Characterisation of plasmatic B-esterases in bottlenose dolphins (Tursiops truncatus) and their potential as biomarkers of xenobiotic chemical exposures

Characterisation of plasmatic B-esterases in bottlenose dolphins (Tursiops truncatus) and their potential as biomarkers of xenobiotic chemical exposures

9 pages, 5 pages, 3 figures, supplementary data https://doi.org/10.1016/j.envpol.2022.120149.-- Data availability: Data will be made available on request

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Bibliographic Details
Main Authors: Solé, Montserrat, Figueres, E., Mañanós, Evaristo L., Rojo-Solís, C., García-Parraga, Daniel
Other Authors: Agencia Estatal de Investigación (España)
Format: artículo biblioteca
Language:English
Published: Elsevier 2022-11
Subjects:Cholinesterases, Carboxylesterases, Marine mammals, Plasma, Albumin,
Online Access:http://hdl.handle.net/10261/281795
http://dx.doi.org/10.13039/501100011033
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spelling dig-icm-es-10261-2817952022-11-04T17:47:46Z Characterisation of plasmatic B-esterases in bottlenose dolphins (Tursiops truncatus) and their potential as biomarkers of xenobiotic chemical exposures Solé, Montserrat Figueres, E. Mañanós, Evaristo L. Rojo-Solís, C. García-Parraga, Daniel Agencia Estatal de Investigación (España) Cholinesterases Carboxylesterases Marine mammals Plasma Albumin 9 pages, 5 pages, 3 figures, supplementary data https://doi.org/10.1016/j.envpol.2022.120149.-- Data availability: Data will be made available on request A total of 164 blood samples from 16 clinically healthy bottlenose dolphins (Tursiops truncatus), were obtained from an aquarium in Spain between 2019 and 2020, as part of their preventive medicine protocol. In addition to conventional haematological and biochemical analyses, plasmatic B-esterase activities were characterised to determine the potential application of such analyses in wild counterparts. The hydrolysis rates for the substrates of acetylcholinesterase (AChE), butyrylcholinesterase (BuChE) and carboxylesterase (CE) activity in plasma were measured, the last using two commercial substrates, p-nitrophenyl acetate (pNPA) and p-nitrophenyl butyrate (pNPB). Activity rates (mean ± SEM in nmol/min/mL plasma) were (in descending order): AChE (125.6 ± 3.8), pNPB-CE (65.0 ± 2.2), pNPA-CE (49.7 ± 1.1) and BuChE (12.8 ± 1.3). These values for dolphins are reported in here for the first time in this species. Additionally, the in vitro sensitivity of two B-esterases (AChE and pNPB-CE) to chemicals of environmental concern was determined, and the protective role of plasmatic albumin assessed. Out of the B-esterases measured in plasma of dolphin, AChE activity was more responsive in vitro to pesticides, while CEs had a low response to plastic additives, likely due to the protective presence of albumin. However, the clear in vitro interaction of these environmental chemicals with purified AChE from electric eels and recombinant human hCEs (hCE1 and hCE2) and albumin, predicts their impact in other tissues that require in vivo validation. A relationship between esterase-like activities and health parameters in terrestrial mammals has already been established. Thus, B-esterase measures could be easily included in marine mammal health assessment protocols for dolphins as well, once the relationship between these measures and the animal's fitness has been established To the institutional support of the ‘Severo Ochoa Centre of Excellence’ accreditation (CEX2019-000928-S) Peer reviewed 2022-10-28T09:16:22Z 2022-10-28T09:16:22Z 2022-11 artículo Environmental Pollution 313: 120149 (2022) 0269-7491 CEX2019-000928-S http://hdl.handle.net/10261/281795 10.1016/j.envpol.2022.120149 1873-6424 http://dx.doi.org/10.13039/501100011033 en Publisher's version https://doi.org/10.1016/j.envpol.2022.120149 Sí open Elsevier
institution ICM ES
collection DSpace
country España
countrycode ES
component Bibliográfico
access En linea
databasecode dig-icm-es
tag biblioteca
region Europa del Sur
libraryname Biblioteca del ICM España
language English
topic Cholinesterases
Carboxylesterases
Marine mammals
Plasma
Albumin
Cholinesterases
Carboxylesterases
Marine mammals
Plasma
Albumin
spellingShingle Cholinesterases
Carboxylesterases
Marine mammals
Plasma
Albumin
Cholinesterases
Carboxylesterases
Marine mammals
Plasma
Albumin
Solé, Montserrat
Figueres, E.
Mañanós, Evaristo L.
Rojo-Solís, C.
García-Parraga, Daniel
Characterisation of plasmatic B-esterases in bottlenose dolphins (Tursiops truncatus) and their potential as biomarkers of xenobiotic chemical exposures
description 9 pages, 5 pages, 3 figures, supplementary data https://doi.org/10.1016/j.envpol.2022.120149.-- Data availability: Data will be made available on request
author2 Agencia Estatal de Investigación (España)
author_facet Agencia Estatal de Investigación (España)
Solé, Montserrat
Figueres, E.
Mañanós, Evaristo L.
Rojo-Solís, C.
García-Parraga, Daniel
format artículo
topic_facet Cholinesterases
Carboxylesterases
Marine mammals
Plasma
Albumin
author Solé, Montserrat
Figueres, E.
Mañanós, Evaristo L.
Rojo-Solís, C.
García-Parraga, Daniel
author_sort Solé, Montserrat
title Characterisation of plasmatic B-esterases in bottlenose dolphins (Tursiops truncatus) and their potential as biomarkers of xenobiotic chemical exposures
title_short Characterisation of plasmatic B-esterases in bottlenose dolphins (Tursiops truncatus) and their potential as biomarkers of xenobiotic chemical exposures
title_full Characterisation of plasmatic B-esterases in bottlenose dolphins (Tursiops truncatus) and their potential as biomarkers of xenobiotic chemical exposures
title_fullStr Characterisation of plasmatic B-esterases in bottlenose dolphins (Tursiops truncatus) and their potential as biomarkers of xenobiotic chemical exposures
title_full_unstemmed Characterisation of plasmatic B-esterases in bottlenose dolphins (Tursiops truncatus) and their potential as biomarkers of xenobiotic chemical exposures
title_sort characterisation of plasmatic b-esterases in bottlenose dolphins (tursiops truncatus) and their potential as biomarkers of xenobiotic chemical exposures
publisher Elsevier
publishDate 2022-11
url http://hdl.handle.net/10261/281795
http://dx.doi.org/10.13039/501100011033
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