Component
The cyclooxygenase-2 homodimer
The cyclooxygenase-2 homodimer. Species, exposure and limitations are retained in each linked claim.
1 recorded relationships. Experimental role, claim status and evidence remain attached to each record.
How nutrients influence it
Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
How nutrients reach it in more than one step
Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.
Tracing routes…
What it does
Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.
What acts on it
Aspirin maximally acetylates one monomer of human cyclooxygenase-2, the acetylated monomer forming 15-hydroperoxyeicosatetraenoic acid from arachidonic acid while the nonacetylated partner monomer forms mainly prostaglandin H2 but at only 15 to 20% of the rate of native enzyme, conclusions based on diclofenac binding a single monomer of native enzyme having an unmodified Ser530 and on diclofenac inhibiting prostaglandin H2 but not 15-hydroperoxyeicosatetraenoic acid formation by the acetylated enzyme.
Experimental context and source evidence
- evidence_span
- {"source_cache": "artifacts/aspirin-research/20194532.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "09427e18078449741ea9ea42dc91a16f50ca9f604ec05c4decbb255731104eaf", "start_char": 0, "end_char": 1441, "text_sha256": "09427e18078449741ea9ea42dc91a16f50ca9f604ec05c4decbb255731104eaf"}
- experimental_model
- Quantitative characterisation of aspirin-acetylated human cyclooxygenase-2 monomers using diclofenac to distinguish them
- exposure
- Aspirin acetylation with arachidonic, eicosapentaenoic and docosahexaenoic acid as substrates
- limitations
- Measures rates rather than presence, and reaches a much less generous estimate of resolvin formation than the reports it tests. It is an in vitro enzyme study, so it does not exclude accumulation or amplification in a living tissue.
- nutrient_topic
- Aspirin research collection; topical membership is not evidence of a direct clinical effect, and aspirin is recorded separately from salicylate, the metabolite it becomes. · Aspirin / acetylsalicylic acid
- organism
- Human enzyme
- plain_language
- Aspirin only ever modifies half of the paired enzyme, and the untouched half carries on at a fifth speed.
- primary_references
- [asa-p20194532] Asymmetric acetylation of the cyclooxygenase-2 homodimer by aspirin and its effects on the oxygenation of arachidonic, eicosapentaenoic, and docosahexaenoic acids. (2010). https://pubmed.ncbi.nlm.nih.gov/20194532/ DOI: 10.1124/mol.109.063115
- tissue_or_cell_type
- Cyclooxygenase-2 homodimer
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Quantitative characterisation of aspirin-acetylated human cyclooxygenase-2 monomers using diclofenac to distinguish them · source_derived_draft · unverified_draft
### asa-only-one-monomer-is-acetylated Aspirin maximally acetylates one monomer of human cyclooxygenase-2, the acetylated monomer forming 15-hydroperoxyeicosatetraenoic acid from arachidonic acid while the nonacetylated partner monomer forms mainly prostaglandin H2 but at only 15 to 20% of the rate of native enzyme, conclusions based on diclofenac binding a single monomer of native enzyme having an unmodified Ser530 and on diclofenac inhibiting prostaglandin H2 but not 15-hydroperoxyeicosatetraenoic acid formation by the acetylated enzyme. Condition category: normal nutrient_topic: Aspirin research collection; topical membership is not evidence of a direct clinical effect, and aspirin is recorded separately from salicylate, the metabolite it becomes. plain_language: Aspirin only ever modifies half of the paired enzyme, and the untouched half carries on at a fifth speed. organism: Human enzyme tissue_or_cell_type: Cyclooxygenase-2 homodimer experimental_model: Quantitative characterisation of aspirin-acetylated human cyclooxygenase-2 monomers using diclofenac to distinguish them limitations: Measures rates rather than presence, and reaches a much less generous estimate of resolvin formation than the reports it tests. It is an in vitro enzyme study, so it does not exclude accumulation or amplification in a living tissue. exposure: Aspirin acetylation with arachidonic, eicosapentaenoic and docosahexaenoic acid as substrates evidence_span: {"source_cache": "artifacts/aspirin-research/20194532.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "09427e18078449741ea9ea42dc91a16f50ca9f604ec05c4decbb255731104eaf", "start_char": 0, "end_char": 1441, "text_sha256": "09427e18078449741ea9ea42dc91a16f50ca9f604ec05c4decbb255731104eaf"} [asa-p20194532] Asymmetric acetylation of the cyclooxygenase-2 homodimer by aspirin and its effects on the oxygenation of arachidonic, eicosapentaenoic, and docosahexaenoic acids. (2010). https://pubmed.ncbi.nlm.nih.gov/20194532/ DOI: 10.1124/mol.109.063115
Complete structured claim and evidence
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.