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Mitochondrial phospholipase A2 activated by reactive oxygen species in heart mitochondria induces mild uncoupling
- 1.0355105 - FGÚ 2011 RIV CZ eng J - Journal Article
Ježek, Jan - Jabůrek, Martin - Zelenka, Jaroslav - Ježek, Petr
Mitochondrial phospholipase A2 activated by reactive oxygen species in heart mitochondria induces mild uncoupling.
Physiological Research. Roč. 59, č. 5 (2010), s. 737-747. ISSN 0862-8408. E-ISSN 1802-9973
R&D Projects: GA ČR(CZ) GA303/07/0105; GA MŠMT ME09018; GA AV ČR(CZ) KJB500110902
Institutional research plan: CEZ:AV0Z50110509
Keywords : Heart mitochondrial phospholipase A2 * Fatty Acids * Adenine nucleotide translocase
Subject RIV: ED - Physiology
Impact factor: 1.646, year: 2010
Homeostasis of reactive oxygen species in cardiomyocytes is critical for elucidation of normal heart physiology and pathology. Mitochondrial phospholipases A2 have been previously suggested to be activated by ROS. We have found that function of a specific i-isoform of mitochondrial phospholipase A2is activated by tert-butylhydroperoxide in isolated rat heart mitochondria. Concomitant uncoupling has been caused by free fatty acids, since it was inhibited by bovine serum albumin. Since this uncoupling was sensitive to carboxyatractyloside and purine nucleotide di- and tri- phosphates, we conclude that it originated from the onset of fatty acid cycling mediated by the adenine nucleotide translocase (major contribution) and mitochondrial uncoupling protein(s) (minor contribution), respectively. In conclusion, ROS-induced function of cardiac mt-iPLA2 may stand on a pro-survival side of ischemia-reperfusion injury
Permanent Link: http://hdl.handle.net/11104/0193948
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