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

Environmental 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...

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Authors: López Rodríguez, Juan Carlos, Manosalva, Juliana, Cabrera-García, J. Daniel, Escribese, María M., Villalba, Mayte, Barber, Domingo, Martínez Ruiz, Antonio, Batanero Cremades, Eva
Format: article
Publication Date:2019
Country:España
Institution:Universidad Complutense de Madrid (UCM)
Repository:Docta Complutense
Language:English
OAI Identifier:oai:docta.ucm.es:20.500.14352/102830
Online Access:https://hdl.handle.net/20.500.14352/102830
Access Level:Open access
Keyword:577.1
577.2
House dust mite
Allergen
Cysteine-protease
Der p 1
GSTmu
GSTpi
Bioquímica (Farmacia)
Biología molecular (Farmacia)
2302 Bioquímica
id ES_6f14335900a46fb90467cbafdc0e3efe
oai_identifier_str oai:docta.ucm.es:20.500.14352/102830
network_acronym_str ES
network_name_str España
repository_id_str
spelling Human glutathione-S-transferase pi potentiates the cysteine-protease activity of the Der p 1 allergen from house dust mite through a cysteine redox mechanismLópez Rodríguez, Juan CarlosManosalva, JulianaCabrera-García, J. DanielEscribese, María M.Villalba, MayteBarber, DomingoMartínez Ruiz, AntonioBatanero Cremades, Eva577.1577.2House dust miteAllergenCysteine-proteaseDer p 1GSTmuGSTpiBioquímica (Farmacia)Biología molecular (Farmacia)2302 BioquímicaEnvironmental 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.Universidad Complutense de Madrid20192019-09-0120192019-09-01journal articlehttp://purl.org/coar/resource_type/c_6501AMhttp://purl.org/coar/version/c_ab4af688f83e57aainfo:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/20.500.14352/102830reponame:Docta Complutenseinstname:Universidad Complutense de Madrid (UCM)Inglésengopen accesshttp://purl.org/coar/access_right/c_abf2Attribution-NonCommercial-NoDerivatives 4.0 Internationalhttp://creativecommons.org/licenses/by-nc-nd/4.0/info:eu-repo/semantics/openAccessoai:docta.ucm.es:20.500.14352/1028302026-06-02T12:44:21Z
dc.title.none.fl_str_mv 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
title 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
spellingShingle 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
López Rodríguez, Juan Carlos
577.1
577.2
House dust mite
Allergen
Cysteine-protease
Der p 1
GSTmu
GSTpi
Bioquímica (Farmacia)
Biología molecular (Farmacia)
2302 Bioquímica
title_short 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
title_full 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
title_fullStr 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
title_full_unstemmed 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
title_sort 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
dc.creator.none.fl_str_mv López Rodríguez, Juan Carlos
Manosalva, Juliana
Cabrera-García, J. Daniel
Escribese, María M.
Villalba, Mayte
Barber, Domingo
Martínez Ruiz, Antonio
Batanero Cremades, Eva
author López Rodríguez, Juan Carlos
author_facet López Rodríguez, Juan Carlos
Manosalva, Juliana
Cabrera-García, J. Daniel
Escribese, María M.
Villalba, Mayte
Barber, Domingo
Martínez Ruiz, Antonio
Batanero Cremades, Eva
author_role author
author2 Manosalva, Juliana
Cabrera-García, J. Daniel
Escribese, María M.
Villalba, Mayte
Barber, Domingo
Martínez Ruiz, Antonio
Batanero Cremades, Eva
author2_role author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidad Complutense de Madrid
dc.subject.none.fl_str_mv 577.1
577.2
House dust mite
Allergen
Cysteine-protease
Der p 1
GSTmu
GSTpi
Bioquímica (Farmacia)
Biología molecular (Farmacia)
2302 Bioquímica
topic 577.1
577.2
House dust mite
Allergen
Cysteine-protease
Der p 1
GSTmu
GSTpi
Bioquímica (Farmacia)
Biología molecular (Farmacia)
2302 Bioquímica
description Environmental 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.
publishDate 2019
dc.date.none.fl_str_mv 2019
2019-09-01
2019
2019-09-01
dc.type.none.fl_str_mv journal article
http://purl.org/coar/resource_type/c_6501
AM
http://purl.org/coar/version/c_ab4af688f83e57aa
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv https://hdl.handle.net/20.500.14352/102830
url https://hdl.handle.net/20.500.14352/102830
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
Attribution-NonCommercial-NoDerivatives 4.0 International
http://creativecommons.org/licenses/by-nc-nd/4.0/
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
Attribution-NonCommercial-NoDerivatives 4.0 International
http://creativecommons.org/licenses/by-nc-nd/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:Docta Complutense
instname:Universidad Complutense de Madrid (UCM)
instname_str Universidad Complutense de Madrid (UCM)
reponame_str Docta Complutense
collection Docta Complutense
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15.300719

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