Multiple pathways for cationic amino acid transport in rat thyroid epithelial cell line PC Cl3

Verri, Tiziano; Dimitri, C.; Treglia, Sonia; Storelli, Fabio; Micheli, Stefania De; Ulianich, Luca; Vito, Pasquale; Marsigliante, Santo; Storelli, Carlo; Jeso, Bruno Di

doi:10.1152/ajpcell.00053.2004

Cited by 11 publications

(2 citation statements)

References 48 publications

(52 reference statements)

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“…Our results also support the involvement of the y ϩ -LAT-2 carrier, in addition to the previously demonstrated y ϩ system, in L-arginine transport in rat adrenal ZF (6). The coexistence of several CATs of high and low affinity in the same cell type has been previously demonstrated in human placental microvascular endothelial cells (13), INF-␥-stimulated human monocytes (29), human platelets (33a), and a rat thyroid cell line (37). The physiological relevance of each transport system in L-arginine transport in adrenal cells is presently difficult to determine.…”

Section: Discussionsupporting

confidence: 91%

Characterization ofl-arginine transport in adrenal cells: effect of ACTH

Repetto¹,

Pannunzio²,

Astort³

et al. 2006

American Journal of Physiology-Endocrinology and Metabolism

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Nitric oxide synthesis depends on the availability of its precursor L-arginine, which could be regulated by the presence of a specific uptake system. In the present report, the characterization of the L-arginine transport system in mouse adrenal Y1 cells was performed. L-arginine transport was mediated by the cationic/neutral amino acid transport system y+L and the cationic amino acid transporter (CAT) y+ in Y1 cells. These Na+-independent transporters were identified by their selectivity for neutral amino acids in both the presence and absence of Na+ and by the effect of N-ethylmaleimide. Transport data correlated to expression of genes encoding for CAT-1, CAT-2, CD-98, and y+LAT-2. A similar expression profile was detected in rat adrenal zona fasciculata. In addition, cationic amino acid uptake in Y1 cells was upregulated by ACTH and/or cAMP with a concomitant increase in nitric oxide (NO) production.

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Section: Discussionsupporting

confidence: 91%

Characterization ofl-arginine transport in adrenal cells: effect of ACTH

Repetto¹,

Pannunzio²,

Astort³

et al. 2006

American Journal of Physiology-Endocrinology and Metabolism

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“…In the present study, we used PC Cl3 cells, which are differentiated thyroid cells sensitive to thyrotropin (TSH) stimulation for their growth (Fusco et al, 1987; Berlingieri et al, 1993) that express the typical markers of thyroid differentiation, such as Tg, thyroperoxidase (TPO), thyrotropin receptor (TSHR) and Na + /I − symporter (NIS). Therefore, this cell line has been used extensively for studying thyroid function, including the detailed study of the thyroid ion transporters (Marsigliante et al, 2002, 2003; Vilella et al, 2003; Ulianich et al, 2004, 2006; Verri et al, 2004). The physiology of PC Cl3 cells, as well as the expression of thyroid‐specific genes, is controlled by hormones such as TSH and insulin (Fusco et al, 1987; Kimura et al, 1999; Trapasso et al, 1999; Villone et al, 2000; Bjorklund et al, 2005).…”

Section: Discussionmentioning

confidence: 99%

PKC‐ε‐dependent cytosol‐to‐membrane translocation of pendrin in rat thyroid PC Cl3 cells

Muscella

Marsigliante

Verri

et al. 2008

Journal Cellular Physiology

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We studied the expression and the hormonal regulation of the PDS gene product, pendrin, which is, in thyrocytes, responsible for the iodide transport out of the cell. We show that PC Cl3 cells, a fully differentiated thyroid cell line, grown without TSH and insulin, express very low level of PDS mRNA; such expression is greatly increased after stimulation with insulin or TSH. (125)I pre-loaded cells showed an (125)I efflux accelerated in chloride-containing buffer with respect to chloride-free buffer, suggesting that this efflux is chloride dependent. By immunoblotting, pendrin was found in agonists-stimulated cells, whereas it was barely detectable in un-stimulated cells. An increase in both PDS mRNA and protein was also obtained using phorbol ester PMA, or using 8-Br-cAMP and forskolin. Stimulation with insulin (1 microg/ml; 0-40 min) provoked the cytosol-to-membrane translocation of pendrin and a decrease of intracellular I(-) content in (125)I pre-loaded cells. Insulin- or PMA-treated cells also showed a cytosol-to-membrane translocation of PKC-delta and -epsilon. Inhibition of both PKC-delta and -epsilon activities by GF109203X blocked pendrin translocation, whilst the inhibition of PKA did not. The selective inhibition of PKC-delta by rottlerin did not affect the insulin-provoked translocation of pendrin whilst it was inhibited by a PKC-epsilon translocation inhibitor peptide and also by PKC-epsilon downregulation using the small interfering RNA, thus indicating that such translocation was due to PKC-epsilon activity. In conclusion, our study demonstrates that, in PC Cl3 cells, pendrin expression and localisation are regulated by insulin and influenced by a PKC-epsilon-dependent intracellular pathway.

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