Sturgeon osteocalcin shares structural features with matrix gla protein evolutionary relationship and functional implications
Autor(a) principal: | |
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Data de Publicação: | 2013 |
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/10400.1/11950 |
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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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 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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1799133268010860544 |