Enzymatic synthesis and degradation of nicotinate adenine dinucleotide phosphate (NAADP), a Ca2+-releasing agonist, in rat tissues

Eduardo Nunes Chini, T. P. Dousa

Research output: Contribution to journalArticle

51 Citations (Scopus)

Abstract

We have recently found that nicotinate adenine dinucleotide phosphate (NAADP) is a potent agonist that triggers Ca2+ release from intracellular stores of sea urchin eggs, and that its action is distinct from effects of IP3 and cyclic ADP-ribose. Now we report that extracts from rat brain, heart, liver, and spleen but not kidney cortex contain enzymatic activity which catalyzes NAADP synthesis by exchange of nicotinamide for nicotinic acid and which is probably catalyzed by NAD(P)-glycohydrolase. Extracts from these tissues also inactivate NAADP in the rank inverse to their ability for NAADP synthesis. These results suggest that NAADP, a Ca2+-releasing agent, can be generated in mammalian tissues, namely in brain.

Original languageEnglish (US)
Pages (from-to)167-174
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume209
Issue number1
DOIs
StatePublished - 1995

Fingerprint

Rats
Tissue
Degradation
Brain
NAD+ Nucleosidase
Cyclic ADP-Ribose
Kidney Cortex
Tissue Extracts
Niacinamide
Sea Urchins
Niacin
Glycoside Hydrolases
Liver
NAD
Eggs
Ion exchange
Thermodynamic properties
Spleen
NAADP

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology
  • Cell Biology

Cite this

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