Staining of E-selectin ligands on paraffin-embedded sections of tumor tissue
Autor(a) principal: | |
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Data de Publicação: | 2018 |
Outros Autores: | , , , , , , , , |
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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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 |
institution |
RCAAP |
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 |
repository.mail.fl_str_mv |
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1799130672855515137 |