Related Experiment Video

Updated: Aug 18, 2026

A Modified Inflammatory Pain Model to Study the Analgesic Effect in Mice
06:54

A Modified Inflammatory Pain Model to Study the Analgesic Effect in Mice

Published on: November 15, 2024

New insights into COX-2 biology and inhibition

Paola Patrignani1, Stefania Tacconelli, Maria Gina Sciulli

  • 1Department of Medicine and Center of Excellence on Aging, G.d'Annunzio University, School of Medicine, Chieti, Italy. paola_patrignani@tin.it

Brain Research. Brain Research Reviews
|April 27, 2005
PubMed

Insights

Cyclooxygenase-2 (COX-2) inhibitors offer pain relief and inflammation control with improved gastrointestinal safety. Research explores their potential in cancer chemoprevention and neurological diseases, including novel roles in the endocannabinoid system.

Area of Science:

  • Biochemistry
  • Pharmacology
  • Oncology

Background:

  • Prostanoids regulate numerous cellular functions and disease processes, including inflammation, cancer, and thrombosis.
  • Cyclooxygenase-1 (COX-1) and Cyclooxygenase-2 (COX-2) enzymes control prostanoid synthesis from arachidonic acid.
  • Selective COX-2 inhibitors (coxibs) provide pain and inflammation relief with better gastrointestinal safety than nonselective NSAIDs.

Purpose of the Study:

  • To review the established and emerging roles of COX-2 in various pathophysiologic processes.
  • To evaluate the efficacy and safety of COX-2 inhibitors in inflammation, cancer, and neurological disorders.
  • To explore the novel involvement of COX-2 in the endogenous cannabinoid system.

Main Methods:

  • Literature review of preclinical and clinical studies on COX-2 inhibitors.
  • Analysis of data on the efficacy of coxibs in pain, inflammation, and cancer chemoprevention.
  • Investigation of COX-2's role in neurological diseases and the endocannabinoid system.

Main Results:

  • COX-2 inhibitors demonstrate comparable efficacy to NSAIDs for pain and inflammation with enhanced gastrointestinal safety.
  • Evidence suggests COX-2's role in cancer development and potential chemopreventive applications for coxibs.
  • COX-2 inhibitors may prevent multidrug resistance protein overexpression, enhancing chemotherapy efficacy.
  • Clinical trials have not confirmed COX-2's role in Alzheimer's disease neurodegeneration.
  • COX-2 mediates the oxygenation of endocannabinoids, producing novel lipid mediators.

Conclusions:

  • COX-2 inhibitors are valuable therapeutic agents for pain and inflammation with significant gastrointestinal benefits.
  • COX-2 inhibitors hold promise as chemopreventive agents and may enhance cancer chemotherapy.
  • Further research is needed to elucidate the complex role of COX-2 in neurological diseases and the endocannabinoid system.

More Related Videos

Structure-Guided Design and Development of Novel Cyclophilin A Inhibitors and Ganoderiol-F Derivatives: An In-Silico Approach10:01

Structure-Guided Design and Development of Novel Cyclophilin A Inhibitors and Ganoderiol-F Derivatives: An In-Silico Approach

Published on: June 23, 2026

Related Concept Videos

Inhibition of Cdk Activity02:34

Inhibition of Cdk Activity

The orderly progression of the cell cycle depends on the activation of Cdk protein by binding to its cyclin partner. However, the cell cycle must be restricted when undergoing abnormal changes. Most cancers correlate to the deregulated cell cycle, and since Cdks are a central component of the cell cycle, Cdk inhibitors are extensively studied to develop anticancer agents. For instance, cyclin D associates with several Cdks, such as Cdk 4/6, to form an active complex. The cyclin D-Cdk4/6 complex...
Inhibition of CDK Activity02:34

Inhibition of CDK Activity

The orderly progression of the cell cycle depends on the activation of Cdk protein by binding to its cyclin partner. However, the cell cycle must be restricted when undergoing abnormal changes. Most cancers correlate to the deregulated cell cycle, and since Cdks are a central component of the cell cycle, Cdk inhibitors are extensively studied to develop anticancer agents. For instance, cyclin D associates with several Cdks, such as Cdk 4/6, to form an active complex. The cyclin D-Cdk4/6 complex...
Enzyme Inhibition01:30

Enzyme Inhibition

Inhibitors are molecules that reduce enzyme activity by binding to the enzyme. In a normally functioning cell, enzymes are regulated by a variety of inhibitors. Drugs and other toxins can also inhibit enzymes. Some inhibitors bind to the enzyme’s active site, while others inhibit enzymatic activity by binding to other sites on the protein structure.
Inhibitors of Bacterial Protein Synthesis01:25

Inhibitors of Bacterial Protein Synthesis

Aminoglycosides constitute a highly potent class of bactericidal antibiotics that exert their antimicrobial effects by targeting the bacterial ribosome, specifically disrupting protein synthesis. These polycationic molecules consist of amino-modified sugars linked via glycosidic bonds to an aminocyclitol core such as 2-deoxystreptamine or streptamine. Their strong positive charges facilitate tight binding to the negatively charged phosphate backbone of ribosomal RNA (rRNA), primarily at the 16S...
Regulation of Angiogenesis and Blood Supply01:24

Regulation of Angiogenesis and Blood Supply

Rapidly dividing tumors, embryos, and wounded tissues require more oxygen than usual, lowering the oxygen concentration in the blood. At low oxygen or hypoxic conditions, an oxygen-sensitive transcription factor called the hypoxia-inducible factor 1 or HIF1 is activated. HIF1 is a dimeric protein of alpha (ɑ) and beta (β) subunits.  Under optimal oxygen conditions, HIF1β is present in the nucleus while HIF1ɑ remains in the cytosol. HIF1ɑ is hydroxylated by prolyl hydroxylase and factor...
Activation of Integrins01:15

Activation of Integrins

Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding events provide an effective stimulus.