Therapeutic inhibition of USP7 promotes antitumor immune responses.

ABSTRACT:

Background

Ubiquitin-specific peptidase 7 (USP7) is a deubiquitinating enzyme that removes ubiquitin from specific protein substrates to modify their degradation rates thereby regulating crucial cellular processes integral to cancer. Conspicuously, overexpression of USP7 is strongly associated with the progression and poor prognosis in various cancers. Therefore, the design of potent and selective USP7 inhibitors poses an attractive therapeutic approach. The mechanism of action of USP7 inhibitors in cancer cells relies on MDM2 depletion and the restoration of p53.

Methods

In this study, we present OAT-4828, a novel and highly potent USP7-selective lead compound with a pharmacokinetic profile suitable for an oral administration. In in vivo models of melanoma and colon cancers

SUBMITTER: Muchowicz A 

PROVIDER: S-EPMC12481409 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature