ArticleiScience2024
Activity-dependent COX-2 proteolysis modulates aerobic respiration and proliferation in a prostaglandin-independent manner.
Article in iScience, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
5 citing papers in PubMed.
- Imaging-guided COX-2 inhibition synergizes with photodynamic immunogenic cell death to potentiate checkpoint blockade in colon cancer.International journal of pharmaceutics: X · 2026Article
- Imbalance of the Arachidonic Acid Metabolism in Neuroinflammation and Cognition Caused by Manganese Exposure: Downregulation of 15d-PGJ2 Levels and Validation of MMP9 as a Target.Environment & health (Washington, D.C.) · 2026Article
- Chitosan-Stabilized Silver-Nimesulide Coordination Complex with Enhanced Anti-Inflammatory and Redox-Modulating Activity.ACS omega · 2026Article
- [Different Astragalus medicinal pairs improve diabetic nephropathy in mice by regulating lipid peroxidation through PTGS2].Nan fang yi ke da xue xue bao = Journal of Southern Medical University · 2026Article
- Integrative transcriptomic and structural analysis identifies PTGS2 as a key target in ischemic stroke associated with neuroinflammation.Molecular diversity · 2026Article
Corrections and comments
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cyclooxygenase-2 (COX-2) catalyzes the oxidation of arachidonic acid (AA) into a single product that is the source of all prostaglandins (PGs), ligands of multiple pro-inflammatory pathways. AA catalysis results in suicide inactivation, rendering the enzyme catalytically inactive. Here, we report that catalytic activity also leads to controlled cleavage of COX-2, an event that is differentially regulated by fatty acids, and blocked by COX inhibitors. We also find COX-2 fragments in human colon tumors. Using mass spectrometry, we identified two adjacent cleavage points within the catalytic domain, which give rise to COX-2 fragments that are catalytically inactive and localize to different cellular compartments. Expression of one of these fragments in cells significantly reduced mitochondrial function, increased lactate production, and enhanced proliferation. We propose that in addition to its role in generating PGs, COX-2 has PG-independent cellular functions that may account for its complex role in proliferative diseases and chronic inflammation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.