Small molecule-mediated ERO1A inhibition in restraining aggressive breast cancer

ABSTRACT: Cancer cells adapt to harsh environmental conditions by inducing the Unfolded Protein Response (UPR), of which ERO1A is one of the mediators. ERO1A aids protein folding by acting as a protein disulfide oxidase, and under cancer-related hypoxia conditions, it favors the folding of angiogenic VEGFA, leading tumor cells to thrive and spread. The upregulation of ERO1A in cancer and the dispensability of ERO1A activity in healthy cells render ERO1 a perfect target for cancer therapy. Here, we report the upregulation of ERO1 in aggressive triple-negative breast cancer (TNBC) patients. Thus, we designed new ERO1A inhibitors in a campaign of lead compound optimization on the prototype EN460 to be tested in TNBC treatment. Cell-based screenings showed that I2 and I3, two novel EN460 analogs, inhibi

INSTRUMENT(S): NextSeq 500

ORGANISM(S): Mus musculus

SUBMITTER: Luca Guarrera 

PROVIDER: E-MTAB-14269 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress