Researchers Identified New Ovarian Cancer Treatment Target

Scientists at UMBC found that inhibiting the enzyme USP15 may slow cancer growth and improve chemotherapy outcomes.

Updated on Sept. 28, 2026 in Cancer

A close-up view of a clear glass petri dish on a stainless steel laboratory bench in a sterile research environment. — Researchers at the University of Maryland, Baltimore County have identified the enzyme USP15 as a key target to improve outcomes for ovarian cancer patients. AI Illustration. Upload story photo >

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Researchers have identified the enzyme USP15 as a promising therapeutic target for ovarian cancer. Lowering levels of this enzyme in laboratory tests caused DNA damage and cell death in cancer cells while increasing their vulnerability to standard chemotherapy treatments.

Why it matters

Ovarian cancer remains difficult to treat once it spreads, with five-year survival rates falling below 30 percent. Targeting USP15 offers a potential new avenue to disrupt tumor growth and improve patient response to existing drugs.

The study tracked the enzyme in cells and mice, noting it stabilizes mutant p53 proteins which are present in two-thirds of ovarian cancer mutations. Reducing USP15 levels directly limits the ability of cancer cells to migrate throughout the body.

The players

University of Maryland, Baltimore County

This public research university serves as the primary site for the laboratory where the USP15 enzyme study was conducted.

Molecular Therapy Oncology

This peer-reviewed medical journal serves as the professional publication platform for the new ovarian cancer research findings.

The details

The research team at the University of Maryland, Baltimore County used laboratory experiments on cells and mice to observe that cancer cells rely more heavily on USP15 than healthy cells. By inhibiting the enzyme, the scientists stripped away protective molecular tags from cancer proteins, forcing the cells into a state of irreparable DNA damage.

Padmanabhan began exploring the roles of USP15 at UMBC in 2019.
Ogunsanya joined the laboratory to focus on USP15 research in 2021.
Findings were published in the journal Molecular Therapy Oncology on September 17, 2026.

The Big Picture

The discovery advances the p53 protein mutation research program by identifying USP15 as a key stabilizer of those dangerous proteins. By targeting the enzyme responsible for protein longevity, researchers are shifting focus toward the cellular mechanisms that allow mutant proteins to persist.

This research provides a long-term goal for developing new inhibitor drugs that could eventually be paired with chemotherapy to increase effectiveness. Patients with ovarian cancer may see future treatment options that specifically target these cellular stabilization pathways.

The takeaway

While clinical applications remain in the future, identifying enzyme vulnerabilities provides a critical blueprint for next-generation drug development. Researchers hope these findings will eventually lead pharmaceutical companies to prioritize the creation of specific USP15 inhibitors.