Thyroid cell growth, differentiation and function in the FRTL-5 cell line: a survey

Bidey, S. P.; Lambert, Adélaïde; Robertson, W. R.

doi:10.1677/joe.0.1190365

Cited by 46 publications

(14 citation statements)

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“…Furthermore, electron microscopic examination of FRTL-5 cells cultured on the permeable filters showed evidence of polarity, with microvilli and clathrin-coated pits at the upper membrane, a finding that indicates the existence of endocytic machinery at this surface. In addition, some other studies (51-53) describe features of polarity in FRTL-5 cells, including the demonstration that they possess microvilli only on the surface facing the medium (51,52) and secrete extracellular matrix only at the opposite surface (53). Nevertheless, other studies (54,55) have concluded that FRTL-5 cells are not polarized and are incapable of forming tight junctions, based on the finding of endogenously synthesized Tg both in the upper and lower chambers of cells cultured on permeable filters and on the relatively low TER, as compared with the known TER of other cells, such as FRT cells (54).…”

Section: Discussionmentioning

confidence: 99%

Role of Megalin (gp330) in Transcytosis of Thyroglobulin by Thyroid Cells

Marinò¹,

Zheng²,

Chiovato³

et al. 2000

Journal of Biological Chemistry

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We also studied Tg transcytosis in vivo, using a rat model of goiter induced by aminotriazole, in which increased release of thyrotropin induces massive colloid endocytosis. This was associated with increased megalin expression on thyrocytes and increased serum Tg levels, with reduced serum T3 levels, supporting the conclusion that megalin mediates Tg transcytosis. Tg transcytosis is a novel function of megalin, which usually transports ligands to lysosomes. Megalin-mediated transcytosis may regulate the extent of thyroid hormone release.

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Section: Discussionmentioning

confidence: 99%

Role of Megalin (gp330) in Transcytosis of Thyroglobulin by Thyroid Cells

Marinò¹,

Zheng²,

Chiovato³

et al. 2000

Journal of Biological Chemistry

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“…The growth of the rat thyroid cell line (FRTL-5 line) is tightly dependent on the presence of TSH in the culture medium (Ambesi-Impiombato et al, 1980; Bidey et al, 1988;see Materials and methods). These cells have been transfected with DNA expression vectors encoding the wild type and four di erent versions of TSH receptor mutated in three residues located in the VI intramembrane loop, previously isolated from thyroid autonomously functioning adenomas (Porcellini et al, 1994(Porcellini et al, , 1995Paschke et al, 1994).…”

Section: Expression Of Human Tsh Receptor Mutants In Rat Thyroid Cellsmentioning

confidence: 99%

“…The plasmid constructs were stably transfected in di erentiated thyroid FRTL-5 cells (Ambesi-Impiombato et al, 1980;Bidey et al, 1988). Five ± ten mg of the appropriate expression vector were stably transfected by the calcium phosphate procedure (Sambrook et al, 1989).…”

Section: Plasmids and Transfectionsmentioning

confidence: 99%

Mutations of thyrotropin receptor isolated from thyroid autonomous functioning adenomas confer TSH-independent growth to thyroid cells

et al. 1997

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TSH receptor mutants in the VI transmembrane segment, found in thyroid autonomously functioning adeonomas, have been expressed in di erentiated thyroid cells. All mutant receptors constitutively stimulated adenylyl cyclase. The biological activity, measured as cAMP production relative to the wild type receptor, was speci®c for each mutant in transient and stable transfection assays. Cells expressing these mutants proliferated in the absence of TSH. The rate of growth in the absence of TSH paralleled basal cAMP production for each mutant receptor. Low TSH concentrations stimulated the growth of mutant receptor-expressing cells, and not of the cells expressing the wild type receptor. Also, the entry in the cell cycle and the plating e ciency were markedly stimulated by the expression of the mutant receptors. These data provide a molecular link between the occurrence of TSH receptor mutations and thyroid autonomously functioning adenomas.

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“…Moreover, the growth of FRTL-5 cells is regulated by several hormones including TSH, insulin and/or IGF-I (Bidey et al 1988, Kohn et al 1989. Importantly, FRTL-5 cells do not exhibit characteristics of tumor cells in vitro or when transplanted in vivo.…”

Section: Introductionmentioning

confidence: 99%

Overexpression of Wnt-1 in thyrocytes enhances cellular growth but suppresses transcription of the thyroperoxidase gene via different signaling mechanisms

Kim

Lewis

McCall

et al. 2007

Journal of Endocrinology

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Wnt binding to cell surface receptors can activate a 'canonical' pathway that increases cellular b-catenin or a 'noncanonical' Ca CC pathway which can increase protein kinase C (PKC) activity. Although components of both Wnt/b-cateninsignaling pathways exist in thyrocytes, their biological role is largely unknown. In evaluating the biological role of Wnt signaling in differentiated FRTL-5 thyroid cells, we showed that TSH increased canonical Wnt-1 but, surprisingly, decreased the active form of b-catenin. In addition, these final results suggest that TSH-induced increase in Wnt-1 levels in thyrocytes contributes to enhanced cellular growth via a PKC pathway that increases STAT3 serine phosphorylation and activation, whereas TSH-induced decrease in activation of bcatenin simultaneously relieves transcriptional suppression of TPO. We hypothesize that Wnt signaling contributes to the ability of TSH to simultaneously increase cell growth and functional, thyroid-specific, gene expression.

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Thyroid cell growth, differentiation and function in the FRTL-5 cell line: a survey

Cited by 46 publications

References 0 publications

Role of Megalin (gp330) in Transcytosis of Thyroglobulin by Thyroid Cells

Role of Megalin (gp330) in Transcytosis of Thyroglobulin by Thyroid Cells

Mutations of thyrotropin receptor isolated from thyroid autonomous functioning adenomas confer TSH-independent growth to thyroid cells

Overexpression of Wnt-1 in thyrocytes enhances cellular growth but suppresses transcription of the thyroperoxidase gene via different signaling mechanisms

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