dc.creatorOliveira, M. M.
dc.creatorSilva, E. S.
dc.creatorCalazans, S. H.
dc.creatorFernandes, F. C.
dc.creatorNeves, M. H. C. Baeta
dc.creatorFerrão Filho, A. S.
dc.creatorHauser Davis, R. A.
dc.creatorLopes, R. M.
dc.creatorBastos, F. F.
dc.creatorBastos, V. L. F. Cunha
dc.creatorBastos, J. Cunha
dc.date2021-11-11T15:17:00Z
dc.date2021-11-11T15:17:00Z
dc.date2021
dc.date.accessioned2023-09-26T20:42:57Z
dc.date.available2023-09-26T20:42:57Z
dc.identifierOLIVEIRA, M. M. et al. Microcystin bioaccumulation in Limnoperna fortunei following Microcystis aeruginosa exposure, analysis of in vivo enzymatic phosphatase, acetylcholinesterase and carboxylesterase effects and in vitro experiments. Ecotoxicol. Environ. Contam., v. 16, n. 1, p. 35-43, 2021.
dc.identifier2317-9643
dc.identifierhttps://www.arca.fiocruz.br/handle/icict/49775
dc.identifier10.5132/eec.2021.01.05
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8862562
dc.descriptionToxic cyanobacteria blooms have been reported in freshwater sources worldwide and may lead to aquatic biota toxin accumulation and trophic chain transfer, resulting in ecological and public health concerns. To assess cyanobacteria effects on microcystin uptake and accumulation and on phosphatase, acethylcholinesterase (AChE) and carboxylesterase (CarbE) enzymatic activities, an in vivo experiment was carried out employing the golden mussel Limnoperna fortunei. These mussels were exposed to a Microcystis aeruginosa NPLJ-4 strain (NPLJ-4) for 48 hours at different cell densities. Subsequently, algal cell counts were carried out and enzymatic activities were assayed. All three enzymes (Phosphatase, AChE and CarbE) were inhibited at the end of the exposure experiment. Mussels exposed to higher in vivo M. aeruginosa densities exhibited microcystin uptake and accumulation. In vitro assays were also carried out, exposing soluble L. fortunei enzyme fractions to M. aeruginosa extracts containing microcystin, and phosphatase inhibition was observed, whereas acetylcholinesterase and carboxylesterase were not inhibited. The results indicate that metabolites other than mycrocystin probably caused the observed in vivo esterase inhibitions, requiring further investigations.
dc.formatapplication/pdf
dc.languageeng
dc.publisherEcotox Brasil
dc.rightsopen access
dc.subjectCianobactérias
dc.subjectColinesterases
dc.subjectCarboxylesterase
dc.subjectMexilhão dourado
dc.subjectMicrocistina
dc.subjectCyanobacteria
dc.subjectGolden mussel
dc.subjectCholinesterases
dc.subjectCarboxylesterase
dc.subjectMicrocystin
dc.titleMicrocystin bioaccumulation in Limnoperna fortunei following Microcystis aeruginosa exposure, analysis of in vivo enzymatic phosphatase, acetylcholinesterase and carboxylesterase effects and in vitro experiments
dc.typeArticle


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