Inhibition of phospholipase D2 augments histone deacetylase inhibitor-induced cell death in breast cancer cells.

ABSTRACT:

Background

Histone deacetylase (HDAC) inhibitors are promising anticancer drugs but their effect on tumor treatment has been disappointing mainly due to the acquisition of HDAC inhibitor resistance. However, the mechanisms underlying such resistance remain unclear.

Methods

In this study, we performed Western blot, q-PCR, and promoter assay to examine the expression of HDAC inhibitor-induced phospholipase D2 (PLD2) in MDA-MB231and MDA-MB435 breast cancer cells. Apoptosis and proliferation were analyzed by flow cytometry. In addition to invasion and migration assay, angiogenesis was further measured using in vitro tube formation and chick embryo chorioallantoic membrane model.

Results

HDAC inhibitors including suberoylanilide hydroxamic acid (SAHA), trichostatin, and ap

SUBMITTER: Hwang WC 

PROVIDER: S-EPMC7528251 | biostudies-literature | 2020 Oct

REPOSITORIES: biostudies-literature