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

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.

1983 ◽  
Vol 103 (2) ◽  
pp. 235-240 ◽  
Author(s):  
Akira Kawaoi ◽  
Tadao Okano ◽  
Norimichi Nemoto ◽  
Toshio Shikata

Abstract. Detection of T4 and T3 in paraffin sections of the rat thyroid gland in various functional states was attempted by an immunoenzyme technique. Both hormones showed a similar localization, being detected mainly in the colloid in the follicular lumen, and sometimes in certain regions of the cytoplasm of the follicular epithelium. Following administration of TSH, their stainability was increased, and the localization within the cytoplasm became more remarkable. Decrease or disappearance of stainability was observed after hypophysectomy or administration of PTU. These findings support the view that the immunostainability of T4 and T3 is closely correlated with the functional state of the thyroid gland.


1987 ◽  
Vol 25 (10) ◽  
pp. 787-794 ◽  
Author(s):  
C.G. Brown ◽  
R.F. Harland ◽  
I.R. Major ◽  
C.K. Atterwill

1963 ◽  
Vol 86 (1) ◽  
pp. 86-92 ◽  
Author(s):  
R PITT-RIVERS ◽  
RR CAVALIERI

1989 ◽  
Vol 37 (5) ◽  
pp. 691-696 ◽  
Author(s):  
Y Uchiyama ◽  
T Watanabe ◽  
M Watanabe ◽  
Y Ishii ◽  
H Matsuba ◽  
...  

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.


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