The fine structure of nerve endings on rat thyroid follicular cells

1985 ◽  
Vol 242 (2) ◽  
Author(s):  
Yasuo Uchiyama ◽  
Gen Murakami ◽  
Yoshiki Ohno
Keyword(s):  
Fine Structure ◽  
Nerve Endings ◽  
Follicular Cells ◽  
Thyroid Follicular Cells ◽  
Rat Thyroid

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.

scholarly journals Transformation of rat thyroid follicular cells stably transfected with cholera toxin A1 fragment.

Endocrinology ◽  
1996 ◽  
Vol 137 (12) ◽  
pp. 5392-5399 ◽  
Author(s):  
M A Zeiger ◽  
M Saji ◽  
P Caturegli ◽  
W H Westra ◽  
L D Kohn ◽  
...  
Keyword(s):  
Cholera Toxin ◽  
Follicular Cells ◽  
Thyroid Follicular Cells ◽  
Rat Thyroid

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.

TGF-β control of rat thyroid follicular cells differentiation

2003 ◽  
Vol 207 (1-2) ◽  
pp. 1-11 ◽  
Author(s):  
Arianna Nicolussi ◽  
Sonia D'Inzeo ◽  
Maria Santulli ◽  
Giulia Colletta ◽  
Anna Coppa
Keyword(s):  
Follicular Cells ◽  
Thyroid Follicular Cells ◽  
Rat Thyroid
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