Metabolism of cyclic ADP-ribose

Zinc is an endogenous modulator of the cyclase/NAD glycohydrolase ratio of a CD38-like enzyme from human seminal fluid

Weronika Zielinska, Hosana Barata, Eduardo Nunes Chini

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

CD38, a bifunctional enzyme capable of both synthesis and hydrolysis of the second messenger cyclic ADP-ribose (cADPR). Using the natural substrate of the enzyme, NAD+, the ratio of ADP-ribosyl cyclase/NAD glycohydrolase of CD38 is about 1/100. Here we describe that human seminal fluid contain a soluble CD38 like enzyme with an apparent M.W. of 49 kDa. When purified this enzyme has a cyclase/NAD glycohydrolase ratio of about 1/120. However, the in situ cyclase/NAD glycohydrolase ratio measured in seminal plasma approaches 1/1. We also found that physiological concentrations of zinc present in the seminal fluid, in the range of 0.6 to 4 mM, are responsible for the modulation of the cyclase/NAD glycohydrolase ratio. This new information indicates that the cyclase/NAD glycohydrolase ratio can be modified in vivo.

Original languageEnglish (US)
Pages (from-to)1781-1790
Number of pages10
JournalLife Sciences
Volume74
Issue number14
DOIs
StatePublished - Feb 20 2004

Fingerprint

NAD+ Nucleosidase
Cyclic ADP-Ribose
Metabolism
Modulators
Zinc
Fluids
Enzymes
ADP-ribosyl Cyclase
Second Messenger Systems
Semen
NAD
Hydrolysis
Modulation
Plasmas
Substrates

Keywords

  • cADPR
  • Endoplasmic reticulum
  • IP
  • NAADP
  • Ryanodine channel
  • Zinc

ASJC Scopus subject areas

  • Pharmacology

Cite this

Metabolism of cyclic ADP-ribose : Zinc is an endogenous modulator of the cyclase/NAD glycohydrolase ratio of a CD38-like enzyme from human seminal fluid. / Zielinska, Weronika; Barata, Hosana; Chini, Eduardo Nunes.

In: Life Sciences, Vol. 74, No. 14, 20.02.2004, p. 1781-1790.

Research output: Contribution to journalArticle

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AB - CD38, a bifunctional enzyme capable of both synthesis and hydrolysis of the second messenger cyclic ADP-ribose (cADPR). Using the natural substrate of the enzyme, NAD+, the ratio of ADP-ribosyl cyclase/NAD glycohydrolase of CD38 is about 1/100. Here we describe that human seminal fluid contain a soluble CD38 like enzyme with an apparent M.W. of 49 kDa. When purified this enzyme has a cyclase/NAD glycohydrolase ratio of about 1/120. However, the in situ cyclase/NAD glycohydrolase ratio measured in seminal plasma approaches 1/1. We also found that physiological concentrations of zinc present in the seminal fluid, in the range of 0.6 to 4 mM, are responsible for the modulation of the cyclase/NAD glycohydrolase ratio. This new information indicates that the cyclase/NAD glycohydrolase ratio can be modified in vivo.

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