Presence of circulatory autoantibodies against glycated histones in diabetic patient in Saudi Arabia

Authors

  • Daheeya Alenazi Department of Clinical Laboratory Science, College of Applied Medical Science, King Saud University, Riyadh, Saudi Arabia
  • Sadia Arjumand Department of Clinical Laboratory Science, College of Applied Medical Science, King Saud University, Riyadh, Saudi Arabia
  • Sana Alqarni Department of Clinical Laboratory Science, College of Applied Medical Science, King Saud University, Riyadh, Saudi Arabia
  • Ali Aljohi Central Military Laboratory and Blood Bank Department, Prince Sultan Military Medical City, Riyadh, Saudi Arabia
  • Manal Abudawood Department of Clinical Laboratory Science, College of Applied Medical Science, King Saud University, Riyadh, Saudi Arabia
  • Majed Alanazi Department of Public Health, General Directorate of Health Affairs, Ministry of Health, Riyadh, Saudi Arabia
  • Khalid Alanazi Department of Public Health, General Directorate of Health Affairs, Ministry of Health, Riyadh, Saudi Arabia
  • Shibli Sayeed Department of Public Health, General Directorate of Health Affairs, Ministry of Health, Riyadh, Saudi Arabia
  • Aminah Alzailai Department of Clinical Laboratory Science, College of Applied Medical Science, King Saud University, Riyadh, Saudi Arabia
  • Meyad Alkarni Department of Clinical Laboratory Science, College of Applied Medical Science, King Saud University, Riyadh, Saudi Arabia

DOI:

https://doi.org/10.18203/2394-6040.ijcmph20233548

Keywords:

Diabetes mellitus, Hyperglycemia, Glycated histones, Advanced glycation end products, Circulating autoantibodies, Enzyme-linked immunosorbent assay

Abstract

Background: Advanced glycation end products (AGEs) in diabetic patients can trigger several autoimmune responses. This article aims to assess the presence of circulating autoantibodies against glycated histones and their role in complications in diabetic patients in the Saudi population.

Methods: A total of one hundred twenty samples were collected from diabetic patients with different age groups and healthy individuals as control. All serum samples were collected from Prince Sultan Military Medical City (PSMMC) in Riyadh City in Saudi Arabia. Glycated H2A was prepared and characterized using different physiochemical techniques. Then, ELISA was performed to assess the presence of circulating autoantibodies against glycated histones in diabetic patients’ samples compared with control healthy individuals in the Saudi population.

Results: The glycation of H2A under our experimental conditions appears to be completed in 14 days. also, our data showed high circulating autoantibodies were detected against glycated H2A in all diabetic patients’ plasma with different dilutions. Remarkably, diabetic patients’ group 1 (under 20 years old group) showed highly significant binding activity values in each dilution. However, diabetic patients in groups 2 and 3 showed less binding but still significant values when compared to control healthy individuals.

Conclusions: This finding provides novel perspectives into existing of circulating autoantibodies against glycated histones in diabetes patients in Saudi Arabia. Therefore, these circulating autoantibodies might be used as valuable tools for understanding the glycation mechanisms in diabetic patients in addition to providing diagnostic and prognostic knowledge. However, their roles in diabetic complications need further investigation.

References

Adamska O, Stolarczyk A, Gondek A, Maciąg B, Świderek J, Czuchaj P, et al. Ligament Alteration in Diabetes Mellitus. J Clin Med. 2022;11(19):5719.

World Health Organization. Diabetes. Available at: https://www.who.int/news-room/fact-sheets/detail/ diabetes. Accessed on 02 August 2023.

Alkhaldi G, Aljohani N, Hussain SD, Alfawaz HA, Hameidi A, Saadawy GM, et al. General Public’s Knowledge of Diabetes and Physical Activity in Saudi Arabia over Time: The Need to Refresh Awareness Campaigns. Healthcare (Switzerland). 2023;11(3).

Marcovecchio ML. Complications of acute and chronic hyperglycemia. US Endocrinology. Touch Briefings. 2017;13:17-21.

Brownlee M. The Pathobiology of Diabetic Complications a Unifying Mechanism. Banting Lecture 2004. Diabetes. 2005;54:1615-25.

Forbes JM, Cooper ME. Mechanisms of Diabetic Complications. Physiol Rev. 2013;93:137-88.

Campos C. Chronic Hyperglycemia and Glucose Toxicity: Pathology and Clinical Sequelae. Postgrad Med. 2012;124(6):90-7.

Ahmed N. Advanced glycation end products—role in pathology of diabetic complications. Diabetes Res Clin Pract. 2005;67(1):3-21.

Negre-Salvayre A, Salvayre R, Augé N, Pamplona R, Portero-Otín M. Hyperglycemia and glycation in diabetic complications. Antioxid Redox Signal. 2009;11(12):3071-109.

Nishikawa T, Edelstein D, Brownlee M. The missing link: a single unifying mechanism for diabetic complications. Kidney Int Suppl. 2000;77:S26-30.

Singh R, Barden A, Mori T, Beilin L. Advanced glycation end-products: a review. Diabetologia. 2001;44(2):129-46.

Qais FA, Sarwar T, Ahmad I, Khan RA, Shahzad SA, Husain FM. Glyburide inhibits non-enzymatic glycation of HSA: An approach for the management of AGEs associated diabetic complications. Int J Biol Macromol. 2021;169:143-52.

Garay-Sevilla ME, Regalado JC, Malacara JM, Nava LE, Wrobel-Zasada K, Castro-Rivas A, et al. Advanced glycosylation end products in skin, serum, saliva and urine and its association with complications of patients with type 2 diabetes mellitus. J Endocrinol Invest. 2005;28(5):223-30.

Ashraf JM, Ahmad S, Rabbani G, Hasan Q, Jan AT, Lee EJ, et al. 3-Deoxyglucosone: A potential glycating agent accountable for structural alteration in H3 histone protein through generation of different AGEs. PLoS One. 2015;10(2).

Brownlee M. Biochemistry and molecular cell biology of diabetic complications. Nature. 2001;414(6865):813.

Lapolla A, Traldi P, Fedele D. Importance of measuring products of non-enzymatic glycation of proteins. Clin Biochem. 2005;38(2):103-15.

Suzuki D, Miyata T, Saotome N, Horie K, Inagi R, Yasuda Y, et al. Immunohistochemical Evidence for an Increased Oxidative Stress and Carbonyl Modification of Proteins in Diabetic Glomerular Lesions. J Am Soc Nephrol. 1999;10(4):822.

Yatscoff RW, Tevaarwerk GJ, MacDonald JC. Quantification of nonenzymically glycated albumin and total serum protein by affinity chromatography. Clin Chem. 1984;30(3):446.

Frye EB, Degenhardt TP, Thorpe SR, Baynes JW. Role of the Maillard reaction in aging of tissue proteins: advanced glycation end product-dependent increase in imidazolium cross-links in human lens proteins. J Biol Chem. 1998;273(30):18714-9.

Choudhary D, Chandra D, Kale RK. Influence of methylglyoxal on antioxidant enzymes and oxidative damage. Toxicol Lett. 1997;93(2):141-52.

Festa A, Schmölzer B, Schernthaner G, Menzel EJ. Differential expression of receptors for advanced glycation end products on monocytes in patients with IDDM. Diabetologia. 1998;41(6):674-80.

Wolffe A. Chromatin. Structure and Function. San Diego: Academic Press. 1998.

Gugliucci A, Bendayan M. Histones from diabetic rats contain increased levels of advanced glycation end products. Biochem Biophys Res Commun. 1995;212(1):56-62.

Turk Z, Ljubic S, Turk N, Benko B. Detection of autoantibodies against advanced glycation endproducts and AGE-immune complexes in serum of patients with diabetes mellitus. Clinica Chimica Acta. 2001;303(1-2):105-15.

Makino H, Shikata K, Hironaka K, Kushiro M, Yamasaki Y, Sugimoto H, et al. Ultrastructure of nonenzymatically glycated mesangial matrix in diabetic nephropathy. Kidney Int. 1995;48(2):517-26.

Ansari NA, Moinuddin, Alam K, Ali A. Preferential recognition of Amadori-rich lysine residues by serum antibodies in diabetes mellitus: Role of protein glycation in the disease process. Hum Immunol. 2009;70(6):417-24.

Thornalley PJ, Langborg A, Minhas HS. Formation of glyoxal, methylglyoxal and 3-deoxyglucosone in the glycation of proteins by glucose. Biochem J. 1999;344(1):109.

Singh VP, Bali A, Singh N, Jaggi AS. Advanced glycation end products and diabetic complications. Korean J Physiol Pharmacol. 2014;18(1):1-14.

Gugliucci A. Advanced Glycation of Rat Liver Histone Octamers: An in Vitro Study. Biochem Biophys Res Commun. 1994;203(1):588-93.

Jobst K, Lakatos A. The liver cell histones of diabetic patients contain glycation endproducts (AGEs) which may be lipofuscin components. Clin Chim Acta. 1996;256(2):203-4.

Rahim M, Iram S, Khan MS, Khan MS, Shukla AR, Srivastava AK, et al. Glycation-assisted synthesized gold nanoparticles inhibit growth of bone cancer cells. Colloids Surf B Biointerfaces. 2014;117:473-9.

Ahmad S, Shahab U, Baig MH, Khan MS, Khan MS, Srivastava AK, et al. Inhibitory effect of metformin and pyridoxamine in the formation of early, intermediate and advanced glycation end-products. PLoS One. 2013;8(9):e72128.

Monnier VM. Nonenzymatic glycosylation, the Maillard reaction and the aging process. J Gerontol. 1990;45(4):B105-11.

Viviani GL, Puddu A, Sacchi G, Garuti A, Storace D, Durante A, et al. Glycated fetal calf serum affects the viability of an insulin-secreting cell line in vitro. Metabolism. 2008;57(2):163-9.

Bucciantini M, Giannoni E, Chiti F, Baroni F, Formigli L, Zurdo J, et al. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature. 2002;416(6880):507.

Grandhee SK, Monnier VM. Mechanism of formation of the Maillard protein cross-link pentosidine. Glucose, fructose, and ascorbate as pentosidine precursors. J Biol Chem. 1991;266(18):11649-53.

Kessel L, Kalinin S, Nagaraj RH, Larsen M, Johansson LB. Time‐resolved and Steady‐state Fluorescence Spectroscopic Studies of the Human Lens with Comparison to Argpyrimidine, Pentosidine and 3‐OH‐kynurenine. Photochem Photobiol. 2002;76(5):549-54.

A Siddiqui A, Sohail A, A Bhat S, Rehman T, Bano B. Non-enzymatic glycation of almond cystatin leads to conformational changes and altered activity. Protein Pept Lett. 2015;22(5):449-59.

Ansari NA, Dash D. Biochemical studies on methylglyoxal-mediated glycated histones: Implications for presence of serum antibodies against the glycated histones in patients with type 1 diabetes mellitus. ISRN Biochem. 2013;198065.

Ashraf JM, Abdullah SMS, Ahmad S, Fatma S, Baig MH, Iqbal J, et al. Prevalence of autoantibodies against 3-DG-glycated H2A protein in type 2 diabetes. Biochemistry (Moscow). 2017;82(5):579-86.

Reddy S, Bichler J, Wells-Knecht KJ, Thorpe SR, Baynes JW. N epsilon-(carboxymethyl) lysine is a dominant advanced glycation end product (AGE) antigen in tissue proteins. Biochemistry. 1995;34(34):10872-8.

Arasteh A, Farahi S, Habibi-Rezaei M, Moosavi-Movahedi AA. Glycated albumin: an overview of the in vitro models of an in vivo potential disease marker. J Diabetes Metab Disord. 2014;13(1):49.

Downloads

Published

2023-11-16

How to Cite

Alenazi, D., Arjumand, S., Alqarni, S., Aljohi, A., Abudawood, M., Alanazi, M., Alanazi, K., Sayeed, S., Alzailai, A., & Alkarni, M. (2023). Presence of circulatory autoantibodies against glycated histones in diabetic patient in Saudi Arabia. International Journal Of Community Medicine And Public Health, 10(12), 4527–4534. https://doi.org/10.18203/2394-6040.ijcmph20233548

Issue

Section

Original Research Articles