Cloning of the Human Sodium-Iodide Symporter Promoter and Characterization in a Differentiated Human Thyroid Cell Line, KAT-50

Thyroid ◽  
1998 ◽  
Vol 8 (1) ◽  
pp. 63-69 ◽  
Author(s):  
GOPALAKRISHNAN M. VENKATARAMAN ◽  
MUSTAFA YATIN ◽  
KENNETH B. AIN
Keyword(s):  
Cell Line ◽  
Sodium Iodide ◽  
Human Thyroid ◽  
Thyroid Cell ◽  
Sodium Iodide Symporter ◽  
Thyroid Cell Line ◽  
Human Thyroid Cell

scholarly journals Expression Profiling of a Human Thyroid Cell Line Stably Expressing the BRAFV600E Mutation

2017 ◽  
Vol 14 (1) ◽  
pp. 53-68 ◽  
Author(s):  
BYOUNG-AE KIM ◽  
HYEON-GUN JEE ◽  
JIN WOOK YI ◽  
SU-JIN KIM ◽  
YOUNG JUN CHAI ◽  
...  
Keyword(s):  
Cell Line ◽  
Expression Profiling ◽  
Human Thyroid ◽  
Thyroid Cell ◽  
Brafv600e Mutation ◽  
Thyroid Cell Line ◽  
Human Thyroid Cell

Growth requirements and oncogene expression in the human thyroid cell line SGHTL-34

Apmis ◽  
1993 ◽  
Vol 101 (7-12) ◽  
pp. 767-776 ◽  
Author(s):  
GRO O. NESS ◽  
REIN AASLAND ◽  
JOHAN R. LILLEHAUG
Keyword(s):  
Cell Line ◽  
Human Thyroid ◽  
Thyroid Cell ◽  
Oncogene Expression ◽  
Growth Requirements ◽  
Thyroid Cell Line ◽  
Human Thyroid Cell

PAX8PPARγ Stimulates Cell Viability and Modulates Expression of Thyroid-Specific Genes in a Human Thyroid Cell Line

Thyroid ◽  
2007 ◽  
Vol 17 (6) ◽  
pp. 497-509 ◽  
Author(s):  
Carla Espadinha ◽  
Branca Maria Cavaco ◽  
Valeriano Leite
Keyword(s):  
Cell Viability ◽  
Cell Line ◽  
Human Thyroid ◽  
Thyroid Cell ◽  
Thyroid Cell Line ◽  
Human Thyroid Cell

scholarly journals Anion Selectivity by the Sodium Iodide Symporter

Endocrinology ◽  
2003 ◽  
Vol 144 (1) ◽  
pp. 247-252 ◽  
Author(s):  
J. Van Sande ◽  
C. Massart ◽  
R. Beauwens ◽  
A. Schoutens ◽  
S. Costagliola ◽  
...  
Keyword(s):  
Cell Line ◽  
Xenopus Oocytes ◽  
Sodium Iodide ◽  
Thyroid Cell ◽  
Sodium Iodide Symporter ◽  
Thyroid Cells ◽  
Anion Selectivity ◽  
Thyroid Cell Line ◽  
Competing Anions ◽  
Electrophysiological Methods

Abstract The iodide transporter of the thyroid (NIS) has been cloned by the group of Carrasco. The NIS-mediated transport was studied by electrophysiological methods in NIS-expressing Xenopus oocytes. Using this method, the anion selectivity of NIS was different from that previously reported for thyroid cells, whereas perchlorate and perrhenate were found not transported. In this study we compared the properties of human NIS, stably transfected in COS-7 cells to those of the transport in a thyroid cell line, the FRTL5 cells, by measuring the transport directly. We measured the uptake of 125I−, 186ReO4−, and 99mTcO4− and studied the effect on it of known competing anions, i.e. ClO4−, SCN−, ClO3−, ReO4−, and Br−. We conclude that the properties of the NIS transporter account by themselves for the properties of the thyroid iodide transporter as described previously in thyroid slices. The order of affinity was: ClO4− > ReO4− > I− ≥ SCN− > ClO3− > Br−. NIS is also inhibited by dysidenin (as in dog thyroid).

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