Investigation of the Effects of Compounds, β-D-Glucan, Lectin, Linoleic Acid and β-Carotene on Carbonic Anhydrase Enzymes

Abstract

β-D-glucan, lectin, linoleic acid and β-carotene are biologically active compounds and they are found in animal, herbal and bacterial sources. Glaucoma is the second most common cause of blindness worldwide after cataract. Carbonic anhydrase (CA) inhibitors have been used in the treatment of glaucoma for years. However, inhibitory agents have a lot of side effects. Research groups have been working on the development of new CA inhibitors. Research into the use of compounds of natural origin as CA inhibitors has also gained popularity in recent years. In this study, the inhibitory effects of β-D-glucan, lectin, linoleic acid and β-carotene on human erythrocyte carbonic anhydrase isoenzymes, hCA I and hCA II, have been studied in vitro. The Ki values of the compounds were in the range of 0.45±0.09 µM − 37.02±17.85 µM for hCA I, and 3.12±1.38 µM − 61.23±25.46 µM for hCA II.

Keywords

• β-D-glucan
• Lectin
• Linoleic acid
• β-carotene
• Carbonic anhydrase

β-D-Glukan, Lektin, Linoleik Asit ve β-Karoten Bileşiklerinin Karbonik Anhidraz Enzimleri Üzerindeki Etkilerinin Araştırılması

Abstract

β-D-glukan, lektin, linoleik asit ve β-karoten; hayvansal, bitkisel ve bakteriyel kaynaklarda bulunan, biyolojik olarak aktif bileşiklerdir. Glokom, dünya genelinde körlüğe neden olma bakımından katarakttan sonra ikinci sırada gelen bir hastalıktır. Karbonik anhidraz (CA) inhibitörleri uzun yıllardır glokom tedavisinde kullanılmaktadır. Ancak, inhibitör ajanların yan etkileri azımsanmayacak derecede çoktur. Yeni CA inhibitörlerinin geliştirilmesi üzerine çeşitli araştırma grupları çalışmalar yapmaktadırlar. Doğal kaynaklı bileşiklerin CA inhibitörü olarak kullanımının araştırılması da son yıllarda popülerlik kazanmıştır. Bu çalışmada, β-D-glukan, lektin, linoleik asit ve β-karoten bileşiklerinin, insan eritrosit CA izoenzimleri olan hCA I ve hCA II üzerine etkileri in vitro koşullarda araştırılmıştır. Bileşiklerin Ki değerleri hCA I için 0.45±0.09 µM − 37.02±17.85 µM aralığında, hCA II için 3.12±1.38 µM − 61.23±25.46 µM aralığındadır.

Keywords

• β-D-glukan
• Lektin
• Linoleik asit
• β-karoten
• Karbonik anhidraz

References

1. [1] Ai, Q., Mai, K., Zhang, L., Tan, B., Zhang, W., Xu, W., Li, H. 2007. Effects of dietary β-1,3 glucan on innate immune response of large yellow croaker, Pseudosciaena crocea. Fish & Shellfish Immunology, 22, 394-402.
2. [2] Tiwari, U., Cummins, E. 2011. Meta-analysis of the effect of β-glucan intake on blood cholesterol and glucose levels. Nutrition, 27, 1008-1016.
3. [3] Dietrich-Muszalska, A., Olas, B., Kontek, B., Rabe-Jabłońska, J. 2011. Beta-glucan from Saccharomyces cerevisiae reduces plasma lipid peroxidation induced by haloperidol. International Journal of Biological Macromolecules, 49, 113-116.
4. [4] Bellande, K., Bono, J. J., Savelli, B., Jamet, E., Canut, H. 2017. Plant lectins and lectin receptor-like kinases: How do they sense outside?. International Journal of Molecular Sciences, 18, 1164.
5. [5] Zheng, S., Li, C., Ng, B. T., Wang, H. X. 2007. A lectin with mitogenic activity from edible wild mushroom Boletus edulis. Process Biochemistry, 42, 1620-1624.
6. [6] Li, Y. R., Liu, Q. H., Wang, H. X., Ng, T. B. 2008. A novel lectin with potent antitumor, mitogenic and HIV-1 reverse transcriptase inhibitory activities from the mushroom Pleutorus citrinopleatus. Biochimica et Biophysica Acta, 1780, 51-57.
7. [7] Dulińska, J., Gil, D., Zagajewski, J., Hartwich, J., Bodzioch, M., Dembińska-Kieć, A., Langmann, T., Schmitz, G., Laidler, P. 2005. Different effect of beta-carotene on proliferation of prostate cancer cells. Biochimica et Biophysica Acta, 1740, 189-201.
8. [8] Qiu, D., Chen, Z. R., Li, H. R. 2009. Effect of heating on solid β-carotene. Food Chemistry, 112, 344-349.

9. [9] Naughton, S. S., Mathai, M. L., Hryciw, D. H., McAinch, A. J. 2016. Linoleic acid and pathogenesis of obesity. Prostaglandins & Other Lipid Mediators, 125, 90-99.
10. [10] Jung, S., Han, B. H., Nam, K., Ahn, D. U., Lee, J. H., Jo, C. 2011. Effect of dietary supplementation of gallic acid and linoleic acid mixture or their synthetic salt on egg quality. Food Chemistry, 129(3), 822-829.
11. [11] Alterio, V., Di Fiore, A., D’Ambrosio, K., Supuran, C. T., De Simone, G. 2012. Multiple binding modes of inhibitors to carbonic anhydrase: How to design specific drugs targeting 15 different isoforms?. Chemical Reviews, 112, 4421-4468.
12. [12] Supuran, C. T. 2008. Carbonic anhydrases: novel therapeutic applications for inhibitors and activators. Nature Reviews Drug Discovery, 7, 168-181.
13. [13] Kikutani, S., Nakajima, K., Nagasato, C., Tsuji, Y., Miyatake, A., Matsuda, Y. 2016. Thylakoid luminal θ-carbonic anhydrase critical for growth and photosynthesis in the marine diatom Phaeodactylum tricornutum. Proceedings of the National Academy of Sciences, 113, 9828-9833.
14. [14] Winum, J. Y., Vullo, D., Casini, A., Montero, J. L., Scozzafava, A., Supuran, C. T. 2003. Carbonic anhydrase inhibitors. Inhibition of cytosolic isozymes I and II and transmembrane tumor associated isozyme IX with sulfamates including EMATE also acting as steroid sulfatase inhibitors. Journal of Medicinal Chemistry, 46, 2197-2204.
15. [15] Şentürk, M., Gülçin, İ., Beydemir, Ş., Küfrevioğlu, Ö. İ., Supuran C. T. 2011. In vitro inhibition of human carbonic anhydrase I and II isozymes with natural phenolic compounds. Chemical Biology and Drug Design, 77, 494-499.
16. [16] Sarıkaya, S. B. Ö, Topal, F., Şentürk, M., Gülçin, İ., Supuran, C. T. 2011. In vitro inhibition of α-carbonic anhydrase isozymes by some phenolic compounds. Bioorganic & Medicinal Chemistry, 21, 4259-4262.
17. [17] Yenikaya, C., İlkimen, H., Demirel, M. M., Ceyhan, B., Bülbül, M., Tunca, E. 2016. Preparation of two maleic acid sulfonamide salts and their copper(II) complexes and antiglaucoma activity studies. Journal of Brazilian Chemical Society, 27(10), 1706-1714.
18. [18] Scozzafava, A., Banciu, M. D., Popescu, A., Supuran, C. T. 2000. Carbonic anhydrase inhibitors: Inhibition of isoenzymes I, II and IV by sulfonamide and sulfamic acid derivatives. Journal of Enzyme Inhibition and Medicinal Chemistry, 15, 443-453.
19. [19] Schuman, J. S. 2000. Antiglaucoma medications: a review of safety and tolerability issues related to their use. Clinical Therapeutics, 22, 167-208.
20. [20] Brzozowski, Z., Słaviński, J., Innocenti, A., Supuran, C. T. 2010. Carbonic anhydrase inhibitors. Regioselective synthesis of novel 1-substituted 1,4-dihydro-4-oxo-3-pyridinesulfon-amides and their inhibition of human cytosolic isozymes I and II and transmembrane cancer-associated isozymes IX and XII. European Journal of Medicinal Chemistry, 45, 3656-3661.
21. [21] Balaydın, H. T., Şentürk M., Göksu, S., Menzek A. 2012. Synthesis and carbonic anhydrase inhibitory properties of novel bromophenols and their derivatives incuding natural products: Vidalol B. European Journal of Medicinal Chemistry, 54, 423-428.
22. [22] Supuran, C. T. 2011. Carbonic anhydrase inhibition with natural products: novel chemotypes and inhibition mechanisms. Molecular Diversity, 15, 305-316.
23. [23] Innocenti, A., Sarıkaya, S. B. Ö., Gülçin, İ, Supuran, C. T. 2010. Carbonic anhydrase inhibitors. Inhibition of mammalian isoforms I-XIV with a series of natural product polyphenols and phenolic acids. Bioorganic & Medicinal Chemistry, 18, 2159-2164.
24. [24] Sarıkaya, S. B. Ö., Gülçin, İ., Supuran, C. T., 2010. Carbonic anhydrase inhibitors: Inhibition of human erythrocyte isozymes I and II with a series of phenolic acids. Chemical Biology and Drug Design, 75, 515-520.
25. [25] Rickli, E. E., Ghazanfar, S. A., Gibbons, B. H., Edsall, J. T. 1964. Carbonic anhydrases from human erythrocytes. Preparation and properties of two enzymes. Journal of Biological Chemistry, 239, 1065-1078.
26. [26] Bradford, M. M. 1976. A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry, 72, 248-254.
27. [27] Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
28. [28] Wilbur, K. M., Anderson, N. G. 1948. Electrometric and colorimetric determination of carbonic anhydrase. Journal of Biological Chemistry, 176, 147-154.
29. [29] Maren, T. H. 1960. A simplified micromethod for the determination of carbonic anhydrase and its inhibitors. Journal of Pharmacology and Experimental Therapeutics, 130, 26-29.
30. [30] Verpoorte, J. A., Mehta, S., Edsall, J. T. 1967. Esterase activities of human carbonic anhydrases B and C. Journal of Biological Chemistry, 242, 4221-4229.
31. [31] Lineweaver, H., Burk, D. 1934. The determination of enzyme dissociation constants. Journal of the American Chemical Society, 56, 658-666.
32. [32] Topal, M. Gülçin, İ. 2014. Rosmarinic acid: a potent carbonic anhydrase isoenzymes inhibitör. Turkish Journal of Chemistry, 38, 894-902.
33. [33] Supuran, C. T. 2016. Structure and function of carbonic anhydrases. Biochemical Journal 473, 2023-2032.
34. [34] Innocenti, A., Vullo, D., Scozzafava, A. Supuran, C. T. 2008. Carbonic anhydrase inhibitors. Interactions of phenols with the 12 catalytically active mammalian isoforms (CA I-XIV). Bioorganic & Medicinal Chemistry Letters, 18, 1583-1587.
35. [35] Innocenti, A., Vullo, D., Scozzafava, A. Supuran, C. T. 2008. Carbonic anhydrase inhibitors. Inhibition of mammalian isoforms I-XIV with a series of substituted phenols including paracetamol and salicylic acid. Bioorganic & Medicinal Chemistry, 16, 7424-7428.
36. [36] Maresca, A., Supuran, C. T. 2010. Coumarins incorporating hydroxy and chloro moieties selectively inhibit the transmembrane, tumor-associated carbonic anhydrase isoforms IX and XII over the cytosolic ones I and II. Bioorganic & Medicinal Chemistry Letters, 20, 4511-4514.
37. [37] Carta, F., Temperini, C., Innocenti, A., Scozzafava, A., Kaila, K., Supuran, C. T. 2010. Polyamines inhibit carbonic anydrases by anchoring to zinc-coordinated water molecule. Journal of Medicinal Chemistry, 53, 5511-5522.
38. [38] Gocer, H., Topal, F., Topal, M., Küçük, M., Teke, D., Gülçin, İ., Alwasel, S. H., Supuran, C. T. 2016. Acetylcholinesterase and carbonic anhydrase isoenzymes I and II inhibition profiles of taxifolin. Journal of Enzyme Inhibition and Medicinal Chemistry, 31(3), 441-447.