Prune cAMP phosphodiesterase binds nm23-H1 and promotes cancer metastasis

Anna D'Angelo, Livia Garzia, Alessandra André, Pietro Carotenuto, Veruska Aglio, Ombretta Guardiola, Gianluigi Arrigoni, Antonio Cossu, Giuseppe Palmieri, L. Aravind, Massimo Zollo

Research output: Contribution to journalArticlepeer-review


We identify a new enzymatic activity underlying metastasis in breast cancer and describe its susceptibility to therapeutic inhibition. We show that human prune (h-prune), a phosphoesterase DHH family appertaining protein, has a hitherto unrecognized cyclic nucleotide phosphodiesterase activity effectively suppressed by dipyridamole, a phosphodiesterase inhibitor. H-prune physically interacts with nm23-H1, a metastasis suppressor gene. The h-prune PDE activity, suppressed by dipyridamole and enhanced by the interaction with nm23-H1, stimulates cellular motility and metastasis processes. Out of 59 metastatic breast cancer cases analyzed, 22 (37%) were found to overexpress h-prune, evidence that this novel enzymatic activity is involved in promoting cancer metastasis.

Original languageEnglish
Pages (from-to)137-149
Number of pages13
JournalCancer Cell
Issue number2
Publication statusPublished - Feb 2004

ASJC Scopus subject areas

  • Cancer Research
  • Cell Biology
  • Oncology


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