The relationship between carbonic anhydrase-III expression and oxidative stress in brown adipose tissue

Year 2018, Volume: 45 Issue: 4, 361 - 368, 13.12.2018

Cemil Kahraman Ahmet Alver Ayşe Şentürk İmran İnce Akça

https://doi.org/10.5798/dicletip.497874

Cited By: 2

Abstract

Objective:
High-fat foods increase adipose tissue size, and induce obesity. Although
carbonic anhydrase III is abundantly found in brown adipose tissue, its
function is not fully defined. In this study, we investigated the relationship
between carbonic anhydrase III enzyme mRNA expression and malondialdehyde,
oxidative stress marker, in brown adipose tissue of rats that were fed high-fat
diets. In addition, we investigated potential effect of N-acetylcysteine as an
antioxidant in this relationship.

Methods: In
our study three experimental groups were formed and each contained 6 rats
(control, obese, and antioxidant groups). The experimental groups were fed for
a duration of 85 days with high fat diets. In these groups, carbonic anhydrase
III mRNA expression, total carbonic anhydrase hydratase activitie, and
malondialdehyde levels were measured in brown adipose tissues dissected from
rat scapula regions.

Results:
According to our findings, carbonic anhydrase III mRNA expression was higher in
the obese group than in the control group (p = 0.004), and malondialdehyde
levels were lower in the obese group than in the control group (p = 0.03). It
was observed that carbonic anhydrase III mRNA expression was higher in the
antioxidant group than in the control group (p = 0.006), and malondialdehyde
levels were lower in the antioxidant group than in the control group (p =
0.006). In addition, in the obese group carbonic anhydrase III mRNA expression
was higher than in the antioxidant group (p=0.01).

Conclusion:
In brown adipose tissue of rats that were fed high-fat diets, this study showed
that the carbonic anhydrase III mRNA expression increased and the
malondialdehyde level decreased.

Keywords

Carbonic anhydrase III, brown adipose tissue, obesity, N-acetylcysteine

References

• 1. Nammi S, Koka S, Chinnala KM, Boini KM. Obesity: An overview on its current perspectives and treatment options. Nutr J. 2004; 3: 1-8.
• 2. Basdevant AB, Aron-Wisnewsky J. Obesity: an evolving process. in: Bastard JP, Feve B (eds) Physiology and physiopathology of adipose tissue. Verlag France: Springer, 2013: 231-42.
• 3. Haslam DW, James WP. Obesity. Lancet. 2005; 366: 1197-209.
• 4. Vázquez-Vela MEF, Torres N, Tovar AR. White adipose tissue as endocrine organ and its role in obesity. Arch Med Res. 2008; 39: 715-28.
• 5. Frühbeck G. Overwiev of adipose tissue and its role in obesity and metabolic disorders. in: Kaiping Yang (ed) Adipose tisue protocols, Second ed. New Jersey: Humana press, 2001: 1-22.
• 6. Gesta S, Tseng YH, Kahn CR. Developmental origin of fat: Tracking obesity to its source. Cell. 2007; 131: 242-56.
• 7. Ibrahim MM. Subcutaneous and visceral adipose tissue: Structural and functional differences. Obes Rev. 2010; 11: 11-8.
• 8. Cannon B, Nedergaard J. Brown Adipose Tissue: Function and physiological significance. Physiol Rev. 2004; 84: 277–359.
• 9. Cinti S. Anatomy of the adipose organ. Eat Weight Disord. 2000; 5: 132–42.
• 10. Ricquier D, Bouillaud F. Mitochondrial uncoupling proteins: from mitochondria to the regulation of energy balance. J Physiol. 2000; 529: 3–10.
• 11. Supuran CT. Carbonic anhydrases: Novel therapeutic applications for inhibitors and activators. Nat Rev Drug Discov. 2008; 7: 168–81.
• 12. Kim G, Lee TH, Wetzel P, et al. Carbonic anhydrase III is not required in the mouse for normal growth, development, and life span. Mol Cell Biol. 2004; 24: 9942-47.
• 13. Sly WS, Hu PY. Human carbonic anhydrases and carbonic anhydrase deficiencies. Annu Rev Biochem. 1995; 64: 375–401.
• 14. Waldén TB, Hansen IR, Timmons JA, Cannon B, Nedergaard J. Nonrecruited molecular signatures of brown, “brite,” and white adipose tissues. Am J Physiol Endocrinol Metab. 2012; 302: E19-E31.
• 15. Raisanen SR, Lehenkari P, Tasanen M, Rahkila P, Harkonen PL, Vaananen HK. Carbonic anhydrase III protects cells from hydrogen peroxide-induced apoptosis. FABES J. 1999; 3: 513-22.
• 16. Available at: https://www.gene-quantification.de/roche-e-method-2006.pdf
• 17. Available at: https://plantbio.okstate.edu/images/pdfs/Roche_RT-PCR_Manual.pdf
• 18. Mihara M, Uchiyama M. Determination of malonaldehyde precursor in tissues by thiobarbituric acid test. Anal Biochem. 1978; 86: 271-78.
• 19. Wilbur KM, Anderson NG. Electrometric and colorimetric determination of carbonic anhydrase. J Biol Chem. 1948; 176: 147-54.
• 20. Alver A, Şentürk A, Çakirbay H, Menteşe A, Gökmen F. Carbonic anhydrase II autoantibody and oxidative stress in rheumatoid arthritis. Clinical Biochemistry. 2011; 44: 1385–9.
• 21. Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976; 72: 248-54.
• 22. Vincent HK, Taylor AG. Biomarkers and potential mechanisms of obesity-induced oxidant stress in humans. Int J Obes. 2006; 30: 400–18.
• 23. Galinier A, Carriere A, Fernandez Y, et al. Site specific changes of redox metabolism in adipose tissue of obese Zucker rats. FEBS Lett. 2006; 580: 6391-98.
• 24. Long EK, Olson DM, Bernlohr DA. High-fat diet induces changes in adipose tissue trans-4-oxo-2-nonenal and trans-4-hydroxy-2-nonenal levels in a depot-specific manner. Free Radic Biolo Med. 2013; 63: 390-8.
• 25. Kelly GS. Clinical applications of N-acetylcysteine. Altern Med Rev. 1998; 3: 114-27.
• 26. Chai YC, Jung CH, Lii CK, et al. Identification of an abundant S-thiolated rat liver protein as carbonic anhydrase III. Characterization of S-thiolation and dethiolation reactions. Arch Biochem Biophys. 1991; 284: 270–8.
• 27. Lii CK, Chai YC, Zhao W, Thomas JA, Hendrich S. S-thiolation and irreversible oxidation of sulfhydryls on carbonic anhydrase III during oxidative stress: A method for studying protein modification in intact cells and tissues. Arch Biochem Biophys. 1994: 308: 231–9.
• 28. Frost SC. Physiological functions of the alpha class of carbonic anhydrases. in: Frost SC, McKenna R (eds) Carbonic anhydrase: Mechanism, regulation, links to disease and industrial applications. Dorthrecht: Springer, 2014: 9-30.
• 29 .Koester MK, Register AM, Nolmann EA. Basic muscle protein, a third genetic locus isoenzyme of carbonic anhydrase? Biochem Biophys Res Commun. 1977; 76: 196–204.
• 30. Koester MK, Pullan LM, Noltmann EA. The p-nitrophenyl phosphatase activity of muscle carbonic anhydrase. Arch Biochem Biophys. 1981; 211: 632–42.