Selenomethionine, a form of selenium, can still prevent cell damage and death in human cells even when the GPX4 protein is completely removed, suggesting it blocks a type of cell death called ferroptosis through a different pathway than previously thought.

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Evidence from Studies

Supporting (1)

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Selenomethionine as a dual-mechanism ferroptosis inhibitor: selenium-supply-driven GPX4 biosynthesis beyond transsulfuration and reductive-capacity-mediated ROS scavenging independent of GPX4 activity

Randomized Controlled Trial

Animal & In Vitro

2026 Feb 14

Even when scientists removed the main protein (GPX4) that usually stops cell death, selenomethionine still protected cells by acting like a chemical sponge for harmful molecules — meaning it works in a totally different way than we thought.

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Source Study

Selenomethionine as a dual-mechanism ferroptosis inhibitor: selenium-supply-driven GPX4 biosynthesis beyond transsulfuration and reductive-capacity-mediated ROS scavenging independent of GPX4 activity

Score: 13

DOI: 10.1038/s41419-026-08466-x

Similar Assertions

Selenomethionine decreases markers of oxidative damage and cell death in human cancer cells under conditions that trigger ferroptosis, such as exposure to RSL3 or lack of cystine.

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80%

Selenomethionine can neutralize reactive oxygen species by undergoing a chemical reaction that produces selenomethionine sulfoxide, and this process reduces ferroptosis without requiring the synthesis of new proteins.

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73%

Selenomethionine raises the levels of the GPX4 protein in specific human cells grown in the lab when those cells are stressed by lack of cystine or exposure to RSL3, and this effect occurs even when two key enzymes in the transsulfuration pathway are blocked.

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73%