Enzyme makes lab-grown human cells more prone to iron-dependent death
Experiments in human fetal lung cells found that reducing a fat-processing enzyme limited membrane fat damage and chemically triggered death, including in cells that had stopped dividing.
Limit: Cell death without a chemical trigger was not measured
Edited by Boris Djordjevic · AgingResearch.News
In experiments with human fetal lung WI-38 fibroblasts, cells that make connective tissue, researchers studied senescence, a state in which cells permanently stop dividing. They grew cells until repeated divisions exhausted their ability to divide, then compared them with dividing cells. They measured survival 24 hours after adding RSL3, a chemical that triggers ferroptosis—iron-dependent cell death involving damage to membrane fats.
Senescent cells were more sensitive to RSL3. Reducing acid ceramidase, an enzyme that breaks down fats called ceramides, reduced membrane fat damage and protected both dividing and senescent cells. In senescent cells, reducing the enzyme also reduced the amounts of several membrane fats containing polyunsaturated fatty acids. Sharing growth liquid with senescent cells, without direct contact, made dividing cells more sensitive to ferroptosis.
Why it matters
Ferroptosis has been implicated in age-related disorders. The authors suggest that understanding acid ceramidase’s role could open avenues for targeting senescence-linked disease.
Caveats
These experiments used cells grown in the lab, not people or intact tissues. They do not establish whether changing this enzyme would benefit aging or disease in a living organism.
- Ferroptosis
- ASAH1
- Cellular senescence
- Lipid peroxidation
- Polyunsaturated fatty acid composition of membrane phospholipids
- Humans
The paper
Salk Institute for Biological Studies
Cell Death & Disease, Jul 10, 2026, Open access
Comments
Be the first to comment.