Staining of E-selectin ligands on paraffin-embedded sections of tumor tissue

Detalhes bibliográficos
Autor(a) principal: Carrascal, MA
Data de Publicação: 2018
Outros Autores: Talina, C, Borralho, P, Gonçalo Mineiro, A, Henriques, AR, Pen, C, Martins, M, Braga, S, Sackstein, R, Videira, PA
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10400.26/22793
Resumo: BACKGROUND: The E-selectin ligands expressed by cancer cells mediate adhesion of circulating cancer cells to endothelial cells, as well as within tissue microenvironments important for tumor progression and metastasis. The identification of E-selectin ligands within cancer tissue could yield new biomarkers for patient stratification and aid in identifying novel therapeutic targets. The determinants of selectin ligands consist of sialylated tetrasaccharides, the sialyl Lewis X and A (sLeX and sLeA), displayed on protein or lipid scaffolds. Standardized procedures for immunohistochemistry make use of the antibodies against sLeX and/or sLeA. However, antibody binding does not define E-selectin binding activity. METHODS: In this study, we developed an immunohistochemical staining technique, using E-selectin-human Ig Fc chimera (E-Ig) to characterize the expression and localization of E-selectin binding sites on paraffin-embedded sections of different cancer tissue. RESULTS: E-Ig successfully stained cancer cells with high specificity. The E-Ig staining show high reactivity scores in colon and lung adenocarcinoma and moderate reactivity in triple negative breast cancer. Compared with reactivity of antibody against sLeX/A, the E-Ig staining presented higher specificity to cancer tissue with better defined borders and less background. CONCLUSIONS: The E-Ig staining technique allows the qualitative and semi-quantitative analysis of E-selectin binding activity on cancer cells. The development of accurate techniques for detection of selectin ligands may contribute to better diagnostic and better understanding of the molecular basis of tumor progression and metastasis.
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spelling Staining of E-selectin ligands on paraffin-embedded sections of tumor tissueNeoplasiasSelectina EInclusão em ParafinaInclusão do TecidoTissue EmbeddingE-SelectinParaffin EmbeddingNeoplasmsBACKGROUND: The E-selectin ligands expressed by cancer cells mediate adhesion of circulating cancer cells to endothelial cells, as well as within tissue microenvironments important for tumor progression and metastasis. The identification of E-selectin ligands within cancer tissue could yield new biomarkers for patient stratification and aid in identifying novel therapeutic targets. The determinants of selectin ligands consist of sialylated tetrasaccharides, the sialyl Lewis X and A (sLeX and sLeA), displayed on protein or lipid scaffolds. Standardized procedures for immunohistochemistry make use of the antibodies against sLeX and/or sLeA. However, antibody binding does not define E-selectin binding activity. METHODS: In this study, we developed an immunohistochemical staining technique, using E-selectin-human Ig Fc chimera (E-Ig) to characterize the expression and localization of E-selectin binding sites on paraffin-embedded sections of different cancer tissue. RESULTS: E-Ig successfully stained cancer cells with high specificity. The E-Ig staining show high reactivity scores in colon and lung adenocarcinoma and moderate reactivity in triple negative breast cancer. Compared with reactivity of antibody against sLeX/A, the E-Ig staining presented higher specificity to cancer tissue with better defined borders and less background. CONCLUSIONS: The E-Ig staining technique allows the qualitative and semi-quantitative analysis of E-selectin binding activity on cancer cells. The development of accurate techniques for detection of selectin ligands may contribute to better diagnostic and better understanding of the molecular basis of tumor progression and metastasis.Repositório ComumCarrascal, MATalina, CBorralho, PGonçalo Mineiro, AHenriques, ARPen, CMartins, MBraga, SSackstein, RVideira, PA2018-05-06T10:24:34Z2018-05-022018-05-02T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.26/22793engBMC Cancer. 2018 May 2;18(1):495.10.1186/s12885-018-4410-xinfo: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:RCAAP2022-12-20T14:25:13Zoai:comum.rcaap.pt:10400.26/22793Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T16:22:46.273823Repositório 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 Staining of E-selectin ligands on paraffin-embedded sections of tumor tissue
title Staining of E-selectin ligands on paraffin-embedded sections of tumor tissue
spellingShingle Staining of E-selectin ligands on paraffin-embedded sections of tumor tissue
Carrascal, MA
Neoplasias
Selectina E
Inclusão em Parafina
Inclusão do Tecido
Tissue Embedding
E-Selectin
Paraffin Embedding
Neoplasms
title_short Staining of E-selectin ligands on paraffin-embedded sections of tumor tissue
title_full Staining of E-selectin ligands on paraffin-embedded sections of tumor tissue
title_fullStr Staining of E-selectin ligands on paraffin-embedded sections of tumor tissue
title_full_unstemmed Staining of E-selectin ligands on paraffin-embedded sections of tumor tissue
title_sort Staining of E-selectin ligands on paraffin-embedded sections of tumor tissue
author Carrascal, MA
author_facet Carrascal, MA
Talina, C
Borralho, P
Gonçalo Mineiro, A
Henriques, AR
Pen, C
Martins, M
Braga, S
Sackstein, R
Videira, PA
author_role author
author2 Talina, C
Borralho, P
Gonçalo Mineiro, A
Henriques, AR
Pen, C
Martins, M
Braga, S
Sackstein, R
Videira, PA
author2_role author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Repositório Comum
dc.contributor.author.fl_str_mv Carrascal, MA
Talina, C
Borralho, P
Gonçalo Mineiro, A
Henriques, AR
Pen, C
Martins, M
Braga, S
Sackstein, R
Videira, PA
dc.subject.por.fl_str_mv Neoplasias
Selectina E
Inclusão em Parafina
Inclusão do Tecido
Tissue Embedding
E-Selectin
Paraffin Embedding
Neoplasms
topic Neoplasias
Selectina E
Inclusão em Parafina
Inclusão do Tecido
Tissue Embedding
E-Selectin
Paraffin Embedding
Neoplasms
description BACKGROUND: The E-selectin ligands expressed by cancer cells mediate adhesion of circulating cancer cells to endothelial cells, as well as within tissue microenvironments important for tumor progression and metastasis. The identification of E-selectin ligands within cancer tissue could yield new biomarkers for patient stratification and aid in identifying novel therapeutic targets. The determinants of selectin ligands consist of sialylated tetrasaccharides, the sialyl Lewis X and A (sLeX and sLeA), displayed on protein or lipid scaffolds. Standardized procedures for immunohistochemistry make use of the antibodies against sLeX and/or sLeA. However, antibody binding does not define E-selectin binding activity. METHODS: In this study, we developed an immunohistochemical staining technique, using E-selectin-human Ig Fc chimera (E-Ig) to characterize the expression and localization of E-selectin binding sites on paraffin-embedded sections of different cancer tissue. RESULTS: E-Ig successfully stained cancer cells with high specificity. The E-Ig staining show high reactivity scores in colon and lung adenocarcinoma and moderate reactivity in triple negative breast cancer. Compared with reactivity of antibody against sLeX/A, the E-Ig staining presented higher specificity to cancer tissue with better defined borders and less background. CONCLUSIONS: The E-Ig staining technique allows the qualitative and semi-quantitative analysis of E-selectin binding activity on cancer cells. The development of accurate techniques for detection of selectin ligands may contribute to better diagnostic and better understanding of the molecular basis of tumor progression and metastasis.
publishDate 2018
dc.date.none.fl_str_mv 2018-05-06T10:24:34Z
2018-05-02
2018-05-02T00:00:00Z
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/10400.26/22793
url http://hdl.handle.net/10400.26/22793
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv BMC Cancer. 2018 May 2;18(1):495.
10.1186/s12885-018-4410-x
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
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
instacron_str RCAAP
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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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