The Effect of Formetanate Hydrochloride on the Glycated Human Hemoglobin

Document Type : Research Article

Authors

Department of Biotechnology, Faculty of Biological Sciences, Alzahra University, Tehran, I.R. IRAN

Abstract

Glycation refers to the nonenzymatic glycosylation of the free amino groups of proteins and sugars. Advanced Glycation End-products (AGEs) are the final stage in the glycation process. AGEs cause many complications in diabetic patients. Fortunate hydrochloride is a highly effective pesticide widely used in agriculture. Hence, all human beings, both healthy and diabetic-affected patients, can be exposed to this toxin. Therefore, the purpose of the present research is to study, the effect of Formetanate hydrochloride on glycated human hemoglobin (GHb). To form glycated hemoglobin, Hb was incubated with glucose for 35 days under physiological conditions (dark, 37 °C, and pH 7.4). The effect of the toxin on GHb was investigated via docking studies, fluorometry, UV-Vis, and circular dichroism spectroscopy. Incubating Hb with glucose could degrade the structure of the protein. Samples containing GHb and formetanate hydrochloride showed remarkable changes in the structure; Heme-group degradation and an increase in β-sheet structures were also observed. The results of docking studies were consistent with these results. As diabetes is rapidly expanding in today's world and formetanate hydrochloride is widely used in agriculture, the impact of this toxin on these patients will be very important. According to the results obtained, this toxin can have a more destructive effect on the glycated Hb in these patients.

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References

[1] Stanley J., Preetha G., Pesticide Toxicity to Non-Target Organisms: Exposure, Toxicity and Risk Assessment Methodologies, Pesticide Toxicity to Non-target Organisms: Exposure, Toxicity and Risk Assessment Methodologies (2016).
        doi:10.1007/978-94-017-7752-0.
[2] Tingle C.C.D., Rother J.A., Dewhurst C.F., Lauer S., King W.J., Fipronil: Environmental Fate, Ecotoxicology, and Human Health Concerns, Rev. Environ. Contam. Toxicol. 176: 1–66 (2003).
[3] Childers C.C., Villanueva R., Aguilar H., Chewning, R., Michaud J.P., Comparative Residual Toxicities of Pesticides to the Predator Agistemus Industani (Acari: Stigmaeidae) on Citrus in Florida. Exp. Appl. Acarol. 25: 461–474 (2001).
[4] Cockcroft D.W., et al. Reproduced with Permission of the Copyright Owner. Further Reproduction Prohibited Without, J. Allergy Clin. Immunol, 130: 556 (2012).
[5] Cartwright R., Book Reviews: Book Reviews, Perspect. Public Health, 130: 239–239 (2010).
[6] Bishop C.A., Collins B., Mineau P., Burgess N.M., Read W.F., Risley Ch., Reproduction of Cavity-Nesting Birds in Pesticide-Sprayed Apple Orchards in Southern Ontario, Canada, 1988-1994, Environ. Toxicol. Chem., 19: 588–599 (2000).
[7] Bakhti H., Hamida N. Ben, Kinetics and Mechanism of Degradation of Aqueous Promecarb Insecticide Studied by UV Spectrophotometry and HPLC, Prog. React. Kinet. Mech., 42: 145–153 (2017).
[8] Pesticides in the Modern World - Trends in Pesticides Analysis. Pesticides in the Modern World - Trends
in Pesticides Analysis (2012).
[9] Ash-Bernal R., Wise R., Wright S.M., Acquired Methemoglobinemia: A Retrospective Series of 138 Cases at 2 Teaching Hospitals, Medicine (Baltimore). 83: 265–273 (2004).
[10] Leonard S.T., Moerschbaecher J.M., Winsauer P.J., Estradiol Replacement in Gonadectomized Male Rats Alters Scopolamine-Induced Disruptions of Nonspatial Learning, Exp. Clin. Psychopharmacol. 16: 532–546 (2008).
[11] Divito C.B., Davies S., Masoudi S., Muhoro C.N., Relative Stability of Formamidine and Carbamate Groups in the Bifunctional Pesticide Formetanate Hydrochloride, J. Agric. Food Chem., 55: 5377–5382 (2007).
[12] Al-Thani R.K., Al-Thani A.S., Elbetieha A, Darmani H., Assessment of Reproductive and Fertility Effects of Amitraz Pesticide in Male Mice, Toxicol. Lett., 138: 253–260 (2003).
[13] Sengupta B., Swenson J., Properties of Normal and Glycated Human Hemoglobin in Presence and Absence of Antioxidant, Biochem. Biophys. Res. Commun. 334: 954–959 (2005).
[14] Venkateshrao S., Manoharan P.T., Conformational Changes Monitored by Fluorescence Study on Reconstituted Hemoglobins, Spectrochim. Acta - Part A Mol. Biomol. Spectrosc., 60: 2523–2526 (2004).
[15] Kameyama M., Okumiya T., Tokuhiro Sh., Matsumura Y., Matsui H., Ono Y., Iwasaka T., Hiratani K., Koga M., Estimation of the Hemoglobin Glycation Rate Constant, bioRxiv (2019),
        doi:10.1101/652818.
[16] Lledó-García R., Mazer N.A., Karlsson M.O.A., Semi-Mechanistic Model of the Relationship Between Average Glucose and Hba1c in Healthy and Diabetic Subjects, J. Pharmacokinet. Pharmacodyn. 40: 129–142 (2013).
[17] Park S.Y., Yokoyama T., Shibayama N., Shiro Y., Tame J.R.H., 1.25 Å Resolution Crystal Structures of Human Haemoglobin in the Oxy, Deoxy and Carbonmonoxy Forms, J. Mol. Biol., 360: 690–701 (2006).
[18] Simm A., Protein Glycation During Aging and in Cardiovascular Disease, J. Proteomics, 92: 248–259 (2013).
[19] Muthenna P. et al. Inhibition of Protein Glycation by Procyanidin-B2 Enriched Fraction of Cinnamon: Delay of Diabetic Cataract in Rats, IUBMB Life, 65: 941–950 (2013).
[20] Awasthi S., Saraswathi N.T., Silybin, a Flavonolignan from Milk Thistle Seeds, Restrains the Early and Advanced Glycation end Product Modification of Albumin, RSC Adv., 5: 87660–87666 (2015).
[21] Dayanand K., HHS Public Access, Physiol. Behav., 176: 139–148 (2018).
[22] Khera P.K. et al. NIH Public Access, 90: 50–55 (2016).
[23] Sacks, D. B. Measurement of Hemoglobin A1c: A New Twist on the Path to Harmony, Diabetes Care, 35: 2674–2680 (2012).
[24] Clark S.L.D., Santin A.E., Bryant P.A., Holman R.W., Rodnick K.J., The Initial Noncovalent Binding of Glucose to Human Hemoglobin in Nonenzymatic Glycation, Glycobiology, 23: 1250–1259 (2013).
[25] Singh V.P., Bali A., Singh N., Jaggi A.S., Advanced Glycation End Products and Diabetic Complications, Korean J. Physiol. Pharmacol., 18: 1–14 (2014).
[26] Vistoli G., De Maddis D., Cipak A., Zarkovic N., Carini M., Aldini G., Advanced Glycoxidation and Lipoxidation end Products (AGEs and ALEs): An Overview of their Mechanisms of Formation, Free Radic. Res. 47, 3–27 (2013).
[27] DeLano W., Pymol: An Open-Source Molecular Graphics Tool, Newsl. Protein Crystallogr, 40: 82–92 (2002).
[28] Elbaz N.M., Khalil I.A., Abd-Rabou A.A., El-Sherbiny I.M., Chitosan-Based Nano-in-Microparticle Carriers for Enhanced Oral Delivery and Anticancer Activity of Propolis, International Journal of Biological Macromolecules, 92, Elsevier (2016).
[29] Kazemi F., Divsalar A., Saboury A.A., Structural Analysis of the Interaction Between Free, Glycated and Fructated Hemoglobin with Propolis Nanoparticles: A Spectroscopic Study, Int. J. Biol. Macromol., 109: 1329–1337 (2018).
[30] Nagababu E., Rifkind J.M., Formation of Fluorescent Heme Degradation Products During the Oxidation Of Hemoglobin by Hydrogen Peroxide, Biochem. Biophys. Res. Commun., 247: 592–596 (1998).
[31] Xie G., Timasheff S.N., Preferential Interactions of Urea with Lysozyme and their Linkage to Protein Denaturation, Biophys. Chem., 105: 421–448 (2003).
[32] Alayash A.I., Patel R.P., Cashon R.E., Abdu I.. Antioxid. Redox Signal. 3, (2001).
[33] Nagababu E., Rifkind J.M., Heme Degradation During Autoxidation of Oxyhemoglobin, Biochem. Biophys. Res. Commun., 273: 839–845 (2000).
[34] Behroozi J., Divsalar A., Saboury A.A., Honey Bee Venom Decreases the Complications of Diabetes by Preventing Hemoglobin Glycation, J. Mol. Liq., 199: 371–375 (2014).
        http://dx.doi.org/10.1016/j.molliq.2014.09.034
[35] Vardapetyan H.R., Martirosyan A.S., Tiratsuyan S.G., Hovhannisyan A.A., Interaction between Hypericin and Hemoglobin, J. Photochem. Photobiol. B Biol., 101: 53–58 (2010).
[36] Gharib R., Khatibi A., Khodarahmi R., Haidari M., Husseinzadeh S., Study of Glycation Process of Human Carbonic Anhydrase II as Well as Investigation Concerning Inhibitory Influence of 3-Beta-Hydroxybutyrate on It, Int. J. Biol. Macromol., 149: 443–449 (2020).
[37] GhoshMoulick R., Bhattacharya J., Roy S., Basak S., Dasgupta A.K., Compensatory Secondary Structure Alterations in Protein Glycation, Biochim. Biophys. Acta - Proteins Proteomics, 1774: 233–242 (2007).

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