Browse > Article
http://dx.doi.org/10.5713/ajas.19.0854

Evaluation of antioxidant property of heat shock protein 90 from duck muscle  

Zhang, Muhan (Key Lab of Meat Processing and Quality Control, Ministry of Education, Nanjing Agricultural University)
Wang, Daoying (Institute of Agricultural Products Processing, Jiangsu Academy of Agricultural Sciences)
Xu, Xinglian (Key Lab of Meat Processing and Quality Control, Ministry of Education, Nanjing Agricultural University)
Xu, Weimin (Institute of Agricultural Products Processing, Jiangsu Academy of Agricultural Sciences)
Publication Information
Animal Bioscience / v.34, no.4, 2021 , pp. 724-733 More about this Journal
Abstract
Objective: The objectives of this study were to investigate the direct antioxidative effect of 90 Kda heat shock protein (Hsp90) obtained from duck muscle. Methods: The interaction of Hsp90 with phospholipids and oxidized phospholipids was studied with surface plasmon resonance (SPR), and their further oxidation in the presence of Hsp90 was evaluated with thiobarbituric acid reactive substances (TBARS) assay. The scavenging effect on the 1,1-diphenyl-2-picrylhydrazyl (DPPH) and 2,2'-azinobis (3-ethylbenzthiazoline-6-sulfonic acid (ABTS) was measured, and the electron paramagnetic resonance (EPR) spectroscopy in combination with 5-tert-Butoxycarbonyl-5-methyl-1-pyrroline-N-oxide and 2-phenyl-4,4,5,5,-tetramethylimidazoline-1-oxyl-3-oxide (PTIO) was utilized to determine the abilities of Hsp90 in scavenging hydroxyl and PTIO radicals. Results: SPR showed Hsp90 could bind with both phospholipids and oxidized phospholipids, and prevent their further oxidation by the TBARS assay. The DPPH and ABTS scavenging activity increased with Hsp90 concentration, and could reach 27% and 20% respectively at the protein concentration of 50 μM. The EPR spectra demonstrated Hsp90 could directly scavenge ·OH and PTIO· radicals. Conclusion: This suggests that Hsp90, a natural antioxidant in meat, may play an important role in cellular defense against oxidative stress, and may have potential use in meat products.
Keywords
90 Kda heat shock protein (Hsp90); Oxidized Phospholipids; Radical; Electron Paramagnetic Resonance (EPR);
Citations & Related Records
연도 인용수 순위
  • Reference
1 Liu R, Xing L, Fu Q, Zhou G, Zhang W. A review of antioxidant peptides derived from meat muscle and by-products. Antioxidants 2016;5:32. https://doi.org/10.3390/antiox5030032   DOI
2 Gueraud F, Atalay M, Bresgen N, et al. Chemistry and biochemistry of lipid peroxidation products. Free Radic Res 2010;44:1098-124. https://doi.org/10.3109/10715762.2010.498477   DOI
3 Fruhwirth GO, Moumtzi A, Loidl A, Ingolic E, Hermetter A. The oxidized phospholipids POVPC and PGPC inhibit growth and induce apoptosis in vascular smooth muscle cells. Biochim Biophys Acta Mol Cell Biol Lipids 2006;1761:1060-9. https://doi.org/10.1016/j.bbalip.2006.06.001   DOI
4 Wang Z, He Z, Emara AM, Gan X, Li H. Effects of malondialdehyde as a byproduct of lipid oxidation on protein oxidation in rabbit meat. Food Chem 2019;288:405-12. https://doi.org/10.1016/j.foodchem.2019.02.126   DOI
5 Pratt WB. The HSP90-based chaperone system: involvement in signal transduction from a variety of hormone and growth factor receptors. Exp Biol Med 1998;217:420-34. https://doi.org/10.3181/00379727-217-44252   DOI
6 Padmini E, Rani MU. Heat-shock protein 90 alpha (HSP90α) modulates signaling pathways towards tolerance of oxidative stress and enhanced survival of hepatocytes of Mugil cephalus. Cell Stress Chaperones 2011;16:411-25. https://doi.org/10.1007/s12192-011-0255-9   DOI
7 Leung AM, Redlak MJ, Miller TA. Role of heat shock proteins in oxygen radical-induced gastric apoptosis. J Surg Res 2015;193:135-44. https://doi.org/10.1016/j.jss.2014.07.013   DOI
8 Kovar J, Stybrova H, Novak P, et al. Heat shock protein 90 recognized as an iron-binding protein associated with the plasma membrane of HeLa cells. Cell Physiol Biochem 2004;14:41-6. https://doi.org/10.1159/000076925   DOI
9 Zhang M, Wang D, Geng Z, Li P, Sun Z, Xu W. Effect of heat shock protein 90 against ROS-induced phospholipid oxidation. Food Chem 2018;240:642-7. https://doi.org/10.1016/j.foodchem.2017.08.005   DOI
10 Serbulea V, DeWeese D, Leitinger N. The effect of oxidized phospholipids on phenotypic polarization and function of macrophages. Free Radic Biol Med 2017;111:156-68. https://doi.org/10.1016/j.freeradbiomed.2017.02.035   DOI
11 Jiang B, Liang P, Deng G, Tu Z, Liu M, Xiao X. Increased stability of bcl-2 in hsp70-mediated protection against apoptosis induced by oxidative stress. Cell Stress Chaperones 2011;16:143-52. https://doi.org/10.1007/s12192-010-0226-6   DOI
12 Schneider C, Tallman KA, Porter NA, Brash AR. Two distinct pathways of formation of 4-hydroxynonenal. Mechanisms of nonenzymatic transformation of the 9- and 13-hydro-peroxides of linoleic acid to 4-hydroxyalkenals. J Biol Chem 2001;276:20831-8. https://doi.org/10.1074/jbc.M101821200   DOI
13 Hayashi T, Uchida K, Takebe G, Takahashi K. Rapid formation of 4-hydroxy-2-nonenal, malondialdehyde, and phosphatidylcholine aldehyde from phospholipid hydroperoxide by hemoproteins. Free Radic Biol Med 2004;36:1025-33. https://doi.org/10.1016/j.freeradbiomed.2004.01.006   DOI
14 Escobedo J, Pucci AM, Koh TJ. Hsp25 protects skeletal muscle cells against oxidative stress. Free Radic Biol Med 2004;37:1455-62. https://doi.org/10.1016/j.freeradbiomed.2004.07.024   DOI
15 Welker S, Rudolph B, Frenzel E, et al. Hsp12 is an intrinsically unstructured stress protein that folds upon membrane association and modulates membrane function. Mol Cell 2010;39:507-20. https://doi.org/10.1016/j.molcel.2010.08.001   DOI
16 Herbertsson H, Kuhme T, Evertsson U, Wigren J, Hammarstrom S. Identification of subunits of the 650 kda 12(s)-hete binding complex in carcinoma cells. J Lipid Res 1998;39:237-44.   DOI
17 Nankar SA, Pande AH. Properties of apolipoprotein E derived peptide modulate their lipid-binding capacity and influence their anti-inflammatory function. Biochim Biophys Acta Mol Cell Biol Lipids 2014;1841:620-9. https://doi.org/10.1016/j.bbalip.2014.01.006   DOI
18 Herbertsson H, Kuhme T, Hammarstrom S. The 650-kda 12(s)-hydroxyeicosatetraenoic acid binding complex: occurrence in human platelets, identification of hsp90 as a constituent, and binding properties of its 50-kda subunit. Arch Biochem Biophys 1999;367:33-8. https://doi.org/10.1006/abbi.1999.1233   DOI
19 Zhang M, Wang D, Li P, et al. Interaction of hsp90 with phospholipid model membranes. Biochim Biophys Acta Biomembr 2018;1860:611-6. https://doi.org/10.1016/j.bbamem.2017.11.011   DOI
20 Rouhanizadeh M, Hwang J, Clempus RE, et al. Oxidized-1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphorylcholine induces vascular endothelial superoxide production: implication of NADPH oxidase. Free Radic Biol Med 2005;39: 1512-22. https://doi.org/10.1016/j.freeradbiomed.2005.07.013   DOI
21 Aviram M, Hardak E, Vaya J, et al. Human serum paraoxonases (PON1) Q and R selectively decrease lipid peroxides in human coronary and carotid atherosclerotic lesions: PON1 esterase and peroxidase-like activities. Circulation 2000;101:2510-7. https://doi.org/10.1161/01.cir.101.21.2510   DOI
22 Prior RL, Wu X, Schaich K. Standardized methods for the determination of antioxidant capacity and phenolics in foods and dietary supplements. J Agric Food Chem 2005;53:4290-302. https://doi.org/10.1021/jf0502698   DOI
23 Cano A, Acosta M, Arnaro MB. A method to measure antioxidant activity in organic media: application to lipophilic vitamins. Redox Rep 2000;5:365-70. https://doi.org/10.1179/135100000101535933   DOI
24 Liu J, Li X, Lin J, et al. Sarcandra glabra (Caoshanhu) protects mesenchymal stem cells from oxidative stress: a bioevaluation and mechanistic chemistry. BMC Complement Altern Med 2016;16:423. https://doi.org/10.1186/s12906-016-1383-7   DOI
25 Li X. 2-Phenyl-4,4,5,5-tetramethylimidazoline-1-oxyl 3-oxide (PTIO•) radical scavenging: a new and simple antioxidant assay in vitro. J Agric Food Chem 2017;65:6288-97. https://doi.org/10.1021/acs.jafc.7b02247   DOI
26 Bolumar T, Andersen ML, Orlien V. Mechanisms of radical formation in beef and chicken meat during high pressure processing evaluated by electron spin resonance detection and the addition of antioxidants. Food Chem 2014;150:422-8. https://doi.org/10.1016/j.foodchem.2013.10.161   DOI
27 Fadda A, Barberis A, Sanna D. Influence of pH, buffers and role of quinolinic acid, a novel iron chelating agent, in the determination of hydroxyl radical scavenging activity of plant extracts by electron paramagnetic resonance (EPR). Food Chem 2018;240:174-82. https://doi.org/10.1016/j.foodchem.2017.07.076   DOI
28 Salgado P, Melin V, Contreras D, Moreno Y, Mansilla HD. Fenton reaction driven by iron ligands. J Chil Chem Soc 2013;58:2096-101. https://doi.org/10.4067/S0717-97072013000400043   DOI