Abstract
The incubation of isolated hepatocytes with the inhibitor of protein mono ADP-ribosylation, m-iodobenzylguanidine (MIBG), resulted in an increase in the size of the mitochondrial Ca 2+ pool, without alteration of the non-mitochondrial Ca 2+ store(s). This increase was abolished when the cytosolic free Ca 2+ concentration ([Ca 2+] i) was buffered by prior loading of the cells with fluo 3. Elevating [Ca 2+] i by releasing the endoplasmic reticular Ca 2+ store with 2,5-di-( tert-butyl)-1,4-hydroquinone resulted in a synergistic increase in the magnitude of the mitochondrial Ca 2+ pool. A role for protein ADP-ribosylation in the intracellular regulation of mitochondrial Ca 2+ homeostasis is suggested.
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