Fatty acid transport protein 1 (FATP1) delivered into skeletal muscle localizes in mitochondria and regulates lipid and ketone body disposal

FATP1 mediates skeletal muscle cell fatty acid import, yet its intracellular localization and metabolic control role are not completely defined. Here, we examine FATP1 localization and metabolic effects of its overexpression in mouse skeletal muscle. The FATP1 protein was detected in mitochondrial a...

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Autores: Guitart de la Rosa, Maria, Osorio Conles, Óscar, Pentinat Pelegrin, Thais, Cebrià, Judith, García Villoria, Judit, Sala Cano, David, Sebastián Muñoz, David, Zorzano Olarte, Antonio, Ribes Rubió, Maria Antònia, Jiménez Chillarón, José Carlos, García Martínez, Celia, Gómez Foix, Anna Maria
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2014
País:España
Institución:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Repositorio:Recercat. Dipósit de la Recerca de Catalunya
OAI Identifier:oai:recercat.cat:2445/59231
Acceso en línea:https://hdl.handle.net/2445/59231
Access Level:acceso abierto
Palabra clave:Aparell locomotor
Metabolisme energètic
Glicogen
Àcids grassos
Diabetis
Proteïnes de membrana
Mitocondris
Musculoskeletal system
Energy metabolism
Glycogen
Fatty acids
Diabetes
Membrane proteins
Mitochondria
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spelling Fatty acid transport protein 1 (FATP1) delivered into skeletal muscle localizes in mitochondria and regulates lipid and ketone body disposalGuitart de la Rosa, MariaOsorio Conles, ÓscarPentinat Pelegrin, ThaisCebrià, JudithGarcía Villoria, JuditSala Cano, DavidSebastián Muñoz, DavidZorzano Olarte, AntonioRibes Rubió, Maria AntòniaJiménez Chillarón, José CarlosGarcía Martínez, CeliaGómez Foix, Anna MariaAparell locomotorMetabolisme energèticGlicogenÀcids grassosDiabetisProteïnes de membranaMitocondrisMusculoskeletal systemEnergy metabolismGlycogenFatty acidsDiabetesMembrane proteinsMitochondriaFATP1 mediates skeletal muscle cell fatty acid import, yet its intracellular localization and metabolic control role are not completely defined. Here, we examine FATP1 localization and metabolic effects of its overexpression in mouse skeletal muscle. The FATP1 protein was detected in mitochondrial and plasma membrane fractions, obtained by differential centrifugation, of mouse gastrocnemius muscle. FATP1 was most abundant in purified mitochondria, and in the outer membrane and soluble intermembrane, but not in the inner membrane plus matrix, enriched subfractions of purified mitochondria. Immunogold electron microscopy localized FATP1-GFP in mitochondria of transfected C2C12 myotubes. FATP1 was overexpressed in gastrocnemius mouse muscle, by adenovirus-mediated delivery of the gene into hindlimb muscles of newborn mice, fed after weaning a chow or high-fat diet. Compared to GFP delivery, FATP1 did not alter body weight, serum fed glucose, insulin and triglyceride levels, and whole-body glucose tolerance, in either diet. However, fatty acid levels were lower and beta-hydroxybutyrate levels were higher in FATP1-than GFP-mice, irrespective of diet. Moreover, intramuscular triglyceride content was lower in FATP1-versus GFP-mice regardless of diet, and beta-hydroxybutyrate content was unchanged in high-fat-fed mice. Electroporation-mediated FATP1 overexpression enhanced palmitate oxidation to CO2, but not to acid-soluble intermediate metabolites, while CO2 production from beta-hydroxybutyrate was inhibited and that from glucose unchanged, in isolated mouse gastrocnemius strips. In summary, FATP1 was localized in mitochondria, in the outer membrane and intermembrane parts, of mouse skeletal muscle, what may be crucial for its metabolic effects. Overexpressed FATP1 enhanced disposal of both systemic fatty acids and intramuscular triglycerides. Consistently, it did not contribute to the high-fat diet-induced metabolic dysregulation. However, FATP1 lead to hyperketonemia, likely secondary to the sparing of ketone body oxidation by the enhanced oxidation of fatty acids.Public Library of Science (PLoS)2014201420142014info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersion15 p.application/pdfhttps://hdl.handle.net/2445/59231Articles publicats en revistes (Bioquímica i Biomedicina Molecular)reponame:Recercat. Dipósit de la Recerca de Catalunyainstname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)InglésReproducció del document publicat a: http://dx.doi.org/10.1371/journal.pone.0098109PLoS One, 2014, vol. 9, num. 5, p. e98109http://dx.doi.org/10.1371/journal.pone.0098109cc-by (c) Guitart de la Rosa, Maria et al., 2014http://creativecommons.org/licenses/by/3.0/esinfo:eu-repo/semantics/openAccessoai:recercat.cat:2445/592312026-05-29T05:05:01Z
dc.title.none.fl_str_mv Fatty acid transport protein 1 (FATP1) delivered into skeletal muscle localizes in mitochondria and regulates lipid and ketone body disposal
title Fatty acid transport protein 1 (FATP1) delivered into skeletal muscle localizes in mitochondria and regulates lipid and ketone body disposal
spellingShingle Fatty acid transport protein 1 (FATP1) delivered into skeletal muscle localizes in mitochondria and regulates lipid and ketone body disposal
Guitart de la Rosa, Maria
Aparell locomotor
Metabolisme energètic
Glicogen
Àcids grassos
Diabetis
Proteïnes de membrana
Mitocondris
Musculoskeletal system
Energy metabolism
Glycogen
Fatty acids
Diabetes
Membrane proteins
Mitochondria
title_short Fatty acid transport protein 1 (FATP1) delivered into skeletal muscle localizes in mitochondria and regulates lipid and ketone body disposal
title_full Fatty acid transport protein 1 (FATP1) delivered into skeletal muscle localizes in mitochondria and regulates lipid and ketone body disposal
title_fullStr Fatty acid transport protein 1 (FATP1) delivered into skeletal muscle localizes in mitochondria and regulates lipid and ketone body disposal
title_full_unstemmed Fatty acid transport protein 1 (FATP1) delivered into skeletal muscle localizes in mitochondria and regulates lipid and ketone body disposal
title_sort Fatty acid transport protein 1 (FATP1) delivered into skeletal muscle localizes in mitochondria and regulates lipid and ketone body disposal
dc.creator.none.fl_str_mv Guitart de la Rosa, Maria
Osorio Conles, Óscar
Pentinat Pelegrin, Thais
Cebrià, Judith
García Villoria, Judit
Sala Cano, David
Sebastián Muñoz, David
Zorzano Olarte, Antonio
Ribes Rubió, Maria Antònia
Jiménez Chillarón, José Carlos
García Martínez, Celia
Gómez Foix, Anna Maria
author Guitart de la Rosa, Maria
author_facet Guitart de la Rosa, Maria
Osorio Conles, Óscar
Pentinat Pelegrin, Thais
Cebrià, Judith
García Villoria, Judit
Sala Cano, David
Sebastián Muñoz, David
Zorzano Olarte, Antonio
Ribes Rubió, Maria Antònia
Jiménez Chillarón, José Carlos
García Martínez, Celia
Gómez Foix, Anna Maria
author_role author
author2 Osorio Conles, Óscar
Pentinat Pelegrin, Thais
Cebrià, Judith
García Villoria, Judit
Sala Cano, David
Sebastián Muñoz, David
Zorzano Olarte, Antonio
Ribes Rubió, Maria Antònia
Jiménez Chillarón, José Carlos
García Martínez, Celia
Gómez Foix, Anna Maria
author2_role author
author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Aparell locomotor
Metabolisme energètic
Glicogen
Àcids grassos
Diabetis
Proteïnes de membrana
Mitocondris
Musculoskeletal system
Energy metabolism
Glycogen
Fatty acids
Diabetes
Membrane proteins
Mitochondria
topic Aparell locomotor
Metabolisme energètic
Glicogen
Àcids grassos
Diabetis
Proteïnes de membrana
Mitocondris
Musculoskeletal system
Energy metabolism
Glycogen
Fatty acids
Diabetes
Membrane proteins
Mitochondria
description FATP1 mediates skeletal muscle cell fatty acid import, yet its intracellular localization and metabolic control role are not completely defined. Here, we examine FATP1 localization and metabolic effects of its overexpression in mouse skeletal muscle. The FATP1 protein was detected in mitochondrial and plasma membrane fractions, obtained by differential centrifugation, of mouse gastrocnemius muscle. FATP1 was most abundant in purified mitochondria, and in the outer membrane and soluble intermembrane, but not in the inner membrane plus matrix, enriched subfractions of purified mitochondria. Immunogold electron microscopy localized FATP1-GFP in mitochondria of transfected C2C12 myotubes. FATP1 was overexpressed in gastrocnemius mouse muscle, by adenovirus-mediated delivery of the gene into hindlimb muscles of newborn mice, fed after weaning a chow or high-fat diet. Compared to GFP delivery, FATP1 did not alter body weight, serum fed glucose, insulin and triglyceride levels, and whole-body glucose tolerance, in either diet. However, fatty acid levels were lower and beta-hydroxybutyrate levels were higher in FATP1-than GFP-mice, irrespective of diet. Moreover, intramuscular triglyceride content was lower in FATP1-versus GFP-mice regardless of diet, and beta-hydroxybutyrate content was unchanged in high-fat-fed mice. Electroporation-mediated FATP1 overexpression enhanced palmitate oxidation to CO2, but not to acid-soluble intermediate metabolites, while CO2 production from beta-hydroxybutyrate was inhibited and that from glucose unchanged, in isolated mouse gastrocnemius strips. In summary, FATP1 was localized in mitochondria, in the outer membrane and intermembrane parts, of mouse skeletal muscle, what may be crucial for its metabolic effects. Overexpressed FATP1 enhanced disposal of both systemic fatty acids and intramuscular triglycerides. Consistently, it did not contribute to the high-fat diet-induced metabolic dysregulation. However, FATP1 lead to hyperketonemia, likely secondary to the sparing of ketone body oxidation by the enhanced oxidation of fatty acids.
publishDate 2014
dc.date.none.fl_str_mv 2014
2014
2014
2014
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2445/59231
url https://hdl.handle.net/2445/59231
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Reproducció del document publicat a: http://dx.doi.org/10.1371/journal.pone.0098109
PLoS One, 2014, vol. 9, num. 5, p. e98109
http://dx.doi.org/10.1371/journal.pone.0098109
dc.rights.none.fl_str_mv cc-by (c) Guitart de la Rosa, Maria et al., 2014
http://creativecommons.org/licenses/by/3.0/es
info:eu-repo/semantics/openAccess
rights_invalid_str_mv cc-by (c) Guitart de la Rosa, Maria et al., 2014
http://creativecommons.org/licenses/by/3.0/es
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 15 p.
application/pdf
dc.publisher.none.fl_str_mv Public Library of Science (PLoS)
publisher.none.fl_str_mv Public Library of Science (PLoS)
dc.source.none.fl_str_mv Articles publicats en revistes (Bioquímica i Biomedicina Molecular)
reponame:Recercat. Dipósit de la Recerca de Catalunya
instname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
instname_str Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
reponame_str Recercat. Dipósit de la Recerca de Catalunya
collection Recercat. Dipósit de la Recerca de Catalunya
repository.name.fl_str_mv
repository.mail.fl_str_mv
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