Modulation of purinergic signaling by NPP-type ectophosphodiesterases

Cristiana Stefan, Silvia Jansen, Mathieu Bollen

Research output: Contribution to journalReview articlepeer-review

123 Scopus citations


Extracellular nucleotides can elicit a wide array of cellular responses by binding to specific purinergic receptors. The level of ectonucleotides is dynamically controlled by their release from cells, synthesis by ectonucleoside diphosphokinases and ectoadenylate kinases, and hydrolysis by ectonucleotidases. One of the four structurally unrelated families of ectonucleotidases is represented by the NPP-type ectophosphodiesterases. Three of the seven members of the NPP family, namely NPP1-3, are known to hydrolyze nucleotides. The enzymatic action of NPP1-3 (in)directly results in the termination of nucleotide signaling, the salvage of nucleotides and/or the generation of new messengers like ADP, adenosine or pyrophosphate. NPP2 is unique in that it hydrolyzes both nucleotides and lysophospholipids and, thereby, generates products that could synergistically promote cell motility. We review here the enzymatic properties of NPPs and analyze current evidence that links their nucleotide-hydrolyzing capability to epithelial and neural functions, the immune response and cell motility.

Original languageEnglish
Pages (from-to)361-370
Number of pages10
JournalPurinergic Signalling
Issue number2
StatePublished - May 2006


  • Alkaline sphingomyelinase
  • ENPP
  • Ectonucleotide pyrophosphatase
  • Ectophosphodiesterase
  • Lysophospholipase D
  • NPP
  • NPP-type ectophosphodiesterase


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