TAILIEUCHUNG - Báo cáo khoa học: A re-evaluation of the role of matrix acidification in uncoupler-induced Ca2+ release from mitochondria

Massive amounts of Ca2+ can accumulate in mitochondria, owing to its complexation with matrix phosphate. Under conditions in which the mito-chondrial uniporter is the foremost pathway for Ca 2+ efflux, the release of sequestered Ca 2+ by protonophoric uncouplers is invariably demonstrated. This has been recently ascribed to matrix acidification, which results in the dissociation of the Ca 2+ –phosphate complex. | ỊFEBS Journal A re-evaluation of the role of matrix acidification in uncoupler-induced Ca2 release from mitochondria Szilvia Vajda Miklos Mandi Csaba Konrad Gergely Kiss Attila Ambrus Vera Adam-Vizi and Christos Chinopoulos NeurobiochemicalGroup Department of MedicalBiochemistry Hungarian Academy of Sciences Szentagothai Knowledge Center Semmelweis University Budapest Hungary Keywords acidification calcium-phosphate complexation mitochondrialCa2 uptake respiratory chain uncoupler Correspondence C. Chinopoulos and V. Adam-Vizi Department of Medical Biochemistry Semmelweis University Budapest Hungary Fax 361 2670031 Tel 361 4591500 ext. 60024 361 4591500 ext. 60011 E-mail Received 7 January 2009 revised 5 March 2009 accepted 6 March 2009 doi Massive amounts of Ca2 can accumulate in mitochondria owing to its complexation with matrix phosphate. Under conditions in which the mitochondrial uniporter is the foremost pathway for Ca2 efflux the release of sequestered Ca2 by protonophoric uncouplers is invariably demonstrated. This has been recently ascribed to matrix acidification which results in the dissociation of the Ca2 -phosphate complex. In the present study we compared the effect of stepwise depolarization on Ca2 release induced by either the complex III inhibitor stigmatellin or an uncoupler in energized Ca2 -loaded rat liver mitochondria in the presence of phosphate at extra-mitochondrial pH pHo and pHo . Both poisons were examined in the presence and absence of oligomycin. Prior to Ca2 loading mitochondria were allowed to phosphorylate mM ADP. Opening of the permeability transition pore was additionally hampered by cyclosporin A and was monitored by changes in light scattering. Na was excluded from the medium preventing Na Ca2 exchange. At both pHo values ApH was in the range . Complete depolarization by uncoupling with or without oligomycin resulted in

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