INHIBITION OF ADVANCED GLYCATION END-PRODUCT FORMATION BY QUERCETIN AND CATECHIN: AN ALTERNATIVE THERAPY FOR TREATING DIABETIC COMPLICATIONS


Angeline Julius, Waheeta Hopper

Abstract


 

 Objective: The objective of this research was to determine early advanced glycation end-product (AGE) inhibition by natural aldose reductase inhibitors (ARIs), quercetin and catechin.

Methods: The assay mixture (4 ml) consisted of 2 ml of 50 mM phosphate-buffered saline (pH 7.4), 50 μg/μl bovine serum albumin (BSA), and 2 mM glucose with or without the inhibitor. The test samples were treated with three different concentrations (10 mM, 20 mM, and 40 mM) of quercetin and catechin. High-throughput screening-based assay was adapted to perform the BSA-glucose test to determine the induction of AGE formation and its inhibition by quercetin, and catechin, using the fluorescence of the AGE-BSA sample at excitation and emission wavelengths of 350 and 450 nm.

Result: The ARIs, quercetin and catechin inhibited early glycation with an inhibitory concentration value of 15.58 mM and 35.01 mM, respectively.

Conclusion: The suppression of AGEs formation by natural inhibitors of aldose reductase would provide an alternative approach to the control of diabetic complications.


Keywords


Aldose reductase inhibitors, Advanced glycation end-products, High-throughput virtual screening, Natural compounds, Diabetic complications.

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References


Available from: http://www.who.int/mediacentre/factsheets/fs355/en.

Forssas E, Arffman M, Manderbacka K, Keskimäki I, Ruuth I, Sund R. Multiple complications among people with diabetes from Finland: An 18-year follow-up in 1994-2011. BMJ Open Diabetes Res Care 2016;4(1):e000254.

Giacco F, Brownlee M. Oxidative stress and diabetic complications. Circ Res 2010;107(9):1058-70.

Yan SF, Ramasamy R, Schmidt AM. The receptor for advanced glycation endproducts (RAGE) and cardiovascular disease. Expert Rev Mol Med 2009;11:e9.

Sadowska-Bartosz I, Bartosz G. Prevention of protein glycation by natural compounds. Molecules 2015;20(2):3309-34.

Thornalley PJ, Langborg A, Minhas HS. Formation of glyoxal, methylglyoxal and 3-deoxyglucosone in the glycation of proteins by glucose. Biochem J 1999;344:109-16.

Stitt AW, Moore JE, Sharkey JA, Murphy G, Simpson DA, Bucala R, et al. Advanced glycation end products in vitreous: Structural and functional implications for diabetic vitreopathy. Invest Ophthalmol Vis Sci 1998;39(13):2517-23.

Tangvarasittichai S, Deebukkhum S, Tangvarasittichai O. Progression of increased oxidative stress and inflammation in chronic kidney disease patients with Type 2 diabetes mellitus. Int J Pharm Clin Res 2016;8(6):596-603.

Lee HS, Hong CO, Lee KW. Advanced glycation endproduct-induced diabetic complications. Food Sci Biotechnol 2008;17(6):1131-8.

More TA, Kulkarni BR, Nalawade ML, Arvindekar AU. Antidiabetic activity of linalool and limonene in streptozotocin-induced diabetic rat: A combinatorial therapy approach. Int J Pharm Pharm Sci 2014;6(8):159-63.

Adeshara KA, Diwan AG, Tupe RS. Diabetes and complications: Cellular signaling pathways, current understanding and targeted therapies. Curr Drug Targets 2016;17(11):1309-28.

Younus H, Anwar S. Prevention of non-enzymatic glycosylation (glycation): Implication in the treatment of diabetic complication. Int J Health Sci (Qassim) 2016;10(2):261-77.

Abdurrazak M, Rao MU, Ado AB, Mohd KS, Thant Z. Some natural products and their secondary metabolites attributed towards diabetic cure: A review. Int J Pharm Pharm Sci 2015;7:22-8.

Rupeshkumar M, Kavitha K, Haldar PK. Role of herbal plants in the diabetes mellitus therapy: An overview. Int J Appl Pharm 2014;6(3):1-3.

Sadowska-Bartosz I, Galiniak S, Bartosz G. Kinetics of glycoxidation of bovine serum albumin by methylglyoxal and glyoxal and its prevention by various compounds. Molecules 2014;19(4):4880-96.

Séro L, Sanguinet L, Blanchard P, Dang BT, Morel S, Richomme P, et al. Tuning a 96-well microtiter plate fluorescence-based assay to identify AGE inhibitors in crude plant extracts. Molecules 2013;18(11):14320-39.

Matsuura N, Aradate T, Sasaki C, Kojima H, Ohara M, Hasegawa J, et al. Screening system for the Maillard reaction inhibitor from natural product extracts. J Health Sci 2002;48(6):520-6.

Koschinsky T, He CJ, Mitsuhashi T, Bucala R, Liu C, Buenting C, et al. Orally absorbed reactive glycation products (glycotoxins): An environmental risk factor in diabetic nephropathy. Proc Natl Acad Sci U S A 1997;94(12):6474-9.

Uribarri J, Peppa M, Cai W, Goldberg T, Lu M, He C, et al. Restriction of dietary glycotoxins reduces excessive advanced glycation end products in renal failure patients. J Am Soc Nephrol 2003;14(3):728-31.

Kaushik G, Satya S, Khandelwal RK, Naik S. Commonly consumed Indian plant food materials in the management of diabetes mellitus. Diabetes Metab Syndr Clin Res Rev 2010;4(1):21-40.

Dzib-Guerra WD, Escalante-Erosa F, García-Sosa K, Derbré S, Blanchard P, Richomme P, et al. Anti-advanced glycation end-product and free radical scavenging activity of plants from the yucatecan flora. Pharmacognosy Res 2016;8(4):276-80.

Pinto MD, Kwon YI, Apostolidis E, Lajolo FM, Genovese MI, Shetty K. Potential of Ginkgo biloba L. leaves in the management of hyperglycemia and hypertension using in vitro models. Bioresour Technol 2009;100(24):6599-609.

Yin XF, Jeon YE, Shim JH, Kang IJ. Inhibitory efficacy of Ligularia fischeri against aldose reductase and advanced glycation end products formation. Food Sci Biotechnol 2014;23(6):1747-52.

Ramkissoon JS, Mahomoodally MF, Ahmed N, Subratty AH. Relationship between total phenolic content, antioxidant potential, and antiglycation abilities of common culinary herbs and spices. J Med Food 2012;15(12):1116-23.

Singh P, Jayaramaiah RH, Agawane SB, Vannuruswamy G, Korwar AM, Anand A, et al. Potential dual role of eugenol in inhibiting advanced glycation end products in diabetes: Proteomic and mechanistic insights. Sci Rep 2016;6:18798.

Jariyapamornkoon N, Yibchok-anun S, Adisakwattana S. Inhibition of advanced glycation end products by red grape skin extract and its antioxidant activity. BMC Complement Altern Med 2013;13:171.

Yeh WJ, Hsia SM, Lee WH, Wu CH. Polyphenols with antiglycation activity and mechanisms of action: A review of recent findings. J Food Drug Anal 2017;25(1):84-92.

Veverka M, Gallovič J, Švajdlenka E, Veverková E, Prónayová N, Miláčková I, et al. Novel quercetin derivatives: Synthesis and screening for anti-oxidant activity and aldose reductase inhibition. Chem Pap 2013;67(1):76-83.

Delgado L, Fernandes I, González-Manzano S, de Freitas V, Mateus N, Santos-Buelga C. Anti-proliferative effects of quercetin and catechin metabolites. Food Funct 2014;5(4):797-803.

Goodarzi M, Zal F, Malakooti M, Safari M, Sadeghian S. Inhibitory activity of flavonoids on the lens aldose reductase of healthy and diabetic rats. Acta Med Iran 2006;44(1):41-5.

Murata M, Irie J, Homma S. Aldose reductase inhibitors from green tea. Food Sci Technol 1994;27(5):401-5.

Begum SF, Hemalatha SP. Characterization, in silico and in vitro determination of antidiabetic and anti-inflammatory potential of ethanolic extract of Sargassum wightii. Asian J Pharm Clin Res 2017;10(4):297-301.

Coughlan MT, Thorburn DR, Penfold SA, Laskowski A, Harcourt BE, Sourris KC, et al. RAGE-induced cytosolic ROS promote mitochondrial superoxide generation in diabetes. J Am Soc Nephrol 2009;20(4):742-52.




About this article

Title

INHIBITION OF ADVANCED GLYCATION END-PRODUCT FORMATION BY QUERCETIN AND CATECHIN: AN ALTERNATIVE THERAPY FOR TREATING DIABETIC COMPLICATIONS

Keywords

Aldose reductase inhibitors, Advanced glycation end-products, High-throughput virtual screening, Natural compounds, Diabetic complications.

DOI

10.22159/ajpcr.2017.v10i11.19412

Date

01-11-2017

Additional Links

Manuscript Submission

Journal

Asian Journal of Pharmaceutical and Clinical Research
Vol 10 Issue 11 November 2017 Page: 173-176

Print ISSN

0974-2441

Online ISSN

2455-3891

Statistics

44 Views | 66 Downloads

Authors & Affiliations

Angeline Julius
Department of Biotechnology, School of Bioengineering, Faculty of Engineering and Technology, SRM University, Chennai, Tamil Nadu, India.
India

Waheeta Hopper
Department of Biotechnology, School of Bioengineering, Faculty of Engineering and Technology, SRM University, Chennai, Tamil Nadu, India.
India


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