Difference between revisions of "Jezek 2010 Physiol Res"
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{{Publication | {{Publication | ||
|title= | |title=Ježek J, Jabůrek M, Zelenka J, Ježek P (2010) Mitochondrial phospholipase A<sub>2</sub> activated by reactive oxygen species in heart mitochondria induces mild uncoupling. Physiol Res 59:737-47. | ||
|info=[http://www.ncbi.nlm.nih.gov/pubmed/20406040 PMID:20406040] | |info=[http://www.ncbi.nlm.nih.gov/pubmed/20406040 PMID: 20406040 Open Access] | ||
|authors=Jezek J, Jaburek M, Zelenka J, Jezek P | |authors=Jezek J, Jaburek M, Zelenka J, Jezek P | ||
|year=2010 | |year=2010 | ||
|journal=Physiol | |journal=Physiol Res | ||
|abstract=Homeostasis of reactive oxygen species (ROS) in cardiomyocytes is critical for elucidation of normal heart physiology and pathology. Mitochondrial phospholipases | |abstract=Homeostasis of reactive oxygen species (ROS) in cardiomyocytes is critical for elucidation of normal heart physiology and pathology. Mitochondrial phospholipases A<sub>2</sub> (mt-PLA<sub>2</sub>) have been previously suggested to be activated by ROS. Therefore, we have attempted to elucidate physiological role of such activation. We have found that function of a specific i-isoform of mitochondrial phospholipase A<sub>2</sub> (mt-iPLA<sub>2</sub>) is activated by ''tert''-butylhydroperoxide in isolated rat heart mitochondria. Isoform specificity was judged from the inhibition by bromoenol lactone (BEL), a specific iPLA<sub>2</sub> inhibitor. Concomitant uncoupling has been caused by free fatty acids, since it was inhibited by bovine serum albumin. The uncoupling was manifested as a respiration burst accompanied by a slight decrease in mitochondrial inner membrane potential. 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. Such a mild uncoupling may provide a feedback downregulation of oxidative stress, since it can further attenuate mitochondrial production of ROS. In conclusion, ROS-induced function of cardiac mt-iPLA<sub>2</sub> may stand on a pro-survival side of ischemia-reperfusion injury. | ||
|keywords= | |keywords=Heart mitochondrial phospholipase A<sub>2</sub>, Fatty acids, Uncoupling of mitochondria, Adenine nucleotide translocase, Defense against oxidative stress | ||
|mipnetlab= | |mipnetlab=CZ Prague Jezek P | ||
}} | }} | ||
{{Labeling | {{Labeling | ||
|organism=Rat | |||
|tissues=Heart | |||
|preparations=Isolated mitochondria | |||
|instruments=Oxygraph-2k | |instruments=Oxygraph-2k | ||
}} | }} | ||
Latest revision as of 15:25, 26 May 2015
| Ježek J, Jabůrek M, Zelenka J, Ježek P (2010) Mitochondrial phospholipase A2 activated by reactive oxygen species in heart mitochondria induces mild uncoupling. Physiol Res 59:737-47. |
Jezek J, Jaburek M, Zelenka J, Jezek P (2010) Physiol Res
Abstract: Homeostasis of reactive oxygen species (ROS) in cardiomyocytes is critical for elucidation of normal heart physiology and pathology. Mitochondrial phospholipases A2 (mt-PLA2) have been previously suggested to be activated by ROS. Therefore, we have attempted to elucidate physiological role of such activation. We have found that function of a specific i-isoform of mitochondrial phospholipase A2 (mt-iPLA2) is activated by tert-butylhydroperoxide in isolated rat heart mitochondria. Isoform specificity was judged from the inhibition by bromoenol lactone (BEL), a specific iPLA2 inhibitor. Concomitant uncoupling has been caused by free fatty acids, since it was inhibited by bovine serum albumin. The uncoupling was manifested as a respiration burst accompanied by a slight decrease in mitochondrial inner membrane potential. 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. Such a mild uncoupling may provide a feedback downregulation of oxidative stress, since it can further attenuate mitochondrial production of ROS. In conclusion, ROS-induced function of cardiac mt-iPLA2 may stand on a pro-survival side of ischemia-reperfusion injury. • Keywords: Heart mitochondrial phospholipase A2, Fatty acids, Uncoupling of mitochondria, Adenine nucleotide translocase, Defense against oxidative stress
• O2k-Network Lab: CZ Prague Jezek P
Labels:
Organism: Rat
Tissue;cell: Heart
Preparation: Isolated mitochondria
HRR: Oxygraph-2k
