Cloning and Functional Assessment of the Recombinant Human Hepcidin-25 in the Baculovirus Expression System
Autor(a) principal: | |
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Data de Publicação: | 2015 |
Outros Autores: | , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Brazilian Archives of Biology and Technology |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132015000100090 |
Resumo: | Hepcidin is the primary regulatory hormone responsible for lowering the iron content in the blood circulation. Due to its biodegradability and low cytotoxicity, hepcidin is considered as an alternative for iron chelators. The baculovirus expression system may be suitable for human hepcidin production because the expressed proteins generally exhibit proper folding, post-translational modifications, and oligomerization. Using data from two vector maps, pFastBac1 and pFastBac HTB, a unique vector was designed encoding human hepcidin-25 as fusion recombinant peptide. Expression analysis showed that it was expressed as a peptide with a molecular weight near to 5 kDa. After purification and TEV treatment, findings revealed that recombinant human hepcidin-25 was functional and its effect was dose dependent (P=0.001). It was concluded that baculovirus expression was a suitable expression system for production of functional recombinant human hepcidin-25. |
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Brazilian Archives of Biology and Technology |
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Cloning and Functional Assessment of the Recombinant Human Hepcidin-25 in the Baculovirus Expression SystemHepcidin-25Iron metabolismSF-9 expression systemHepcidin is the primary regulatory hormone responsible for lowering the iron content in the blood circulation. Due to its biodegradability and low cytotoxicity, hepcidin is considered as an alternative for iron chelators. The baculovirus expression system may be suitable for human hepcidin production because the expressed proteins generally exhibit proper folding, post-translational modifications, and oligomerization. Using data from two vector maps, pFastBac1 and pFastBac HTB, a unique vector was designed encoding human hepcidin-25 as fusion recombinant peptide. Expression analysis showed that it was expressed as a peptide with a molecular weight near to 5 kDa. After purification and TEV treatment, findings revealed that recombinant human hepcidin-25 was functional and its effect was dose dependent (P=0.001). It was concluded that baculovirus expression was a suitable expression system for production of functional recombinant human hepcidin-25.Instituto de Tecnologia do Paraná - Tecpar2015-02-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132015000100090Brazilian Archives of Biology and Technology v.58 n.1 2015reponame:Brazilian Archives of Biology and Technologyinstname:Instituto de Tecnologia do Paraná (Tecpar)instacron:TECPAR10.1590/S1516-8913201400018info:eu-repo/semantics/openAccessYazdani,YaghoubKeyhanvar,NedaTabaraei,Alijaneng2015-10-26T00:00:00Zoai:scielo:S1516-89132015000100090Revistahttps://www.scielo.br/j/babt/https://old.scielo.br/oai/scielo-oai.phpbabt@tecpar.br||babt@tecpar.br1678-43241516-8913opendoar:2015-10-26T00:00Brazilian Archives of Biology and Technology - Instituto de Tecnologia do Paraná (Tecpar)false |
dc.title.none.fl_str_mv |
Cloning and Functional Assessment of the Recombinant Human Hepcidin-25 in the Baculovirus Expression System |
title |
Cloning and Functional Assessment of the Recombinant Human Hepcidin-25 in the Baculovirus Expression System |
spellingShingle |
Cloning and Functional Assessment of the Recombinant Human Hepcidin-25 in the Baculovirus Expression System Yazdani,Yaghoub Hepcidin-25 Iron metabolism SF-9 expression system |
title_short |
Cloning and Functional Assessment of the Recombinant Human Hepcidin-25 in the Baculovirus Expression System |
title_full |
Cloning and Functional Assessment of the Recombinant Human Hepcidin-25 in the Baculovirus Expression System |
title_fullStr |
Cloning and Functional Assessment of the Recombinant Human Hepcidin-25 in the Baculovirus Expression System |
title_full_unstemmed |
Cloning and Functional Assessment of the Recombinant Human Hepcidin-25 in the Baculovirus Expression System |
title_sort |
Cloning and Functional Assessment of the Recombinant Human Hepcidin-25 in the Baculovirus Expression System |
author |
Yazdani,Yaghoub |
author_facet |
Yazdani,Yaghoub Keyhanvar,Neda Tabaraei,Alijan |
author_role |
author |
author2 |
Keyhanvar,Neda Tabaraei,Alijan |
author2_role |
author author |
dc.contributor.author.fl_str_mv |
Yazdani,Yaghoub Keyhanvar,Neda Tabaraei,Alijan |
dc.subject.por.fl_str_mv |
Hepcidin-25 Iron metabolism SF-9 expression system |
topic |
Hepcidin-25 Iron metabolism SF-9 expression system |
description |
Hepcidin is the primary regulatory hormone responsible for lowering the iron content in the blood circulation. Due to its biodegradability and low cytotoxicity, hepcidin is considered as an alternative for iron chelators. The baculovirus expression system may be suitable for human hepcidin production because the expressed proteins generally exhibit proper folding, post-translational modifications, and oligomerization. Using data from two vector maps, pFastBac1 and pFastBac HTB, a unique vector was designed encoding human hepcidin-25 as fusion recombinant peptide. Expression analysis showed that it was expressed as a peptide with a molecular weight near to 5 kDa. After purification and TEV treatment, findings revealed that recombinant human hepcidin-25 was functional and its effect was dose dependent (P=0.001). It was concluded that baculovirus expression was a suitable expression system for production of functional recombinant human hepcidin-25. |
publishDate |
2015 |
dc.date.none.fl_str_mv |
2015-02-01 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132015000100090 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132015000100090 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S1516-8913201400018 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
text/html |
dc.publisher.none.fl_str_mv |
Instituto de Tecnologia do Paraná - Tecpar |
publisher.none.fl_str_mv |
Instituto de Tecnologia do Paraná - Tecpar |
dc.source.none.fl_str_mv |
Brazilian Archives of Biology and Technology v.58 n.1 2015 reponame:Brazilian Archives of Biology and Technology instname:Instituto de Tecnologia do Paraná (Tecpar) instacron:TECPAR |
instname_str |
Instituto de Tecnologia do Paraná (Tecpar) |
instacron_str |
TECPAR |
institution |
TECPAR |
reponame_str |
Brazilian Archives of Biology and Technology |
collection |
Brazilian Archives of Biology and Technology |
repository.name.fl_str_mv |
Brazilian Archives of Biology and Technology - Instituto de Tecnologia do Paraná (Tecpar) |
repository.mail.fl_str_mv |
babt@tecpar.br||babt@tecpar.br |
_version_ |
1750318276839211008 |