Journal of Veterinary Clinics (한국임상수의학회지)

The Korean Society of Veterinary Clinics (한국임상수의학회)
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Streptozotocin-Induced Pro-Inflammatory Response in Rat Blood and its Attenuation by External Albumin Administration

  • Bae, Chun-Sik (College of Veterinary Medicine, Chonnam National University) ;
  • Lee, Chang-Min (College of Veterinary Medicine, Chonnam National University) ;
  • Kim, Dong-il (College of Veterinary Medicine, Chonnam National University) ;
  • Ahn, Taeho (College of Veterinary Medicine, Chonnam National University)
  • Received : 2019.03.21
  • Accepted : 2019.06.13
  • Published : 2019.06.30
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Abstract

Previous report has suggested that the albumin levels were reduced in the peripheral blood mononuclear cells (PBMCs) and consequently oxidative stress was elevated in streptozotocin (STZ)-induced diabetic rats as albumin is the predominant antioxidant in plasma. In this study, we suggest that the levels of pro-inflammatory cytokine such as interleukin-6 (IL-6) and tumor necrosis factor-${\alpha}$ ($TNF-{\alpha}$) were increased by approximately 3.4- and 2.9-fold, respectively, in the serum of STZ-diabetic rats, compared to those of normal rat. In addition to the cytokines, the levels of C-reactive protein (CRP) were also about 3.6-fold higher, indicating that STZ induced a pro-inflammatory response in rat blood. However, when purified rat albumin was externally co-administrated with STZ through the tail vein, the serum levels of IL-6, $TNF-{\alpha}$, and CRP were markedly reduced, although the values were still higher than those of normal (non-diabetic) rats. Albumin administration also decreased STZ-induced oxidative stress in serum and PBMCs. Moreover, the decrease in cytokine and CRP levels was dependent on the dose of injected albumin. These results suggest that STZ-induced pro-inflammation and oxidative stress in rat blood might be attenuated by treatment with exogenous albumin.

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References

  1. Ansar W, Ghosh S. C-reactive protein and the biology of disease. Immunol Res 2013; 56: 131-142. https://doi.org/10.1007/s12026-013-8384-0
  2. Bathina S, Srinivas N, Das UN. Streptozotocin produces oxidative stress, inflammation and decreases BDNF concentrations to induce apoptosis of RIN5F cells and type 2 diabetes mellitus in Wistar rats. Biochem Biophys Res Commun 2017; 486: 406-413. https://doi.org/10.1016/j.bbrc.2017.03.054
  3. Bourdon E, Blache D. The importance of proteins in defense against oxidation. Antioxid. Redox Signal 2001; 3: 293-311. https://doi.org/10.1089/152308601300185241
  4. Chan LL, Laverty DJ, Smith T, Nejad P, Hei H, Gandhi R, Kuksin D, Qiu J. Accurate measurement of peripheral blood mononuclear cell concentration using image cytometry to eliminate RBC-induced counting error. J Immunol Methods 2013; 388: 25-32. https://doi.org/10.1016/j.jim.2012.11.010
  5. Desco MC, Asensi M, Marquez R, Martinez-Valls J, Vento M, Pallardo FV, Sastre J, Vina J. Xanthine oxidase is involved in free radical production in type 1 diabetes: protection by allopurinol. Diabetes 2002; 51: 1118-1124. https://doi.org/10.2337/diabetes.51.4.1118
  6. Du Clos TW, Mold C. C-reactive protein: an activator of innate immunity and a modulator of adaptive immunity. Immunol Res 2004; 30: 261-277. https://doi.org/10.1385/IR:30:3:261
  7. Dziarski R. Cell-bound albumin is the 70-kDa peptidoglycan-, lipopolysaccharide-, and lipoteichoic acid-binding protein on lymphocytes and macrophages. J Biol Chem 1994; 269: 20431-20436. https://doi.org/10.1016/S0021-9258(17)32010-0
  8. Eleazu CO, Eleazu KC, Chukwuma S, Essien UN. Review of the mechanism of cell death resulting from streptozotocin challenge in experimental animals, its practical use and potential risk to humans. J Diabetes Metab Disord 2013; 12: 60. https://doi.org/10.1186/2251-6581-12-60
  9. Low PA, Nickander KK, Tritschler HJ. The roles of oxidative stress and antioxidant treatment in experimental diabetic neuropathy. Diabetes 1997; 46 (Suppl. 2): S38-S42. https://doi.org/10.2337/diab.46.2.S38
  10. Medzhitov R. Origin and physiological roles of inflammation. Nature 2008; 454: 429-435. https://doi.org/10.1038/nature07201
  11. Nathan C. Neutrophils and immunity: challenges and opportunities. Nature Rev Immunol 2006; 6: 173-182. https://doi.org/10.1038/nri1785
  12. Nicholson JP, Wolmarans MR, Park GR. The role of albumin in critical illness. Br J Anaesth 2000; 85: 599-610. https://doi.org/10.1093/bja/85.4.599
  13. Niu S, Bian Z, Tremblay A, Luo Y, Kidder K, Mansour A, Zen K, Liu Y. Broad infiltration of macrophages leads to a proinflammatory state in streptozotocin-induced hyperglycemic mice. J Immunol 2016; 197: 3293-3301. https://doi.org/10.4049/jimmunol.1502494
  14. Ohkawa H, Ohishi N, Yagi K. Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction. Anal Biochem 1979; 95: 351-358. https://doi.org/10.1016/0003-2697(79)90738-3
  15. Park KT, Yun CH, Bae CS, Ahn T. Decreased level of albumin in peripheral blood mononuclear cells of streptozotocininduced diabetic rats. J Vet Med Sci 2014; 76: 1087-1092. https://doi.org/10.1292/jvms.13-0631
  16. Rasheed Z, Ali R. Reactive oxygen species damaged human serum albumin in patients with type 1 diabetes mellitus: biochemical and immunological studies. Life Sci 2006; 79: 2320-2328. https://doi.org/10.1016/j.lfs.2006.07.041
  17. Roche M, Rondeau P, Singh NR, Tarnus E, Bourdon E. The antioxidant properties of serum albumin. FEBS Lett 2008; 582: 1783-1787. https://doi.org/10.1016/j.febslet.2008.04.057
  18. Ryter SW, Kim HP, Hoetzel A, Park JW, Nakahira K, Wang X, Choi AM. Mechanisms of cell death in oxidative stress. Antioxid Redox Signal 2007; 9: 49-89. https://doi.org/10.1089/ars.2007.9.49
  19. Seidkhani-Nahal A, Allameh A, Soleimani M. Antioxidant and reactive oxygen species scavenging properties of cellular albumin in HepG2 cells is mediated by the glutathione redox system. Biotechnol Appl Biochem 2019; 66: 163-171. https://doi.org/10.1002/bab.1708
  20. Sproston NR, Ashworth JJ. Role of C-reactive protein at sites of inflammation and infection. Front Immunol 2018; 9: 754. https://doi.org/10.3389/fimmu.2018.00754
  21. Xiao TS. Innate immunity and inflammation. Cell Mol Immunol 2017; 14: 1-3. https://doi.org/10.1038/cmi.2016.45
  22. Yang Y, Cao J, Shi Y. Identification and characterization of a gene encoding human LPGAT1, an endoplasmic reticulumassociated lysophosphatidylglycerol acyltransferase. J Biol Chem 2004; 279: 55866-55874. https://doi.org/10.1074/jbc.M406710200