A comparative study of recombinant and native frutalin binding to human prostate tissues
Autor(a) principal: | |
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Data de Publicação: | 2009 |
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/1822/10304 |
Resumo: | Background Numerous studies indicate that cancer cells present an aberrant glycosylation pattern that can be detected by lectin histochemistry. Lectins have shown the ability to recognise these modifications in several carcinomas, namely in the prostate carcinoma, one of the most lethal diseases in man. Thus, the aim of this work was to investigate if the α-D-galactose-binding plant lectin frutalin is able to detect such changes in the referred carcinoma. Frutalin was obtained from different sources namely, its natural source (plant origin) and a recombinant source (Pichia expression system). Finally, the results obtained with the two lectins were compared and their potential use as prostate tumour biomarkers was discussed. Results The binding of recombinant and native frutalin to specific glycoconjugates expressed in human prostate tissues was assessed by using an immuhistochemical technique. A total of 20 cases of prostate carcinoma and 25 cases of benign prostate hyperplasia were studied. Lectins bound directly to the tissues and anti-frutalin polyclonal antibody was used as the bridge to react with the complex biotinilated anti-rabbit IgG plus streptavidin-conjugated peroxidase. DAB was used as visual indicator to specifically localise the binding of the lectins to the tissues. Both lectins bound to the cells cytoplasm of the prostate carcinoma glands. The binding intensity of native frutalin was stronger in the neoplasic cells than in hyperplasic cells; however no significant statistical correlation could be found (P = 0.051). On the other hand, recombinant frutalin bound exclusively to the neoplasic cells and a significant positive statistical correlation was obtained (P < 0.00001). However, recombinant frutalin did not recognise all malignant prostate cases and, when positive, the binding to those tissues was heterogeneous. Conclusion Native and recombinant frutalin yielded different binding responses in the prostate tissues due to their differences in carbohydrate-binding affinities. Also, this study shows that both lectins may be used as histochemical biomarkers for the prostate cancer. Moreover, the successful use of a recombinant lectin in immunohistochemical studies of prostate cancer was for the first time demonstrated, highlighting the advantages of using recombinant systems in the preparation of pure lectin samples for diagnostic purpose. |
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A comparative study of recombinant and native frutalin binding to human prostate tissuesScience & TechnologyBackground Numerous studies indicate that cancer cells present an aberrant glycosylation pattern that can be detected by lectin histochemistry. Lectins have shown the ability to recognise these modifications in several carcinomas, namely in the prostate carcinoma, one of the most lethal diseases in man. Thus, the aim of this work was to investigate if the α-D-galactose-binding plant lectin frutalin is able to detect such changes in the referred carcinoma. Frutalin was obtained from different sources namely, its natural source (plant origin) and a recombinant source (Pichia expression system). Finally, the results obtained with the two lectins were compared and their potential use as prostate tumour biomarkers was discussed. Results The binding of recombinant and native frutalin to specific glycoconjugates expressed in human prostate tissues was assessed by using an immuhistochemical technique. A total of 20 cases of prostate carcinoma and 25 cases of benign prostate hyperplasia were studied. Lectins bound directly to the tissues and anti-frutalin polyclonal antibody was used as the bridge to react with the complex biotinilated anti-rabbit IgG plus streptavidin-conjugated peroxidase. DAB was used as visual indicator to specifically localise the binding of the lectins to the tissues. Both lectins bound to the cells cytoplasm of the prostate carcinoma glands. The binding intensity of native frutalin was stronger in the neoplasic cells than in hyperplasic cells; however no significant statistical correlation could be found (P = 0.051). On the other hand, recombinant frutalin bound exclusively to the neoplasic cells and a significant positive statistical correlation was obtained (P < 0.00001). However, recombinant frutalin did not recognise all malignant prostate cases and, when positive, the binding to those tissues was heterogeneous. Conclusion Native and recombinant frutalin yielded different binding responses in the prostate tissues due to their differences in carbohydrate-binding affinities. Also, this study shows that both lectins may be used as histochemical biomarkers for the prostate cancer. Moreover, the successful use of a recombinant lectin in immunohistochemical studies of prostate cancer was for the first time demonstrated, highlighting the advantages of using recombinant systems in the preparation of pure lectin samples for diagnostic purpose.Fundação para a Ciência e a Tecnologia (FCT) - SFRH/BD/19099/2004BioMed Central (BMC)Universidade do MinhoOliveira, Carla Cristina Marques deTeixeira, J. A.Schmitt, Fernando C.Domingues, Lucília2009-092009-09-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/10304engOLIVEIRA, Carla Cristina Marques de [et al.] - A comparative study of recombinant and native frutalin binding to human prostate tissues. “BMC Biotechnology” [Em linha] 9:78 (2009). [Consult. 3 Jan. 2010]. Disponível em: http://www.biomedcentral.com/1472-6750/9/78. ISSN 1472-6750.1472-675010.1186/1472-6750-9-7819740412http://www.biomedcentral.com/1472-6750/9/78info: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:RCAAP2023-07-21T12:03:06Zoai:repositorium.sdum.uminho.pt:1822/10304Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T18:53:11.480875Repositório 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 |
A comparative study of recombinant and native frutalin binding to human prostate tissues |
title |
A comparative study of recombinant and native frutalin binding to human prostate tissues |
spellingShingle |
A comparative study of recombinant and native frutalin binding to human prostate tissues Oliveira, Carla Cristina Marques de Science & Technology |
title_short |
A comparative study of recombinant and native frutalin binding to human prostate tissues |
title_full |
A comparative study of recombinant and native frutalin binding to human prostate tissues |
title_fullStr |
A comparative study of recombinant and native frutalin binding to human prostate tissues |
title_full_unstemmed |
A comparative study of recombinant and native frutalin binding to human prostate tissues |
title_sort |
A comparative study of recombinant and native frutalin binding to human prostate tissues |
author |
Oliveira, Carla Cristina Marques de |
author_facet |
Oliveira, Carla Cristina Marques de Teixeira, J. A. Schmitt, Fernando C. Domingues, Lucília |
author_role |
author |
author2 |
Teixeira, J. A. Schmitt, Fernando C. Domingues, Lucília |
author2_role |
author author author |
dc.contributor.none.fl_str_mv |
Universidade do Minho |
dc.contributor.author.fl_str_mv |
Oliveira, Carla Cristina Marques de Teixeira, J. A. Schmitt, Fernando C. Domingues, Lucília |
dc.subject.por.fl_str_mv |
Science & Technology |
topic |
Science & Technology |
description |
Background Numerous studies indicate that cancer cells present an aberrant glycosylation pattern that can be detected by lectin histochemistry. Lectins have shown the ability to recognise these modifications in several carcinomas, namely in the prostate carcinoma, one of the most lethal diseases in man. Thus, the aim of this work was to investigate if the α-D-galactose-binding plant lectin frutalin is able to detect such changes in the referred carcinoma. Frutalin was obtained from different sources namely, its natural source (plant origin) and a recombinant source (Pichia expression system). Finally, the results obtained with the two lectins were compared and their potential use as prostate tumour biomarkers was discussed. Results The binding of recombinant and native frutalin to specific glycoconjugates expressed in human prostate tissues was assessed by using an immuhistochemical technique. A total of 20 cases of prostate carcinoma and 25 cases of benign prostate hyperplasia were studied. Lectins bound directly to the tissues and anti-frutalin polyclonal antibody was used as the bridge to react with the complex biotinilated anti-rabbit IgG plus streptavidin-conjugated peroxidase. DAB was used as visual indicator to specifically localise the binding of the lectins to the tissues. Both lectins bound to the cells cytoplasm of the prostate carcinoma glands. The binding intensity of native frutalin was stronger in the neoplasic cells than in hyperplasic cells; however no significant statistical correlation could be found (P = 0.051). On the other hand, recombinant frutalin bound exclusively to the neoplasic cells and a significant positive statistical correlation was obtained (P < 0.00001). However, recombinant frutalin did not recognise all malignant prostate cases and, when positive, the binding to those tissues was heterogeneous. Conclusion Native and recombinant frutalin yielded different binding responses in the prostate tissues due to their differences in carbohydrate-binding affinities. Also, this study shows that both lectins may be used as histochemical biomarkers for the prostate cancer. Moreover, the successful use of a recombinant lectin in immunohistochemical studies of prostate cancer was for the first time demonstrated, highlighting the advantages of using recombinant systems in the preparation of pure lectin samples for diagnostic purpose. |
publishDate |
2009 |
dc.date.none.fl_str_mv |
2009-09 2009-09-01T00:00:00Z |
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/1822/10304 |
url |
http://hdl.handle.net/1822/10304 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
OLIVEIRA, Carla Cristina Marques de [et al.] - A comparative study of recombinant and native frutalin binding to human prostate tissues. “BMC Biotechnology” [Em linha] 9:78 (2009). [Consult. 3 Jan. 2010]. Disponível em: http://www.biomedcentral.com/1472-6750/9/78. ISSN 1472-6750. 1472-6750 10.1186/1472-6750-9-78 19740412 http://www.biomedcentral.com/1472-6750/9/78 |
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.publisher.none.fl_str_mv |
BioMed Central (BMC) |
publisher.none.fl_str_mv |
BioMed Central (BMC) |
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 |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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1799132310530949120 |