Jan M. Schwab , Hermann J. Schluesener , Richard Meyermann , Charles N. Serhan
{"title":"COX-3酶和概念:迈向高度专业化途径和精确治疗的步骤?","authors":"Jan M. Schwab , Hermann J. Schluesener , Richard Meyermann , Charles N. Serhan","doi":"10.1016/j.plefa.2003.07.003","DOIUrl":null,"url":null,"abstract":"<div><div><span><span>Cyclooxygenases<span> (COXs) catalyse the key rate-limiting step in prostanoid and </span></span>thromboxane<span> biosynthesis<span> and are targets of non-steroidal anti-inflammatory drugs (NSAIDs). Until recently, the presence of only two isoforms—COX-1 and COX-2—remained in question because the potent anti-pyretic and analgesic effects of acetaminophen (paracetamol, tylenol</span></span></span><sup>®</sup> ben-u-ron<sup>®</sup><span><span><span>) could not be explained by either COX-1 or COX-2 blockades. A novel COX-1 splice variant termed COX-3, sensitive to acetaminophen, was recently discovered by Simmons et al., and is considered to play a key role in the biosynthesis of prostanoids known to be important mediators in pain and fever. Drugs that preferential block COX-1 also appear to act at COX-3. However the existence of COX-3 at the </span>nucleotide sequence level in humans has been called to question. A functional COX-3 in humans is still to come underlining that the concept of COX-3 is still attractive. Here, we discuss some of the implications drawn from the identification of additional functional cyclooxygenase members in the generation of bioactive </span>autacoids.</span></div></div>","PeriodicalId":94179,"journal":{"name":"Prostaglandins, leukotrienes, and essential fatty acids","volume":"69 5","pages":"Pages 339-343"},"PeriodicalIF":3.0000,"publicationDate":"2003-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"COX-3 the enzyme and the concept: steps towards highly specialized pathways and precision therapeutics?\",\"authors\":\"Jan M. Schwab , Hermann J. Schluesener , Richard Meyermann , Charles N. Serhan\",\"doi\":\"10.1016/j.plefa.2003.07.003\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><div><span><span>Cyclooxygenases<span> (COXs) catalyse the key rate-limiting step in prostanoid and </span></span>thromboxane<span> biosynthesis<span> and are targets of non-steroidal anti-inflammatory drugs (NSAIDs). Until recently, the presence of only two isoforms—COX-1 and COX-2—remained in question because the potent anti-pyretic and analgesic effects of acetaminophen (paracetamol, tylenol</span></span></span><sup>®</sup> ben-u-ron<sup>®</sup><span><span><span>) could not be explained by either COX-1 or COX-2 blockades. A novel COX-1 splice variant termed COX-3, sensitive to acetaminophen, was recently discovered by Simmons et al., and is considered to play a key role in the biosynthesis of prostanoids known to be important mediators in pain and fever. Drugs that preferential block COX-1 also appear to act at COX-3. However the existence of COX-3 at the </span>nucleotide sequence level in humans has been called to question. A functional COX-3 in humans is still to come underlining that the concept of COX-3 is still attractive. Here, we discuss some of the implications drawn from the identification of additional functional cyclooxygenase members in the generation of bioactive </span>autacoids.</span></div></div>\",\"PeriodicalId\":94179,\"journal\":{\"name\":\"Prostaglandins, leukotrienes, and essential fatty acids\",\"volume\":\"69 5\",\"pages\":\"Pages 339-343\"},\"PeriodicalIF\":3.0000,\"publicationDate\":\"2003-11-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Prostaglandins, leukotrienes, and essential fatty acids\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0952327803001479\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Prostaglandins, leukotrienes, and essential fatty acids","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0952327803001479","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
COX-3 the enzyme and the concept: steps towards highly specialized pathways and precision therapeutics?
Cyclooxygenases (COXs) catalyse the key rate-limiting step in prostanoid and thromboxane biosynthesis and are targets of non-steroidal anti-inflammatory drugs (NSAIDs). Until recently, the presence of only two isoforms—COX-1 and COX-2—remained in question because the potent anti-pyretic and analgesic effects of acetaminophen (paracetamol, tylenol® ben-u-ron®) could not be explained by either COX-1 or COX-2 blockades. A novel COX-1 splice variant termed COX-3, sensitive to acetaminophen, was recently discovered by Simmons et al., and is considered to play a key role in the biosynthesis of prostanoids known to be important mediators in pain and fever. Drugs that preferential block COX-1 also appear to act at COX-3. However the existence of COX-3 at the nucleotide sequence level in humans has been called to question. A functional COX-3 in humans is still to come underlining that the concept of COX-3 is still attractive. Here, we discuss some of the implications drawn from the identification of additional functional cyclooxygenase members in the generation of bioactive autacoids.