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Current Topics in Peptide & Protein Research   Volumes    Volume 13 
The sensitivity of the adenylyl cyclase system in rat thyroidal and extrathyroidal tissues to peptides corresponding to the third intracellular loop of thyroid-stimulating hormone receptor
Alexander O. Shpakov, Elena A. Shpakova, Kira V. Derkach
Pages: 61 - 73
Number of pages: 13
Current Topics in Peptide & Protein Research
Volume 13 

Copyright © 2012 Research Trends. All rights reserved

The importance of selective regulators of thyroid functions is dictated by a key role the hypothalamic-pituitary-thyroid axis plays in the control of biochemical and physiological processes and by the fact that only a limited number of drugs with thyrotropic potency is available today. We synthesized peptide corresponding to 612-627 region of third intracellular loop of rat thyroid-stimulating hormone (TSH) receptor and its palmitoylated analogue 612–627-K(Pal)A and studied their influence on adenylyl cyclase (AC) signaling system in the thyroid and the extrathyroidal tissues. Peptide 612–627-K(Pal)A at micromolar concentrations stimulated basal AC activity and GppNHp binding of Gs and Gq proteins and inhibited TSH-stimulating AC activity in the thyroidal membranes but had little influence on AC system in synaptosomal, myocardial and testicular membranes, which indicates the receptor and tissue specificity of 612–627-K(Pal)A. In the thyroid 612–627-K(Pal)A also decreased PACAP-38- and human chorionic gonadotropin-stimulated AC activity, which is most likely to be due to inhibiting of TSH-mimicking effect of these hormones on AC. Unmodified peptide 612–627-KA was effective to a much lesser extent, indicating the importance of hydrophobic moiety for 612–627-K(Pal)A activity. The obtained data suggest the possibility to develop thyroid regulators and modulators on the basis of TSH receptor-derived peptides.
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