The Adipokine Chemerin Induces Apoptosis in Cardiomyocytes
Background: The adipokine chemerin has been associated with cardiovascular disease. We investigated the effects of chemerin on viability and intracellular signalling in murine cardiomyocytes, and the effects of insulin and TNF-α on cardiomyocyte chemerin production. Methods: Hoechst dye vital staini...
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Format: | Article |
Language: | English |
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Cell Physiol Biochem Press GmbH & Co KG
2015-08-01
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Series: | Cellular Physiology and Biochemistry |
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Online Access: | http://www.karger.com/Article/FullText/430343 |
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author | Diego Rodríguez-Penas Sandra Feijóo-Bandín Vanessa García-Rúa Ana Mosquera-Leal Darío Durán Alfonso Varela Manuel Portolés Esther Roselló-Lletí Miguel Rivera Carlos Diéguez Oreste Gualillo José Ramón González-Juanatey Francisca Lago |
author_facet | Diego Rodríguez-Penas Sandra Feijóo-Bandín Vanessa García-Rúa Ana Mosquera-Leal Darío Durán Alfonso Varela Manuel Portolés Esther Roselló-Lletí Miguel Rivera Carlos Diéguez Oreste Gualillo José Ramón González-Juanatey Francisca Lago |
author_sort | Diego Rodríguez-Penas |
collection | DOAJ |
description | Background: The adipokine chemerin has been associated with cardiovascular disease. We investigated the effects of chemerin on viability and intracellular signalling in murine cardiomyocytes, and the effects of insulin and TNF-α on cardiomyocyte chemerin production. Methods: Hoechst dye vital staining and cell cycle analysis were used to analyse the viability of murine cardiac cells in culture. Western blot was used to explore the phosphorylation of AKT and caspase-9 activity in neonatal rat cardiomyocytes and HL-1 cells. Finally, RT-qPCR, ELISA and western blot were performed to examine chemerin and CMKLR1 expression after insulin and TNF-α treatment in cardiac cells. Results: Chemerin treatment increased apoptosis, reduced phosphorylation of AKT at Thr308 and increased caspase-9 activity in murine cardiomyocytes. Insulin treatment lowered chemerin and CMKLR1 mRNA and protein levels, and the amount of chemerin in the cell media, while TNF-α treatment increased chemerin mRNA and protein levels but decreased expression of the CMKLR1 gene. Conclusion: Chemerin induces apoptosis, reduces AKT phosphorylation and increases the cleavage of caspase-9 in murine cardiomyocytes. The expression of chemerin is regulated by important metabolic (insulin) and inflammatory (TNF-α) mediators at cardiac level. Our results suggest that chemerin could play a role in the physiopathology of cardiac diseases. |
first_indexed | 2024-04-13T05:59:24Z |
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id | doaj.art-4c84243e242d4378be8f0d275c4b1ff1 |
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issn | 1015-8987 1421-9778 |
language | English |
last_indexed | 2024-04-13T05:59:24Z |
publishDate | 2015-08-01 |
publisher | Cell Physiol Biochem Press GmbH & Co KG |
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series | Cellular Physiology and Biochemistry |
spelling | doaj.art-4c84243e242d4378be8f0d275c4b1ff12022-12-22T02:59:29ZengCell Physiol Biochem Press GmbH & Co KGCellular Physiology and Biochemistry1015-89871421-97782015-08-0137117619210.1159/000430343430343The Adipokine Chemerin Induces Apoptosis in CardiomyocytesDiego Rodríguez-PenasSandra Feijóo-BandínVanessa García-RúaAna Mosquera-LealDarío DuránAlfonso VarelaManuel PortolésEsther Roselló-LletíMiguel RiveraCarlos DiéguezOreste GualilloJosé Ramón González-JuanateyFrancisca LagoBackground: The adipokine chemerin has been associated with cardiovascular disease. We investigated the effects of chemerin on viability and intracellular signalling in murine cardiomyocytes, and the effects of insulin and TNF-α on cardiomyocyte chemerin production. Methods: Hoechst dye vital staining and cell cycle analysis were used to analyse the viability of murine cardiac cells in culture. Western blot was used to explore the phosphorylation of AKT and caspase-9 activity in neonatal rat cardiomyocytes and HL-1 cells. Finally, RT-qPCR, ELISA and western blot were performed to examine chemerin and CMKLR1 expression after insulin and TNF-α treatment in cardiac cells. Results: Chemerin treatment increased apoptosis, reduced phosphorylation of AKT at Thr308 and increased caspase-9 activity in murine cardiomyocytes. Insulin treatment lowered chemerin and CMKLR1 mRNA and protein levels, and the amount of chemerin in the cell media, while TNF-α treatment increased chemerin mRNA and protein levels but decreased expression of the CMKLR1 gene. Conclusion: Chemerin induces apoptosis, reduces AKT phosphorylation and increases the cleavage of caspase-9 in murine cardiomyocytes. The expression of chemerin is regulated by important metabolic (insulin) and inflammatory (TNF-α) mediators at cardiac level. Our results suggest that chemerin could play a role in the physiopathology of cardiac diseases.http://www.karger.com/Article/FullText/430343CardiomyocyteTNF-αInsulin resistanceAKTHL-1ApoptosisChemerin |
spellingShingle | Diego Rodríguez-Penas Sandra Feijóo-Bandín Vanessa García-Rúa Ana Mosquera-Leal Darío Durán Alfonso Varela Manuel Portolés Esther Roselló-Lletí Miguel Rivera Carlos Diéguez Oreste Gualillo José Ramón González-Juanatey Francisca Lago The Adipokine Chemerin Induces Apoptosis in Cardiomyocytes Cellular Physiology and Biochemistry Cardiomyocyte TNF-α Insulin resistance AKT HL-1 Apoptosis Chemerin |
title | The Adipokine Chemerin Induces Apoptosis in Cardiomyocytes |
title_full | The Adipokine Chemerin Induces Apoptosis in Cardiomyocytes |
title_fullStr | The Adipokine Chemerin Induces Apoptosis in Cardiomyocytes |
title_full_unstemmed | The Adipokine Chemerin Induces Apoptosis in Cardiomyocytes |
title_short | The Adipokine Chemerin Induces Apoptosis in Cardiomyocytes |
title_sort | adipokine chemerin induces apoptosis in cardiomyocytes |
topic | Cardiomyocyte TNF-α Insulin resistance AKT HL-1 Apoptosis Chemerin |
url | http://www.karger.com/Article/FullText/430343 |
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