Characterization of α-actin isoforms in white and red skeletal muscle types of Leporinus macrocephalus (Characiformes, Anostomidae)
Autor(a) principal: | |
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Data de Publicação: | 2015 |
Outros Autores: | , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1590/0001-3765201520140278 http://hdl.handle.net/11449/172313 |
Resumo: | Two α-actin genes of the fish Leporinus macrocephalus, referring to white and red muscle tissues, were isolated. Actin isoforms, that mainly differed by a Ser/Ala155 substitution, can have a functional significance related to actin-ATP interaction. An Ala155 residue, as observed in the α-skeletal actin from red muscle, results in a decrease in actin’s affinity for ATP, which may also be associated to the slow contractile performance of this tissue. Furthermore, a Phe/Ile262 substitution at the red muscle actin leads to a hydrophobicity variation at the D-plug of the protein, which could alter its stability. Data on qRTPCR evidenced a significant higher actin mRNA level in white muscle when compared to red muscle (T=105 Mann Whitney; p<0.001). This finding could be related to the energetic demands of the white muscle tissue, with fast contraction fibers and glycolytic metabolism for energy supply. Available data on muscle actins lead to the proposal that white and red α-skeletal actins are genetically and functionally distinguishable in fish species, a feature that is not found in other vertebrate groups. |
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Characterization of α-actin isoforms in white and red skeletal muscle types of Leporinus macrocephalus (Characiformes, Anostomidae)ATP interactionBinding sitePhe/Ile262 substitutionSer/Ala155 substitutionTwo α-actin genes of the fish Leporinus macrocephalus, referring to white and red muscle tissues, were isolated. Actin isoforms, that mainly differed by a Ser/Ala155 substitution, can have a functional significance related to actin-ATP interaction. An Ala155 residue, as observed in the α-skeletal actin from red muscle, results in a decrease in actin’s affinity for ATP, which may also be associated to the slow contractile performance of this tissue. Furthermore, a Phe/Ile262 substitution at the red muscle actin leads to a hydrophobicity variation at the D-plug of the protein, which could alter its stability. Data on qRTPCR evidenced a significant higher actin mRNA level in white muscle when compared to red muscle (T=105 Mann Whitney; p<0.001). This finding could be related to the energetic demands of the white muscle tissue, with fast contraction fibers and glycolytic metabolism for energy supply. Available data on muscle actins lead to the proposal that white and red α-skeletal actins are genetically and functionally distinguishable in fish species, a feature that is not found in other vertebrate groups.Universidade Paulista/UNIP Instituto de Ciências da Saúde, Rua Luiz Levorato, 20108Universidade Estadual Paulista/UNESP Instituto de Biociências Departamento de Morfologia, Distrito de Rubião Júnior, s/nUniversidade Estadual Paulista/UNESP Instituto de Biociências Departamento de Genética, Distrito de Rubião Júnior, s/nUniversidade Estadual Paulista/UNESP Instituto de Biociências Departamento de Morfologia, Distrito de Rubião Júnior, s/nUniversidade Estadual Paulista/UNESP Instituto de Biociências Departamento de Genética, Distrito de Rubião Júnior, s/nInstituto de Ciências da SaúdeUniversidade Estadual Paulista (Unesp)Alves-Costa, Fernanda AntunesSilva, Maeli D. P. [UNESP]Wasko, Adriane P. [UNESP]2018-12-11T16:59:39Z2018-12-11T16:59:39Z2015-10-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article2055-2066application/pdfhttp://dx.doi.org/10.1590/0001-3765201520140278Anais da Academia Brasileira de Ciencias, v. 87, n. 4, p. 2055-2066, 2015.1678-26900001-3765http://hdl.handle.net/11449/17231310.1590/0001-3765201520140278S0001-376520150005020552-s2.0-84949972743S0001-37652015000502055.pdf19268639173789090000-0003-4600-0367Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengAnais da Academia Brasileira de Ciencias0,4180,418info:eu-repo/semantics/openAccess2023-10-28T06:06:24Zoai:repositorio.unesp.br:11449/172313Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T16:13:59.382831Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Characterization of α-actin isoforms in white and red skeletal muscle types of Leporinus macrocephalus (Characiformes, Anostomidae) |
title |
Characterization of α-actin isoforms in white and red skeletal muscle types of Leporinus macrocephalus (Characiformes, Anostomidae) |
spellingShingle |
Characterization of α-actin isoforms in white and red skeletal muscle types of Leporinus macrocephalus (Characiformes, Anostomidae) Alves-Costa, Fernanda Antunes ATP interaction Binding site Phe/Ile262 substitution Ser/Ala155 substitution |
title_short |
Characterization of α-actin isoforms in white and red skeletal muscle types of Leporinus macrocephalus (Characiformes, Anostomidae) |
title_full |
Characterization of α-actin isoforms in white and red skeletal muscle types of Leporinus macrocephalus (Characiformes, Anostomidae) |
title_fullStr |
Characterization of α-actin isoforms in white and red skeletal muscle types of Leporinus macrocephalus (Characiformes, Anostomidae) |
title_full_unstemmed |
Characterization of α-actin isoforms in white and red skeletal muscle types of Leporinus macrocephalus (Characiformes, Anostomidae) |
title_sort |
Characterization of α-actin isoforms in white and red skeletal muscle types of Leporinus macrocephalus (Characiformes, Anostomidae) |
author |
Alves-Costa, Fernanda Antunes |
author_facet |
Alves-Costa, Fernanda Antunes Silva, Maeli D. P. [UNESP] Wasko, Adriane P. [UNESP] |
author_role |
author |
author2 |
Silva, Maeli D. P. [UNESP] Wasko, Adriane P. [UNESP] |
author2_role |
author author |
dc.contributor.none.fl_str_mv |
Instituto de Ciências da Saúde Universidade Estadual Paulista (Unesp) |
dc.contributor.author.fl_str_mv |
Alves-Costa, Fernanda Antunes Silva, Maeli D. P. [UNESP] Wasko, Adriane P. [UNESP] |
dc.subject.por.fl_str_mv |
ATP interaction Binding site Phe/Ile262 substitution Ser/Ala155 substitution |
topic |
ATP interaction Binding site Phe/Ile262 substitution Ser/Ala155 substitution |
description |
Two α-actin genes of the fish Leporinus macrocephalus, referring to white and red muscle tissues, were isolated. Actin isoforms, that mainly differed by a Ser/Ala155 substitution, can have a functional significance related to actin-ATP interaction. An Ala155 residue, as observed in the α-skeletal actin from red muscle, results in a decrease in actin’s affinity for ATP, which may also be associated to the slow contractile performance of this tissue. Furthermore, a Phe/Ile262 substitution at the red muscle actin leads to a hydrophobicity variation at the D-plug of the protein, which could alter its stability. Data on qRTPCR evidenced a significant higher actin mRNA level in white muscle when compared to red muscle (T=105 Mann Whitney; p<0.001). This finding could be related to the energetic demands of the white muscle tissue, with fast contraction fibers and glycolytic metabolism for energy supply. Available data on muscle actins lead to the proposal that white and red α-skeletal actins are genetically and functionally distinguishable in fish species, a feature that is not found in other vertebrate groups. |
publishDate |
2015 |
dc.date.none.fl_str_mv |
2015-10-01 2018-12-11T16:59:39Z 2018-12-11T16:59:39Z |
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://dx.doi.org/10.1590/0001-3765201520140278 Anais da Academia Brasileira de Ciencias, v. 87, n. 4, p. 2055-2066, 2015. 1678-2690 0001-3765 http://hdl.handle.net/11449/172313 10.1590/0001-3765201520140278 S0001-37652015000502055 2-s2.0-84949972743 S0001-37652015000502055.pdf 1926863917378909 0000-0003-4600-0367 |
url |
http://dx.doi.org/10.1590/0001-3765201520140278 http://hdl.handle.net/11449/172313 |
identifier_str_mv |
Anais da Academia Brasileira de Ciencias, v. 87, n. 4, p. 2055-2066, 2015. 1678-2690 0001-3765 10.1590/0001-3765201520140278 S0001-37652015000502055 2-s2.0-84949972743 S0001-37652015000502055.pdf 1926863917378909 0000-0003-4600-0367 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Anais da Academia Brasileira de Ciencias 0,418 0,418 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
2055-2066 application/pdf |
dc.source.none.fl_str_mv |
Scopus reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
|
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1808128621909377024 |