Different Growth Control of the Two Human Thyroid Cell Lines of Adenomatous Goiter and Papillary Carcinoma

Thyroid ◽  
1995 ◽  
Vol 5 (1) ◽  
pp. 41-46 ◽  
Author(s):  
AKIRA HISHINUMA ◽  
TOHRU YAMANARA ◽  
KIKUO KASAI ◽  
SHINBU SO ◽  
CHEN-CHIANG TSENG ◽  
...  
Keyword(s):  
Papillary Carcinoma ◽  
Cell Lines ◽  
Growth Control ◽  
Human Thyroid ◽  
Thyroid Cell ◽  
Adenomatous Goiter ◽  
Human Thyroid Cell

scholarly journals Raman spectroscopy and advanced mathematical modelling in the discrimination of human thyroid cell lines

2009 ◽  
Vol 1 (1) ◽  
Author(s):  
Andrew T Harris ◽  
Manjree Garg ◽  
Xuebin B Yang ◽  
Sheila E Fisher ◽  
Jennifer Kirkham ◽  
...  
Keyword(s):  
Raman Spectroscopy ◽  
Mathematical Modelling ◽  
Cell Lines ◽  
Human Thyroid ◽  
Thyroid Cell ◽  
Human Thyroid Cell

Desensitization in Normal and Neoplastic Human Thyroid Cell Lines

1998 ◽  
Vol 22 (6) ◽  
pp. 552-557 ◽  
Author(s):  
Saif S. Al-Sobhi ◽  
Euy Y. Soh ◽  
Mariwil G. Wong ◽  
Allan E. Siperstein ◽  
Quan-Yang Duh ‡, § , Orlo H. Clark
Keyword(s):  
Cell Lines ◽  
Human Thyroid ◽  
Thyroid Cell ◽  
Human Thyroid Cell

A proteomic approach to analysing spheroid formation of two human thyroid cell lines cultured on a random positioning machine

PROTEOMICS ◽  
2011 ◽  
Vol 11 (10) ◽  
pp. 2095-2104 ◽  
Author(s):  
Jessica Pietsch ◽  
Albert Sickmann ◽  
Gerhard Weber ◽  
Johann Bauer ◽  
Marcel Egli ◽  
...  
Keyword(s):  
Cell Lines ◽  
Human Thyroid ◽  
Thyroid Cell ◽  
Spheroid Formation ◽  
Random Positioning Machine ◽  
Proteomic Approach ◽  
Human Thyroid Cell

Metabolic enzyme diversity in different human thyroid cell lines and their sensitivity to gravitational forces

PROTEOMICS ◽  
2012 ◽  
Vol 12 (15-16) ◽  
pp. 2539-2546 ◽  
Author(s):  
Jessica Pietsch ◽  
Albert Sickmann ◽  
Gerhard Weber ◽  
Johann Bauer ◽  
Marcel Egli ◽  
...  
Keyword(s):  
Cell Lines ◽  
Human Thyroid ◽  
Metabolic Enzyme ◽  
Thyroid Cell ◽  
Gravitational Forces ◽  
Human Thyroid Cell

scholarly journals Trace Amine-Associated Receptor 1 Trafficking to Cilia of Thyroid Epithelial Cells

Cells ◽  
2021 ◽  
Vol 10 (6) ◽  
pp. 1518
Author(s):  
Maria Qatato ◽  
Vaishnavi Venugopalan ◽  
Alaa Al-Hashimi ◽  
Maren Rehders ◽  
Aaron D. Valentine ◽  
...  
Keyword(s):  
Cell Surface ◽  
Cell Lines ◽  
Human Thyroid ◽  
Apical Plasma Membrane ◽  
Thyroid Cell ◽  
Thyroid Cells ◽  
Trace Amine ◽  
Rat Thyroid

Trace amine-associated receptor 1 (rodent Taar1/human TAAR1) is a G protein-coupled receptor that is mainly recognized for its functions in neuromodulation. Previous in vitro studies suggested that Taar1 may signal from intracellular compartments. However, we have shown Taar1 to localize apically and on ciliary extensions in rodent thyrocytes, suggesting that at least in the thyroid, Taar1 may signal from the cilia at the apical plasma membrane domain of thyrocytes in situ, where it is exposed to the content of the follicle lumen containing putative Taar1 ligands. This study was designed to explore mouse Taar1 (mTaar1) trafficking, heterologously expressed in human and rat thyroid cell lines in order to establish an in vitro system in which Taar1 signaling from the cell surface can be studied in future. The results showed that chimeric mTaar1-EGFP traffics to the apical cell surface and localizes particularly to spherical structures of polarized thyroid cells, procilia, and primary cilia upon serum-starvation. Moreover, mTaar1-EGFP appears to form high molecular mass forms, possibly homodimers and tetramers, in stably expressing human thyroid cell lines. However, only monomeric mTaar1-EGFP was cell surface biotinylated in polarized human thyrocytes. In polarized rat thyrocytes, mTaar1-EGFP is retained in the endoplasmic reticulum, while cilia were reached by mTaar1-EGFP transiently co-expressed in combination with an HA-tagged construct of the related mTaar5. We conclude that Taar1 trafficking to cilia depends on their integrity. The results further suggest that an in vitro cell model was established that recapitulates Taar1 trafficking in thyrocytes in situ, in principle, and will enable studying Taar1 signaling in future, thus extending our general understanding of its potential significance for thyroid autoregulation.

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