Presence of N-acetylgalactosamine/galactose residues on bronchioloalveolar cells during rat postnatal development

Detalhes bibliográficos
Autor(a) principal: Martins, Maria de Fátima
Data de Publicação: 2019
Outros Autores: Martins, Paula, Gonçalves, Carlos Alberto
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10316/106890
https://doi.org/10.4081/ejh.2019.3040
Resumo: In mammals, the alveolarization process develops predominantly after birth. Airway cells display a complex assemblage of glycans on their surface. These glycans, particularly terminal glycan extensions, are important effective carriers of information that change during the differentiation process. Nevertheless, few systematic data are reported about the cell surface sugar residue content during post-natal lung development. In the present work, we aimed to identify and semi-quantify N-acetylgalactosamine (GalNAc)/galactose (Gal) residues on the bronchioloalveolar cell surface in rat lung sections from 1-, 4-, 8- day old and adult animals and link these data with the lung glycocalyx composition. Horseradish peroxidase-conjugated lectin from Glycine max (soybean agglutinin, SBA) was used, and light microscopy methodologies were performed. SBA labelling intensity was studied before and after sialidase pre-treatment, at one-, four- and eight-day-old animals and adult animals. For semi-quantitative evaluation of SBA binding intensity, two investigators performed the analysis independently, blinded to the type of experiment. Reactivity of the lectin was assessed in bronchiolar and respiratory portion/alveolar epithelial cell surfaces. We evidenced a stronger positive reaction when lung sections were pre-treated with neuraminidase before incubation with the lectin in one- and four-day-old animals and adult animals. These results were not so manifest in eight-day-old animals. This binding pattern, generally points towards the presence of terminal but mainly sub-terminal GalNAc/Gal residues probably capped by sialic acids on the rat bronchiolar/respiratory tract epithelial cells. As this glycan extension is common in O- and N-glycans, our results suggest that these glycan classes can be present in bronchioloalveolar cells immediately after birth and exist during the postnatal period. The results observed in eight-day-old rat lung sections may be due to the dramatic lung morphologic changes and the possible underlying biological mechanisms that occur during this age-moment.
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spelling Presence of N-acetylgalactosamine/galactose residues on bronchioloalveolar cells during rat postnatal developmentBronchioloalveolar cellsN-acetylgalactosamine (GalNAc)/galactose (Gal) residuesratAcetylgalactosamineAnimalsBronchiEpithelial CellsFemaleGalactoseHistocytochemistryHorseradish PeroxidaseNeuraminidasePlant LectinsPregnancyPulmonary AlveoliRats, WistarSoybean ProteinsIn mammals, the alveolarization process develops predominantly after birth. Airway cells display a complex assemblage of glycans on their surface. These glycans, particularly terminal glycan extensions, are important effective carriers of information that change during the differentiation process. Nevertheless, few systematic data are reported about the cell surface sugar residue content during post-natal lung development. In the present work, we aimed to identify and semi-quantify N-acetylgalactosamine (GalNAc)/galactose (Gal) residues on the bronchioloalveolar cell surface in rat lung sections from 1-, 4-, 8- day old and adult animals and link these data with the lung glycocalyx composition. Horseradish peroxidase-conjugated lectin from Glycine max (soybean agglutinin, SBA) was used, and light microscopy methodologies were performed. SBA labelling intensity was studied before and after sialidase pre-treatment, at one-, four- and eight-day-old animals and adult animals. For semi-quantitative evaluation of SBA binding intensity, two investigators performed the analysis independently, blinded to the type of experiment. Reactivity of the lectin was assessed in bronchiolar and respiratory portion/alveolar epithelial cell surfaces. We evidenced a stronger positive reaction when lung sections were pre-treated with neuraminidase before incubation with the lectin in one- and four-day-old animals and adult animals. These results were not so manifest in eight-day-old animals. This binding pattern, generally points towards the presence of terminal but mainly sub-terminal GalNAc/Gal residues probably capped by sialic acids on the rat bronchiolar/respiratory tract epithelial cells. As this glycan extension is common in O- and N-glycans, our results suggest that these glycan classes can be present in bronchioloalveolar cells immediately after birth and exist during the postnatal period. The results observed in eight-day-old rat lung sections may be due to the dramatic lung morphologic changes and the possible underlying biological mechanisms that occur during this age-moment.PagePress2019-09-11info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttp://hdl.handle.net/10316/106890http://hdl.handle.net/10316/106890https://doi.org/10.4081/ejh.2019.3040eng2038-83061121-760XMartins, Maria de FátimaMartins, PaulaGonçalves, Carlos Albertoinfo: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:RCAAP2023-04-28T11:52:48Zoai:estudogeral.uc.pt:10316/106890Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T21:23:17.450565Repositório 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 Presence of N-acetylgalactosamine/galactose residues on bronchioloalveolar cells during rat postnatal development
title Presence of N-acetylgalactosamine/galactose residues on bronchioloalveolar cells during rat postnatal development
spellingShingle Presence of N-acetylgalactosamine/galactose residues on bronchioloalveolar cells during rat postnatal development
Martins, Maria de Fátima
Bronchioloalveolar cells
N-acetylgalactosamine (GalNAc)/galactose (Gal) residues
rat
Acetylgalactosamine
Animals
Bronchi
Epithelial Cells
Female
Galactose
Histocytochemistry
Horseradish Peroxidase
Neuraminidase
Plant Lectins
Pregnancy
Pulmonary Alveoli
Rats, Wistar
Soybean Proteins
title_short Presence of N-acetylgalactosamine/galactose residues on bronchioloalveolar cells during rat postnatal development
title_full Presence of N-acetylgalactosamine/galactose residues on bronchioloalveolar cells during rat postnatal development
title_fullStr Presence of N-acetylgalactosamine/galactose residues on bronchioloalveolar cells during rat postnatal development
title_full_unstemmed Presence of N-acetylgalactosamine/galactose residues on bronchioloalveolar cells during rat postnatal development
title_sort Presence of N-acetylgalactosamine/galactose residues on bronchioloalveolar cells during rat postnatal development
author Martins, Maria de Fátima
author_facet Martins, Maria de Fátima
Martins, Paula
Gonçalves, Carlos Alberto
author_role author
author2 Martins, Paula
Gonçalves, Carlos Alberto
author2_role author
author
dc.contributor.author.fl_str_mv Martins, Maria de Fátima
Martins, Paula
Gonçalves, Carlos Alberto
dc.subject.por.fl_str_mv Bronchioloalveolar cells
N-acetylgalactosamine (GalNAc)/galactose (Gal) residues
rat
Acetylgalactosamine
Animals
Bronchi
Epithelial Cells
Female
Galactose
Histocytochemistry
Horseradish Peroxidase
Neuraminidase
Plant Lectins
Pregnancy
Pulmonary Alveoli
Rats, Wistar
Soybean Proteins
topic Bronchioloalveolar cells
N-acetylgalactosamine (GalNAc)/galactose (Gal) residues
rat
Acetylgalactosamine
Animals
Bronchi
Epithelial Cells
Female
Galactose
Histocytochemistry
Horseradish Peroxidase
Neuraminidase
Plant Lectins
Pregnancy
Pulmonary Alveoli
Rats, Wistar
Soybean Proteins
description In mammals, the alveolarization process develops predominantly after birth. Airway cells display a complex assemblage of glycans on their surface. These glycans, particularly terminal glycan extensions, are important effective carriers of information that change during the differentiation process. Nevertheless, few systematic data are reported about the cell surface sugar residue content during post-natal lung development. In the present work, we aimed to identify and semi-quantify N-acetylgalactosamine (GalNAc)/galactose (Gal) residues on the bronchioloalveolar cell surface in rat lung sections from 1-, 4-, 8- day old and adult animals and link these data with the lung glycocalyx composition. Horseradish peroxidase-conjugated lectin from Glycine max (soybean agglutinin, SBA) was used, and light microscopy methodologies were performed. SBA labelling intensity was studied before and after sialidase pre-treatment, at one-, four- and eight-day-old animals and adult animals. For semi-quantitative evaluation of SBA binding intensity, two investigators performed the analysis independently, blinded to the type of experiment. Reactivity of the lectin was assessed in bronchiolar and respiratory portion/alveolar epithelial cell surfaces. We evidenced a stronger positive reaction when lung sections were pre-treated with neuraminidase before incubation with the lectin in one- and four-day-old animals and adult animals. These results were not so manifest in eight-day-old animals. This binding pattern, generally points towards the presence of terminal but mainly sub-terminal GalNAc/Gal residues probably capped by sialic acids on the rat bronchiolar/respiratory tract epithelial cells. As this glycan extension is common in O- and N-glycans, our results suggest that these glycan classes can be present in bronchioloalveolar cells immediately after birth and exist during the postnatal period. The results observed in eight-day-old rat lung sections may be due to the dramatic lung morphologic changes and the possible underlying biological mechanisms that occur during this age-moment.
publishDate 2019
dc.date.none.fl_str_mv 2019-09-11
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/10316/106890
http://hdl.handle.net/10316/106890
https://doi.org/10.4081/ejh.2019.3040
url http://hdl.handle.net/10316/106890
https://doi.org/10.4081/ejh.2019.3040
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 2038-8306
1121-760X
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
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dc.publisher.none.fl_str_mv PagePress
publisher.none.fl_str_mv PagePress
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron:RCAAP
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
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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)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
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