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; . Universidad Autónoma de Madrid; España
Fil: Gómez Puertas, Paulino. CENTRO DE BIOLOGIA MOLECULAR SEVERO OCHOA (CBMSO) ; UNIVERSIDAD AUTONOMA DE MADRID; . Universidad Autónoma de Madrid; España
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/2.5/ar/
- Repositorio
.jpg)
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/198211
Ver los metadatos del registro completo
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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; . Universidad Autónoma de Madrid; EspañaFil: Gómez Puertas, Paulino. CENTRO DE BIOLOGIA MOLECULAR SEVERO OCHOA (CBMSO) ; UNIVERSIDAD AUTONOMA DE MADRID; . Universidad Autónoma de Madrid; EspañaFil: 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/11336/198211Arnedo, 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/doi/10.1194/jlr.M025700info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:08:59Zoai:ri.conicet.gov.ar:11336/198211instacron: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 11:08:59.995CONICET 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; . Universidad Autónoma de Madrid; España Fil: Gómez Puertas, Paulino. CENTRO DE BIOLOGIA MOLECULAR SEVERO OCHOA (CBMSO) ; UNIVERSIDAD AUTONOMA DE MADRID; . Universidad Autónoma de Madrid; España 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/11336/198211 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/11336/198211 |
| 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 |
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eng |
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eng |
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info:eu-repo/semantics/altIdentifier/doi/10.1194/jlr.M025700 |
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openAccess |
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https://creativecommons.org/licenses/by/2.5/ar/ |
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application/pdf application/pdf |
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American Society for Biochemistry and Molecular Biology |
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American Society for Biochemistry and Molecular Biology |
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CONICET Digital (CONICET) |
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Consejo Nacional de Investigaciones Científicas y Técnicas |
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CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
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dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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