A high-throughput fluorimetric assay for 2-Hydroxyglutarate Identifies Zaprinast as a Glutaminase Inhibitor

Adnan Elhammali, Joseph E. Ippolito, Lynne Collins, Jan Crowley, Jayne Marasa, David Piwnica-Worms

Research output: Contribution to journalArticlepeer-review

69 Scopus citations

Abstract

Recently identified isocitrate dehydrogenase (IDH) mutations lead to the production of 2-hydroxyglutarate (2HG), an oncometabolite aberrantly elevated in selected cancers. We developed a facile and inexpensive fluorimetric microplate assay for the quantitation of 2HG and performed an unbiased small-molecule screen in live cells to identify compounds capable of perturbing 2HG production. Zaprinast, a phosphodiesterase 5 inhibitor, was identified as an efficacious modulator of 2HG production and confirmed to lower 2HG levels in vivo. The mechanism of action was not due to cGMP stabilization, but rather, profiling of metabolites upstream of mutant IDH1 pointed to targeted inhibition of the enzyme glutaminase (GLS). Zaprinast treatment reversed histone hypermethylation and soft-agar growth of IDH1-mutant cells, and treatment of glutamine-addicted pancreatic cancer cells reduced growth and sensitized cells to oxidative damage. Thus, Zaprinast is efficacious against glutamine metabolism and further establishes the therapeutic linkages between GLS and 2HG-mediated oncogenesis.

Original languageEnglish
Pages (from-to)828-839
Number of pages12
JournalCancer discovery
Volume4
Issue number7
DOIs
StatePublished - Jul 2014

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