Pollen Proteases Play Multiple Roles in Allergic Disorders

Detalhes bibliográficos
Autor(a) principal: Gaspar, Ricardo
Data de Publicação: 2020
Outros Autores: Matos, Mafalda Ramos de, Cortes, Luísa, Nunes-Correia, Isabel, Todo-Bom, Ana, Pires, Euclides, Veríssimo, Paula
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10316/106210
https://doi.org/10.3390/ijms21103578
Resumo: Allergic diseases are a major health concern worldwide. Pollens are important triggers for allergic rhinitis, conjunctivitis and asthma. Proteases released upon pollen grain hydration appear to play a major role in the typical immunological and inflammatory responses that occur in patients with allergic disorders. In this study, we aimed to identify specific proteolytic activity in a set of pollens with diverse allergenic potential. Diffusates from Chenopodium album, Plantago lanceolata and Eucalyptus globulus were added to a confluent monolayer of Calu-3 cells grown in an air-liquid interface system. We identified serine proteases and metalloproteinases in all pollen diffusates investigated. Proteases found in these pollen diffusates were shown to compromise the integrity of the lung epithelial barrier by disrupting transmembrane adhesion proteins E-cadherin, claudin-1 and Occludin, as well as, the cytosolic complex zonula occludens-1 (ZO-1) resulting in a time-dependent increase in transepithelial permeability. Tight junction disruption and increased transepithelial permeability facilitates allergen exposure to epithelial sub-layers contributing to the sensitization to a wide range of allergens. These pollen extracts also induced an increase in the release of interleukin 6 (IL-6) and interleukin 8 (IL-8) cytokines measured by flow cytometry possibly as a result of the activation of protease-activated receptors 2 (PAR-2).
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spelling Pollen Proteases Play Multiple Roles in Allergic Disordersallergypollen proteasestransepithelial permeabilityIL-6IL-8 and PAR-2Cell LineChenopodiumEucalyptusHumansHypersensitivityInterleukin-6Interleukin-8Peptide HydrolasesPlantagoPollenReceptor, PAR-2WaterAllergic diseases are a major health concern worldwide. Pollens are important triggers for allergic rhinitis, conjunctivitis and asthma. Proteases released upon pollen grain hydration appear to play a major role in the typical immunological and inflammatory responses that occur in patients with allergic disorders. In this study, we aimed to identify specific proteolytic activity in a set of pollens with diverse allergenic potential. Diffusates from Chenopodium album, Plantago lanceolata and Eucalyptus globulus were added to a confluent monolayer of Calu-3 cells grown in an air-liquid interface system. We identified serine proteases and metalloproteinases in all pollen diffusates investigated. Proteases found in these pollen diffusates were shown to compromise the integrity of the lung epithelial barrier by disrupting transmembrane adhesion proteins E-cadherin, claudin-1 and Occludin, as well as, the cytosolic complex zonula occludens-1 (ZO-1) resulting in a time-dependent increase in transepithelial permeability. Tight junction disruption and increased transepithelial permeability facilitates allergen exposure to epithelial sub-layers contributing to the sensitization to a wide range of allergens. These pollen extracts also induced an increase in the release of interleukin 6 (IL-6) and interleukin 8 (IL-8) cytokines measured by flow cytometry possibly as a result of the activation of protease-activated receptors 2 (PAR-2).MDPI2020-05-19info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://hdl.handle.net/10316/106210http://hdl.handle.net/10316/106210https://doi.org/10.3390/ijms21103578eng1422-0067Gaspar, RicardoMatos, Mafalda Ramos deCortes, LuísaNunes-Correia, IsabelTodo-Bom, AnaPires, EuclidesVeríssimo, Paulainfo:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-03-24T21:34:00Zoai:estudogeral.uc.pt:10316/106210Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T21:22:42.014556Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Pollen Proteases Play Multiple Roles in Allergic Disorders
title Pollen Proteases Play Multiple Roles in Allergic Disorders
spellingShingle Pollen Proteases Play Multiple Roles in Allergic Disorders
Gaspar, Ricardo
allergy
pollen proteases
transepithelial permeability
IL-6
IL-8 and PAR-2
Cell Line
Chenopodium
Eucalyptus
Humans
Hypersensitivity
Interleukin-6
Interleukin-8
Peptide Hydrolases
Plantago
Pollen
Receptor, PAR-2
Water
title_short Pollen Proteases Play Multiple Roles in Allergic Disorders
title_full Pollen Proteases Play Multiple Roles in Allergic Disorders
title_fullStr Pollen Proteases Play Multiple Roles in Allergic Disorders
title_full_unstemmed Pollen Proteases Play Multiple Roles in Allergic Disorders
title_sort Pollen Proteases Play Multiple Roles in Allergic Disorders
author Gaspar, Ricardo
author_facet Gaspar, Ricardo
Matos, Mafalda Ramos de
Cortes, Luísa
Nunes-Correia, Isabel
Todo-Bom, Ana
Pires, Euclides
Veríssimo, Paula
author_role author
author2 Matos, Mafalda Ramos de
Cortes, Luísa
Nunes-Correia, Isabel
Todo-Bom, Ana
Pires, Euclides
Veríssimo, Paula
author2_role author
author
author
author
author
author
dc.contributor.author.fl_str_mv Gaspar, Ricardo
Matos, Mafalda Ramos de
Cortes, Luísa
Nunes-Correia, Isabel
Todo-Bom, Ana
Pires, Euclides
Veríssimo, Paula
dc.subject.por.fl_str_mv allergy
pollen proteases
transepithelial permeability
IL-6
IL-8 and PAR-2
Cell Line
Chenopodium
Eucalyptus
Humans
Hypersensitivity
Interleukin-6
Interleukin-8
Peptide Hydrolases
Plantago
Pollen
Receptor, PAR-2
Water
topic allergy
pollen proteases
transepithelial permeability
IL-6
IL-8 and PAR-2
Cell Line
Chenopodium
Eucalyptus
Humans
Hypersensitivity
Interleukin-6
Interleukin-8
Peptide Hydrolases
Plantago
Pollen
Receptor, PAR-2
Water
description Allergic diseases are a major health concern worldwide. Pollens are important triggers for allergic rhinitis, conjunctivitis and asthma. Proteases released upon pollen grain hydration appear to play a major role in the typical immunological and inflammatory responses that occur in patients with allergic disorders. In this study, we aimed to identify specific proteolytic activity in a set of pollens with diverse allergenic potential. Diffusates from Chenopodium album, Plantago lanceolata and Eucalyptus globulus were added to a confluent monolayer of Calu-3 cells grown in an air-liquid interface system. We identified serine proteases and metalloproteinases in all pollen diffusates investigated. Proteases found in these pollen diffusates were shown to compromise the integrity of the lung epithelial barrier by disrupting transmembrane adhesion proteins E-cadherin, claudin-1 and Occludin, as well as, the cytosolic complex zonula occludens-1 (ZO-1) resulting in a time-dependent increase in transepithelial permeability. Tight junction disruption and increased transepithelial permeability facilitates allergen exposure to epithelial sub-layers contributing to the sensitization to a wide range of allergens. These pollen extracts also induced an increase in the release of interleukin 6 (IL-6) and interleukin 8 (IL-8) cytokines measured by flow cytometry possibly as a result of the activation of protease-activated receptors 2 (PAR-2).
publishDate 2020
dc.date.none.fl_str_mv 2020-05-19
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/10316/106210
http://hdl.handle.net/10316/106210
https://doi.org/10.3390/ijms21103578
url http://hdl.handle.net/10316/106210
https://doi.org/10.3390/ijms21103578
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 1422-0067
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publisher.none.fl_str_mv MDPI
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reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
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