Study of metalloproteinases in the blood of goats experimentally infected with caprine encephalitis arthritis virus
DOI:
https://doi.org/10.5433/1679-0359.2020v41n6Supl2p3165Palabras clave:
Lentivirus, MMPs, Proteases, Zymography.Resumen
Caprine arthritis encephalitis is a lentiviral disease that leads to considerable losses in goat farming. In the acute phase of viral infection, though antiviral antibodies are produced by the host’s immune system, they are not sufficient to be detected by serological tests. Acute infections begin with an incubation period, during which the viral genome replicates and host innate responses are initiated. Matrix metalloproteinases (MMPs) are enzymes that play an important role in the physiological and pathological processes of tissue remodeling. The present study aimed to evaluate the expression of MMPs and their activity in the blood serum of goats experimentally infected with caprine arthritis encephalitis virus (CAEV). Five dairy goats, aged 3-4 years, were intravenously inoculated with CAEV Cork strain (titer: 105-6 TCID50/mL) after being tested negative for CAEV thrice at consecutive intervals of 30 days using western blot analysis and nested-PCR. The study included three stages: S1 or pre-infection stage; S2 or seroconversion stage, corresponding to the occurrence of first seroconversion; and S3 or post-seroconversion stage, corresponding to 23 weeks after seroconversion. Zymography was performed for the samples using gelatin zymography gels (12.5%), which were subjected to electrophoresis at 170V, 1A, and 300W for 50-70 min. The density of MMP-2 was found to be lower at S1 (1456.20 pixels) than that at S2 and S3 (1943.80 and 2104.40 pixels, respectively) (P < 0.05); and the density of MMP-9 was found to be lower at S3 (133.60 pixels) than that at S1 and S2 (359.60 and 370.60 pixels, respectively). The density of proMMP-2 was low at S1 and S3 (130.45 and 145.20 pixels, respectively). On the other hand, the density of proMMP-9 was statistically different between S1 and S3 (89.22 vs. 415.60 pixels). Both proMMP-2 and proMMP-9 were absent at S2. Thus, MMP-2 and MMP-9 exhibited opposite behaviors depending on the stage of infection. As the greatest activity of MMP-2 was detected at stage S3, we suggest that MMP-2 can be used as a biomarker for complementary diagnosis of acute CAEV infection. In addition, the presence of proMMP-13 can be used to indicate active viral infection.Métricas
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Hu, J., Steen, P. E. van den., Sang, Q. X. A., & Opdenakker, G. (2007). Matrix metalloproteinase inhibitors as therapy for inflammatory and vascular diseases. Nature Reviews Drug Discovery, 6(6), 480-498. doi: 10.1038/nrd2308
Iwamoto, N., Kawakami, A., Arima, K., Tamai, M., Nakamura, H., Kawashiri, S.,… Eguchi, K. (2011). Contribution of an adenine to guanine single nucleotide polymorphism of the matrix metalloproteinase-13 (MMP-13) -77 promoter region to the production of anticyclic citrullinated peptide antibodies in patients with HLA-DRB1*shared epitope-negative rheumatoid arthritis. Journal of Modern Rheumatology, 21(3), 240-243. doi: 10.1007/s10165-010-0375-6
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Kuzuya, M., & Iguchi, A. (2003). Role of matrix metalloproteinases in vascular remodeling. Journal of Atherosclerosis and Thrombosis, 10(5), 275-282. doi: 10.5551 / jat.10.275
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Lopez-Avila, V., & Spencer, J. V. (2008). Methods for detection of matrix metalloproteinases as biomarkers in cardiovascular disease. Clinical Medicine Insights: Cardiology, 2(1), 75-87. doi: 10.4137/CMC.S484
Mannello, F., & Medda, V. (2012). Nuclear localization of matrix metalloproteinases, Progress in Histochemistry and Cytochemistry, 47(1), 27-58. doi: 10.1016/j.proghi.2011.12.002
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Bezerra, R. Q., Jr., Eloy, A. M. X., Furtado, J. R., Pinheiro, R. R., Andrioli, A. P., Moreno, F. B.,... Teixeira, M. F. S. (2017). A panel of protein candidates for comprehensive study of Caprine Arthritis Encephalitis (CAE) infection. Tropical Animal Health and Production, 50(1) 43-48, 2017. doi: 10.1007 /s11250-017-1398-1
Bezerra, R. Q., Jr., Eloy, A. M. X., Perreira, E. P., Furtado, J. R., Souza, K. C. S., Lima, A. R.,... Teixeira, M. F. S. (2015). Avaliação das metaloproteinases de matriz no sangue de reprodutores caprinos naturalmente infectados com artrite encefalite caprina na região Semiárida do Brasil. Acta Scientiae Veterinariae, 43(1258), 1-7. Recuperado de http://www.ufrgs.br/actavet/43/PUB%201258.pdf
Blacklaws, B. A. (2012). Small ruminant lentiviruses: immunopathogenesis of visna-maedi and caprine arthritis and encephalitis vírus. Comparative Immunology, Microbiology and Infectious Diseases, 35(3), 259-269. doi: 10.1016/j.cimid.2011.12.003
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Concha, H. A. R. (2010). Papel das metaloproteinases de matriz nas alterações da barreira hematoencefálica em ratos submetidos à sepse severa. Dissertação de mestrado, Ciências da Saúde, Universidade do Extremo Sul Catarinense, Criciúma, RS, Brasil. Recuperado de http://www.bib.unesc. net/pergamum/biblioteca/index.php?codAcervo=99541
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Dawson, M. (1987). Pathogenesis of maedi-visna. Veterinary Record, 120(19), 451-454. doi: 10.1136/vr. 120.19.451
Diffay, B. C., Mckenzie, D., Wolf, C., & Pugh, D. G. (2005). Abordagem e exame de ovinos e caprinos. In D. G. Pugh (Eds.), Clínica de ovinos e caprinos (pp. 1-19). São Paulo, SP: Roca.
Elkington, H., White, P., Addington-Hall, J., Higgs, R., & Edmonds, P. (2005). The healthcare needs of chronic obstructive pulmonary disease patients in the last year of life. Palliative Medicine, 19(6), 485-491. doi: 10.1191/0269216305pm1056oa
Eloy, A. M. X., Bezerra, R. Q., Jr., Pinheiro, R. R., & Andrioli, A. (2015). Técnica Zimográfica como método para monitoramento da Artrite Encefalite Caprina (CAE). (Comunicado Técnico, 155). Sobral, CE: Embrapa Caprinos e Ovinos, CNPC. 1-6. Recuperado de http://ainfo.cnptia.embrapa.br/digital/ bitstream/item/146807/1/ CNPC-2015-Cot155.pdf
Franke, C. R. (1998). Controle sanitário da artrite-encefalite caprina (CAE). Salvador, BA: EDUFBA.
Geurts, N., Opdenakker, G., & Steen, P. E. van den. (2012). Matrix Metalloproteinases as therapeutic targets in protozoan parasitic infections. Pharmacology & therapeutics, 133(3), 257-279. doi: 10.1016/j. pharmthera.2011.11.008
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Hernández Rios, M., Sorsa T., Obrego´n, F., Tervahartiala, T., Valenzuela, M. A., Pozo, P.,… Gamonal, J. (2009). Proteolytic roles of matrix metalloproteinases (MMP)-13 during progression of chronic periodontitis: initial evidence for MMP-13/MMP-9 activation cascade. Journal of Clinical Periodontology, 36(12), 1011-1017. doi: 10.1111/j.1600-051X.2009.01488.x
Houwers, D. J., & Nauta, I. M. (1989). Immunoblot analysis of the antibody response to ovine lentivirus infections. Veterinary Microbiology, 19(2), 127-139. doi: 10.1016/0378-1135(89)90078-3
Hu, J., Steen, P. E. van den., Sang, Q. X. A., & Opdenakker, G. (2007). Matrix metalloproteinase inhibitors as therapy for inflammatory and vascular diseases. Nature Reviews Drug Discovery, 6(6), 480-498. doi: 10.1038/nrd2308
Iwamoto, N., Kawakami, A., Arima, K., Tamai, M., Nakamura, H., Kawashiri, S.,… Eguchi, K. (2011). Contribution of an adenine to guanine single nucleotide polymorphism of the matrix metalloproteinase-13 (MMP-13) -77 promoter region to the production of anticyclic citrullinated peptide antibodies in patients with HLA-DRB1*shared epitope-negative rheumatoid arthritis. Journal of Modern Rheumatology, 21(3), 240-243. doi: 10.1007/s10165-010-0375-6
Jones, B. T. (2014). The current prevalence of caprine arthritis-encephalitis virus in midwestern goat herds. Doctoral thesis, University of Nebraska, Lincoln, NE, USA. Retrieved from http://digitalcommons.unl. edu/cgi/viewcontent.cgi?article=1014&context=vetscidiss
Klein, T., & Bischoff, R. (2011). Physiology and pathophysiology of matrix metalloproteases. Amino Acids, 41(2), 271-290. doi: 10.1007/s00726-010-0689-x
Knäuper, V., Bailey, L., Worley, J. R., Soloway, P., Patterson, M. L., & Murphy, G. (2002). Cellular activation of pro-MMP-13 by MTI-MMP depends on the C-terminal domain of MMP-13. FEBS Letters, 532(1-2), 127-130. doi: 10.1016/s0014-5793(02)03654-2
Knäuper, V., Cowell, S., Smith, B., Lopez-Otin, C., O'Shea, M., & Morris, H. (1997). The role of the C-terminal domain of human collagenase-3 (MMP-13) in the activation of pr collagenase-3, substrate specificity, and tissue inhibitor of metalloproteinase interaction. Journal of Biological Chemistry, 272(12), 7608-7616. doi: 10.1074 / jbc.272.12.7608
Knäuper, V., López-Otín, C., Smith, B., Knight, G., & Murphy, G. (1996). Biochemical characterization of human collagenase-3. Journal of Biological Chemistry, 271(3), 1544-5150. doi: 10.1074/jbc.271. 3.1544
Kupai, K., Szucs, G., Cseh, S., Hajdu, I., Csonka, C., Csont, T., & Ferdinandy, P. (2010). Matrix metalloproteinase activity assays: Importance of zymography. Journal of Pharmacology and Toxicology Methods, 61(2), 205-209. doi: 10.1016/j.vascn.2010.02.011
Kuzuya, M., & Iguchi, A. (2003). Role of matrix metalloproteinases in vascular remodeling. Journal of Atherosclerosis and Thrombosis, 10(5), 275-282. doi: 10.5551 / jat.10.275
Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227(5259), 680-685. doi: 10.1038/227680a0
Lara, M. C. C. S. H., Birgel, E. H., Jr., Fernandes, M. A., & Birgel, E. H. (2003). Infecção experimental do vírus da Artrite Encefalite dos caprinos em cabritos. Arquivos do Instituto Biológico, 70(1), 51-54. Recuperado de http://www.biologico.agricultura.sp.gov.br/uploads/docs/arq/V70_1/lara.pdf
Lofstedt, J. (2014). Overview of caprine arthritis and encephalitis. Retrieved from http://www. msdvetmanual.com/generalized-conditions/caprine-arthritis-and-encephalitis/overview-of-caprine-arthritis-and-encephalitis
Lopez-Avila, V., & Spencer, J. V. (2008). Methods for detection of matrix metalloproteinases as biomarkers in cardiovascular disease. Clinical Medicine Insights: Cardiology, 2(1), 75-87. doi: 10.4137/CMC.S484
Mannello, F., & Medda, V. (2012). Nuclear localization of matrix metalloproteinases, Progress in Histochemistry and Cytochemistry, 47(1), 27-58. doi: 10.1016/j.proghi.2011.12.002
Matrisian, L. M. (1990). Metalloproteinases and their inhibitors in matrix remodeling. Trends in Genetics, 6(4), 121-125. doi: 10.1016 / 0168-9525 (90) 90126-q
Navarro, V. P., Nelson, P., Fº., Silva, L. A. B., & Freitas, A. C. A. (2006). Participação das metaloproteinases da matriz nos processos fisiopatológicos da cavidade bucal. Revista de Odontologia da UNESP, Araraquara, 35(4), 233-238. Recuperado de http://www.revodontolunesp.com.br/article /588017de7f8c9d0a098b4951
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2020-11-06
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Galiza, Y. S. de, Eloy, A. M. X., Pinheiro, R. R., Peixoto, R. M., Lima, A. M. C., Barroso, M. L. da S., & Fonseca, L. M. (2020). Study of metalloproteinases in the blood of goats experimentally infected with caprine encephalitis arthritis virus. Semina: Ciências Agrárias, 41(6Supl2), 3165–3176. https://doi.org/10.5433/1679-0359.2020v41n6Supl2p3165
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