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Bovine Liver Mitochondrial NAD+ Glycohydrolase

Relationship to ADP-Ribosylation and Calcium Fluxes
  • Mathias Ziegler
  • Dierk Jorcke
  • Andrés Herrero-Yraola
  • Manfred Schweiger
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 419)

Abstract

Mitochondrial NAD+ glycohydrolase (NADase) has been proposed to be required for (nonenzymatic) ADP-ribosylation and subsequent activation of a Ca2+ release pathway. In our studies it has been found that several agents including nicotinamide, dithiothreitol, and EDTA exert no or little effect on ADP-ribosylation in isolated bovine liver mitochondria, while strongly inhibiting the NADase. The NADase did, however, catalyze the formation of cyclic purine nucleoside diphosphoriboses (similar to cyclic ADP-ribose) from NAD+ analogs. It appears possible, therefore, that this enzyme may be involved in the regulation of mitochondrial Ca2+ fluxes by forming a potent Ca2+-mobilizing agent, rather than by providing the substrate for non-enzymatic ADP-ribosylation.

Keywords

None None Bovine Liver Release Pathway Fluorescent Analog Signalling Cyclic Nucleotide 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1997

Authors and Affiliations

  • Mathias Ziegler
    • 1
  • Dierk Jorcke
    • 1
  • Andrés Herrero-Yraola
    • 1
  • Manfred Schweiger
    • 1
  1. 1.Institut f. BiochemieFreie Univ. BerlinBerlinGermany

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