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Small heat shock proteins as relevant biomarkers for anthropogenic stressors in earthworms

dc.contributor.authorTilikj, Natasha
dc.contributor.authorFuente, Mercedes de la
dc.contributor.authorMuñiz-González, Ana Belén
dc.contributor.authorMartínez-Guitarte, José Luis
dc.contributor.authorCaballero-Carretero, Patricia
dc.contributor.authorNovo Rodríguez, Marta
dc.date.accessioned2025-01-21T17:05:37Z
dc.date.available2025-01-21T17:05:37Z
dc.date.issued2024-11-23
dc.descriptionWe would like to thank the members of the Soil Zoology Group from Complutense University of Madrid for laboratory support. MN was supported by a Ramón y Cajal Fellowship (RYC2018-024654-I), and this study was funded by grants PGC2018-094112-A-I00 and PID2021-122243NB-I00, from MCIN/AEI/10.13039/501100011033 and by “ESF: Investing in your future” and “ERDF: A way of making Europe”.
dc.description.abstractAnthropogenic stressors in terrestrial ecosystems require focused research on adaptive responses in soil organisms such as Eisenia fetida, a model earthworm species. We analyzed the gene expression of five small heat shock proteins (sHSPs) in response to various stressors: heat stress (31 and 35 °C), desiccation (10 % and 20 % humidity), and chemical exposure (bisphenol A and endosulfan) under standard and elevated temperatures. Under moderate heat (31 °C), early upregulation of sHSP transcripts suggests their involvement in initial stress responses, possibly mitigating protein aggregation. At the higher temperature (35 °C), three sHSPs served as a defense against severe protein aggregation, a significant finding as previous studies identified only one activated heat shock protein (HSP70) in E. fetida under similar conditions. Desiccation stress at 10 % humidity activated more sHSPs than at 20 % humidity, and the expression profile at 10 % humidity closely resembled that observed under heat stress, suggesting overlapping adaptation pathways. Heat combined with chemical stress, particularly endosulfan, elevated sHSP transcription and underscored the potential of these proteins as biomarkers in multi-stressor environments. Monomeric sHSPs from E. fetida, which share homology with human sHSPs, showed the highest activity across all stressors, suggesting their key role in earthworm adaptation.
dc.description.departmentDepto. de Biodiversidad, Ecología y Evolución
dc.description.facultyFac. de Ciencias Biológicas
dc.description.refereedTRUE
dc.description.sponsorshipMinisterio de Ciencia e Innovación (España)
dc.description.statuspub
dc.identifier.citationTilikj, N., De La Fuente, M., Muñiz-González, A. B., Martínez-Guitarte, J.-L., Caballero-Carretero, P., & Novo, M. (2025). Small heat shock proteins as relevant biomarkers for anthropogenic stressors in earthworms. Comparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology, 300, 111785. https://doi.org/10.1016/j.cbpa.2024.111785
dc.identifier.doi10.1016/j.cbpa.2024.111785
dc.identifier.essn1531-4332
dc.identifier.issn1095-6433
dc.identifier.officialurlhttps://doi.org/10.1016/j.cbpa.2024.111785
dc.identifier.urihttps://hdl.handle.net/20.500.14352/115451
dc.journal.titleComparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology
dc.language.isoeng
dc.publisherElsevier
dc.relation.projectIDinfo:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/PGC2018-094112-A-I00/ES/FUTUROS DESAFIOS EN ECOSISTEMAS EDAFICOS: APROXIMACION MOLECULAR AL ESTUDIO DE LA ADAPTACION DE LOMBRICES DE TIERRA AL CAMBIO CLIMATICO/
dc.rights.accessRightsrestricted access
dc.subject.cdu577.1
dc.subject.cdu574
dc.subject.cdu591.5
dc.subject.cdu595.14
dc.subject.cdu502.7
dc.subject.keywordAnthropogenic stress
dc.subject.keywordInvertebrates
dc.subject.keywordBiomarkers
dc.subject.keywordHeat shock proteins
dc.subject.keywordAdaptation
dc.subject.ucmEcología (Biología)
dc.subject.unesco2401.06 Ecología Animal
dc.titleSmall heat shock proteins as relevant biomarkers for anthropogenic stressors in earthworms
dc.typejournal article
dc.type.hasVersionVoR
dc.volume.number300
dspace.entity.typePublication
relation.isAuthorOfPublicationb13cb4ea-7e39-42c2-ba90-cf245d4f30bb
relation.isAuthorOfPublicationbfd879cc-7de6-436d-9014-ade424850638
relation.isAuthorOfPublication.latestForDiscoveryb13cb4ea-7e39-42c2-ba90-cf245d4f30bb

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