ANTIGLYCATION AND ANTI-AGES ACTIVITY OF SULFOSALICYLIC ACID (IN VITRO STUDY)

Main Article Content

Tanzila Sahar
Farah Naz Channa
Irum Javid
Shamim Khan
Nageen
Rimsha Saleem
Naila Rafiq

Keywords

Hyperglycemia, advanced glycation end products (AGEs), Sulfosalicylic acid, Periodate borohydride, TBA, bovine serum albumin (BSA).

Abstract

Diabetes mellitus is one of the most common diseases that is present nearly all over the world and it is characterized by hyperglycemia. Hyperglycemia results from protein glycation and the continuing increase of AGEs. These AGEs form on biomolecules and possess complex structures that produce protein fluorescence and cross-linking that leads to tissue damage. Salicylic acid is known as a potent inhibitor of glycation and AGEs. A number of its derivatives i.e. salicylate, 5-aminosalicylic acid, acetylsalicylic acid (aspirin), and para-amino salicylic acid are known to have the potential to reduce glycation levels and AGEs. Our study investigated glycation and AGEs inhibitory activity of sulfosalicylic acid, a synthetic compound using glucose-BSA invitro conditions. The study was performed by making sixteen combinations using different concentrations of glucose, inhibitors with BSA and these were incubated at 37oC and 50oC simultaneously for five weeks.  Glycation level was assessed by TBA and periodate assays. ELISA measured AGEs. The formation of glycated BSA was quantitated by measuring browning intensity. The results showed that browning was increased from 1st to 5th week of incubation due to an increase in glycation. Our results showed that a 10 mM concentration of sulfosalicylic acid showed a good response to minimize the glycation and AGE production as compared to its lower concentrations.  The results of this study demonstrated that sulfosalicylic acid inhibited the glycation of BSA by glucose in a dose-dependent manner. Periodate borohydride assay showed that it is a more suitable glycation method when compared to the TBA method. 


 


 

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References

1. J.E. Shaw, R.A. Sicree, P.Z. Zimmet. Diabetes Atlas. Global estimates of the prevalence of diabetes for 2010 and 2030. Diabetes research and clinical practice. 2010; 8(7): 4–1 4.
2. Melpomeni Peppa, Helen Vlassara. Review Advanced glycation end products and diabetic complications: A General overview. Hormones. 2005; 4(1): 28-37.
3. Nessar Ahmed. Review Advanced glycation endproducts—role in the pathology of diabetic complications. Diabetes Research and Clinical Practice 2005; 67: 3–21.
4. World diabetes foundation. 2012. IDF, Diabetes Atlas, 4th edition.
5. Rashid M. Ansari. Clinical Study. Effect of Physical Activity and Obesity on Type 2 Diabetes in a Middle-Aged Population. Hindawi Publishing Corporation Journal of Environmental and Public Health. 2009; 5: Article ID 195285.
6. Melpomeni Peppa, Helen Vlassara. Glucose, Advanced Glycation End Products, and Diabetes Complications: What Is New and What Works. Clinical Diabetes. 2005; 21(4): 186-187.
7. Puddu A, Viviani GL. Advanced glycation endproducts and diabetes. Beyond vascular complications. Endocr Metab Immune Disord Drug Targets. 2011 Jun;11(2):132-40.
8. Jose´ D. Me´ndez, Jianling Xie, Montserrat Aguilar-Herna´ndez, Verna Me´ndez-Valenzuela. Trends in advanced glycation end products research in diabetes mellitus and its complications. Mol Cell Biochem. 2010; 341: 33–41.
9. Benjamin S. Szwergold, Scott Howell, and Paul J. Beisswenger. 2001. Human Fructosamine-3-Kinase. Purification, Sequencing, Substrate Specificity, and Evidence of Activity In Vivo. Diabetes., SEPTEMBER 2001; Vol. 50: 2139- 2147.
10. Amy G. Huebschmann, Judith G. Regensteiner, Helen Vlassara, and Jane E.B. Reusch. Diabetes and Advanced Glycoxidation End Products. Diabetes Care June 2006; 29(6): 1420-1432.
11. Takeuchi, M., S. Yamagishi, M. Iwaki, K. Nakamura and T. Imaizumi. Advanced glycation end product (AGE) inhibitors and their therapeutic implications in diseases. Int. J. Clin. Pharm. Res. 2004; 24(2): 95-101.
12. Tatiana Shcheglova, Sudesh Makker, and Alfonso Tramontano. 2009. Reactive Immunization Suppresses Advanced Glycation and Mitigates Diabetic Nephropathy. J Am Soc Nephrol. May 2009; 20(5): 1012–1019.
13. Samuel Rahbar and James L. Figarola. Minireview. Novel inhibitors of advanced glycation endproducts. Archives of Biochemistry and Biophysics 2003; 419(2003): 63–79.
14. Gornall AG, Bardawill CS, David MM. Determination of serum proteins by means of biuret reaction. J BioI Chem; 1949;177(2): 751-766.
15. Furth AJ. Methods for assaying non enzymatic glycosylation: A review. Anal Biochem; 1988;175(2): 347-360.
16. Gallop PM, Fluckiger R, Hanneken A, Mininshon MM, Gabbay KH. Chemical quantitation of hemoglobin glycosylation: Fluorometric detection of formaldehyde released upon periodate oxidation of glycoglobin. Anal Biochem 1981;117(2): 427-432.
17. Zhang EY, Swaan PW. Determination of Membrane Protein Glycation in Diabetic Tissue. AAPS Pharm Sci.1999; 1(4): 20-24.
18. X. Zhang, M. Frischmann, R.K. Engel, K. Steinmann, H. Stopper, T. Niwa and M. Pischetsrieder, Clin. Chem. Lab. Med. 2005; 43(5): 503.
19. Huby, R., and J. J. Harding. Non-enzymatic glycosylation (glycation) of lens protein by galactose and protection by aspirin and reduced glutathione. Exp. Eye Res. 1988; 47:53-59.
20. Yue, D. K., S. Mclennen, D. J. Handelsman, L. Deibridge, T. Reeve, J. R. Turtle. The effect of salicylates on nonenzamatic glycosylaion and thermal stability of collagen in diabetic rats. Diabetes. 1984; 33: 745-751.
21. Rao, G. N., M. P. Lardis, E. Cotlier. Acetylation of lens crystalline: a possible mechanism by which aspirin could prevent cataract formation. Biochem. Biophys. Res. Commun. 1985; 128: 1125-1132.
22. Duraisamy, Y., J. Gaffney, M. Slevin, C. A. Smith, K. Williamson, and N. Ahmad. Aminosalicylic acid reduces the antiproliferative effect of hyperglycemia, advanced glycation endproducts, and glycated basic fibroblast growth factor in cultured bovine aortic endothelial cells: comparison with aminoguanidine. Mol Cell Biochem. 2003; 246(1-2): 143-153.
23. Rahbar S, Figarola JL. Inhibitors and breakers of advanced glycation end products (AGEs): A Review. Curr Med Chem Imun Endoc & Metab Agents 2002; 2: 135-161.
24. Hatton, W., Mark, R. Mary, and D. W. Peter. On glucose transport and the non-enzymatic glycation of protein in vivo. J. Theorbiol. 1993; 161(4): 481-490.
25. Winocour, P.D., C. Watala, D.W. Perry and R.L. Kinlough-Rathbone. Decreased platelets membrane fluidity due to glycation or acetylation of membrane protein. Thromb. Haemost. 1992; 68(5): 577-582.
26. Eble, A.S. S.R. Thorpe and J.W. Baynes. Non-enzymatic glucosylation and glucose-dependent crosslinking of protein. J. Biol.Chem. 1983; 258: 9406-9412.
27. Brownlee, M. Non-enzymatic glycosylation and the pathogenesis of diabetic complications. Annal. Internal Med. 1984;101: 527-537.
28. Vinson, J. A., and T. B. Howard. Inhibition of protein glycation and advanced glycation end products by ascorbic acid and other vitamins and nutrients. Journal of nutritional biochemistry. J. Nutr. Biochem. 1996; 7: 659-663.
29. Kennedy, L., T. D. Mehl, E. Elder, M. Varghese, T. J. Merimee. Nonenzymatic glucosylation of serum and plasma proteins. Diabetes. 1982; 31: 52-56.
30. Rendell, M., J. Nierenberg, C. Brannan, J. L. Valentine, P. M. Stephen, S. Dodds, P. Mercer, P. K. Smith and J. Walder. Inhibition of glycation of albumin and hemoglobin by acetylation invitro and invivo. J Lab Clin Med. 1986; 108(4): 286-293.
31. Swamy, M. S., and E. C. Abraham. Inhibition of lens crystalline glycation and high molecular weight aggregate formation by aspirin in-vitro and in-vivo. Invest. Ophthalmol. Vis. Sci. 1989; 30: 1120-1126.
32. Stoynev, G.A., L.N. Srebreva and I. G. Ivonov. Histine H1 as a reporter protein to investigate glycation in bacteria. Current Microbial. 2004; 49: 423-427.
33. Zhang, J., M. Slevin, Y. Duraisamy, J. Gaffney, C. A. Smith, and N. Ahmad. Comparison of protective effects of aspirin, D-penicillamine, and vitamin E against high glucose-mediated toxicity in cultured endothelial cells, Biochemica Et Biophysica Acta. 2006; 1762(5): 551-557.
34. Gillery, P. Advanced glycation end products” (AGEs), free radicals, and diabetes. J. Soc. Biol. 2001; 4: 387-390.
35. Day, J. F., S. R. Thorpe, J. W. Baynes. Nonenzymatically glucosylated albumin. invitro preparation and isolation from normal human serum. J. Biol. Chem. 1979a;254: 595-597.
36. Day, J. F., R. W. Thornburg, S. R. Thorpe, J. W. Baynes. Nonenzymatic glucosylation of rat albumin. Studied invitro and invivo. J. Biol. Chem. 1979b;254: 9394-9400.

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