PMID: 7371640Mar 1, 1980Paper

The Ca2+-binding glycoprotein as the site of metabolic regulation of mitochondrial Ca2+ movements

European Journal of Biochemistry
E PanfiliG Liut

Abstract

A change in the redox state of pyridine nucleotides such as that evoked by addition of oxaloacetate has been shown to promote Ca2+ efflux from Ca2+ pre-loaded respiring mitochondria. An affinity-chromatography-purified antibody preparation obtained against the mitochondrial Ca2+-binding glycoprotein inhibits the phenomenon. This finding suggests that the glycoprotein is involved also in the oxaloacetate-induced Ca2+ release. This conclusion is reinforced by the finding that Ca2+-binding glycoprotein shows four sites per molecule where the pyridine nucleotides may be bound. Binding of NAD+ occurs preferentially over the others and the binding shows positive cooperativity, indicating that the glycoprotein undergoes an allosteric change upon NAD+ binding. Interestingly, in addition, NAD+ lowers the affinity of the glycoprotein for Ca2+. The effect cannot be induced by NADH. Pyridine nucleotide phosphates, NADP+ and NADPH, are essentially not bound. The results are consistent with the view that the glycoprotein is the site of regulation of Ca2+ equilibration across the mitochondrial membrane and make it possible to conclude that the effector in the phenomenon is NAD+.

References

Apr 1, 1978·Proceedings of the National Academy of Sciences of the United States of America·A L LehningerE A Bababunmi
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Citations

Oct 1, 1994·Journal of Bioenergetics and Biomembranes·C ZazuetaE Chávez
Jul 28, 2010·The FEBS Journal·Anatoly A Starkov
Feb 29, 1984·Biochemical and Biophysical Research Communications·A E Vercesi
Jan 9, 2008·Journal of Cellular Biochemistry·Masayoshi YamaguchiTaeko Nakagawa
Jun 11, 1992·Chronobiology International·L N EdmundsJ Tong
Jan 1, 1987·Annals of the New York Academy of Sciences·L N EdmundsK Goto
Dec 30, 1981·Biochimica Et Biophysica Acta·H Tedeschi
Sep 1, 1982·Biochimica Et Biophysica Acta·D Nicholls, K Akerman
Jul 1, 1981·Archives of Biochemistry and Biophysics·P E Wolkowicz, J McMillin-Wood

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