| Literature DB >> 32386594 |
Matteo Marchesini1, Andrea Gherli1, Anna Montanaro1, Laura Patrizi2, Claudia Sorrentino1, Luca Pagliaro1, Chiara Rompietti2, Samuel Kitara3, Sabine Heit4, Claus E Olesen5, Jesper V Møller5, Monia Savi6, Leonardo Bocchi6, Rocchina Vilella6, Federica Rizzi7, Marilena Baglione1, Giorgia Rastelli1, Caterina Loiacono1, Roberta La Starza2, Cristina Mecucci2, Kimberly Stegmaier8, Franco Aversa1, Donatella Stilli6, Anne-Marie Lund Winther9, Paolo Sportoletti2, Maike Bublitz4, William Dalby-Brown9, Giovanni Roti10.
Abstract
The identification of SERCA (sarco/endoplasmic reticulum calcium ATPase) as a target for modulating gain-of-function NOTCH1 mutations in Notch-dependent cancers has spurred the development of this compound class for cancer therapeutics. Despite the innate toxicity challenge associated with SERCA inhibition, we identified CAD204520, a small molecule with better drug-like properties and reduced off-target Ca2+ toxicity compared with the SERCA inhibitor thapsigargin. In this work, we describe the properties and complex structure of CAD204520 and show that CAD204520 preferentially targets mutated over wild-type NOTCH1 proteins in T cell acute lymphoblastic leukemia (T-ALL) and mantle cell lymphoma (MCL). Uniquely among SERCA inhibitors, CAD204520 suppresses NOTCH1-mutated leukemic cells in a T-ALL xenografted model without causing cardiac toxicity. This study supports the development of SERCA inhibitors for Notch-dependent cancers and extends their application to cases with isolated mutations in the PEST degradation domain of NOTCH1, such as MCL or chronic lymphocytic leukemia (CLL).Entities:
Keywords: CAD204520; NOTCH1; NOTCH1 mutation; P-type ATPases screening; PEST mutation; SERCA; T cell acute lymphoblastic leukemia (T-ALL); crystal structure; mantle cell lymphoma (MCL); thapsigargin
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Year: 2020 PMID: 32386594 PMCID: PMC7305996 DOI: 10.1016/j.chembiol.2020.04.002
Source DB: PubMed Journal: Cell Chem Biol ISSN: 2451-9448 Impact factor: 8.116