Thyroid hormones differentially regulate phosphorylation of ERK and Akt via integrin αvβ3 receptor in undifferentiated and differentiated PC-12 cells.

2881 4 13461 1 35685 document 13461 Barbakadze et al., 2013.pdf application/pdf 108e7a8cb8701d91fcc860e5e1cafce9 MD5 285101 2015-06-17 18:50:26 http://eprints.iliauni.edu.ge/2881/1/Barbakadze%20et%20al.%2C%202013.pdf 2881 1 1 application/pdf text en public

Barbakadze et al., 2013.pdf

13462 2 35688 document 13462 lightbox.jpg image/png 30d146e75df140b779703bc0c2c7519b MD5 53689 2015-06-17 19:00:42 http://eprints.iliauni.edu.ge/2881/2/lightbox.jpg 2881 2 2 image/png other Thumbnails conversion from text to thumbnail_lightbox ge public

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http://eprints.org/relation/isVersionOf http://eprints.iliauni.edu.ge/id/document/13461 http://eprints.org/relation/isVolatileVersionOf http://eprints.iliauni.edu.ge/id/document/13461 http://eprints.org/relation/isIndexCodesVersionOf http://eprints.iliauni.edu.ge/id/document/13461 archive 119 disk0/00/00/28/81 2015-06-22 05:35:02 2015-06-22 05:35:02 2015-06-22 05:35:02 article 361 show Barbakadze Tamar tamar_barbakadze@iliauni.edu.ge Natsvlishvili Nino Mikeladze David Thyroid hormones differentially regulate phosphorylation of ERK and Akt via integrin αvβ3 receptor in undifferentiated and differentiated PC-12 cells. pub QH301 public The effects of 3,5,3'-triiodo-l-thyronine (T3) and l-thyroxine (T4) on the integrin αvβ3 receptor of thyroid hormones (TH) were investigated in pheochromocytoma PC-12 cells. Differentiation was induced by treatment of PC-12 cells with fisetin and the levels of phosphorylated extracellular signal-regulated kinase (ERK) and Akt in cytoplasm, as well as the content of FoxO6 transcription factor in nuclei was analysed in undifferentiated and differentiated conditions. We have found that in undifferentiated PC-12 cells, tetraiodothyroacetic acid (TETRAC), a known inhibitor of binding of T4 and T3 to plasma membrane integrin αvβ3 receptor inhibits T4-dependent phosphorylation of ERK, whereas in differentiated PC-12 cells, TETRAC abolishes the effect of T3. In undifferentiated PC-12 cells, both TH increase the level of p-Akt, and this enhancement is not sensitive to TETRAC. In differentiated PC-12 cells, both TH increase the level of p-Akt; however, only T3-dependent activation of Akt is sensitive to the TETRAC. Furthermore, our results have shown that in differentiated PC-12 cells, the expression of FoxO6 was higher than in undifferentiated PC-12 cells, and this elevation has not changed under the action of TH. Only in undifferentiated PC-12 cells the T3-dependent expression of FoxO6 was sensitive to the TETRAC. We propose that PC-12 cells contain integrin αvβ3 receptor, which T3 and T3/T4 sites are differentially regulated by TH in undifferentiated and differentiated conditions. Copyright © 2013 John Wiley & Sons, Ltd. 2013-11-11 published Cell biochemistry and function TRUE 1099-0844