Phosphofructokinase and Malate Dehydrogenase Participate in the In Vitro Maturation of Porcine Oocytes
- Autores
- Cetica, Pablo Daniel; Gutnisky, Cynthia; Alvarez, Gabriel Martin; Vecchi Galenda, Bruno; Breininger, Elizabeth
- Año de publicación
- 2014
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Oocyte maturation depends on the metabolic activity of cumulus-oocyte complex (COC) that performs nutritive and regulatory functions during this process. In this work, the enzymes [phosphofructokinase (PFK) and malate dehydrogenase (MDH)] were tested to elucidate the metabolic profile of porcine COCs during the in vitro maturation (IVM). Enzymatic activity was expressed in U/COC and U/mg protein (specific activity) as mean SEM. In vitro maturation was performed with 2-oxoglutarate (5, 10 and 20 mM) or hydroxymalonate (30, 60 and 100 mM) inhibitors of PFK and MDH, respectively. The PFK and MDH activities (U) remained constant during maturation. For PFK, the U were (2.48 0.23) 10 5 and (2.54 0.32) 10 5, and for MDH, the U were (4.72 0.42) 10 5 and (4.38 0.25) 10 5 for immature and in vitro matured COCs, respectively. The specific activities were significantly lower after IVM, for PFK (4.29 0.48) 10 3 and (0.94 0.12) 10 3, and for MDH (9.08 0.93) 10 3 and (1.89 0.10) 10 3 for immature and in vitro matured COCs, respectively. In vitro maturation percentages and enzymatic activity diminished with 20 mM 2-oxoglutarate or 60 mM hydroxymalonate (p < 0.05). Viability was not affected by any concentration of the inhibitors evaluated. The U remained unchanged during IVM; however, the increase in the total protein content per COC provoked a decrease in the specific activity of both enzymes. Phosphofructokinase and MDH necessary for oocyte IVM would be already present in the immature oocyte. The presence of inhibitors of these enzymes impairs the meiotic maturation. Therefore, the participation of these enzymes in the energy metabolism of the porcine oocyte during IVM is confirmed in this study.
Fil: Cetica, Pablo Daniel. Universidad de Buenos Aires. Facultad de Ciencias Veterinarias. Instituto de Investigacion y Tecnología en Reproducción Animal; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Unidad Ejecutora de Investigaciones en Produccion Animal; Argentina
Fil: Gutnisky, Cynthia. Universidad de Buenos Aires. Facultad de Ciencias Veterinarias. Instituto de Investigacion y Tecnología en Reproducción Animal; Argentina
Fil: Alvarez, Gabriel Martin. Universidad de Buenos Aires. Facultad de Ciencias Veterinarias. Instituto de Investigacion y Tecnología en Reproducción Animal; Argentina
Fil: Vecchi Galenda, Bruno. Universidad de Buenos Aires. Facultad de Ciencias Veterinarias. Instituto de Investigacion y Tecnología en Reproducción Animal; Argentina
Fil: Breininger, Elizabeth. Universidad de Buenos Aires. Facultad de Ciencias Veterinarias. Instituto de Investigacion y Tecnología en Reproducción Animal; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Unidad Ejecutora de Investigaciones en Produccion Animal; Argentina - Materia
-
Phosphofructokinase
Malate Dehydrogenase
Oocyte
Pig - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/8084
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Phosphofructokinase and Malate Dehydrogenase Participate in the In Vitro Maturation of Porcine OocytesCetica, Pablo DanielGutnisky, CynthiaAlvarez, Gabriel MartinVecchi Galenda, BrunoBreininger, ElizabethPhosphofructokinaseMalate DehydrogenaseOocytePighttps://purl.org/becyt/ford/4.3https://purl.org/becyt/ford/4Oocyte maturation depends on the metabolic activity of cumulus-oocyte complex (COC) that performs nutritive and regulatory functions during this process. In this work, the enzymes [phosphofructokinase (PFK) and malate dehydrogenase (MDH)] were tested to elucidate the metabolic profile of porcine COCs during the in vitro maturation (IVM). Enzymatic activity was expressed in U/COC and U/mg protein (specific activity) as mean SEM. In vitro maturation was performed with 2-oxoglutarate (5, 10 and 20 mM) or hydroxymalonate (30, 60 and 100 mM) inhibitors of PFK and MDH, respectively. The PFK and MDH activities (U) remained constant during maturation. For PFK, the U were (2.48 0.23) 10 5 and (2.54 0.32) 10 5, and for MDH, the U were (4.72 0.42) 10 5 and (4.38 0.25) 10 5 for immature and in vitro matured COCs, respectively. The specific activities were significantly lower after IVM, for PFK (4.29 0.48) 10 3 and (0.94 0.12) 10 3, and for MDH (9.08 0.93) 10 3 and (1.89 0.10) 10 3 for immature and in vitro matured COCs, respectively. In vitro maturation percentages and enzymatic activity diminished with 20 mM 2-oxoglutarate or 60 mM hydroxymalonate (p < 0.05). Viability was not affected by any concentration of the inhibitors evaluated. The U remained unchanged during IVM; however, the increase in the total protein content per COC provoked a decrease in the specific activity of both enzymes. Phosphofructokinase and MDH necessary for oocyte IVM would be already present in the immature oocyte. The presence of inhibitors of these enzymes impairs the meiotic maturation. Therefore, the participation of these enzymes in the energy metabolism of the porcine oocyte during IVM is confirmed in this study.Fil: Cetica, Pablo Daniel. Universidad de Buenos Aires. Facultad de Ciencias Veterinarias. Instituto de Investigacion y Tecnología en Reproducción Animal; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Unidad Ejecutora de Investigaciones en Produccion Animal; ArgentinaFil: Gutnisky, Cynthia. Universidad de Buenos Aires. Facultad de Ciencias Veterinarias. Instituto de Investigacion y Tecnología en Reproducción Animal; ArgentinaFil: Alvarez, Gabriel Martin. Universidad de Buenos Aires. Facultad de Ciencias Veterinarias. Instituto de Investigacion y Tecnología en Reproducción Animal; ArgentinaFil: Vecchi Galenda, Bruno. Universidad de Buenos Aires. Facultad de Ciencias Veterinarias. Instituto de Investigacion y Tecnología en Reproducción Animal; ArgentinaFil: Breininger, Elizabeth. Universidad de Buenos Aires. Facultad de Ciencias Veterinarias. Instituto de Investigacion y Tecnología en Reproducción Animal; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Unidad Ejecutora de Investigaciones en Produccion Animal; ArgentinaWiley2014-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/8084Cetica, Pablo Daniel; Gutnisky, Cynthia; Alvarez, Gabriel Martin; Vecchi Galenda, Bruno; Breininger, Elizabeth; Phosphofructokinase and Malate Dehydrogenase Participate in the In Vitro Maturation of Porcine Oocytes; Wiley; Reproduction In Domestic Animals; 49; 6; 12-2014; 1068-10730936-6768enginfo:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1111/rda.12437/abstractinfo:eu-repo/semantics/altIdentifier/doi/10.1111/rda.12437info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:47:00Zoai:ri.conicet.gov.ar:11336/8084instacron: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:34982025-09-29 09:47:00.749CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Phosphofructokinase and Malate Dehydrogenase Participate in the In Vitro Maturation of Porcine Oocytes |
title |
Phosphofructokinase and Malate Dehydrogenase Participate in the In Vitro Maturation of Porcine Oocytes |
spellingShingle |
Phosphofructokinase and Malate Dehydrogenase Participate in the In Vitro Maturation of Porcine Oocytes Cetica, Pablo Daniel Phosphofructokinase Malate Dehydrogenase Oocyte Pig |
title_short |
Phosphofructokinase and Malate Dehydrogenase Participate in the In Vitro Maturation of Porcine Oocytes |
title_full |
Phosphofructokinase and Malate Dehydrogenase Participate in the In Vitro Maturation of Porcine Oocytes |
title_fullStr |
Phosphofructokinase and Malate Dehydrogenase Participate in the In Vitro Maturation of Porcine Oocytes |
title_full_unstemmed |
Phosphofructokinase and Malate Dehydrogenase Participate in the In Vitro Maturation of Porcine Oocytes |
title_sort |
Phosphofructokinase and Malate Dehydrogenase Participate in the In Vitro Maturation of Porcine Oocytes |
dc.creator.none.fl_str_mv |
Cetica, Pablo Daniel Gutnisky, Cynthia Alvarez, Gabriel Martin Vecchi Galenda, Bruno Breininger, Elizabeth |
author |
Cetica, Pablo Daniel |
author_facet |
Cetica, Pablo Daniel Gutnisky, Cynthia Alvarez, Gabriel Martin Vecchi Galenda, Bruno Breininger, Elizabeth |
author_role |
author |
author2 |
Gutnisky, Cynthia Alvarez, Gabriel Martin Vecchi Galenda, Bruno Breininger, Elizabeth |
author2_role |
author author author author |
dc.subject.none.fl_str_mv |
Phosphofructokinase Malate Dehydrogenase Oocyte Pig |
topic |
Phosphofructokinase Malate Dehydrogenase Oocyte Pig |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/4.3 https://purl.org/becyt/ford/4 |
dc.description.none.fl_txt_mv |
Oocyte maturation depends on the metabolic activity of cumulus-oocyte complex (COC) that performs nutritive and regulatory functions during this process. In this work, the enzymes [phosphofructokinase (PFK) and malate dehydrogenase (MDH)] were tested to elucidate the metabolic profile of porcine COCs during the in vitro maturation (IVM). Enzymatic activity was expressed in U/COC and U/mg protein (specific activity) as mean SEM. In vitro maturation was performed with 2-oxoglutarate (5, 10 and 20 mM) or hydroxymalonate (30, 60 and 100 mM) inhibitors of PFK and MDH, respectively. The PFK and MDH activities (U) remained constant during maturation. For PFK, the U were (2.48 0.23) 10 5 and (2.54 0.32) 10 5, and for MDH, the U were (4.72 0.42) 10 5 and (4.38 0.25) 10 5 for immature and in vitro matured COCs, respectively. The specific activities were significantly lower after IVM, for PFK (4.29 0.48) 10 3 and (0.94 0.12) 10 3, and for MDH (9.08 0.93) 10 3 and (1.89 0.10) 10 3 for immature and in vitro matured COCs, respectively. In vitro maturation percentages and enzymatic activity diminished with 20 mM 2-oxoglutarate or 60 mM hydroxymalonate (p < 0.05). Viability was not affected by any concentration of the inhibitors evaluated. The U remained unchanged during IVM; however, the increase in the total protein content per COC provoked a decrease in the specific activity of both enzymes. Phosphofructokinase and MDH necessary for oocyte IVM would be already present in the immature oocyte. The presence of inhibitors of these enzymes impairs the meiotic maturation. Therefore, the participation of these enzymes in the energy metabolism of the porcine oocyte during IVM is confirmed in this study. Fil: Cetica, Pablo Daniel. Universidad de Buenos Aires. Facultad de Ciencias Veterinarias. Instituto de Investigacion y Tecnología en Reproducción Animal; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Unidad Ejecutora de Investigaciones en Produccion Animal; Argentina Fil: Gutnisky, Cynthia. Universidad de Buenos Aires. Facultad de Ciencias Veterinarias. Instituto de Investigacion y Tecnología en Reproducción Animal; Argentina Fil: Alvarez, Gabriel Martin. Universidad de Buenos Aires. Facultad de Ciencias Veterinarias. Instituto de Investigacion y Tecnología en Reproducción Animal; Argentina Fil: Vecchi Galenda, Bruno. Universidad de Buenos Aires. Facultad de Ciencias Veterinarias. Instituto de Investigacion y Tecnología en Reproducción Animal; Argentina Fil: Breininger, Elizabeth. Universidad de Buenos Aires. Facultad de Ciencias Veterinarias. Instituto de Investigacion y Tecnología en Reproducción Animal; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Unidad Ejecutora de Investigaciones en Produccion Animal; Argentina |
description |
Oocyte maturation depends on the metabolic activity of cumulus-oocyte complex (COC) that performs nutritive and regulatory functions during this process. In this work, the enzymes [phosphofructokinase (PFK) and malate dehydrogenase (MDH)] were tested to elucidate the metabolic profile of porcine COCs during the in vitro maturation (IVM). Enzymatic activity was expressed in U/COC and U/mg protein (specific activity) as mean SEM. In vitro maturation was performed with 2-oxoglutarate (5, 10 and 20 mM) or hydroxymalonate (30, 60 and 100 mM) inhibitors of PFK and MDH, respectively. The PFK and MDH activities (U) remained constant during maturation. For PFK, the U were (2.48 0.23) 10 5 and (2.54 0.32) 10 5, and for MDH, the U were (4.72 0.42) 10 5 and (4.38 0.25) 10 5 for immature and in vitro matured COCs, respectively. The specific activities were significantly lower after IVM, for PFK (4.29 0.48) 10 3 and (0.94 0.12) 10 3, and for MDH (9.08 0.93) 10 3 and (1.89 0.10) 10 3 for immature and in vitro matured COCs, respectively. In vitro maturation percentages and enzymatic activity diminished with 20 mM 2-oxoglutarate or 60 mM hydroxymalonate (p < 0.05). Viability was not affected by any concentration of the inhibitors evaluated. The U remained unchanged during IVM; however, the increase in the total protein content per COC provoked a decrease in the specific activity of both enzymes. Phosphofructokinase and MDH necessary for oocyte IVM would be already present in the immature oocyte. The presence of inhibitors of these enzymes impairs the meiotic maturation. Therefore, the participation of these enzymes in the energy metabolism of the porcine oocyte during IVM is confirmed in this study. |
publishDate |
2014 |
dc.date.none.fl_str_mv |
2014-12 |
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/11336/8084 Cetica, Pablo Daniel; Gutnisky, Cynthia; Alvarez, Gabriel Martin; Vecchi Galenda, Bruno; Breininger, Elizabeth; Phosphofructokinase and Malate Dehydrogenase Participate in the In Vitro Maturation of Porcine Oocytes; Wiley; Reproduction In Domestic Animals; 49; 6; 12-2014; 1068-1073 0936-6768 |
url |
http://hdl.handle.net/11336/8084 |
identifier_str_mv |
Cetica, Pablo Daniel; Gutnisky, Cynthia; Alvarez, Gabriel Martin; Vecchi Galenda, Bruno; Breininger, Elizabeth; Phosphofructokinase and Malate Dehydrogenase Participate in the In Vitro Maturation of Porcine Oocytes; Wiley; Reproduction In Domestic Animals; 49; 6; 12-2014; 1068-1073 0936-6768 |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1111/rda.12437/abstract info:eu-repo/semantics/altIdentifier/doi/10.1111/rda.12437 |
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 application/pdf application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Wiley |
publisher.none.fl_str_mv |
Wiley |
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 |
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1844613465569755136 |
score |
13.070432 |