Microtubular integrity differentially modifies the saturated and unsaturated fatty acid metabolism in cultured hep G2 human hepatoma cells

Autores
Marra, Carlos Alberto; Tacconi de Alaniz, María Josefa
Año de publicación
2005
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The influence of cytoskeleton integrity on the metabolism of saturated and unsaturated FA was studied in surface cultures and cell suspensions of human Hep G2 hepatoma cells. We found that colchicine (COL), nocodazol, and vinblastin produced a significant inhibition in the incorporation of labeled saturated FA, whereas incorporation of the unsaturated FA remained unaltered. These microtubule-disrupting drugs also diminished Δ9-, Δ5-, and Δ6-desaturase capacities. The effects produced by COL were dose (0–50 μM) and time (0–300 min) dependent, and were antagonized by stabilizing agents (phalloidin and DMSO). Dihydrocytochalasin B (20μM) was tested as a microfilament-disrupting drug and produced no changes in either the incorporation of [14C]FA or the desaturase conversion of the substrates. We hypothesized that the interactions between cytoskeleton and membrane proteins such as FA desaturases may explain the functional organization, facilitating both substrate channeling and regulation of unsaturated FA biosynthesis.
Instituto de Investigaciones Bioquímicas de La Plata
Materia
Bioquímica
Cytoskeleton
Hep G2 hepatoma cells
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/143599

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network_name_str SEDICI (UNLP)
spelling Microtubular integrity differentially modifies the saturated and unsaturated fatty acid metabolism in cultured hep G2 human hepatoma cellsMarra, Carlos AlbertoTacconi de Alaniz, María JosefaBioquímicaCytoskeletonHep G2 hepatoma cellsThe influence of cytoskeleton integrity on the metabolism of saturated and unsaturated FA was studied in surface cultures and cell suspensions of human Hep G2 hepatoma cells. We found that colchicine (COL), nocodazol, and vinblastin produced a significant inhibition in the incorporation of labeled saturated FA, whereas incorporation of the unsaturated FA remained unaltered. These microtubule-disrupting drugs also diminished Δ9-, Δ5-, and Δ6-desaturase capacities. The effects produced by COL were dose (0–50 μM) and time (0–300 min) dependent, and were antagonized by stabilizing agents (phalloidin and DMSO). Dihydrocytochalasin B (20μM) was tested as a microfilament-disrupting drug and produced no changes in either the incorporation of [14C]FA or the desaturase conversion of the substrates. We hypothesized that the interactions between cytoskeleton and membrane proteins such as FA desaturases may explain the functional organization, facilitating both substrate channeling and regulation of unsaturated FA biosynthesis.Instituto de Investigaciones Bioquímicas de La Plata2005info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf999-1006http://sedici.unlp.edu.ar/handle/10915/143599enginfo:eu-repo/semantics/altIdentifier/issn/0024-4201info:eu-repo/semantics/altIdentifier/issn/1558-9307info:eu-repo/semantics/altIdentifier/doi/10.1007/s11745-005-1462-5info:eu-repo/semantics/altIdentifier/pmid/16382571info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-03T11:04:18Zoai:sedici.unlp.edu.ar:10915/143599Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-03 11:04:18.546SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Microtubular integrity differentially modifies the saturated and unsaturated fatty acid metabolism in cultured hep G2 human hepatoma cells
title Microtubular integrity differentially modifies the saturated and unsaturated fatty acid metabolism in cultured hep G2 human hepatoma cells
spellingShingle Microtubular integrity differentially modifies the saturated and unsaturated fatty acid metabolism in cultured hep G2 human hepatoma cells
Marra, Carlos Alberto
Bioquímica
Cytoskeleton
Hep G2 hepatoma cells
title_short Microtubular integrity differentially modifies the saturated and unsaturated fatty acid metabolism in cultured hep G2 human hepatoma cells
title_full Microtubular integrity differentially modifies the saturated and unsaturated fatty acid metabolism in cultured hep G2 human hepatoma cells
title_fullStr Microtubular integrity differentially modifies the saturated and unsaturated fatty acid metabolism in cultured hep G2 human hepatoma cells
title_full_unstemmed Microtubular integrity differentially modifies the saturated and unsaturated fatty acid metabolism in cultured hep G2 human hepatoma cells
title_sort Microtubular integrity differentially modifies the saturated and unsaturated fatty acid metabolism in cultured hep G2 human hepatoma cells
dc.creator.none.fl_str_mv Marra, Carlos Alberto
Tacconi de Alaniz, María Josefa
author Marra, Carlos Alberto
author_facet Marra, Carlos Alberto
Tacconi de Alaniz, María Josefa
author_role author
author2 Tacconi de Alaniz, María Josefa
author2_role author
dc.subject.none.fl_str_mv Bioquímica
Cytoskeleton
Hep G2 hepatoma cells
topic Bioquímica
Cytoskeleton
Hep G2 hepatoma cells
dc.description.none.fl_txt_mv The influence of cytoskeleton integrity on the metabolism of saturated and unsaturated FA was studied in surface cultures and cell suspensions of human Hep G2 hepatoma cells. We found that colchicine (COL), nocodazol, and vinblastin produced a significant inhibition in the incorporation of labeled saturated FA, whereas incorporation of the unsaturated FA remained unaltered. These microtubule-disrupting drugs also diminished Δ9-, Δ5-, and Δ6-desaturase capacities. The effects produced by COL were dose (0–50 μM) and time (0–300 min) dependent, and were antagonized by stabilizing agents (phalloidin and DMSO). Dihydrocytochalasin B (20μM) was tested as a microfilament-disrupting drug and produced no changes in either the incorporation of [14C]FA or the desaturase conversion of the substrates. We hypothesized that the interactions between cytoskeleton and membrane proteins such as FA desaturases may explain the functional organization, facilitating both substrate channeling and regulation of unsaturated FA biosynthesis.
Instituto de Investigaciones Bioquímicas de La Plata
description The influence of cytoskeleton integrity on the metabolism of saturated and unsaturated FA was studied in surface cultures and cell suspensions of human Hep G2 hepatoma cells. We found that colchicine (COL), nocodazol, and vinblastin produced a significant inhibition in the incorporation of labeled saturated FA, whereas incorporation of the unsaturated FA remained unaltered. These microtubule-disrupting drugs also diminished Δ9-, Δ5-, and Δ6-desaturase capacities. The effects produced by COL were dose (0–50 μM) and time (0–300 min) dependent, and were antagonized by stabilizing agents (phalloidin and DMSO). Dihydrocytochalasin B (20μM) was tested as a microfilament-disrupting drug and produced no changes in either the incorporation of [14C]FA or the desaturase conversion of the substrates. We hypothesized that the interactions between cytoskeleton and membrane proteins such as FA desaturases may explain the functional organization, facilitating both substrate channeling and regulation of unsaturated FA biosynthesis.
publishDate 2005
dc.date.none.fl_str_mv 2005
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://sedici.unlp.edu.ar/handle/10915/143599
url http://sedici.unlp.edu.ar/handle/10915/143599
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/0024-4201
info:eu-repo/semantics/altIdentifier/issn/1558-9307
info:eu-repo/semantics/altIdentifier/doi/10.1007/s11745-005-1462-5
info:eu-repo/semantics/altIdentifier/pmid/16382571
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
999-1006
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
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institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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