Skip to main content

Advertisement

Log in

The Effects of Thyroid Status on the Proteolysis System in Stress

  • Published:
Neuroscience and Behavioral Physiology Aims and scope Submit manuscript

Treatment of rats with mercazolyl (25 mg/kg for 20 days), which decreases blood levels of iodine-containing thyroid hormones (ITH), decreased trypsin-like activity (TLA) and α1-antitrypsin (α1-AT) and α2-macroglobulin (α2-MG) activities in the liver and blood; in the stage of anxiety associated with the stress reaction (1 h after swimming in a vessel for 1 h), experimental rats showed more marked stimulation of proteolysis than seen in euthyroid animals, due to decreases in α1-AT and α2-MG activities, while in the resistance stage (at 48 h), the normalization of TLA and α1-AT and α2-MG levels occurring in stressed euthyroid rats was blocked; in the exhaustion stage (stressing for 1 h for 10 days), there was greater activation of proteolysis in experimental rats due to profound suppression of α1-AT and α2-MG activities. Administration of L-thyroxine (1.5–3.0 μg/kg for 28 days, which did not alter the blood ITH concentration, had no effect on the proteolysis system; in the anxiety and exhaustion stages, the increase in TLA was limited, while in the resistance stage this was prevented, with elimination of the depression of α1-AT and α2-MG activities. These results demonstrated a novel aspect of the involvement of ITH in the body’s antistress system, i.e., their influences on the proteinase/inhibitors system.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  1. S. N. Bondarenko, N. A. Bondarenko, and E. B. Manukhina, “Effects of different methods of stressing and adaptation to behavioral and somatic parameters in rats,” Byull. Eksperim. Biol. Med., 128, No. 8, 157–160 (1999).

    Google Scholar 

  2. K. N. Veremeenko, P. P. Goloborod’ko, and A. I. Kizim, Proteolysis in Health and Pathology, Zdorov’ya, Kiev (1988).

    Google Scholar 

  3. A. F. Vismont and L. M. Lobanok, “The involvement of liver arginase in detoxification and thermoregulation processes in endotoxin fever,” Voenn. Med. No. 1, 105–109 (2011).

  4. Yu. A. Vladimirov and A. I. Archakov, Lipid Peroxidation in Biological Membranes, Nauka, Moscow (1972).

    Google Scholar 

  5. V. R. Ibragimov, V. N. Kozlov, Yu. V. Kas’yanova, and G. R. Timerbulatova, “Effects of thyrostatic agents on the histological structure of the liver in experimental studies in rats,” Pratsi TDATU, 2, No. 12, 141–146 (2010).

    Google Scholar 

  6. I. Yu. Karyagina, R. A. Zarembskii, and M. D. Balyabina, “Use of a complex method to measure the activity of trypsin-like proteases, α1-antitrypsin, and α2-macroglobulin in the gastroenterology clinic,” Lab. Delo, No. 2, 10–13 (1990).

  7. N. G. Makarova, L. S. Vasil’eva, and D. V. Garmaeva, “Liver structure in experimental hypothyroidism,” Sib. Med. Zh., 93, No. 2, 42–44 (2010).

    Google Scholar 

  8. I. Yu. Malyshev, L. Yu. Golubeva, A. P. Bozhko, and I. V. Gorodetskii, “The role of local stress-limiting systems in the myocardium in the protective cardiac effect of low doses of thyroid hormones in restraint stress in rats,” Ros. Fiziol. Zh., 86, No. 1, 62–67 (2000).

    Google Scholar 

  9. D. K. Mardas, V. N. Nikandrov, et al., “The role of m-cholinoreceptors in controlling the balance of the proteolysis in heat stress,” in: Functional Systems of the Body in Health and Pathology, RICVSh, Minsk (2008), pp. 147–150.

  10. N. L. Rendakov, “Changes in the activity of proteolytic activity of lysosomes on exposure to mercazolyl and thyroxine in foxes,” Vestn. Molod. Uchen. Ser. Nauk. Zhizn. No. 1, 61–67 (2004).

  11. T. G. Sazonova and A. A. Matskevich, “Tissue specificity of the protective actions of cytoplasmic factors in a membrane-bound Ca2+ transport system in the sarcoplasmic reticulum of the heart and skeletal muscle,” Patol. Fiziol. Eksperim. Terr., 2, 3–6 (2000).

    Google Scholar 

  12. A. F. Ajayi and R. E. Akhigbe, “Implication of altered thyroid state on liver function,” Thyroid Res. Pract., 9, 84–87 (2012).

    Article  Google Scholar 

  13. G. Capasso, G. De Tommaso, A. Pica, et al., “Effects of thyroid hormones on heart and kidney functions,” Miner. Electrolyte Metab., 25, No. 1–2, 56–64 (1999).

    Article  CAS  PubMed  Google Scholar 

  14. V. I. Chernaia, “Effect of one-time and chronic low-intensity irradiation on cathepsin L activity in rat brain,” Ukr. Biokhim. Zh., 73, No. 2, 97–101 (2001).

    CAS  Google Scholar 

  15. G. Fuhrmann, E. Kempf, and A. Ebel, “Effects of hormone therapy on the central cholinergic neurotransmission of the Snell dwarf mouse,” J. Neurosci. Res., 16, No. 3, 527–539 (1986).

    Article  CAS  PubMed  Google Scholar 

  16. R. Gredilla, M. López Torres, M. Portero-Otín, et al., “Influence of hyper- and hypothyroidsm on lipid peroxidation, unsaturation of phospholipids, glutathione system and oxidative damage to nuclear and mitochondrial DNA in mice skeletal muscle,” Mol. Cell. Biochem., 221, No. 1–2, 41–48 (2001).

    Article  CAS  PubMed  Google Scholar 

  17. M. E. Harper and E. L. Seifert, “Thyroid hormone effects on mitochondrial energetics,” Thyroid, 18, No. 2, 145–156 (2008).

    Article  CAS  PubMed  Google Scholar 

  18. B. Kim, S. D. Carvalho-Bianco, and P. R. Larsen, “Thyroid hormone and adrenergic signaling in the heart,” Arq. Bras. Endocrinol. Metab., 48, No. 1, 171–175 (2004).

    Article  Google Scholar 

  19. O. H. Lowry, N. J. Rosebrough, A. L. Farr, and R. J. Randall, “Protein measurement with the Folin phenol reagent,” J. Biol. Chem., 193, No. 1, 265–275 (1951).

    CAS  PubMed  Google Scholar 

  20. A. Negre-Salvayre, C. Coatrieux, C. Ingueneau, and R. Salvayre, “Advanced lipid peroxidation end products in oxidative damage to proteins. Potential role in diseases and therapeutic prospects for the inhibitors,” Br. J. Pharmacol., 153, No. 1, 6–20 (2008).

    Article  CAS  PubMed Central  PubMed  Google Scholar 

  21. D. Neil, N. D. Rawlings, and G. Salvesen, Handbook of Proteolytic Enzymes, Academic Press, Oxford (2013).

    Google Scholar 

  22. X. G. Zhu, P. McPhie, K. H. Lin, and S. Y. Cheng, “The differential hormone-dependent transcriptional activation of thyroid hormone receptor isoforms is mediated by interplay of their domains,” J. Biol. Chem., 272, No. 14, 9048–9054 (1997).

    Article  CAS  PubMed  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Corresponding authors

Correspondence to I. V. Gorodetskaya or E. A. Gusakova.

Additional information

Translated from Rossiiskii Fiziologicheskii Zhurnal imeni I. M. Sechenova, Vol. 99, No. 12, pp. 1378–1388, December, 2013.

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Gorodetskaya, I.V., Gusakova, E.A. The Effects of Thyroid Status on the Proteolysis System in Stress. Neurosci Behav Physi 45, 693–700 (2015). https://doi.org/10.1007/s11055-015-0130-8

Download citation

  • Received:

  • Revised:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s11055-015-0130-8

Keywords

Navigation