“HETE”ing up mitochondria in human heart failure [Metabolism]
| Publication Date: |
2018-01-06
|
|---|---|
| Publisher: |
The American Society for Biochemistry and Molecular Biology (ASBMB)
|
| Print ISSN: |
0021-9258
|
| Electronic ISSN: |
1083-351X
|
| Topics: |
Biology
Chemistry and Pharmacology
|
| Published by: |
| _version_ | 1836398737975410688 |
|---|---|
| autor | Matthew J. Wolf |
| beschreibung | A decade of research has established the phospholipase iPLA2γ as being involved in cardiomyocyte dysfunction and necrosis leading to heart failure, but the mechanisms by which iPLA2γ acts and its interaction with the mitochondrial permeability transition pore (mPTP) that is critical for cardiac homeostasis are unclear. New investigations by Moon et al. demonstrate that mitochondria in failing hearts undergo dynamic shifts in PLA2 isoform expression, leading to a redistribution of eicosanoid composition that contributes to pathologic mPTP opening. |
| citation_standardnr | 6131958 |
| datenlieferant | ipn_articles |
| feed_id | 43 |
| feed_publisher | The American Society for Biochemistry and Molecular Biology (ASBMB) |
| feed_publisher_url | http://www.asbmb.org/ |
| insertion_date | 2018-01-06 |
| journaleissn | 1083-351X |
| journalissn | 0021-9258 |
| publikationsjahr_anzeige | 2018 |
| publikationsjahr_facette | 2018 |
| publikationsjahr_intervall | 7984:2015-2019 |
| publikationsjahr_sort | 2018 |
| publisher | The American Society for Biochemistry and Molecular Biology (ASBMB) |
| quelle | Journal of Biological Chemistry |
| relation | http://feedproxy.google.com/~r/jbc/SUcv/~3/1NlXWXjYOJ0/130.short |
| search_space | articles |
| shingle_author_1 | Matthew J. Wolf |
| shingle_author_2 | Matthew J. Wolf |
| shingle_author_3 | Matthew J. Wolf |
| shingle_author_4 | Matthew J. Wolf |
| shingle_catch_all_1 | “HETE”ing up mitochondria in human heart failure [Metabolism] A decade of research has established the phospholipase iPLA2γ as being involved in cardiomyocyte dysfunction and necrosis leading to heart failure, but the mechanisms by which iPLA2γ acts and its interaction with the mitochondrial permeability transition pore (mPTP) that is critical for cardiac homeostasis are unclear. New investigations by Moon et al. demonstrate that mitochondria in failing hearts undergo dynamic shifts in PLA2 isoform expression, leading to a redistribution of eicosanoid composition that contributes to pathologic mPTP opening. Matthew J. Wolf The American Society for Biochemistry and Molecular Biology (ASBMB) 0021-9258 00219258 1083-351X 1083351X |
| shingle_catch_all_2 | “HETE”ing up mitochondria in human heart failure [Metabolism] A decade of research has established the phospholipase iPLA2γ as being involved in cardiomyocyte dysfunction and necrosis leading to heart failure, but the mechanisms by which iPLA2γ acts and its interaction with the mitochondrial permeability transition pore (mPTP) that is critical for cardiac homeostasis are unclear. New investigations by Moon et al. demonstrate that mitochondria in failing hearts undergo dynamic shifts in PLA2 isoform expression, leading to a redistribution of eicosanoid composition that contributes to pathologic mPTP opening. Matthew J. Wolf The American Society for Biochemistry and Molecular Biology (ASBMB) 0021-9258 00219258 1083-351X 1083351X |
| shingle_catch_all_3 | “HETE”ing up mitochondria in human heart failure [Metabolism] A decade of research has established the phospholipase iPLA2γ as being involved in cardiomyocyte dysfunction and necrosis leading to heart failure, but the mechanisms by which iPLA2γ acts and its interaction with the mitochondrial permeability transition pore (mPTP) that is critical for cardiac homeostasis are unclear. New investigations by Moon et al. demonstrate that mitochondria in failing hearts undergo dynamic shifts in PLA2 isoform expression, leading to a redistribution of eicosanoid composition that contributes to pathologic mPTP opening. Matthew J. Wolf The American Society for Biochemistry and Molecular Biology (ASBMB) 0021-9258 00219258 1083-351X 1083351X |
| shingle_catch_all_4 | “HETE”ing up mitochondria in human heart failure [Metabolism] A decade of research has established the phospholipase iPLA2γ as being involved in cardiomyocyte dysfunction and necrosis leading to heart failure, but the mechanisms by which iPLA2γ acts and its interaction with the mitochondrial permeability transition pore (mPTP) that is critical for cardiac homeostasis are unclear. New investigations by Moon et al. demonstrate that mitochondria in failing hearts undergo dynamic shifts in PLA2 isoform expression, leading to a redistribution of eicosanoid composition that contributes to pathologic mPTP opening. Matthew J. Wolf The American Society for Biochemistry and Molecular Biology (ASBMB) 0021-9258 00219258 1083-351X 1083351X |
| shingle_title_1 | “HETE”ing up mitochondria in human heart failure [Metabolism] |
| shingle_title_2 | “HETE”ing up mitochondria in human heart failure [Metabolism] |
| shingle_title_3 | “HETE”ing up mitochondria in human heart failure [Metabolism] |
| shingle_title_4 | “HETE”ing up mitochondria in human heart failure [Metabolism] |
| timestamp | 2025-06-30T23:31:50.006Z |
| titel | “HETE”ing up mitochondria in human heart failure [Metabolism] |
| titel_suche | “HETE”ing up mitochondria in human heart failure [Metabolism] |
| topic | W V |
| uid | ipn_articles_6131958 |