Iloprost-induced nociception: determination of the site of anti-nociceptive action of cyclooxygenase inhibitors and the involvement of cyclooxygenase products in central mechanisms of nociception.

The writhing response to acute nociception has been used to test the analgesic activity of drugs in rodents. Dilute acetic acid is the most frequently used irritant to induce writhing behaviour. The administration of acetic acid intraperitoneally activates both peripheral and central mechanisms of nociception.

Vane's discovery of the mechanism of action of aspirin changed our understanding of its clinical pharmacology.

Aspirin exerts its analgesic, antipyretic and anti-inflammatory actions by inhibiting the enzyme cyclooxygenase and thus preventing the formation and release of prostaglandins. The elucidation by John Vane of the mechanism of action of aspirin in 1971 was followed twenty years later by the discovery of a second cyclooxygenase enzyme, COX-2 and the rapid development of selective inhibitors of this enzyme. The COX-2 inhibitors are potent anti-inflammatory drugs without the damaging side effects on the stomach mucosa of the non-selective aspirin-like inhibitors.

Activation of macrophage peroxisome proliferator-activated receptor-gamma by diclofenac results in the induction of cyclooxygenase-2 protein and the synthesis of anti-inflammatory cytokines.

Cyclooxygenase-2 (COX-2) is an inducible isoform of the COX family of enzymes central to the synthesis of pro-inflammatory prostaglandins. Induction of COX-2 is mediated by many endogenous and exogenous molecules that include pro-inflammatory cytokines and bacterial lipopolysaccharide (LPS). It has been demonstrated that COX-2 can also be induced by diclofenac in cultured J774.

The involvement of a cyclooxygenase 1 gene-derived protein in the antinociceptive action of paracetamol in mice.

Paracetamol is a widely used analgesic and antipyretic with weak anti-inflammatory properties. Experimental evidence suggests that inhibition of prostaglandin biosynthesis contributes to its pharmacological actions. Three cyclooxygenase (COX) isoenzymes are involved in prostaglandin biosynthesis, COX-1, COX-2 and a recently discovered splice-variant of COX-1, COX-3.

Cyclooxygenase isozymes: the biology of prostaglandin synthesis and inhibition.

Nonsteroidal anti-inflammatory drugs (NSAIDs) represent one of the most highly utilized classes of pharmaceutical agents in medicine. All NSAIDs act through inhibiting prostaglandin synthesis, a catalytic activity possessed by two distinct cyclooxygenase (COX) isozymes encoded by separate genes. The discovery of COX-2 launched a new era in NSAID pharmacology, resulting in the synthesis, marketing, and widespread use of COX-2 selective drugs.

Acetaminophen-induced hypothermia in mice is mediated by a prostaglandin endoperoxide synthase 1 gene-derived protein.

Acetaminophen is a widely used antipyretic analgesic, reducing fever caused by bacterial and viral infections and by clinical trauma such as cancer or stroke. In rare cases in humans, e.g.

Actions of paracetamol on cyclooxygenases in tissue and cell homogenates of mouse and rabbit.

Background: Paracetamol is a potent analgesic and antipyretic drug, but has only weak anti-inflammatory activity. Unlike aspirin-like drugs, paracetamol does not damage the stomach mucosa or inhibit the aggregation of platelets. The analgesic action of paracetamol is on the central nervous system.