Valores normais da atividade da colinesterase plasmática em anseriformes, com destaque para Alopochen aegyptiacus
pdf

Palavras-chave

Butirilcolinesterase
Inseticidas
Organofosforados
Carbamatos
Biomarcadores
Gansos

Como Citar

1.
Becegato EZ, Westphalen EVN, Westphalen S da R, Tolezano JE, Oshiro M, Salzone CM, Fernandes NCC de A, Guerra JM. Valores normais da atividade da colinesterase plasmática em anseriformes, com destaque para Alopochen aegyptiacus. Rev Inst Adolfo Lutz [Internet]. 30º de dezembro de 2021 [citado 28º de março de 2024];80:1-9,e37277. Disponível em: https://periodicos.saude.sp.gov.br/RIAL/article/view/37277

Resumo

A inibição da enzima colinesterase plasmática (BChE) pode ser utilizada como biomarcador para os efeitos da intoxicação por organofosforados e carbamatos. Nas aves, esta inibição ocorre de forma mais acentuada que nos mamíferos, porém poucos são os trabalhos publicados nestas espécies. O objetivo do estudo foi a dosagem da BChE em gansos-egípcios (Alopochen aegyptiacus) e nos anseriformes domésticos:  gansos-domésticos (Anser anser domesticus) e marrecos (Anas platyrhynchos domesticus), para o estabelecimento de valores de referência normais. O trabalho possui ineditismo com relação à determinação desta enzima nos gansos-egípcios e domésticos. Os gansos e marrecos são mantidos em confinamento com fornecimento de alimentos e água ad libitum e em espaço adequado à sua manutenção no Instituto Adolfo Lutz (IAL), com a finalidade de fornecimento de sangue para a alimentação de triatomídeos do insetário de criação no Núcleo de Parasitoses Sistêmicas. Nos Alopochen aegyptiacus a média e o desvio padrão da BChE foram de 1.868 + 263,6 U/L, nos Anser anser domesticus 2.311 + 673,2 U/L e nos Anas platyrhynchos domesticus 4.290 + 86,11 U/L.

https://doi.org/10.53393/rial.2021.v80.37277
pdf

Referências

1. Alias AS, Al-Zubaidy MHI, Mousa YJ, Mohammad FK. Plasma and whole brain cholinesterase activities in three wild bird species in Mosul, IRAQ: In vitro inhibition by insecticides. Interdiscip Toxicol. 2011;4(3):144-8. https://doi.org/10.2478/v10102-011-0022-x

2. Horowitz IH, Yanco EG, Landau S, Nadler-Valency R, Anglister N, Bueller-Rosenzweig A et al. Whole blood cholinesterase activity in 20 species of wild birds. J Avian Med Surg. 2016;30(2):122-6. https://doi.org/10.1647/2014-044

3. Fildes K, Szabo JK, Hooper MJ, Buttemer WA, Astheimer LB. Plasma cholinesterase characteristics in native Australian birds : significance for monitoring avian species for pesticide exposure. Emu-Austral Ornithology 2009;109(1):41-7. https://doi.org/10.1071/MU08027

4. Desneux N, Decourtye A, Delpuech JM. The sublethal effects of pesticides on beneficial arthropods. Annu Rev Entomol. 2007;52:81-106. https://doi.org/10.1146/annurev.ento.52.110405.091440

5. Bertero A, Fossati P, Caloni F. Indoor poisoning of companion animals by chemicals. Sci Total Environ. 2020;733:139366. https://doi.org/10.1016/j.scitotenv.2020.139366

6. Franson JC, Smith MR. Poisoning of wild birds from exposure to anticholinesterase compounds and lead: Diagnostic methods and selected cases. Semin Avian Exot Pet Med. 1999;8(1):3-11. https://doi.org/10.1016/S1055-937X(99)80030-9

7. Oropesa AL, Sánchez S, Soler F. Characterization of plasma cholinesterase activity in the Eurasian Griffon Vulture Gyps fulvus and its in vitro inhibition by carbamate pesticides. Ibis. 2017;159(3):510-8. https://doi.org/10.1111/ibi.12476

8. Del Hoyo, J Elliot, A Sargatal, J, editors. Handbook of the Birds of the World: Ostrich to Ducks. vol.1, 1. ed. Barcelona, Spain: Lynx Edicions; 1992. 696.p.

9. Kear, J, edithor. Ducks, geese and swans. Part I: general chapters; Part II: species accounts (Anhima to Salvadorina). Oxford. U.K.: Oxford University Press; 2005a.

10. Gyimesi A, Lensink R. Egyptian goose Alopochen aegyptiaca: an introduced species spreading in and from the Netherlands. Wildfowl. 2012;62:126-43.

11. Fairbrother A, Bennett RS, Bennett JK. Sequential sampling of plasma cholinesterase in mallards (Anas platyrhynchos) as an indicator of exposure to cholinesterase inhibitors. Environ Toxicol Chem. 1989;8(2):117-22. https://doi.org/10.1002/etc.5620080202

12. Hill EF. Brain cholinesterase activity of apparently normal wild birds. J Wildl Dis. 1988;24(1):51-61. https://doi.org/10.7589/0090-3558-24.1.51

13. Quero AÁM, Zarco A, Landa FB, Gorla NBM. Plasma cholinesterase activity in wild birds from undisturbed woodlands in the Central Monte Desert. Environ Toxicol Chem. 2019:38(8):1692-700. https://doi.org/10.1002/etc.4458

14. Grosset C, Bougerol C, Sanchez-Migallon Guzman D. Plasma butyrylcholinesterase concentrations in psittacine birds: reference values, factors of variation and association with feather-damaging behavior. J Avian Med Surg. 2014;28(1):6-15. https://doi.org/10.1647/1082-6742-28.1.6

15. Santos CSA, Monteiro MS, Soares AMVM, Loureiro S. Characterization of cholinesterases in plasma of three Portuguese native bird species: application to biomonitoring. PLoS One. 2012;7(3):e33975. https://doi.org/10.1371/journal.pone.0033975

16. Zwarg T, Prioste F, Vanstreels RET, Santos RJ, Matushima ER. Normal plasma cholinesterase activity of neotropical falconiformes and strigiformes. J Raptor Res. 2012;46(2):201-7. https://doi.org/10.3356/JRR-11-50.1

17. Bennett RS, Bennett JK. Age-dependent changes in activity of mallard cholinesterases. J Wildl Dis. 1991;27(1):166-8. https://doi.org/10.7589/0090-3558-27.1.116

18. Lanzarot MP, Barahona MV, San Andrés MI, Fernández-García M, Rodríguez C. Hematologic, protein electrophoresis, biochemistry, and cholinesterase values of free-living black stork nestlings (Ciconia nigra). J Wildl Dis. 2005;41(2):379-86. https://doi.org/10.7589/0090-3558-41.2.379

19. Strum KM, Alfaro M, Haase B, Hooper MJ, Johnson KA, Lanctot RB et al. Plasma cholinesterases for monitoring pesticide exposure in nearctic-neotropical migratory shorebirds. Ornitol Neotrop. 2008;19(Suppl.):641-51.

20. Coraiola AM. Indicadores clínicos, hematológicos, bioquímicos e toxicológicos na pré e pós-reabilitação de Pinguins-de-Magalhães (Spheniscus magellanicus) no sul do Brasil [dissertação de mestrado]. Curitiba (PR): Universidade Federal do Paraná; 2012. Disponível em: https://acervodigital.ufpr.br/handle/1884/27613?show=full

21. Martin PA, Solomon KR, Forsyth DJ, Boermans HJ, Westcott ND. Effects of exposure to carbofuran-sprayed vegetation on the behavior, cholinesterase activity and growth of mallard ducklings (Anas platyrhynchos). Environ Toxicol Chem. 1991;10(7):901-9. https://doi.org/10.1002/etc.5620100706

22. Ludke JL, Hill EF, Dieter MP. Cholinesterase (ChE) response and related mortality among birds fed ChE inhibitors. Arch Environ Contam Toxicol. 1975; 3(1):1-21. https://doi.org/10.1007/BF02221128

23. Fonseca LA, Fagundes V, Girardi FM, Maia NL, Pimentel FG, Braga FR et al. Atividade da colinesterase plasmática como biomarcador de impacto ambiental em tartarugas verdes (Chelonia mydas) no litoral do Arquipélago de Fernando de Noronha, Pernambuco. Pesqu Vet Bras. 2015;35(4):385-9. https://doi.org/10.1590/S0100-736X2015000400012

24. Tully TN, Osofsky A, Jowett PLH, Hosgood G. Acetylcholinesterase concentrations in heparinized blood of hispaniolan amazon parrots (Amazona ventralis). J Zoo Wildl Med. 2003;34(4):411-3. https://doi.org/10.1638/02-004

25. Oropesa AL, Gravato C, Sánchez S, Soler F. Characterization of plasma cholinesterase from the White stork (Ciconia ciconia) and its in vitro inhibition by anticholinesterase pesticides. Ecotoxicol Environ Saf. 2013;97:131-8. https:// doi.org/10.1016/j.ecoenv.2013.07.022

26. González-Escalante L, Mercado-Hernández R, González-Rojas JI, Bermúdez De León M. Plasma cholinesterase activity in the house finch, Carpodacus mexicanus, and the house sparrow, Passer domesticus, collected from pesticide-exposed agricultural land. Bull Environ Contam Toxicol. 2013;90(1):9-11. https://link.springer.com/article/10.1007%2Fs00128-012-0864-8
Creative Commons License
Este trabalho está licenciado sob uma licença Creative Commons Attribution 4.0 International License.

Copyright (c) 2021 Estella Zago Becegato, Elizabeth Visone Nunes Westphalen, Sansão da Rocha Westphalen, José Eduardo Tolezano, Marilena Oshiro, Cristiani Martinez Salzone, Natália Coelho Couto de Azevedo Fernandes, Juliana Mariotti Guerra

Downloads

Não há dados estatísticos.