Characterization of a novel HMG-CoA lyase enzyme with a dual location in endoplasmic reticulum and cytosol

Autores
Arnedo, María; Menao, Sebastián; Puisac, Beatriz; Teresa Rodrigo, María E.; Gil Rodríguez, María C.; López Viñas, Eduardo; Gómez Puertas, Paulino; Casals, Nuria; Casale, Cesar Horacio; Hegardt, Fausto G.; Pié, Juan
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
A novel lyase activity enzyme is characterized for the first time: HMG-CoA lyase-like1 (er-cHL), which is a close homolog of mitochondrial HMG-CoA lyase (mHL). Initial data show that there are nine mature transcripts for the novel gene HMGCLL1, although none of them has all its exons. The most abundant transcript is called "variant b," and it lacks exons 2 and 3. Moreover, a three-dimensional model of the novel enzyme is proposed. Colocalization studies show a dual location of the er-cHL in the endoplasmic reticulum (ER) and cytosol, but not in mitochondria or peroxisomes. Furthermore, the dissociation experiment suggests that it is a nonendoplasmic reticulum integral membrane protein. The kinetic parameters of er-cHL indicate that it has a lower Vmax and a higher substrate affinity than mHL. Protein expression and lyase activity were found in several tissues, and were particularly strong in lung and kidney. The occurrence of er-cHL in brain is surprising, as mHL has not been found there. Although mHL activity is clearly associated with energy metabolism, the results suggest that er-cHL is more closely related to another metabolic function, mostly at the pulmonary and brain level.
Fil: Arnedo, María. Universidad de Zaragoza; España
Fil: Menao, Sebastián. Universidad de Zaragoza; España
Fil: Puisac, Beatriz. Universidad de Zaragoza; España
Fil: Teresa Rodrigo, María E.. Universidad de Zaragoza; España
Fil: Gil Rodríguez, María C.. Universidad de Zaragoza; España
Fil: López Viñas, Eduardo. CENTRO DE BIOLOGIA MOLECULAR SEVERO OCHOA (CBMSO) ; UNIVERSIDAD AUTONOMA DE MADRID;
Fil: Gómez Puertas, Paulino. CENTRO DE BIOLOGIA MOLECULAR SEVERO OCHOA (CBMSO) ; UNIVERSIDAD AUTONOMA DE MADRID;
Fil: Casals, Nuria. Universitat Internacional de Catalunya; España
Fil: Casale, Cesar Horacio. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Instituto de Biotecnología Ambiental y Salud - Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Biotecnología Ambiental y Salud; Argentina
Fil: Hegardt, Fausto G.. Universidad de Barcelona; España
Fil: Pié, Juan. Universidad de Zaragoza; España
Materia
BRAIN
ENDOPLASMIC RETICULUM-CYTOSOLIC HMG-COA LYASE
ENZYMOLOGY
KETONE BODIES
KINETICS
LIVER
LUNG
LYASE ACTIVITY
MITOCHONDRIAL HMG-COA LYASE
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/198855
Acceder
id CONICETDig_b0f2d5e321c6b675290ec1c283e38410
oai_identifier_str oai:ri.conicet.gov.ar:11336/198855
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Characterization of a novel HMG-CoA lyase enzyme with a dual location in endoplasmic reticulum and cytosolArnedo, MaríaMenao, SebastiánPuisac, BeatrizTeresa Rodrigo, María E.Gil Rodríguez, María C.López Viñas, EduardoGómez Puertas, PaulinoCasals, NuriaCasale, Cesar HoracioHegardt, Fausto G.Pié, JuanBRAINENDOPLASMIC RETICULUM-CYTOSOLIC HMG-COA LYASEENZYMOLOGYKETONE BODIESKINETICSLIVERLUNGLYASE ACTIVITYMITOCHONDRIAL HMG-COA LYASEhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1A novel lyase activity enzyme is characterized for the first time: HMG-CoA lyase-like1 (er-cHL), which is a close homolog of mitochondrial HMG-CoA lyase (mHL). Initial data show that there are nine mature transcripts for the novel gene HMGCLL1, although none of them has all its exons. The most abundant transcript is called "variant b," and it lacks exons 2 and 3. Moreover, a three-dimensional model of the novel enzyme is proposed. Colocalization studies show a dual location of the er-cHL in the endoplasmic reticulum (ER) and cytosol, but not in mitochondria or peroxisomes. Furthermore, the dissociation experiment suggests that it is a nonendoplasmic reticulum integral membrane protein. The kinetic parameters of er-cHL indicate that it has a lower Vmax and a higher substrate affinity than mHL. Protein expression and lyase activity were found in several tissues, and were particularly strong in lung and kidney. The occurrence of er-cHL in brain is surprising, as mHL has not been found there. Although mHL activity is clearly associated with energy metabolism, the results suggest that er-cHL is more closely related to another metabolic function, mostly at the pulmonary and brain level.Fil: Arnedo, María. Universidad de Zaragoza; EspañaFil: Menao, Sebastián. Universidad de Zaragoza; EspañaFil: Puisac, Beatriz. Universidad de Zaragoza; EspañaFil: Teresa Rodrigo, María E.. Universidad de Zaragoza; EspañaFil: Gil Rodríguez, María C.. Universidad de Zaragoza; EspañaFil: López Viñas, Eduardo. CENTRO DE BIOLOGIA MOLECULAR SEVERO OCHOA (CBMSO) ; UNIVERSIDAD AUTONOMA DE MADRID;Fil: Gómez Puertas, Paulino. CENTRO DE BIOLOGIA MOLECULAR SEVERO OCHOA (CBMSO) ; UNIVERSIDAD AUTONOMA DE MADRID;Fil: Casals, Nuria. Universitat Internacional de Catalunya; EspañaFil: Casale, Cesar Horacio. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Instituto de Biotecnología Ambiental y Salud - Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Biotecnología Ambiental y Salud; ArgentinaFil: Hegardt, Fausto G.. Universidad de Barcelona; EspañaFil: Pié, Juan. Universidad de Zaragoza; EspañaAmerican Society for Biochemistry and Molecular Biology2012-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/198855Arnedo, María; Menao, Sebastián; Puisac, Beatriz; Teresa Rodrigo, María E.; Gil Rodríguez, María C.; et al.; Characterization of a novel HMG-CoA lyase enzyme with a dual location in endoplasmic reticulum and cytosol; American Society for Biochemistry and Molecular Biology; Journal of Lipid Research Papers In Press; 53; 10; 10-2012; 2046-20560022-22751539-7262CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://pubmed.ncbi.nlm.nih.gov/22847177/info:eu-repo/semantics/altIdentifier/doi/10.1194/jlr.M025700info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:52:27Zoai:ri.conicet.gov.ar:11336/198855instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-22 11:52:28.115CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Characterization of a novel HMG-CoA lyase enzyme with a dual location in endoplasmic reticulum and cytosol
title Characterization of a novel HMG-CoA lyase enzyme with a dual location in endoplasmic reticulum and cytosol
spellingShingle Characterization of a novel HMG-CoA lyase enzyme with a dual location in endoplasmic reticulum and cytosol
Arnedo, María
BRAIN
ENDOPLASMIC RETICULUM-CYTOSOLIC HMG-COA LYASE
ENZYMOLOGY
KETONE BODIES
KINETICS
LIVER
LUNG
LYASE ACTIVITY
MITOCHONDRIAL HMG-COA LYASE
title_short Characterization of a novel HMG-CoA lyase enzyme with a dual location in endoplasmic reticulum and cytosol
title_full Characterization of a novel HMG-CoA lyase enzyme with a dual location in endoplasmic reticulum and cytosol
title_fullStr Characterization of a novel HMG-CoA lyase enzyme with a dual location in endoplasmic reticulum and cytosol
title_full_unstemmed Characterization of a novel HMG-CoA lyase enzyme with a dual location in endoplasmic reticulum and cytosol
title_sort Characterization of a novel HMG-CoA lyase enzyme with a dual location in endoplasmic reticulum and cytosol
dc.creator.none.fl_str_mv Arnedo, María
Menao, Sebastián
Puisac, Beatriz
Teresa Rodrigo, María E.
Gil Rodríguez, María C.
López Viñas, Eduardo
Gómez Puertas, Paulino
Casals, Nuria
Casale, Cesar Horacio
Hegardt, Fausto G.
Pié, Juan
author Arnedo, María
author_facet Arnedo, María
Menao, Sebastián
Puisac, Beatriz
Teresa Rodrigo, María E.
Gil Rodríguez, María C.
López Viñas, Eduardo
Gómez Puertas, Paulino
Casals, Nuria
Casale, Cesar Horacio
Hegardt, Fausto G.
Pié, Juan
author_role author
author2 Menao, Sebastián
Puisac, Beatriz
Teresa Rodrigo, María E.
Gil Rodríguez, María C.
López Viñas, Eduardo
Gómez Puertas, Paulino
Casals, Nuria
Casale, Cesar Horacio
Hegardt, Fausto G.
Pié, Juan
author2_role author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv BRAIN
ENDOPLASMIC RETICULUM-CYTOSOLIC HMG-COA LYASE
ENZYMOLOGY
KETONE BODIES
KINETICS
LIVER
LUNG
LYASE ACTIVITY
MITOCHONDRIAL HMG-COA LYASE
topic BRAIN
ENDOPLASMIC RETICULUM-CYTOSOLIC HMG-COA LYASE
ENZYMOLOGY
KETONE BODIES
KINETICS
LIVER
LUNG
LYASE ACTIVITY
MITOCHONDRIAL HMG-COA LYASE
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv A novel lyase activity enzyme is characterized for the first time: HMG-CoA lyase-like1 (er-cHL), which is a close homolog of mitochondrial HMG-CoA lyase (mHL). Initial data show that there are nine mature transcripts for the novel gene HMGCLL1, although none of them has all its exons. The most abundant transcript is called "variant b," and it lacks exons 2 and 3. Moreover, a three-dimensional model of the novel enzyme is proposed. Colocalization studies show a dual location of the er-cHL in the endoplasmic reticulum (ER) and cytosol, but not in mitochondria or peroxisomes. Furthermore, the dissociation experiment suggests that it is a nonendoplasmic reticulum integral membrane protein. The kinetic parameters of er-cHL indicate that it has a lower Vmax and a higher substrate affinity than mHL. Protein expression and lyase activity were found in several tissues, and were particularly strong in lung and kidney. The occurrence of er-cHL in brain is surprising, as mHL has not been found there. Although mHL activity is clearly associated with energy metabolism, the results suggest that er-cHL is more closely related to another metabolic function, mostly at the pulmonary and brain level.
Fil: Arnedo, María. Universidad de Zaragoza; España
Fil: Menao, Sebastián. Universidad de Zaragoza; España
Fil: Puisac, Beatriz. Universidad de Zaragoza; España
Fil: Teresa Rodrigo, María E.. Universidad de Zaragoza; España
Fil: Gil Rodríguez, María C.. Universidad de Zaragoza; España
Fil: López Viñas, Eduardo. CENTRO DE BIOLOGIA MOLECULAR SEVERO OCHOA (CBMSO) ; UNIVERSIDAD AUTONOMA DE MADRID;
Fil: Gómez Puertas, Paulino. CENTRO DE BIOLOGIA MOLECULAR SEVERO OCHOA (CBMSO) ; UNIVERSIDAD AUTONOMA DE MADRID;
Fil: Casals, Nuria. Universitat Internacional de Catalunya; España
Fil: Casale, Cesar Horacio. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Instituto de Biotecnología Ambiental y Salud - Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Biotecnología Ambiental y Salud; Argentina
Fil: Hegardt, Fausto G.. Universidad de Barcelona; España
Fil: Pié, Juan. Universidad de Zaragoza; España
description A novel lyase activity enzyme is characterized for the first time: HMG-CoA lyase-like1 (er-cHL), which is a close homolog of mitochondrial HMG-CoA lyase (mHL). Initial data show that there are nine mature transcripts for the novel gene HMGCLL1, although none of them has all its exons. The most abundant transcript is called "variant b," and it lacks exons 2 and 3. Moreover, a three-dimensional model of the novel enzyme is proposed. Colocalization studies show a dual location of the er-cHL in the endoplasmic reticulum (ER) and cytosol, but not in mitochondria or peroxisomes. Furthermore, the dissociation experiment suggests that it is a nonendoplasmic reticulum integral membrane protein. The kinetic parameters of er-cHL indicate that it has a lower Vmax and a higher substrate affinity than mHL. Protein expression and lyase activity were found in several tissues, and were particularly strong in lung and kidney. The occurrence of er-cHL in brain is surprising, as mHL has not been found there. Although mHL activity is clearly associated with energy metabolism, the results suggest that er-cHL is more closely related to another metabolic function, mostly at the pulmonary and brain level.
publishDate 2012
dc.date.none.fl_str_mv 2012-10
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
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://hdl.handle.net/11336/198855
Arnedo, María; Menao, Sebastián; Puisac, Beatriz; Teresa Rodrigo, María E.; Gil Rodríguez, María C.; et al.; Characterization of a novel HMG-CoA lyase enzyme with a dual location in endoplasmic reticulum and cytosol; American Society for Biochemistry and Molecular Biology; Journal of Lipid Research Papers In Press; 53; 10; 10-2012; 2046-2056
0022-2275
1539-7262
CONICET Digital
CONICET
url http://hdl.handle.net/11336/198855
identifier_str_mv Arnedo, María; Menao, Sebastián; Puisac, Beatriz; Teresa Rodrigo, María E.; Gil Rodríguez, María C.; et al.; Characterization of a novel HMG-CoA lyase enzyme with a dual location in endoplasmic reticulum and cytosol; American Society for Biochemistry and Molecular Biology; Journal of Lipid Research Papers In Press; 53; 10; 10-2012; 2046-2056
0022-2275
1539-7262
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://pubmed.ncbi.nlm.nih.gov/22847177/
info:eu-repo/semantics/altIdentifier/doi/10.1194/jlr.M025700
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
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:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1846782215985299456
score 12.982451

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