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

doi:10.1016/S1535-6108(04)00021-2

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

IRCCS Ospedale San Raffaele

Research output: Contribution to journal › Article › peer-review

Abstract

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 language	English
Pages (from-to)	137-149
Number of pages	13
Journal	Cancer Cell
Volume	5
Issue number	2
DOIs	https://doi.org/10.1016/S1535-6108(04)00021-2
Publication status	Published - Feb 2004

ASJC Scopus subject areas

Cancer Research
Cell Biology
Oncology

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Prune cAMP phosphodiesterase binds nm23-H1 and promotes cancer metastasis. / D'Angelo, Anna; Garzia, Livia; André, Alessandra; Carotenuto, Pietro; Aglio, Veruska; Guardiola, Ombretta; Arrigoni, Gianluigi; Cossu, Antonio; Palmieri, Giuseppe; Aravind, L.; Zollo, Massimo.

In: Cancer Cell, Vol. 5, No. 2, 02.2004, p. 137-149.

Research output: Contribution to journal › Article › peer-review

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title = "Prune cAMP phosphodiesterase binds nm23-H1 and promotes cancer metastasis",

abstract = "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.",

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AU - D'Angelo, Anna

AU - Garzia, Livia

AU - André, Alessandra

AU - Carotenuto, Pietro

AU - Aglio, Veruska

AU - Guardiola, Ombretta

AU - Arrigoni, Gianluigi

AU - Cossu, Antonio

AU - Palmieri, Giuseppe

AU - Aravind, L.

AU - Zollo, Massimo

PY - 2004/2

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N2 - 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.

AB - 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.

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