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COX-3, a Cyclooxygenase-1 Variant Inhibited by Acetaminophen and Other Analgesic/Antipyretic Drugs: Cloning, Structure, and Expression
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COX-3, a Cyclooxygenase-1 Variant Inhibited by Acetaminophen and Other Analgesic/Antipyretic Drugs: Cloning, Structure, and Expression
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COX-3, a Cyclooxygenase-1 Variant Inhibited by Acetaminophen and Other Analgesic/Antipyretic Drugs: Cloning, Structure, and Expression
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Journal Article
COX-3, a Cyclooxygenase-1 Variant Inhibited by Acetaminophen and Other Analgesic/Antipyretic Drugs: Cloning, Structure, and Expression
2002
Overview
Two cyclooxygenase isozymes, COX-1 and -2, are known to catalyze the rate-limiting step of prostaglandin synthesis and are the targets of nonsteroidal antiinflammatory drugs. Here we describe a third distinct COX isozyme, COX-3, as well as two smaller COX-1-derived proteins (partial COX-1 or PCOX-1 proteins). COX-3 and one of the PCOX-1 proteins (PCOX-1a) are made from the COX-1 gene but retain intron 1 in their mRNAs. PCOX-1 proteins additionally contain an in-frame deletion of exons 5-8 of the COX-1 mRNA. COX-3 and PCOX mRNAs are expressed in canine cerebral cortex and in lesser amounts in other tissues analyzed. In human, COX-3 mRNA is expressed as an ≈5.2-kb transcript and is most abundant in cerebral cortex and heart. Intron 1 is conserved in length and in sequence in mammalian COX-1 genes. This intron contains an ORF that introduces an insertion of 30-34 aa, depending on the mammalian species, into the hydrophobic signal peptide that directs COX-1 into the lumen of the endoplasmic reticulum and nuclear envelope. COX-3 and PCOX-1a are expressed efficiently in insect cells as membrane-bound proteins. The signal peptide is not cleaved from either protein and both proteins are glycosylated. COX-3, but not PCOX-1a, possesses glycosylation-dependent cyclooxygenase activity. Comparison of canine COX-3 activity with murine COX-1 and -2 demonstrates that this enzyme is selectively inhibited by analgesic/antipyretic drugs such as acetaminophen, phenacetin, antipyrine, and dipyrone, and is potently inhibited by some nonsteroidal antiinflammatory drugs. Thus, inhibition of COX-3 could represent a primary central mechanism by which these drugs decrease pain and possibly fever.
Publisher
National Academy of Sciences,National Acad Sciences,The National Academy of Sciences
Subject
/ Analgesics, Non-Narcotic - pharmacology
/ Animals
/ Canines
/ Cerebral Cortex - enzymology
/ Cloning
/ Cyclooxygenase Inhibitors - pharmacology
/ Dogs
/ Enzymes
/ Fever
/ Humans
/ Introns
/ Mammals
/ Mice
/ Nonsteroidal anti-inflammatory drugs
/ Nonsteroidal antiinflammatory agents
/ Pain
/ Prostaglandin-Endoperoxide Synthases - chemistry
/ Prostaglandin-Endoperoxide Synthases - genetics
/ Prostaglandin-Endoperoxide Synthases - metabolism
/ Proteins
/ Recombinant Proteins - chemistry
/ Recombinant Proteins - genetics
/ Recombinant Proteins - metabolism
/ RNA
