Research Article
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Farelerde Yüksek Yağlı Diyetin Karaciğer Karbonik Anhidraz Aktivitesi Üzerine Etkisinin Araştırılması

Year 2024, Volume: 3 Issue: 3, 79 - 84, 01.10.2024
https://doi.org/10.59518/farabimedj.1545667

Abstract

Prokaryotlardan ökaryotlara kadar çok geniş bir dağılıma sahip olan karbonik anhidrazlar (CA, E.C.4.2.1.1, karbonat hidroliyaz), bikarbonatın (HCO3-) dehidrasyon veya (CO2) karbodioksitin hidrasyonunu dönüşümlü olarak katalizleyen, aktif bölgesinde prostetik grup olarak Zn2+ içeren metaloenzimlerdir. Bu enzimler CO2 taşınması, dokularda elektrolit salgılanması, kemik resorpsiyonu, tümör oluşumu ve idrar asidifikasyonu gibi birçok fizyolojik süreçte görev almaktadır. Çalışmada yüksek yağlı diyetin de novo lipit sentezinin öncü bileşiği olan HCO3-'ı senteleyen CA aktivitesi üzerine etkilerinin, fare karaciğerinde incelenmesi amaçlanmıştır. Çalışma kapsamında, 16 adet erkek C57BL/6J ırkı fare Research Diets' ten alınan yüksek yağlı ve standart fare yemleri ile beslendi. Dört aylık beslenme periyodunun sonunda farelerin ağırlıkları ölçüldü ve dekapitasyon ile sakrifiye edildi. Karaciğer dokuları homojenize edildikten sonra CA aktiviteleri potansiyometrik metod ile ölçüldü. Standart diyet ile beslenen farelerin CA aktivitesi 0.87±0.26 U/mg protein olarak ölçülürken, Yüksek yağlı diyet grubundaki farelerde ise aktivite 0,60±0,15 U/mg protein olarak bulundu (p=0.038). Sonuç olarak, yüksek yağlı diyet kullanımının de novo lipit sentezinde öncü bileşiği sentezleyen CA aktivitesini fare karaciğerinde azalttığı ve bu azalışa metabolik ve hormonal değişikliklerin sebep olabileceği kanaatine varıldı.

Ethical Statement

Yapılan deneylerin tamamı, Karadeniz Teknik Üniversitesi Hayvan deneyleri yerel etik kurulunun 2010/39 protokol no’lu etik kurul onayı ile sakrifiye edilmiş hayvanların karaciğerlerinde yapılmıştır.

References

  • Frost SC. Carbonic Anhydrase: Mechanism, Regulation, Links to Disease, and Industrial Applications. Springer; 2014.
  • Senturk A, Alver A, Karkucak M, Küçük M, Ahmadi Rendi T. Oxidative modification of carbonic anhydrase by peroxynitrite trigger immune response in mice and rheumatic disease patients. Am J Med Sci. 2023;366(6):438-448. doi:10.1016/j.amjms.2023.09.002
  • Pocker Y, Sarkanen S. Oxonase and esterase activities of erythrocyte carbonic anhydrase. Biochemistry. 1978;17(6):1110-1118. doi:10.1021/bi00599a027
  • Alver A, Şentürk A, Çakirbay H, et al. Carbonic anhydrase II autoantibody and oxidative stress in rheumatoid arthritis. Clin Biochem. 2011;44(17-18):1385-1389. doi:10.1016/j.clinbiochem.2011.09.014
  • Saleem M, Saeed A, Khan A, et al. Benzamide sulfonamide derivatives: potent inhibitors of carbonic anhydrase-II. Medicinal Chemistry Research. 2016;25(3): 438-448.
  • Supuran CT. Carbonic anhydrase inhibitors: an editorial. Expert Opin Ther Pat. 2013;23(6):677-679. doi:10.1517/13543776.2013.778246
  • Burtis CA, Bruns DE. Tietz Fundamentals of Clinical Chemistry and Molecular Diagnostics. Elsevier Health Sciences; 2014.
  • Dodgson SJ. Why are there carbonic anhydrases in the liver?. Biochem Cell Biol. 1991;69(12):761-763. doi:10.1139/o91-116
  • King RW, Garg LC, Huckson J, Maren TH. The isolation and partial characterization of sulfonamide-resistant carbonic anhydrases from the liver of the male rat. Mol Pharmacol. 1974;10(2):335-343.
  • Ronchi VP, Conde RD, Guillemot JC, Sanllorenti PM. The mouse liver content of carbonic anhydrase III and glutathione S-tranferases A3 and P1 depend on dietary supply of methionine and cysteine. Int J Biochem Cell Biol. 2004;36(10):1993-2004. doi:10.1016/j.biocel.2004.02.019
  • Wilbur KM, Anderson NG. Electrometric and colorimetric determination of carbonic anhydrase. J Biol Chem. 1948;176(1):147-154.
  • Wang B. Drug design of zinc-enzyme inhibitors: functional, structural, and disease applications. John Wiley & Sons; 2009.
  • Hazen SA, Waheed A, Sly WS, LaNoue KF, Lynch CJ. Differentiation-dependent expression of CA V and the role of carbonic anhydrase isozymes in pyruvate carboxylation in adipocytes. FASEB J. 1996;10(4):481-490. doi:10.1096/fasebj.10.4.8647347
  • Ibrahim SI, Ameh DA, Atawodi SE, Umar IA. Carbonic anhydrase: a new therapeutic target for managing diabetes. J Metabolic Synd. 2016;5(196):2167-0943.
  • Alver A, Uçar F, Keha EE, Kalay E, Ovali E. Effects of leptin and insulin on CA III expression in rat adipose tissue. J Enzyme Inhib Med Chem. 2004;19(3):279-281. doi:10.1080/14756360410001720445

Investigation of The Effect of High Fat Diet on Liver Carbonic Anhydrase Activity in Mice

Year 2024, Volume: 3 Issue: 3, 79 - 84, 01.10.2024
https://doi.org/10.59518/farabimedj.1545667

Abstract

Carbonic anhydrases (CA, E.C.4.2.1.1, carbonate hydrolase), which have a very wide distribution from prokaryotes to eukaryotes, are metalloenzymes containing Zn2+ as a prosthetic group in the active site that alternately catalyze the dehydration of bicarbonate (HCO3-) or hydration of carbodioxide (CO2). These enzymes are involved in many physiological processes such as transport of CO2, electrolyte secretion in tissues, bone resorption, tumorigenesis and urinary acidification. In this study, it is aimed to investigate of the effect's high fat diet on the activity of CA, synthesized HCO3- that is the precursor of de novo lipid synthesis, in mice liver. Within the study, 16 male C57BL / 6J mice fed with high fat and standard mouse feed from Research Diets. At the end of the four-month feeding period, mice were weighed and sacrificed by decapitation. After the liver tissues were homogenized, CA activities were measured by potentiometric method. The activity of the standard diet fed mice was measured as 0.87±0.26 U/mg protein. For the rats in the high fat dietary group, the activity was 0.60±0.15 U/mg protein (p=0.038). As a result, it was concluded that the use of high-fat diet reduced activity of CA synthesized the precursor substance for de novo lipid synthesis in mice live and metabolic and hormonal changes may be caused this decrease.

Ethical Statement

All experiments were performed on the livers of sacrificed animals with the approval of the Karadeniz Technical University Animal Experiments Local Ethics Committee under protocol no. 2010/39.

References

  • Frost SC. Carbonic Anhydrase: Mechanism, Regulation, Links to Disease, and Industrial Applications. Springer; 2014.
  • Senturk A, Alver A, Karkucak M, Küçük M, Ahmadi Rendi T. Oxidative modification of carbonic anhydrase by peroxynitrite trigger immune response in mice and rheumatic disease patients. Am J Med Sci. 2023;366(6):438-448. doi:10.1016/j.amjms.2023.09.002
  • Pocker Y, Sarkanen S. Oxonase and esterase activities of erythrocyte carbonic anhydrase. Biochemistry. 1978;17(6):1110-1118. doi:10.1021/bi00599a027
  • Alver A, Şentürk A, Çakirbay H, et al. Carbonic anhydrase II autoantibody and oxidative stress in rheumatoid arthritis. Clin Biochem. 2011;44(17-18):1385-1389. doi:10.1016/j.clinbiochem.2011.09.014
  • Saleem M, Saeed A, Khan A, et al. Benzamide sulfonamide derivatives: potent inhibitors of carbonic anhydrase-II. Medicinal Chemistry Research. 2016;25(3): 438-448.
  • Supuran CT. Carbonic anhydrase inhibitors: an editorial. Expert Opin Ther Pat. 2013;23(6):677-679. doi:10.1517/13543776.2013.778246
  • Burtis CA, Bruns DE. Tietz Fundamentals of Clinical Chemistry and Molecular Diagnostics. Elsevier Health Sciences; 2014.
  • Dodgson SJ. Why are there carbonic anhydrases in the liver?. Biochem Cell Biol. 1991;69(12):761-763. doi:10.1139/o91-116
  • King RW, Garg LC, Huckson J, Maren TH. The isolation and partial characterization of sulfonamide-resistant carbonic anhydrases from the liver of the male rat. Mol Pharmacol. 1974;10(2):335-343.
  • Ronchi VP, Conde RD, Guillemot JC, Sanllorenti PM. The mouse liver content of carbonic anhydrase III and glutathione S-tranferases A3 and P1 depend on dietary supply of methionine and cysteine. Int J Biochem Cell Biol. 2004;36(10):1993-2004. doi:10.1016/j.biocel.2004.02.019
  • Wilbur KM, Anderson NG. Electrometric and colorimetric determination of carbonic anhydrase. J Biol Chem. 1948;176(1):147-154.
  • Wang B. Drug design of zinc-enzyme inhibitors: functional, structural, and disease applications. John Wiley & Sons; 2009.
  • Hazen SA, Waheed A, Sly WS, LaNoue KF, Lynch CJ. Differentiation-dependent expression of CA V and the role of carbonic anhydrase isozymes in pyruvate carboxylation in adipocytes. FASEB J. 1996;10(4):481-490. doi:10.1096/fasebj.10.4.8647347
  • Ibrahim SI, Ameh DA, Atawodi SE, Umar IA. Carbonic anhydrase: a new therapeutic target for managing diabetes. J Metabolic Synd. 2016;5(196):2167-0943.
  • Alver A, Uçar F, Keha EE, Kalay E, Ovali E. Effects of leptin and insulin on CA III expression in rat adipose tissue. J Enzyme Inhib Med Chem. 2004;19(3):279-281. doi:10.1080/14756360410001720445
There are 15 citations in total.

Details

Primary Language Turkish
Subjects Medical Biochemistry - Amino Acids and Metabolites
Journal Section Research Articles
Authors

Pınar Sarışın 0009-0009-3841-662X

İmran İnce Akça 0000-0003-2232-3444

Ahmet Alver 0000-0002-9617-6689

Publication Date October 1, 2024
Submission Date September 10, 2024
Acceptance Date September 19, 2024
Published in Issue Year 2024 Volume: 3 Issue: 3

Cite

AMA Sarışın P, İnce Akça İ, Alver A. Farelerde Yüksek Yağlı Diyetin Karaciğer Karbonik Anhidraz Aktivitesi Üzerine Etkisinin Araştırılması. Farabi Med J. October 2024;3(3):79-84. doi:10.59518/farabimedj.1545667

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