@2024 Afarand., IRAN
ISSN: 2252-0805 The Horizon of Medical Sciences 2014;20(1):1-7
ISSN: 2252-0805 The Horizon of Medical Sciences 2014;20(1):1-7
Comparison of Bee Venom’s - and Aspirin’s Effect on Fructation of Human Hemoglobin
ARTICLE INFO
Article Type
Original ResearchAuthors
Behroozi J. (1)Divsalar A. (*)
(*) Cell & Molecular Biology Department, Biological Sciences Faculty, Kharazmi University, Tehran, Iran
(1) Cell & Molecular Biology Department, Biological Sciences Faculty, Kharazmi University, Tehran, Iran
Correspondence
Address: Cell & Molecular Biology Department, Biological Sciences Faculty, Kharazmi University, Shahid Mofatteh Street, Tehran, IranPhone: +982161113381
Fax: +982166404680
divsalar@khu.ac.ir
Article History
Received: September 29, 2013Accepted: March 6, 2014
ePublished: February 1, 2014
ABSTRACT
Aims
Fructation causes structural changes in the proteins which finally changes
or destroys the protein's function. The aim of this study was to investigate the antifructation
effect of honey bee venom and compare it with aspirin.
Materials & Methods Hemoglobin extracted from healthy and nonsmoker subjects and its concentration was determined using optical- UV spectrometry. The bovine serum albumin (BSA) was used as the standard protein. In order to evaluate the effect of honey bee venom and aspirin, hemoglobin in the presence of these two substances was also fructuated. The release of heme group from protein and the changes in hemoglobin soret band was done by optical-UV spectrometry. The amount of free amines available in hemoglobin during fructation in the presence of aspirin and honey bee venom was measured by changes in the fluorescence florscasmine emission method. To investigate the structural changes of fructated hemoglobin protein spectropolaimetry and circular bicolor spectrophotometery method were used. Data were analyzed using InStat 3 software and One-way ANOVA test.
Findings Hemoglobin incubation in the presence of fructose decreased the absorption of soret band of fructated hemoglobin compared to control. The amount of free amine in the presence of honey bee venom in of 20 and 40μg/ml had no significant difference with free amine in the presence of aspirin. Honey bee venom inhibited the change in second structure of hemoglobin dose-dependently during fructation.
Conclusion Honey bee venom has relatively similar effect with aspirin to inhibit hemoglobin fructation process.
Materials & Methods Hemoglobin extracted from healthy and nonsmoker subjects and its concentration was determined using optical- UV spectrometry. The bovine serum albumin (BSA) was used as the standard protein. In order to evaluate the effect of honey bee venom and aspirin, hemoglobin in the presence of these two substances was also fructuated. The release of heme group from protein and the changes in hemoglobin soret band was done by optical-UV spectrometry. The amount of free amines available in hemoglobin during fructation in the presence of aspirin and honey bee venom was measured by changes in the fluorescence florscasmine emission method. To investigate the structural changes of fructated hemoglobin protein spectropolaimetry and circular bicolor spectrophotometery method were used. Data were analyzed using InStat 3 software and One-way ANOVA test.
Findings Hemoglobin incubation in the presence of fructose decreased the absorption of soret band of fructated hemoglobin compared to control. The amount of free amine in the presence of honey bee venom in of 20 and 40μg/ml had no significant difference with free amine in the presence of aspirin. Honey bee venom inhibited the change in second structure of hemoglobin dose-dependently during fructation.
Conclusion Honey bee venom has relatively similar effect with aspirin to inhibit hemoglobin fructation process.
CITATION LINKS
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[13]Bathaie SZ, Jafarnejad A, Hosseinkhani S, Nakhjavani M. The effect of hot-tub therapy on serum Hsp70 level and its benefit on diabetic rats: a preliminary report. Int J Hyperthermia. 2010;26(6):577-85.
[14]Jafarnejad A, Bathaie SZ, Nakhjavani M, Hassan MZ, Banasadegh S. The improvement effect of L-Lys as a chemical chaperone on STZ-induced diabetic rats, protein structure and function. Diabetes Metab Res Rev. 2008;24(1):64-73.
[15]Jafarnejad A, Bathaie SZ, Nakhjavani M, Hassan MZ. Investigation of the mechanisms involved in the high-dose and long-term acetyl salicylic acid therapy of type I diabetic rats. J Pharmacol Exp Ther. 2008;324(2):850-7.
[16]Riggs A. Preparation of blood hemoglobins of vertebrates. Methods Enzymol. 1981;76:5-29.
[17]Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976;72(1):248-54.
[18]Schmitt A, Schmitt J, Münch G, Gasic-Milencovic J. Characterization of advanced glycation end products for biochemical studies: side chain modifications and fluorescence characteristics. Anal Biochem. 2005;338(2):201-15.
[19]Bakhti M, Moosavi-Movahedi AA, Khazaei MR. Consequential alterations in haemoglobin structure upon glycation with fructose: prevention by acetylsalicylic acid. J Biochem. 2007;141(6):827-33.
[20]Méndez JD, Xie J, Aguilar-Hernández M, Méndez-Valenzuela V. Molecular susceptibility to glycation and its implication in diabetes mellitus and related diseases. Mol Cell Biochem. 2010;344(1-2):185-93.
[21]Selvaraj N, Bobby Z, Sridhar MG. Increased glycation of hemoglobin in chronic renal failure: potential role of oxidative stress. Arch Med Res. 2008;39(3):277-84.
[22]Cussimanio BL, Booth AA, Todd P, Hudson BG, Khalifah RG. Unusual susceptibility of heme proteins to damage by glucose during non-enzymatic glycation. Biophys Chem. 2003;105(2-3):743-55.
[23]Rahbar S. The discovery of glycated hemoglobin: a major event in the study of nonenzymatic chemistry in biological systems. Ann NY Acad Sci. 2005;1043(1):9-19.
[24]Sen S, Kar M, Roy A, Chakraborti AS. Effect of nonenzymatic glycation on functional and structural properties of hemoglobin. Biophys Chem. 2005;113(3):289-98.
[25]Krautwald M, Münch G. Advanced glycation end products as biomarkers and gerontotoxins - A basis to explore methylglyoxal-lowering agents for Alzheimer's disease? Exp Gerontol. 2010;45(10):744-51.
[26]Peng X, Ma J, Chen F, Wang M. Naturally occurring inhibitors against the formation of advanced glycation end-products. Food Funct. 2011;2(6):289-301.
[27]Ansari NA, Dash D. Amadori glycated proteins: role in production of autoantibodies in diabetes mellitus and effect of inhibitors on non-enzymatic glycation. Aging Dis. 2013;4(1):50-6.
[28]Capuano E, Fedele F, Mennella C, Visciano M, Napolitano A, Lanzuise S, et al. Studies on the effect of Amadoriase from Aspergillus fumigatus on peptide and protein glycation in vitro. J Agri Food Chem. 2007;55(10):4189-95.
[29]Jomova K, Valko M. Importance of iron chelation in free radical-induced oxidative stress and human disease. Curr Pharm Des. 2011;17(31):3460-73.
[30]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(1):171.
[31]Chen J, Lariviere WR. The nociceptive and antinociceptive effects of bee venom injection and therapy: A double-edged sword. Prog Neurobiol. 2010;92(2):151-83.
[32]Li R, Zhang L, Fang Y, Han B, Lu X, Zhou T, et al. Proteome and phosphoproteome analysis of honeybee (Apis mellifera) venom collected from electrical stimulation and manual extraction of the venom gland. BMC Genomics. 2013;14(1):766-87.
[33]Hood JL, Jallouk AP, Campbell N, Ratner L, Wickline SA. Cytolytic nanoparticles attenuate HIV-1 infectivity. Antivir Ther. 2013;18(1):95-103.
[2]Ahmed N. Advanced glycation endproducts: role in pathology of diabetic complications. Diabetes Res Clin Pract. 2005;67(1):3-21.
[3]Koga M, Murai J, Saito H, Yamada Y, Mori T, Suno S, et al. Measurement of glycated hemoglobin and glycated albumin in umbilical cord: evaluation of the glycemic control indicators in neonates. J Perinatol. 2011;31(6):430-3.
[4]Nawale RB, Mourya VK, Bhise SB. Non-enzymatic glycation of proteins: a cause for complications in diabetes. Indian J Biochem Biophys. 2006;43(6):337-44.
[5]Daroux M, Prevost G, Maillard-Lefebvre H, Gaxatte C, D'Agati VD, Schmidt AM, et al. Advanced glycation end-products: implications for diabetic and non-diabetic nephropathies. Diabetes Metab. 2010;36(1):1-10.
[6]Takeuchi M, Iwaki M, Takino J, Shirai H, Kawakami M, Bucala R, et al. Immunological detection of fructose-derived advanced glycation end-products. Lab Invest. 2010;90(7):1117-27.
[7]Birmann BM, Giovannucci EL, Rosner BA, Colditz GA. Regular aspirin use and risk of multiple myeloma: a prospective analysis in the health professionals follow-up study and nurses' health study. Cancer Prev Res. 2014;7(1):33-41.
[8]Fitzgerald R, Pirmohamed M. Aspirin resistance: effect of clinical, biochemical and genetic factors. Pharmacol Ther. 2011;130(2):213-25.
[9]Tehrani S, Antovic A, Mobarrez F, Mageed K, Lins PE, Adamson U, et al. High-dose aspirin is required to influence plasma fibrin network structure in patients with type 1 diabetes. Diabetes Care. 2012;35(2):404-8.
[10]Harding JJ, Ganea E. Protection against glycation and similar post-translational modifications of proteins. Biochim Biophys Acta. 2006;1764(9):1436-46.
[11]Jang MH, Shin MC, Lim S, Han SM, Park HJ, Shin L, et al. Bee venom induces apoptosis and inhibits expression of cyclooxygenase-2 mRNA in human lung cancer cell line NCI-H1299. J Pharmacal Sci. 2003;91(2):95-104.
[12]Son DJ , Lee YH, Song SH, Lee CK, Hong JT. Therapeutic application of anti- arthritis, pain-releasing and anti-cancer effects of bee venom and its constituent compounds. Pharmacol Ther. 2007;115(2):246-70.
[13]Bathaie SZ, Jafarnejad A, Hosseinkhani S, Nakhjavani M. The effect of hot-tub therapy on serum Hsp70 level and its benefit on diabetic rats: a preliminary report. Int J Hyperthermia. 2010;26(6):577-85.
[14]Jafarnejad A, Bathaie SZ, Nakhjavani M, Hassan MZ, Banasadegh S. The improvement effect of L-Lys as a chemical chaperone on STZ-induced diabetic rats, protein structure and function. Diabetes Metab Res Rev. 2008;24(1):64-73.
[15]Jafarnejad A, Bathaie SZ, Nakhjavani M, Hassan MZ. Investigation of the mechanisms involved in the high-dose and long-term acetyl salicylic acid therapy of type I diabetic rats. J Pharmacol Exp Ther. 2008;324(2):850-7.
[16]Riggs A. Preparation of blood hemoglobins of vertebrates. Methods Enzymol. 1981;76:5-29.
[17]Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976;72(1):248-54.
[18]Schmitt A, Schmitt J, Münch G, Gasic-Milencovic J. Characterization of advanced glycation end products for biochemical studies: side chain modifications and fluorescence characteristics. Anal Biochem. 2005;338(2):201-15.
[19]Bakhti M, Moosavi-Movahedi AA, Khazaei MR. Consequential alterations in haemoglobin structure upon glycation with fructose: prevention by acetylsalicylic acid. J Biochem. 2007;141(6):827-33.
[20]Méndez JD, Xie J, Aguilar-Hernández M, Méndez-Valenzuela V. Molecular susceptibility to glycation and its implication in diabetes mellitus and related diseases. Mol Cell Biochem. 2010;344(1-2):185-93.
[21]Selvaraj N, Bobby Z, Sridhar MG. Increased glycation of hemoglobin in chronic renal failure: potential role of oxidative stress. Arch Med Res. 2008;39(3):277-84.
[22]Cussimanio BL, Booth AA, Todd P, Hudson BG, Khalifah RG. Unusual susceptibility of heme proteins to damage by glucose during non-enzymatic glycation. Biophys Chem. 2003;105(2-3):743-55.
[23]Rahbar S. The discovery of glycated hemoglobin: a major event in the study of nonenzymatic chemistry in biological systems. Ann NY Acad Sci. 2005;1043(1):9-19.
[24]Sen S, Kar M, Roy A, Chakraborti AS. Effect of nonenzymatic glycation on functional and structural properties of hemoglobin. Biophys Chem. 2005;113(3):289-98.
[25]Krautwald M, Münch G. Advanced glycation end products as biomarkers and gerontotoxins - A basis to explore methylglyoxal-lowering agents for Alzheimer's disease? Exp Gerontol. 2010;45(10):744-51.
[26]Peng X, Ma J, Chen F, Wang M. Naturally occurring inhibitors against the formation of advanced glycation end-products. Food Funct. 2011;2(6):289-301.
[27]Ansari NA, Dash D. Amadori glycated proteins: role in production of autoantibodies in diabetes mellitus and effect of inhibitors on non-enzymatic glycation. Aging Dis. 2013;4(1):50-6.
[28]Capuano E, Fedele F, Mennella C, Visciano M, Napolitano A, Lanzuise S, et al. Studies on the effect of Amadoriase from Aspergillus fumigatus on peptide and protein glycation in vitro. J Agri Food Chem. 2007;55(10):4189-95.
[29]Jomova K, Valko M. Importance of iron chelation in free radical-induced oxidative stress and human disease. Curr Pharm Des. 2011;17(31):3460-73.
[30]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(1):171.
[31]Chen J, Lariviere WR. The nociceptive and antinociceptive effects of bee venom injection and therapy: A double-edged sword. Prog Neurobiol. 2010;92(2):151-83.
[32]Li R, Zhang L, Fang Y, Han B, Lu X, Zhou T, et al. Proteome and phosphoproteome analysis of honeybee (Apis mellifera) venom collected from electrical stimulation and manual extraction of the venom gland. BMC Genomics. 2013;14(1):766-87.
[33]Hood JL, Jallouk AP, Campbell N, Ratner L, Wickline SA. Cytolytic nanoparticles attenuate HIV-1 infectivity. Antivir Ther. 2013;18(1):95-103.