ArticleThe Journal of biological chemistry2015
A cyclooxygenase-2-dependent prostaglandin E2 biosynthetic system in the Golgi apparatus.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 49 citations in OpenAlex.
- The role of prostanoids in the retina and optic nerve in health and disease.Progress in retinal and eye research · 2026Review
- Small-molecule probes for imaging and impairing the Golgi apparatus in cancer.RSC medicinal chemistry · 2025Review
- Crosstalk between P2Y receptors and cyclooxygenase activity in inflammation and tissue repair.Purinergic signalling · 2024Review
- From transcriptomics to digital twins of organ function.Frontiers in cell and developmental biology · 2024Article
- Prostaglandins limit nuclear actin to control nucleolar function during oogenesis.Frontiers in cell and developmental biology · 2023Article
- Microglia as a cellular target of diclofenac therapy in Alzheimer's disease.Therapeutic advances in neurological disorders · 2023Review
- Lipid Dyshomeostasis and Inherited Cerebellar Ataxia.Molecular neurobiology · 2022Review
- Is cyclooxygenase-1 involved in neuroinflammation?Journal of neuroscience research · 2021Review
- Cyclooxygenase-2 Glycosylation Is Affected by Peroxynitrite in Endothelial Cells: Impact on Enzyme Activity and Degradation.Antioxidants (Basel, Switzerland) · 2021Article
- Design, Synthesis and Biological Evaluation of 1,3-Diphenyl-3-(phenylthio)propan-1-ones as New Cytotoxic Agents.Iranian journal of pharmaceutical research : IJPR · 2021Article
- The Biosynthesis of Enzymatically Oxidized Lipids.Frontiers in endocrinology · 2020Review
- A seven-step plan for becoming a moderately rich and famous biochemist.The Journal of biological chemistry · 2019Article
- Interactions of fatty acids, nonsteroidal anti-inflammatory drugs, and coxibs with the catalytic and allosteric subunits of cyclooxygenases-1 and -2.The Journal of biological chemistry · 2019Review
- Post-translational modifications of prostaglandin-endoperoxide synthase 2 in colorectal cancer: An update.World journal of gastroenterology · 2018Review
- Isoform-Specific Compensation of Cyclooxygenase (Ptgs) Genes during Implantation and Late-Stage Pregnancy.Scientific reports · 2018Article
- Flipping the cyclooxygenase (Journal of lipid research · 2018Article
- Adaptor protein p62 promotes skin tumor growth and metastasis and is induced by UVA radiation.The Journal of biological chemistry · 2017Article
- Bifunctional conjugates with potent inhibitory activity towards cyclooxygenase and histone deacetylase.Bioorganic & medicinal chemistry · 2017Article
- Different Fatty Acids Compete with Arachidonic Acid for Binding to the Allosteric or Catalytic Subunits of Cyclooxygenases to Regulate Prostanoid Synthesis.The Journal of biological chemistry · 2016Article
- Potential Antifungal Targets against a Candida Biofilm Based on an Enzyme in the Arachidonic Acid Cascade-A Review.Frontiers in microbiology · 2016Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Cyclooxygenases (COXs) catalyze the committed step in prostaglandin (PG) biosynthesis. COX-1 is constitutively expressed and stable, whereas COX-2 is inducible and short lived. COX-2 is degraded via endoplasmic reticulum (ER)-associated degradation (ERAD) following post-translational glycosylation of Asn-594. COX-1 and COX-2 are found in abundance on the luminal surfaces of the ER and inner membrane of the nuclear envelope. Using confocal immunocytofluorescence, we detected both COX-2 and microsomal PGE synthase-1 (mPGES-1) but not COX-1 in the Golgi apparatus. Inhibition of trafficking between the ER and Golgi retarded COX-2 ERAD. COX-2 has a C-terminal STEL sequence, which is an inefficient ER retention signal. Substituting this sequence with KDEL, a robust ER retention signal, concentrated COX-2 in the ER where it was stable and slowly glycosylated on Asn-594. Native COX-2 and a recombinant COX-2 having a Golgi targeting signal but not native COX-1 exhibited efficient catalytic coupling to mPGES-1. We conclude that N-glycosylation of Asn-594 of COX-2 occurs in the ER, leading to anterograde movement of COX-2 to the Golgi where the Asn-594-linked glycan is trimmed prior to retrograde COX-2 transport to the ER for ERAD. Having an inefficient ER retention signal leads to sluggish Golgi to ER transit of COX-2. This permits significant Golgi residence time during which COX-2 can function catalytically. Cytosolic phospholipase A2α, which mobilizes arachidonic acid for PG synthesis, preferentially translocates to the Golgi in response to physiologic Ca(2+) mobilization. We propose that cytosolic phospholipase A2α, COX-2, and mPGES-1 in the Golgi comprise a dedicated system for COX-2-dependent PGE2 biosynthesis.
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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 OpenQuestion graph.