽  
Fine Particles ◽  
Periodic Acid ◽  
Follicular Cells ◽  
Periodic Acid Schiff ◽  
Intense Staining ◽  
Thin Sections ◽  
Rat Thyroid

Two carbohydrate staining techniques were applied to sections of rat thyroid gland: periodic acid-silver methenamine to thin sections for electron microscopy, and periodic acid-Schiff to thick sections for light microscopy. The latter were compared with adjacent thin sections for identificatoin with the electron microscope. Two types of globules in thyroid follicular cells stained with both methods. Globules of the first type are relatively large (usually 0.5 to 3 µ) with electron opacity very similar to that of follicular colloid; when stained with toluidine blue they have the same gray shade as follicular colloid. These similarities suggest that their periodic acid reactivity is due to the same glycoprotein as that of follicular colloid, namely thyroglobulin, and that the origin of these "intracellular colloid droplets" is the colloid in the lumen. The second type comprises medium-sized (usually 0.1 to 1 µ) fairly electron opaque globules having fine particles (~70 Å) dispersed in their matrices and sometimes containing membrane fragments or other irregularities; when stained with toluidine blue these globules stand out dark blue. Although their periodic acid reactivity indicates that these globules also contain glycoprotein, their ultrastructure and staining characteristics suggest that their composition differs from colloid. It is possible that they represent enzyme or zymogen-containing granules. A third type of globule, which on account of its intense staining in some periodic acid silver methenamine preparations could perhaps also be periodic acid reactive, concerns small (usually 0.02 to 0.2 µ) globules, mainly accumulated beneath the apical border of the cell. These globules, known as "apical vesicles," are believed to contain the not-yet-iodinated precursor of thyroglobulin.

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.

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
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