Difference between revisions of "Gizatullina 2005 Biochim Biophys Acta"
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{{Publication | {{Publication | ||
|title=Gizatullina ZZ, Chen Y, Zierz S, Gellerich FN (2005) Effects of extramitochondrial ADP on permeability transition of mouse liver mitochondria. Biochim | |title=Gizatullina ZZ, Chen Y, Zierz S, Gellerich FN (2005) Effects of extramitochondrial ADP on permeability transition of mouse liver mitochondria. Biochim Biophys Acta 1706:98-104. | ||
|info=[http://www.ncbi.nlm.nih.gov/pubmed/15620369 PMID: 15620369 Open Access] | |||
|authors=Gizatullina ZZ, Chen Y, Zierz S, Gellerich FN | |authors=Gizatullina ZZ, Chen Y, Zierz S, Gellerich FN | ||
|year=2005 | |year=2005 | ||
|journal=Biochim | |journal=Biochim Biophys Acta | ||
|abstract=Carboxyatractylate (CAT) and atractylate inhibit the mitochondrial adenine nucleotide translocator (ANT) and stimulate the opening of permeability transition pore (PTP). Following pretreatment of mouse liver mitochondria with 5 μM CAT and 75 μM Ca<sup>2+</sup>, the activity of PTP increased, but addition of 2 mM ADP inhibited the swelling of mitochondria. Extramitochondrial Ca2+ concentration measured with Calcium-Green 5N evidenced that 2 mM ADP did not remarkably decrease the free Ca<sup>2+</sup> but the release of Ca<sup>2+</sup> from loaded mitochondria was stopped effectively after addition of 2 mM ADP. CAT caused a remarkable decrease of the maximum amount of calcium ions, which can be accumulated by mitochondria. Addition of 2 mM ADP after 5 μM CAT did not change the respiration, but increased the mitochondrial capacity for Ca<sup>2+</sup> at more than five times. Bongkrekic acid (BA) had a biphasic effect on PT. In the first minutes 5 μM BA increased the stability of mitochondrial membrane followed by a pronounced opening of PTP too. BA abolished the action about of 1 mM ADP, but was not able to induce swelling of mitochondria in the presence of 2 mM ADP. | |abstract=Carboxyatractylate (CAT) and atractylate inhibit the mitochondrial adenine nucleotide translocator (ANT) and stimulate the opening of permeability transition pore (PTP). Following pretreatment of mouse liver mitochondria with 5 μM CAT and 75 μM Ca<sup>2+</sup>, the activity of PTP increased, but addition of 2 mM ADP inhibited the swelling of mitochondria. Extramitochondrial Ca2+ concentration measured with Calcium-Green 5N evidenced that 2 mM ADP did not remarkably decrease the free Ca<sup>2+</sup> but the release of Ca<sup>2+</sup> from loaded mitochondria was stopped effectively after addition of 2 mM ADP. CAT caused a remarkable decrease of the maximum amount of calcium ions, which can be accumulated by mitochondria. Addition of 2 mM ADP after 5 μM CAT did not change the respiration, but increased the mitochondrial capacity for Ca<sup>2+</sup> at more than five times. Bongkrekic acid (BA) had a biphasic effect on PT. In the first minutes 5 μM BA increased the stability of mitochondrial membrane followed by a pronounced opening of PTP too. BA abolished the action about of 1 mM ADP, but was not able to induce swelling of mitochondria in the presence of 2 mM ADP. | ||
We conclude that the outer side of inner mitochondrial membrane has a low affinity sensor for ADP, modifying the activity of PTP. The pathophysiological importance of this process could be an endogenous prevention of PT at conditions of energetic depression. | We conclude that the outer side of inner mitochondrial membrane has a low affinity sensor for ADP, modifying the activity of PTP. The pathophysiological importance of this process could be an endogenous prevention of PT at conditions of energetic depression. | ||
|keywords=Mitochondria, Permeability transition pore, Adenine nucleotide translocator, Carboxyatractyloside, Bongkrekic acid | |keywords=Mitochondria, Permeability transition pore, Adenine nucleotide translocator, Carboxyatractyloside, Bongkrekic acid | ||
|mipnetlab=DE Magdeburg Gellerich FN | |||
}} | }} | ||
{{Labeling | {{Labeling | ||
|organism=Mouse | |||
|tissues=Liver | |||
|preparations=Isolated mitochondria | |||
|instruments=Oxygraph-2k | |instruments=Oxygraph-2k | ||
}} | }} |
Latest revision as of 15:07, 24 March 2015
Gizatullina ZZ, Chen Y, Zierz S, Gellerich FN (2005) Effects of extramitochondrial ADP on permeability transition of mouse liver mitochondria. Biochim Biophys Acta 1706:98-104. |
Gizatullina ZZ, Chen Y, Zierz S, Gellerich FN (2005) Biochim Biophys Acta
Abstract: Carboxyatractylate (CAT) and atractylate inhibit the mitochondrial adenine nucleotide translocator (ANT) and stimulate the opening of permeability transition pore (PTP). Following pretreatment of mouse liver mitochondria with 5 μM CAT and 75 μM Ca2+, the activity of PTP increased, but addition of 2 mM ADP inhibited the swelling of mitochondria. Extramitochondrial Ca2+ concentration measured with Calcium-Green 5N evidenced that 2 mM ADP did not remarkably decrease the free Ca2+ but the release of Ca2+ from loaded mitochondria was stopped effectively after addition of 2 mM ADP. CAT caused a remarkable decrease of the maximum amount of calcium ions, which can be accumulated by mitochondria. Addition of 2 mM ADP after 5 μM CAT did not change the respiration, but increased the mitochondrial capacity for Ca2+ at more than five times. Bongkrekic acid (BA) had a biphasic effect on PT. In the first minutes 5 μM BA increased the stability of mitochondrial membrane followed by a pronounced opening of PTP too. BA abolished the action about of 1 mM ADP, but was not able to induce swelling of mitochondria in the presence of 2 mM ADP.
We conclude that the outer side of inner mitochondrial membrane has a low affinity sensor for ADP, modifying the activity of PTP. The pathophysiological importance of this process could be an endogenous prevention of PT at conditions of energetic depression. • Keywords: Mitochondria, Permeability transition pore, Adenine nucleotide translocator, Carboxyatractyloside, Bongkrekic acid
• O2k-Network Lab: DE Magdeburg Gellerich FN
Labels:
Organism: Mouse
Tissue;cell: Liver
Preparation: Isolated mitochondria
HRR: Oxygraph-2k