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Merck
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LMO2 Confers Synthetic Lethality to PARP Inhibition in DLBCL.

Cancer cell (2019-08-27)
Salma Parvin, Ariel Ramirez-Labrada, Shlomzion Aumann, XiaoQing Lu, Natalia Weich, Gabriel Santiago, Elena M Cortizas, Eden Sharabi, Yu Zhang, Isidro Sanchez-Garcia, Andrew J Gentles, Evan Roberts, Daniel Bilbao-Cortes, Francisco Vega, Jennifer R Chapman, Ramiro E Verdun, Izidore S Lossos
ABSTRACT

Deficiency in DNA double-strand break (DSB) repair mechanisms has been widely exploited for the treatment of different malignances, including homologous recombination (HR)-deficient breast and ovarian cancers. Here we demonstrate that diffuse large B cell lymphomas (DLBCLs) expressing LMO2 protein are functionally deficient in HR-mediated DSB repair. Mechanistically, LMO2 inhibits BRCA1 recruitment to DSBs by interacting with 53BP1 during repair. Similar to BRCA1-deficient cells, LMO2-positive DLBCLs and T cell acute lymphoblastic leukemia (T-ALL) cells exhibit a high sensitivity to poly(ADP-ribose) polymerase (PARP) inhibitors. Furthermore, chemotherapy and PARP inhibitors synergize to inhibit the growth of LMO2-positive tumors. Together, our results reveal that LMO2 expression predicts HR deficiency and the potential therapeutic use of PARP inhibitors in DLBCL and T-ALL.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Anti-γ-Tubulin antibody, Mouse monoclonal, clone GTU-88, purified from hybridoma cell culture
Sigma-Aldrich
DAPI, Dihydrochloride, Cell-permeable DNA-binding dye.
Sigma-Aldrich
Anti-53BP1 Antibody, clone BP18, ascites fluid, clone BP18, Chemicon®
Sigma-Aldrich
Anti-phospho-Histone H2A.X (Ser139) Antibody, clone JBW301, clone JBW301, Upstate®, from mouse
Sigma-Aldrich
Anti-Actin antibody produced in rabbit, affinity isolated antibody, buffered aqueous solution
Sigma-Aldrich
Monoclonal Anti-HA antibody produced in mouse, clone HA-7, ascites fluid