Sturgeon osteocalcin shares structural features with matrix gla protein evolutionary relationship and functional implications

Detalhes bibliográficos
Autor(a) principal: S B Viegas, Carla
Data de Publicação: 2013
Outros Autores: Simes, Dina, Williamson, Matthew K., Cavaco, Sofia, Laizé, Vincent, Price, Paul A., Leonor Cancela, M.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10400.1/11950
Resumo: Osteocalcin (OC) and matrix Gla protein (MGP) are considered evolutionarily related because they share key structural features, although they have been described to exert different functions. In this work, we report the identification and characterization of both OC and MGP from the Adriatic sturgeon, a ray-finned fish characterized by a slow evolution and the retention of many ancestral features. Sturgeon MGP shows a primary structure, post-translation modifications, and patterns of mRNA/protein distribution and accumulation typical of known MGPs, and it contains seven possible Gla residues that would make the sturgeon protein the most gamma-carboxylated among known MGPs. In contrast, sturgeon OC was found to present a hybrid structure. Indeed, although exhibiting protein domains typical of known OCs, it also contains structural features usually found in MGPs (e. g. a putative phosphorylated propeptide). Moreover, patterns of OC gene expression and protein accumulation overlap with those reported for MGP; OC was detected in bone cells and mineralized structures but also in soft and cartilaginous tissues. We propose that, in a context of a reduced rate of evolution, sturgeon OC has retained structural features of the ancestral protein that emerged millions of years ago from the duplication of an ancient MGP gene and may exhibit intermediate functional features.
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spelling Sturgeon osteocalcin shares structural features with matrix gla protein evolutionary relationship and functional implicationsGamma-carboxyglutamic acidFish Sparus-AurataVitamin-KXenopus-LaevisTeleost fishCalcified cartilageTissue distributionOrganic matrixMessenger-RnaBoneOsteocalcin (OC) and matrix Gla protein (MGP) are considered evolutionarily related because they share key structural features, although they have been described to exert different functions. In this work, we report the identification and characterization of both OC and MGP from the Adriatic sturgeon, a ray-finned fish characterized by a slow evolution and the retention of many ancestral features. Sturgeon MGP shows a primary structure, post-translation modifications, and patterns of mRNA/protein distribution and accumulation typical of known MGPs, and it contains seven possible Gla residues that would make the sturgeon protein the most gamma-carboxylated among known MGPs. In contrast, sturgeon OC was found to present a hybrid structure. Indeed, although exhibiting protein domains typical of known OCs, it also contains structural features usually found in MGPs (e. g. a putative phosphorylated propeptide). Moreover, patterns of OC gene expression and protein accumulation overlap with those reported for MGP; OC was detected in bone cells and mineralized structures but also in soft and cartilaginous tissues. We propose that, in a context of a reduced rate of evolution, sturgeon OC has retained structural features of the ancestral protein that emerged millions of years ago from the duplication of an ancient MGP gene and may exhibit intermediate functional features.Portuguese Science and Technology Foundation [POCTI/MAR/57921/2004, SFRH/BD/9077/2002]; Fundo Europeu De Desenvolvimento Regional (FEDER) (Portugal); National Funding; Center of Marine Sciences (CCMAR)American Society for Biochemistry and Molecular BiologySapientiaS B Viegas, CarlaSimes, DinaWilliamson, Matthew K.Cavaco, SofiaLaizé, VincentPrice, Paul A.Leonor Cancela, M.2018-12-07T14:58:18Z2013-092013-09-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.1/11950eng0021-925810.1074/jbc.M113.450213info: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:RCAAP2023-07-24T10:23:51Zoai:sapientia.ualg.pt:10400.1/11950Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T20:03:23.116108Repositório 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 Sturgeon osteocalcin shares structural features with matrix gla protein evolutionary relationship and functional implications
title Sturgeon osteocalcin shares structural features with matrix gla protein evolutionary relationship and functional implications
spellingShingle Sturgeon osteocalcin shares structural features with matrix gla protein evolutionary relationship and functional implications
S B Viegas, Carla
Gamma-carboxyglutamic acid
Fish Sparus-Aurata
Vitamin-K
Xenopus-Laevis
Teleost fish
Calcified cartilage
Tissue distribution
Organic matrix
Messenger-Rna
Bone
title_short Sturgeon osteocalcin shares structural features with matrix gla protein evolutionary relationship and functional implications
title_full Sturgeon osteocalcin shares structural features with matrix gla protein evolutionary relationship and functional implications
title_fullStr Sturgeon osteocalcin shares structural features with matrix gla protein evolutionary relationship and functional implications
title_full_unstemmed Sturgeon osteocalcin shares structural features with matrix gla protein evolutionary relationship and functional implications
title_sort Sturgeon osteocalcin shares structural features with matrix gla protein evolutionary relationship and functional implications
author S B Viegas, Carla
author_facet S B Viegas, Carla
Simes, Dina
Williamson, Matthew K.
Cavaco, Sofia
Laizé, Vincent
Price, Paul A.
Leonor Cancela, M.
author_role author
author2 Simes, Dina
Williamson, Matthew K.
Cavaco, Sofia
Laizé, Vincent
Price, Paul A.
Leonor Cancela, M.
author2_role author
author
author
author
author
author
dc.contributor.none.fl_str_mv Sapientia
dc.contributor.author.fl_str_mv S B Viegas, Carla
Simes, Dina
Williamson, Matthew K.
Cavaco, Sofia
Laizé, Vincent
Price, Paul A.
Leonor Cancela, M.
dc.subject.por.fl_str_mv Gamma-carboxyglutamic acid
Fish Sparus-Aurata
Vitamin-K
Xenopus-Laevis
Teleost fish
Calcified cartilage
Tissue distribution
Organic matrix
Messenger-Rna
Bone
topic Gamma-carboxyglutamic acid
Fish Sparus-Aurata
Vitamin-K
Xenopus-Laevis
Teleost fish
Calcified cartilage
Tissue distribution
Organic matrix
Messenger-Rna
Bone
description Osteocalcin (OC) and matrix Gla protein (MGP) are considered evolutionarily related because they share key structural features, although they have been described to exert different functions. In this work, we report the identification and characterization of both OC and MGP from the Adriatic sturgeon, a ray-finned fish characterized by a slow evolution and the retention of many ancestral features. Sturgeon MGP shows a primary structure, post-translation modifications, and patterns of mRNA/protein distribution and accumulation typical of known MGPs, and it contains seven possible Gla residues that would make the sturgeon protein the most gamma-carboxylated among known MGPs. In contrast, sturgeon OC was found to present a hybrid structure. Indeed, although exhibiting protein domains typical of known OCs, it also contains structural features usually found in MGPs (e. g. a putative phosphorylated propeptide). Moreover, patterns of OC gene expression and protein accumulation overlap with those reported for MGP; OC was detected in bone cells and mineralized structures but also in soft and cartilaginous tissues. We propose that, in a context of a reduced rate of evolution, sturgeon OC has retained structural features of the ancestral protein that emerged millions of years ago from the duplication of an ancient MGP gene and may exhibit intermediate functional features.
publishDate 2013
dc.date.none.fl_str_mv 2013-09
2013-09-01T00:00:00Z
2018-12-07T14:58:18Z
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/10400.1/11950
url http://hdl.handle.net/10400.1/11950
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 0021-9258
10.1074/jbc.M113.450213
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 American Society for Biochemistry and Molecular Biology
publisher.none.fl_str_mv American Society for Biochemistry and Molecular Biology
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
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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)
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