Human glutathione-S-transferase pi potentiates the cysteine-protease activity of the Der p 1 allergen from house dust mite through a cysteine redox mechanism

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dc.contributor.authorLópez Rodríguez, Juan Carlos
dc.contributor.authorManosalva, Juliana
dc.contributor.authorCabrera-García, J. Daniel
dc.contributor.authorEscribese, María M.
dc.contributor.authorVillalba, Mayte
dc.contributor.authorBarber, Domingo
dc.contributor.authorMartínez Ruiz, Antonio
dc.contributor.authorBatanero Cremades, Eva
dc.date.accessioned2024-04-08T12:52:18Z
dc.date.available2024-04-08T12:52:18Z
dc.date.issued2019-09
dc.description.abstractEnvironmental proteases have been widely associated to the pathogenesis of allergic disorders. Der p 1, a cysteine-protease from house dust mite (HDM) Dermatophagoides pteronyssinus, constitutes one of the most clinically relevant indoor aeroallergens worldwide. Der p 1 protease activity depends on the redox status of its catalytic cysteine residue, which has to be in the reduced state to be active. So far, it is unknown whether Der p 1-protease activity could be regulated by host redox microenvironment once it reaches the lung epithelial lining fluid in addition to endogenous mite components. In this sense, Glutathione-S-transferase pi (GSTpi), an enzyme traditionally linked to phase II detoxification, is highly expressed in human lung epithelial cells, which represent the first line of defence against aeroallergens. Moreover, GSTpi is a generalist catalyst of protein S-glutathionylation reactions, and some polymorphic variants of this enzyme has been associated to the development of allergic asthma. Here, we showed that human GSTpi increased the cysteine-protease activity of Der p 1, while GSTmu (the isoenzyme produced by the mite) did not alter it. GSTpi induces the reduction of Cys residues in Der p 1, probably by rearranging its disulphide bridges. Furthermore, GSTpi was detected in the apical medium collected from human bronchial epithelial cell cultures, and more interesting, it increased cysteine-protease activity of Der p 1. Our findings support the role of human GSTpi from airways in modulating of Der p 1 cysteineprotease activity, which may have important clinical implications for immune response to this aeroallergen in genetically susceptible individuals.
dc.description.departmentDepto. de Bioquímica y Biología Molecular
dc.description.facultyFac. de Farmacia
dc.description.refereedTRUE
dc.description.sponsorshipSpanish Government
dc.description.sponsorshipEuropean Union ERDF
dc.description.statuspub
dc.identifier.doi10.1016/j.redox.2019.101256
dc.identifier.issn2213-2317
dc.identifier.officialurlhttps://www.sciencedirect.com/science/article/pii/S2213231719304744
dc.identifier.urihttps://hdl.handle.net/20.500.14352/102830
dc.journal.titleRedox Biology
dc.language.isoeng
dc.relation.projectIDSAF2014-53209-R
dc.relation.projectIDinfo:eu-repo/grantAgreement/MINECO//PI15%2F00107/ES/Señalización en hipoxia por especies reactivas de oxígeno, y proteómica redox: de los mecanismos moleculares a las aplicaciones clínicas/
dc.relation.projectIDinfo:eu-repo/grantAgreement/MINECO//PI15%2F02256/ES/Identificación de biomarcadores asociados con el proceso de remodelado epitelial en asma alérgico/
dc.relation.projectIDinfo:eu-repo/grantAgreement/MINECO//PI16%2F00249/ES/BUSQUEDA DE BIOMARCADORES Y DESARROLLO DE NUEVAS ESTRATEGIAS DE DIAGNOSTICO Y TRATAMIENTO DE PACIENTES ALERGICOS DE FENOTIPO GRAVE/
dc.relation.projectIDinfo:eu-repo/grantAgreement/MINECO//RD16%2F0006%2F0014/ES/Asma, Reacciones Adversas y Alérgicas (ARADYAL)/
dc.relation.projectIDinfo:eu-repo/grantAgreement/MINECO//RD16%2F0006%2F0015/ES/Asma, Reacciones Adversas y Alérgicas (ARADYAL)/
dc.relation.projectIDinfo:eu-repo/grantAgreement/MECD//FPU13%2F02393/ES/FPU13%2F02393/
dc.relation.projectIDPRB3-ISCIII
dc.relation.projectIDinfo:eu-repo/grantAgreement/MINECO//PT13%2F0001%2F0024/ES/Plataforma de recursos biomoleculares y bioinformaticos/
dc.relation.projectIDPT17/0019/0018
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internationalen
dc.rights.accessRightsopen access
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subject.cdu577.1
dc.subject.cdu577.2
dc.subject.keywordHouse dust mite
dc.subject.keywordAllergen
dc.subject.keywordCysteine-protease
dc.subject.keywordDer p 1
dc.subject.keywordGSTmu
dc.subject.keywordGSTpi
dc.subject.ucmBioquímica (Farmacia)
dc.subject.ucmBiología molecular (Farmacia)
dc.subject.unesco2302 Bioquímica
dc.titleHuman glutathione-S-transferase pi potentiates the cysteine-protease activity of the Der p 1 allergen from house dust mite through a cysteine redox mechanism
dc.typejournal article
dc.type.hasVersionAM
dc.volume.number26
dspace.entity.typePublication
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relation.isAuthorOfPublicationeec0b303-34c9-47dd-9ec6-704b6c6c7acd
relation.isAuthorOfPublication862e3690-e517-4123-8c8f-41ed416ffe4c
relation.isAuthorOfPublication.latestForDiscoveryb9515131-fd92-4e57-923d-84da1d3bc75e
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