全部 标题 作者
关键词 摘要

OALib Journal期刊
ISSN: 2333-9721
费用:99美元

查看量下载量

相关文章

更多...

Effects of Purified Indian Cattle Tick Rhipicephalus microplus Saliva Toxins on Various Enzymes in Blood Serum, Liver and Muscles of Albino Mice

DOI: 10.4236/aer.2023.112005, PP. 82-112

Keywords: Rhipicephalus microplus, Serum, Liver and Rectus Abdominis, Gastrocnemius, Muscle, Atria and Ventricle Acid Phosphatase (ACP), Alkaline Phosphatase (ALP), Glutamate Pyruvate Transaminase (GPT) and Glutamate Oxaloacetate Transaminase (GOT), Lactic Dehydrogenase (LDH) and Acetylcholinesterase (AchE)

Full-Text   Cite this paper   Add to My Lib

Abstract:

In the present investigation, in vivo effects of purified ticks’ saliva toxin were evaluated on the level of certain important cellular metabolic enzymes i.e. acid phosphatase (ACP), alkaline phosphatase (ALP), glutamate pyruvate transaminase, glutamate oxaloacetate transaminase and lactic dehydrogenase. For this purpose, sub-lethal doses, 40% and 80% of 24 h LD50 purified saliva toxins of Rhipicephalus microplus (Canestrini, 1888) were injected subcutaneously in the albino mice. In treated mice saliva toxins targeted membrane-bound enzymes i.e. serum acid phosphatase and alkaline phosphatase, its level was increased from 118.30% to 163.63% at the 6th hr in comparison to the control. Besides this, the levels of serum glutamate pyruvate transaminase (GPT) and glutamate oxaloacetate transaminase (GOT) and lactic dehydrogenase (LDH) also increased up to 161.11% (at 6th hr), 148.27 (at 8th hr) and 125.45% (at 6th hr) respectively in comparison to control. An increase in the level of LDH showed insufficient oxygen supply, massive disintegration of cells and leakage of the enzyme into the circulation. It clearly indicated the toxic effects of saliva toxins on the membrane of blood cells, hepatocytes and myocardial muscle cell functions in albino mice. On the other hand activity of acetyl cholinesterase was reduced by 65.51% at the 6th hr of the saliva toxin injection in comparison to the control. This inhibition of acetyl cholinesterase activity caused the accumulation of acetylcholine molecules at the synaptic junctions and led to prolonged activation of acetylcholine receptors. It caused permanent stimulation of nerves and muscle cells that may result in muscular paralysis and finally death of the animal.

References

[1]  Blisnick, A.A., Simo, L., Grillon, C., Fasani, F., Brulé, S., Le Bonniec, B., Prina, E., Marsot, M., Relmy, A., Blaise-Boisseau, S., Richardson, J. and Bonnet, S.I. (2019) The Immunomodulatory Effect of IrSPI, a Tick Salivary Gland Serine Protease Inhibitor Involved in Ixodes ricinus Tick Feeding. Vaccines (Basel), 7, Article No. 148.
https://doi.org/10.3390/vaccines7040148
[2]  Fogaca, A.C., Sousa, G., Pavanelo, D.B., Esteves, E., Martins, L.A. and Urbanová, V. (2021) Tick Immune System: What Is Known, the Interconnections, the Gaps, and the Challenges. Frontiers in Immunology, 12, Article ID: 628054.
https://doi.org/10.3389/fimmu.2021.628054
[3]  Vancová, M., Bíly, T., Simo, L., et al. (2020) Three-Dimensional Reconstruction of the Feeding Apparatus of the Tick Ixodes ricinus (Acari: Ixodidae): A New Insight into the Mechanism of Blood-Feeding. Scientific Reports, 10, Article No. 165.
https://doi.org/10.1038/s41598-019-56811-2
[4]  Perveen, N., Muzaffar, S.B. and Al-Deeb, M.A. (2021) Ticks and Tick-Borne Diseases of Livestock in the Middle East and North Africa: A Review. Insects, 2, Article No. 83.
https://doi.org/10.3390/insects12010083
[5]  Obaid, M.K., Islam, N., Alouffi, A., Khan, A.Z., da Silva Vaz, I., Tanaka, T. and Ali, A. (2022) Acaricides Resistance in Ticks: Selection, Diagnosis, Mechanisms, and Mitigation. Frontiers in Cellular and Infection Microbiology, 12, Article ID: 941831.
https://doi.org/10.3389/fcimb.2022.941831
[6]  Hrnková, J., Schneiderová, I., Golovchenko, M., Grubhoffer, L., Rudenko, N. and Cerny, J. (2021) Role of Zoo-Housed Animals in the Ecology of Ticks and Tick-Borne Pathogens—A Review. Pathogens, 10, Article No. 210.
https://doi.org/10.3390/pathogens10020210
[7]  Feng, L.L., Liu, L. and Cheng, T.Y. (2019) Proteomic Analysis of Saliva from Partially and Fully Engorged Adult Female Rhipicephalus microplus (Acari: Ixodidae). Experimental and Applied Acarology, 78, 443-460.
https://doi.org/10.1007/s10493-019-00390-4
[8]  Galay, R.L., Umemiya-Shirafuji, R., Bacolod, E.T., Maeda, H., Kusakisako, K., Koyama, J., Tsuji, N., Mochizuki, M., Fujisaki, K. and Tanaka, T. (2014) Two Kinds of Ferritin Protect Ixodid Ticks from Iron Overload and Consequent Oxidative Stress. PLOS ONE, 9, e90661.
https://doi.org/10.1371/journal.pone.0090661
[9]  Dai, O., Sojka, D., Kopacek, P., Buresova, V., Franta, Z., Sauman, I., Winzerling, J. and Grubhoffer, L. (2009) Knockdown of Proteins Involved in Iron Metabolism Limits Tick Reproduction and Development. Proceedings of the National Academy of Sciences of the United States of America, 106, 1033-1038.
https://doi.org/10.1073/pnas.0807961106
[10]  Chmelar, J., Kotál, J., Kovaríková, A. and Kotsyfakis, M. (2019) The Use of Tick Salivary Proteins as Novel Therapeutics. Frontiers in Physiology, 10, Article No. 812.
https://doi.org/10.3389/fphys.2019.00812
[11]  Calic, M., Vrdoljak, A.L., Radic, B., Jelic, D., Jun, D., Kuca, K., Kovarik, Z. (2006) In Vitro and in Vivo Evaluation of Pyridinium Oximes: Mode of Interaction with Acetylcholinesterase, Effect on Tabun- and Soman-Poisoned Mice and Their Cytotoxicity. Toxicology, 219, 85-96.
https://doi.org/10.1016/j.tox.2005.11.003
[12]  Kendig, D.M. and Tarloff, J.B. (2007) Inactivation of Lactate Dehydrogenase by Several Chemicals: Implications for in Vitro Toxicology Studies. Toxicology in Vitro, 21, 125-132.
https://doi.org/10.1016/j.tiv.2006.08.004
[13]  Asha, S. and Radha, E. (1985) Effect of Age and Myocardial Infarction on Serum and Heart Lactic Dehydrogenase. Experimental Gerontology, 20, 67-70.
https://doi.org/10.1016/0531-5565(85)90010-5
[14]  Danaei, G.H., Amali, A., Karami, M., Khorrami, M.B., Riahi-Zanjani, B. and Sadeghi, M. (2022) The Significance of Thymoquinone Administration on Liver Toxicity of Diazinon and Cholinesterase Activity; a Recommendation for Prophylaxis among Individuals at Risk. BMC Complementary Medicine and Therapies, 22, Article No. 321.
https://doi.org/10.1186/s12906-022-03806-8
[15]  Huang, X.J., Choi, Y.K., Im, H.S., Yarimaga, O., Yoon, E. and Kim, H.S. (2006) Aspartate Aminotransferase (AST/GOT) and Alanine Aminotransferase (ALT/GPT) Detection Techniques. Sensors (Basel), 6, 756-782.
https://doi.org/10.3390/s6070756
[16]  Nwani, C.D., Lakra, W.S., Nagpure, N.S., Kumar, R., Kushwaha, B. and Srivastava, S.K. (2010) Toxicity of the Herbicide Atrazine: Effects on Lipid Peroxidation and Activities of Antioxidant Enzymes in the Freshwater Fish Channa punctatus (Bloch). International Journal of Environmental Research Public and Health, 7, 3298-3312.
https://doi.org/10.3390/ijerph7083298
[17]  Wang, X., Li, P., Ding, Q., Wu, C., Zhang, W. and Tang, B. (2019) Observation of Acetylcholinesterase in Stress-Induced Depression Phenotypes by Two-Photon Fluorescence Imaging in the Mouse Brain. Journal of the American Chemical Society, 141, 2061-2068.
https://doi.org/10.1021/jacs.8b11414
[18]  Kourouma, A., Quan, C., Duan, P., Qi, S.Q., Yu, T.T., Wang, Y.N. and Yang, K.D. (2015) Bisphenol A Induces Apoptosis in Liver Cells through Induction of ROS. Advances in Toxicology, 2015, Article ID: 901983.
https://doi.org/10.1155/2015/901983
[19]  Lowry, O.H., Rosenburgh, N.J., Farr, A.L. and Randall, R.J. (1951) Protein Measurement with the Folin Phenol Reagent. Journal of Biological Chemistry, 193, 265-275.
https://doi.org/10.1016/S0021-9258(19)52451-6
[20]  Spier, R.E. (1982) The Confidence Limits Were Calculated at 95% Probability Levels. Spier, R.E. 1982Gel Filtration Column, Animal Cell Technology: An Overview. Journal of Chemical Technology and Biotechnology, 32, 304-312.
https://doi.org/10.1002/jctb.5030320134
[21]  Andrech and Szeypiaske, A.J. (1947) Use of p-Nitrophenylphosphate as the Substrate in Determination of Serum Acid Phosphatase. American Journal of Clinical Pathology, 17, 571-574.
https://doi.org/10.1093/ajcp/17.7_ts.571
[22]  Bergmeyer, U.H. (1967) Determination of Alkaline Phophatase and Acid Phosphatase. Academic Press, New York, 1129.
[23]  Reitman, A. and Frankel, S. (1957) A Colorimetric Method for the Determination of Glutamate-Oxaloacetate and Serum Glutamate-Pyruvate Transaminase. American Journal of Clinical Pathology, 28, 56-63.
https://doi.org/10.1093/ajcp/28.1.56
[24]  Ellman, G.L., Courtney, K.D., Andres, V. and Featherstone, R.M. (1961) A New and Rapid Colorimetric Determination of Acetylcholinesterase Activity. Biochemical Pharmacology, 7, 88-95.
https://doi.org/10.1016/0006-2952(61)90145-9
[25]  Annon, T.M. (1984) Sigma Diagnostic: Lactate Dehydrogenase (Quantitative, Colorimeteric Determination in Serum, Urine and Cerebrospinal Fluid) at 400-500 nm. Procedure No. 500.
[26]  Abou-Donia, M.B. (1978) Increase in Acid Phosphatase Activity in Hens Following an Oral Dose of Leptophos. Toxicology Letters, 2, 199-203.
https://doi.org/10.1016/0378-4274(78)90067-X
[27]  Bouck, G.R. (1966) Changes in Blood and Muscle Composition of Rock Bass (Ambloplites rupestris) as Physiological Criteria of Stressful Conditions. Ph.D. Dissertation, Michigan State University, East Lansing.
[28]  Abraham, R., Goldberg, L. and Grasso, P. (1967) Hepatic Response to Lysosomal Effects of Hypoxia, Natural Red and Chloroquine. Nature, 215, 195-196.
https://doi.org/10.1038/215194a0
[29]  Pillo, B., Ansani, M.V. and Shah, R.V. (1972) Studies on Wound Healing and Repair in Pigeon Liver II: Histochemical Studies on Acid and Alkaline Phosphatase during the Process. The Journal of Animal Morphology and Physiology, 19, 205-221.
[30]  Khan, M.N. and Tahira, S. (2003) Pesticide-Induced Changes in Serum Levels of Acid Phosphatase, Alkaline Phosphates and Glutamate Oxaloacetate Transaminase in Rats. Pakistan Journal of Biological Sciences, 6, 359-362.
https://doi.org/10.3923/pjbs.2003.359.362
[31]  Saigal, S., Bhatnagar, V.K. and Malviya, A.N. (1982) Effect of Selected Pesticides on Alkaline and Acid Phosphatase in the Rat. Toxicology Letters, 12, 177-180.
https://doi.org/10.1016/0378-4274(82)90182-5
[32]  Srinivas, R., Udikeri, S.S., Jayalakshmi, S.K. and Sreeramulu, K. (2004) Identification of Factors Responsible for Insecticide Resistance in Helicoverpa Armigera. Comp Biochem Physiol C Toxicol Pharmacol, 137, 261-269.
https://doi.org/10.1016/j.cca.2004.02.002
[33]  Jaffrezic-Renault, N. (2001) New Trends in Biosensor for Organophosphorus Pesticides. Sensors, 1, 60-74.
https://doi.org/10.3390/s10100060
[34]  Lusková, V., Svoboda, M. and Koláfiová, J. (2002) The Effect of Diazinon on Blood Plasma Biochemistry in Carp (Cyprinus carpio L.). Acta Veterinaria Brno, 71, 117-123.
https://doi.org/10.2754/avb200271010117
[35]  Hopkins, B.J. and Hodgson, W.C. (1998) Enzyme and Biochemical Studies of Stonefish (Synanceja trachynis) and Soldierfish (Gymnapistes marmoratus) Venoms. Toxicon, 36, 791-793.
https://doi.org/10.1016/S0041-0101(97)00167-0
[36]  Krauze, M., Truchlinski, J. and Cendrowaka-Pinkosz, M. (2007) Some Biochemical Parameters of Plasma of Turkey-Hens Following Administration of 1,2,4-Triasole Derivative. Polish Journal of Veterinary Sciences, 10, 109-112.
[37]  Vaillant, A. (2021) Transaminase Elevations during Treatment of Chronic Hepatitis B Infection: Safety Considerations and Role in Achieving Functional Cure. Viruses, 13, Article No. 745.
https://doi.org/10.3390/v13050745
[38]  Ibrahim, N.M., Eweis, E.A., El-Beltagi, H.S. and Abdel-Mobdy, Y.E. (2012) Effect of Lead Acetate Toxicity on Experimental Male Albino Rat. Asian Pacific Journal of Tropical Biomedicine, 2, 41-46.
https://doi.org/10.1016/S2221-1691(11)60187-1
[39]  Nelson, D.L. and Cox, M.M. (2000) Lehninger Principles of Biochemistry. 3rd Edition, Worth Publishers, New York, 628-631.
[40]  Schmidt, E. and Schmidt, F.W. (1974) The Importance of Enzymatic Analysis in Medicine. In: Bergmeyer, H.U., Ed., Methods of Enzymatic Analysis, Vol. 1, Academic Press, New York, 6-14.
[41]  Krajnovic-Ozretic, M. and Ozretic, B. (1987) Estimation of the Enzymes LDH, GOT, and GPT in Plasma of Grey Mullet, Mugil auratus and Their Significance in Liver Intoxication. Diseases of Aquatic Organisms, 3, 187-193.
https://doi.org/10.3354/dao003187
[42]  Lehninger, A.L., Cox, M.M. and Nelson, D.L. (2000) Principles of Biochemistry. 2nd Edition, Worth Publishers, New York, 633.
[43]  Lehninger, A.L., Cox, M.M. and Nelson, D.L. (2000) Principles of Biochemistry. 2nd Edition, Worth Publishers, New York, 542.
[44]  Cuppolatti, J. and Abbott, A.J. (1990) Interaction of Melittin with the (Na+ + K+) ATPase: Evidence for a Melittin-Induced Conformational Changes. Archives of Biochemistry and Biophysics, 283, 249-257.
https://doi.org/10.1016/0003-9861(90)90639-G
[45]  Omran, M.A. and Abdel-Rahman, M.S. (1992) Effect of Scorpion Leiurus quinquestriatus (H&E) Venom on the Clinical Chemistry Parameters of the Rat. Toxicology Letters, 61, 99-109.
https://doi.org/10.1016/0378-4274(92)90068-U
[46]  Murthy, K. and Haghanazari, L. (1999) The Blood Level of Glucagons, Cortisol and Insulin Following the Injection of Venom by the Scorpion (mesobuthus tamulus concanesis, Pocock) in Dogs. Journal of Venomous Animals and Toxins, 5, 48-53.
https://doi.org/10.1590/S0104-79301999000200004
[47]  Prochownik, E.V. and Wang, H. (2021) The Metabolic Fates of Pyruvate in Normal and Neoplastic Cells. Cells, 10, Article No. 762.
https://doi.org/10.3390/cells10040762
[48]  Barcellini, W. and Fattizzo, B. (2015) Clinical Applications of Hemolytic Markers in the Differential Diagnosis and Management of Hemolytic Anemia. Disease Markers, 2015, Article ID: 635670.
https://doi.org/10.1155/2015/635670
[49]  Betten, D.P., Richardson, W.H., Tong, T.C. and Clark, R.F. (2006) Massive Honeybee Envenomation-Induced Rhabdomyolysis in an Adolescent. Pediatrics, 117, 231-235.
https://doi.org/10.1542/peds.2005-1075
[50]  Fischer, E.H., HeilMeyer, L.M.G. and Hashcke, R.H. (1971) Phosphorylase and the Control of Glycogen Degradation. Current Topics in Cellular Regulation, 4, 211-251.
https://doi.org/10.1016/B978-0-12-152804-1.50012-X
[51]  Zeni, A.L.B., Becker, A., Krug, M. and Albuquerque, C.A.C. (2007) Histological and Biochemical Effects Induced by Sublethal Doses of Bothrops jararacussu Venom in Mice. Journal of Venomous Animals and Toxins Including Tropical Diseases, 13, 664-676.
https://doi.org/10.1590/S1678-91992007000300009
[52]  Lessenger, J.E. and Reese, B.E. (1999) Rational Use of Cholinesterase Activity Testing in Pesticide Poisoning. The Journal of the American Board of Family Practice, 12, 307-314.
https://doi.org/10.3122/jabfm.12.4.307
[53]  Salari, M., Rahimi, J., Moradnia, M., Tarin, Z., Darvishmotevalli, M., Eslami, F., Shabanloo, A., Avval, M.Y. and Karimi, H. (2019) Evaluation of the Relation of Acetylcholinesterase Enzyme Level of the Worker of a Poison-Producing Industry with the Application of Personal Protective Equipment and the Amount of Poison Production within 2012-2015. International Journal of Environmental Health Engineering, 8, 3.
https://doi.org/10.4103/ijehe.ijehe_7_18
[54]  Lutovac, M., Popova, O.V., Jovanovic, Z., Berisa, H., Kristina, R., Ketin, S. and Bojic, M. (2017) Management, Diagnostic and Prognostic Significance of Acetylcholinesterase as a Biomarker of the Toxic Effects of Pesticides in People Occupationally Exposed. Open Access Macedonian Journal of Medical Sciences, 5, 1021-1027.
https://doi.org/10.3889/oamjms.2017.200

Full-Text

Contact Us

service@oalib.com

QQ:3279437679

WhatsApp +8615387084133