Study of serum heat shock protein-27, adenosine deaminase, homocysteine and lipid profiles in bovine leptospirosis in Kurdistan province
Subject Areas :
Veterinary Clinical Pathology
kave azimzade
1
1 - استادیار گروه علوم درمانگاهی، واحد اورمیه، دانشگاه آزاد اسلامی، اورمیه، ایران.
Received: 2015-08-30
Accepted : 2015-10-19
Published : 2015-08-23
Keywords:
Biochemical parameters,
Kurdistan province,
Cattle leptospirosis,
Abstract :
The aim of this study was to investigate changes of serum parameters such as adenosine deaminase (ADA), heat shock protein-27 (HSP-27), homocysteine (Hcy) and lipid profiles (LDL,HDL,VLDL and Triglyceride) in bovine leptospirosis. After diagnosis of acute leptospirosis in cattle, blood samples were collected from 12 cases of bovine leptospirosis and 12 healthy samples via jugular vein and all parameters along with zinc (Zn2+) were measured. The results denoted a significant increase in Hcy, HSP-27, TG, VLDL, along with a significant decrease in HDL-C, ADA, LDL-C and zinc (Zn2+) in patients compared to healthy ones (p≤0.01). Based on the results, the listed parameters may be used in the management of bovine leptospirosis.
References:
رامین، ع.، عبداله پور، غ.، عزیززاد ،ف.، قهرمانی، پ.، مسعودی، ا. و رامین، س. (1392). جستجوی پادتنهای ضد لپتوسپیرا در سرم خون گاو و گوسفندان ارومیه. مجله دامپزشکی ایران، دوره نهم، شماره 3، صفحات: 62-54.
حسن پور، ع.، فرتاشوند، م.، عبدالهپور، غ.، غلامعلی، م.، نادعلیان، م.ق. و ستاری، س. (1386). تعیین میزان شیوع سرولوژیک آلودگی به لپتوسپیرا در گاوداریهای شیری اطراف تبریز. مجله پژوهش وسازندگی در امور دام و آبزیان، شماره 74، صفحات: 77-67.
Adamu, S., Ige, A.A., Jatau, I.D., Neils, J.S., Useh, N.M., Bisalla, M., et al. (2008). Changes in the serum profiles of lipids and cholesterol in sheep experimental model of acute African trypanosomiasis. African Journal of Biotechnology, 7(12): 2090-2098
Arrigo, A. and Landry, J. (1994). Expression and function of the low-molecular-weight heat shock proteins. In: The biology of heat shock proteins and molecular chaperones. Moriomto, R.I. and Georgopoulos, A.T. editors. Cold Spring Harbor Laboratory Press, Plainville, N.Y, pp: 335- 374.
Aşkar, T.K., Ergün, N. and Turunç, V. (2007). Isı şok proteinler ve fizyolojik rolleri. Kafkas Universitesi Veteriner Fakultesi Dergisi, 13: 109-114
Atakisi, E., Karapehlivan, M., Atakisi, O., Kontas, T., Marasli, S. (2006). Adenosine deaminase and Biochemical Liver Function Tests in the Dermatophytic Cattle. Bulletin Veterinary Institute Pulawy, 50: 481-483
Aydin, I., Bulbul, T., Polat, E.S. and Yazar, E. (2010). Serum antioxidant status and adenosine deaminase activity during the gestational period of sheep. Revue de Médecine Véterinaire, 161: 479-484.
Azimzadeh, K., Nouri, K., Farougi, H., Rasouli, S. and Zamani, N. (2013). Plasma Malondialdehyde, Thyroid Hormones and Some Blood Profiles in Ovine Babesiosis. Kafkas Universitesi Veteriner Fakultesi Dergisi, 19(3): 489-493
Bao, X.Q. and Liu, G.T. (2009). Induction of overexpression of the 27- and 70-kda heat shock proteins by bicyclol attenuates concanavalin A-induced liver injury through suppression of Nuclear Factor-kB in mice. Molecular Pharmacology, 75: 1180-1188.
Bharti, A.R., Nally, J.E., Ricaldi, J.N., Matthias, M.A., Diaz, M.M., Lovett, M.A., et al. (2003). Leptospirosis: a zoonotic disease of global importance. Lancet Infectious Disease, 3(12): 757-771
Chillemi, R.,Zappacosta, B.,Simporè, J., Persichilli, S.,Musumeci, M. andMusumeci, S. (2004). Hyperhomocysteinemia in acute Plasmodium falciparum malaria: an effect of host-parasite interaction. Clinica Chimica Acta, 348(1-2): 113-120.
Ciocca, D.R., Oesterreich, S., Chamness, G.C., McGuire, W.L. and Fugua, S.A. (1993). Biological and clinical implications of heat shock protein 27 (Hsp27). Journal of National Cancer Institution, 85: 1558-1570.
Cooper, B.F., Sideraki, V., Wilson, D.K., Dominguez, D.Y., Clark, S.W., Quiocho, F.A., et al. (1997). The role of divalent cations in structure and function of murine adenosine deaminase. Protein Science, 6: 1031-1037.
Cronstein, B.N., Levin, R.I., Belanoff, J., Weissmann, G. and Hirschhorn, R. (1986). Adenosine: an endogenous inhibitor of neutrophil-mediated injury to endothelial cells. Journal of Clinical Investment, 78(3): 760-770.
Erdogan, H.M., Karapehlivan, M., Citil, M., Atakisi, O., Uzlu, E. and Unver, A. (2008). Serum sialic acid and oxidative stress parameters changes in cattle with leptospirosis. Veterinary Research Communication, 32: 333-339.
Ergönül, S. and Aşkar, T.K. (2009). The investigation of heat shock protein (HSP 27), Malondialdehyde (MDA), Nitric Oxide (NO) and Interleukin (IL-6, IL-10) levels in cattle with anaplasmosis. Kafkas Universitesi Veteriner Fakultesi Dergisi, 15: 575-579.
Gazi, I.F., Apostolou, F.A., Liberopoulos, E.N., Filippatos, T.D., Tellis, C.C., Elisaf, M.S., et al. (2011). Leptospirosis is Associated with Markedly Increased Triglycerides and Small Dense Low-Density Lipoprotein and Decreased High-Density Lipoprotein. Lipids, 46: 953-960.
Gierens, H., Nauck, M., Roth, M., Schinker, R., Schurmann, C., Scharnagl, H., et al. (2000). Interleukin-6 stimulates LDL receptor gene expression via activation of sterol-responsive and Sp binding elements. Arteriosclerosis Thrombosis Vascular Biology, 20: 1777-1783.
Gopi, A., Madhavan, S.M., Sharma, S.K. and Sahn, S.A. (2007). Diagnosis and treatment of tuberculosis pleural effusion in 2006. Chest, 131: 880-889.
Guay, J., Lambert, H., Gingras-Breton, G., Lavoie, J.N., Huot, J. and Landry, J. (1997). Regulation of actin filament dynamics by p38 map kinase-mediated phosphorylation of heat shock protein 27. Journal of Cell Science, 110: 357-368.
Guo, L., Ai1, J., Zheng, Z., Howatt, D.A., Daugherty, A., Huang, B., et al. (2013). HDL protects against polymicrobial-induced sepsis in mice. The Journal of Biological Chemistry, 289(21): 14666–14673.
Heidarian, E., Amini, M., Parham, M. and Aminorroaya, A. (2009). Effect of Zinc Supplementation on Serum Homocysteine in Type 2 Diabetic Patients with Microalbuminuria. The Review of Diabetic Studies, 6: 1.
Hoshino, T., Yamada, K., Masuoka, K., Tsuboi, I., Itoh, K., Nonaka, K., et al. (1994). Elevated adenosine deaminase activity in the serum of patients with diabetes mellitus. Diabetes Research Clinical Practice, 25: 97-102.
Hönscheid, A., Rink, L. and Haase, H. (2009). T Lymphocytes: A Target for Stimulatory and Inhibitory Effects of Zinc Ions. Endocrine, Metabolic and Immune Disorders-Drug Targets, 9: 132-144.
Jacobsen, D.W. (2000). Hyperhomocysteinemia and Oxidative Stress Time for a Reality Check? Arteriosclerosis Thrombosis and Vascular Biology, 20: 1182-1184.
Karaman, U., Beytur, L., Raika Kıran, T. and Çolak, C. (2009). Adenosine deaminase level in the serum of the patients Toxoplasma gondii seropositive and Giardia intestinalis. African Journal of Microbiology Research, 3(10): 654-657.
Kettler, S.I., Eder, K., Kettler, A. and Kirchgessner, M. (2000). Zinc deficiency and the activities of lipoprotein lipase in plasma and tissues of rats force-fed diets with coconut oil or fish oil. Journal of Nutritional Biochemistry, 11(3): 132-138.
Khovidhunkit, W., Kim, M.S., Memon, R.A., Shigenaga, J.K., Moser, A.H. and Feingold, K.R. (2004). Effects of infection and inflammation on lipid and lipoprotein metabolism: mechanisms and consequences to the host. Journal of Lipid Research, 45:1169-1196.
Khovidhunkit, W., Memon, R.A., Feingold, K.R. and Grunfeld, C. (2000) Infection and inflammationinduced proatherogenic changes of lipoproteins. Journal of Infectious Diseases, 181(3): 462-472.
Mc Cully, K.S. (1969). Vascular pathology of homocysteinemia: implication for the pathogenesis of arteriosclerosis. American Journal of Pathology, 56: 111-128.
Mymrikov, E.V., Seit-Nebi, A.S. and Gusev, N.B. (2011). Large potentials of small heat shock proteins. Physiology Review, 91: 1123-1159.
Nazifi, S., Razavi, S.M., Safi, N. and Rakhshandehroo, E. (2012). Malignant Ovine Theileriosis: Alterations in the Levels of Homocysteine, Thyroid Hormones and Serum Trace Elements. Journal of Bacteriology and Parasitology, 3: 7.
Nehler, M.R., Talor, L.M. and Porter, J.M. (1997): Homocysteine as a risk factor for atherosclerosis: a review. Journal of Cardiovascular Surgery, 5: 559-567.
Plank, R. and Dean, D. (2000). Overview of the epidemiology, microbiology, and pathogenesis of Leptospira spp. in humans. Microbes and Infection, 2: 1265-1276.
Powell, S.R. (2000). The Antioxidant Properties of Zinc. Journal of Nutrition, 5: 1447-1454.
Quinn, P.J., Carter, M.E., Markey, B. and Carter, G.R. (1994). Clinical Veterinary Microbiology. 1st ed., UK: London, Wolfe Publishing, pp: 292-298.
Radostits, O.M., Blood, D.C. and Gay, C.C. (1994). Veterinary Medicine: A Textbook of the Diseases of Cattle, Hhorses, Sheep, Pigs and Goats. 8th ed., UK: London, Baillaire Tindall, pp: 884-908.
Rasoulinejad, M., Mousavi, S.J., Abdollahi, A., Fattahi, F. and Sarbiaei, A. (2009). Serum Adenosine Deaminase Activity and C-reactive protein Levels in Patients with Brucellosis Iranian Journal of Pathology, 4(3): 113-117.
Rodriguez, L.F.S., Oliveirab, M.E.F., Teixeirab, P.P.M., Cavalcantec, J.M. and Valec, M.R. (2012). Adenosine deaminase activity as a biochemical marker of inflammatory response in goats infected by caprine arthritis–encephalitis virus. Small Ruminant Research, 108: 120-126.
Sideraki, V., Mohamedali, K.A., Wilson, D.K., Chang, Z., Kellems, R.E., Quiocho, F.A., et al. (1996). Probing the functional role of two conserved active site aspartates in mouse adenosine deaminase. Biochemistry, 35: 7862-7872.
Tissieres, A., Mitchell, H.K. and Tracy, U.M. (1974). Protein synthesis in salivary glands of Drosophila melanogaster: relation to chromosome puffs. Journal of Molecular Biology, 85: 389-398.
Thambyrajah, J. and Townend, J.N. (2000). Homocysteine and atherothrombosis- mechanisms for Injury. European Heart Journal, 21: 967-974.
Toth, P.P. (2005). The ''Good Cholesterol'': High-Density Lipoprotein. Circulation, 111: e89-e91.
Turunc, V. and Kontas-Askar, T. (2012). The Determination of Oxidative Stress by Paraoxonase Activity, Heat Shock Protein and Lipid Profile Levels in Cattle with Theileriosis. Kafkas Universitesi Veteriner Fakultesi Dergisi, 18(4): 647-651.
Tyagi, N., Sedoris, K.C., Steed, M., Ovechkin, A.V., Moshal, K.S. and Tyagi, S.C. (2005). Mechanisms of homocysteine-induced oxidative stress. American Journal of Physiology Heart Circulation Physiology, 289: 2649-2656.
Vernel-Pauillac, F. and Merien, F. (2006). Proinflammatory and Immunomodulatory Cytokine m-RNA Time Course Profiles in Hamsters Infected with a Virulent Variant of Leptospira interrogans. Infection and Immunity, 4172-4179.
Vidyasagar, A., Nancy, A.W. and Djamal, A. (2012). Heat shock protein 27 (HSP27): biomarker of disease and therapeutic target. Fibrogenesis and Tissue Repair, 5: 7.
Wang, H., Wu, Y., Ojcius, D.M., Yang, F., Zhang, C., Ding, S., et al. (2012). Leptospiral hemolysins induce pro-inflammatory cytokines through toll-like receptor 2-and 4mediated JNK and NF-kB signaling pathways. PLoS ONE, 7(8): e42266. doi:10.1371/journal.pone.0042266.
Wagner, C. (1995). Biochemical role of folate in cellular metabolism. In: Folate in Health and Disease. Marcel Dekker editor. New York: Bailey, publishing, pp: 23-42.
Yamamoto, M. and Katoh, N. (2000). Decreased Apolipoprotein C-III Concentration in the High-Density Lipoprotein Fraction from Calves Inoculated with Pasteurella haemolytica and Bovine Herpes Virus-1. Journal of Veterinary Medicine Science, 62(1): 49-52.
Yang, C.W., Wu, M.S. and Pan, M.J. (2001). Leptospirosis renal disease. Nephrology Dialyses Transplantation, 5: 73-77.