{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,7]],"date-time":"2025-11-07T09:41:31Z","timestamp":1762508491881,"version":"3.37.3"},"reference-count":66,"publisher":"Public Library of Science (PLoS)","issue":"4","license":[{"start":{"date-parts":[[2021,4,22]],"date-time":"2021-04-22T00:00:00Z","timestamp":1619049600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100004396","name":"Thailand Research Fund","doi-asserted-by":"publisher","award":["RSA6180007"],"award-info":[{"award-number":["RSA6180007"]}],"id":[{"id":"10.13039\/501100004396","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100011057","name":"National Center for Genetic Engineering and Biotechnology","doi-asserted-by":"publisher","award":["P16-50758"],"award-info":[{"award-number":["P16-50758"]}],"id":[{"id":"10.13039\/501100011057","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Research and Platform Technology Management Grant from the National Center for Genetic Engineering and Biotechnology","award":["P1750566"],"award-info":[{"award-number":["P1750566"]}]}],"content-domain":{"domain":["www.plosone.org"],"crossmark-restriction":false},"short-container-title":["PLoS ONE"],"abstract":"<jats:p>Cyclooxygenase (COX) is a two-step enzyme that converts arachidonic acid into prostaglandin H<jats:sub>2<\/jats:sub>, a labile intermediate used in the production of prostaglandin E<jats:sub>2<\/jats:sub> (PGE<jats:sub>2<\/jats:sub>) and prostaglandin F<jats:sub>2\u03b1<\/jats:sub> (PGF<jats:sub>2\u03b1<\/jats:sub>). In vertebrates and corals, COX must be <jats:italic>N<\/jats:italic>-glycosylated on at least two asparagine residues in the N-(X)-S\/T motif to be catalytically active. Although COX glycosylation requirement is well-characterized in many species, whether crustacean COXs require <jats:italic>N<\/jats:italic>-glycosylation for their enzymatic function have not been investigated. In this study, a 1,842-base pair <jats:italic>cox<\/jats:italic> gene was obtained from ovarian cDNA of the black tiger shrimp <jats:italic>Penaeus monodon<\/jats:italic>. Sequence analysis revealed that essential catalytic residues and putative catalytic domains of <jats:italic>P<\/jats:italic>. <jats:italic>monodon<\/jats:italic> COX (PmCOX) were well-conserved in relation to other vertebrate and crustacean COXs. Expression of PmCOX in 293T cells increased levels of secreted PGE<jats:sub>2<\/jats:sub> and PGF<jats:sub>2\u03b1<\/jats:sub> up to 60- and 77-fold, respectively, compared to control cells. Incubation of purified PmCOX with endoglycosidase H, which cleaves oligosaccharides from <jats:italic>N<\/jats:italic>-linked glycoproteins, reduced the molecular mass of PmCOX. Similarly, addition of tunicamycin, which inhibits <jats:italic>N<\/jats:italic>-linked glycosylation, in PmCOX-expressing cells resulted in PmCOX protein with lower molecular mass than those obtained from untreated cells, suggesting that PmCOX was <jats:italic>N<\/jats:italic>-glycosylated. Three potential glycosylation sites of PmCOX were identified at N79, N170 and N424. Mutational analysis revealed that although all three residues were glycosylated, only mutations at N170 and N424 completely abolished catalytic function. Inhibition of COX activity by ibuprofen treatment also decreased the levels of PGE<jats:sub>2<\/jats:sub> in shrimp haemolymph. This study not only establishes the presence of the COX enzyme in penaeid shrimp, but also reveals that <jats:italic>N<\/jats:italic>-glycosylation sites are highly conserved and required for COX function in crustaceans.<\/jats:p>","DOI":"10.1371\/journal.pone.0250276","type":"journal-article","created":{"date-parts":[[2021,4,22]],"date-time":"2021-04-22T20:01:59Z","timestamp":1619121719000},"page":"e0250276","update-policy":"https:\/\/doi.org\/10.1371\/journal.pone.corrections_policy","source":"Crossref","is-referenced-by-count":6,"title":["Biochemical characterization of the cyclooxygenase enzyme in penaeid shrimp"],"prefix":"10.1371","volume":"16","author":[{"given":"Punsa","family":"Tobwor","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Pacharawan","family":"Deenarn","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Thapanee","family":"Pruksatrakul","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Surasak","family":"Jiemsup","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Suganya","family":"Yongkiettrakul","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Vanicha","family":"Vichai","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Metavee","family":"Phromson","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sage","family":"Chaiyapechara","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Waraporn","family":"Jangsutthivorawat","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Pisut","family":"Yotbuntueng","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4251-3707","authenticated-orcid":true,"given":"Oliver George","family":"Hargreaves","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0897-506X","authenticated-orcid":true,"given":"Wananit","family":"Wimuttisuk","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"340","published-online":{"date-parts":[[2021,4,22]]},"reference":[{"key":"pone.0250276.ref001","doi-asserted-by":"crossref","first-page":"986","DOI":"10.1161\/ATVBAHA.110.207449","article-title":"Prostaglandins and inflammation","volume":"31","author":"E Ricciotti","year":"2011","journal-title":"Arterioscler Thromb Vasc Biol"},{"key":"pone.0250276.ref002","first-page":"89","article-title":"Prostaglandin E2 as a modulator of viral infections","author":"WJ Sander","year":"2017","journal-title":"Frontiers in Physiology. 2017"},{"key":"pone.0250276.ref003","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1136\/pgmj.51.592.74","article-title":"Prostaglandins in reproductive physiology","volume":"51","author":"GM Craig","year":"1975","journal-title":"Postgrad Med J"},{"key":"pone.0250276.ref004","article-title":"Blood clotting: the role of the prostaglandins","volume":"196","author":"JL Marx","year":"1977","journal-title":"Science (80-)"},{"key":"pone.0250276.ref005","article-title":"Prostaglandins and leukotrienes: advances in eicosanoid biology","volume":"294","author":"CD Funk","year":"2001","journal-title":"Science (80-)"},{"key":"pone.0250276.ref006","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/0005-2760(91)90119-3","article-title":"Prostaglandin endoperoxide synthase: structure and catalysis","volume":"1083","author":"WL Smith","year":"1991","journal-title":"Biochim Biophys Acta\u2014Lipids Lipid Metab"},{"key":"pone.0250276.ref007","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1186\/gb-2004-5-9-241","article-title":"The cyclooxygenases","volume":"5","author":"N V Chandrasekharan","year":"2004","journal-title":"Genome Biol"},{"key":"pone.0250276.ref008","doi-asserted-by":"crossref","first-page":"34","DOI":"10.1016\/j.bbrc.2005.07.198","article-title":"Structural and functional differences between cyclooxygenases: Fatty acid oxygenases with a critical role in cell signaling","volume":"338","author":"CA Rouzer","year":"2005","journal-title":"Biochem Biophys Res Commun"},{"key":"pone.0250276.ref009","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1146\/annurev.biochem.69.1.145","article-title":"Cyclooxygenase: structural, cellular, and molecular biology","volume":"69","author":"WL Smith","year":"2000","journal-title":"Annu Rev Biochem"},{"key":"pone.0250276.ref010","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1194\/jlr.R800042-JLR200","article-title":"Cyclooxygenases: structural and functional insights","volume":"50","author":"CA Rouzer","year":"2009","journal-title":"J Lipid Res"},{"key":"pone.0250276.ref011","doi-asserted-by":"crossref","first-page":"4084","DOI":"10.1074\/jbc.M304762200","article-title":"Role of Asn-382 and Thr-383 in activation and inactivation of human prostaglandin H synthase cyclooxygenase catalysis","volume":"279","author":"B Bambai","year":"2004","journal-title":"J Biol Chem"},{"key":"pone.0250276.ref012","doi-asserted-by":"crossref","first-page":"29830","DOI":"10.1074\/jbc.273.45.29830","article-title":"The membrane association sequences of the prostaglandin endoperoxide synthases-1 and -2 isozymes","volume":"273","author":"Y Li","year":"1998","journal-title":"J Biol Chem"},{"key":"pone.0250276.ref013","doi-asserted-by":"crossref","first-page":"32936","DOI":"10.1074\/jbc.274.46.32936","article-title":"The membrane binding domains of prostaglandin endoperoxide H synthases 1 and 2. Peptide mapping and mutational analysis","volume":"274","author":"AG Spencer","year":"1999","journal-title":"J Biol Chem"},{"key":"pone.0250276.ref014","doi-asserted-by":"crossref","first-page":"6168","DOI":"10.1016\/S0021-9258(18)38099-2","article-title":"Essential histidines of prostaglandin endoperoxide synthase: His-309 is involved in heme binding","volume":"266","author":"T Shimokawa","year":"1991","journal-title":"J Biol Chem"},{"key":"pone.0250276.ref015","doi-asserted-by":"crossref","first-page":"503","DOI":"10.1016\/j.jmb.2003.10.073","article-title":"The 2.0\u00c5 resolution crystal structure of prostaglandin H2 synthase-1: structural insights into an unusual peroxidase","volume":"335","author":"K Gupta","year":"2004","journal-title":"J Mol Biol"},{"key":"pone.0250276.ref016","doi-asserted-by":"crossref","first-page":"21565","DOI":"10.1074\/jbc.272.34.21565","article-title":"Mutational analysis of the role of the distal histidine and glutamine residues of prostaglandin-endoperoxide synthase-2 in peroxidase catalysis, hydroperoxide reduction, and cyclooxygenase activation","volume":"272","author":"LM Landino","year":"1997","journal-title":"J Biol Chem"},{"key":"pone.0250276.ref017","doi-asserted-by":"crossref","first-page":"388","DOI":"10.1006\/prep.1996.0685","article-title":"Investigation of human cyclooxygenase-2 glycosylation heterogeneity and protein expression in insect and mammalian cell expression systems","volume":"9","author":"MD Percival","year":"1997","journal-title":"Protein Expr Purif"},{"key":"pone.0250276.ref018","doi-asserted-by":"crossref","first-page":"6533","DOI":"10.1016\/j.febslet.2006.10.073","article-title":"Glycosylation regulates turnover of cyclooxygenase-2","volume":"580","author":"MB Sevigny","year":"2006","journal-title":"FEBS Lett"},{"key":"pone.0250276.ref019","doi-asserted-by":"crossref","first-page":"18234","DOI":"10.1016\/S0021-9258(17)46835-9","article-title":"N-glycosylation of prostaglandin endoperoxide synthases-1 and -2 and their orientations in the endoplasmic reticulum","volume":"268","author":"JC Otto","year":"1993","journal-title":"J Biol Chem"},{"key":"pone.0250276.ref020","first-page":"7033","article-title":"The basis of prostaglandin synthesis in coral. Molecular cloning and expression of a cyclooxygenase from the arctic soft coral Gersemia fruticosa","volume":"276","author":"R Koljak","year":"2001","journal-title":"J Biol Chem"},{"key":"pone.0250276.ref021","first-page":"13624","article-title":"isozymes: characterization of marine invertebrate COX genes points to independent duplication events in vertebrate and invertebrate lineages","volume":"279","author":"R Jarving","year":"2004","journal-title":"J Biol Chem"},{"key":"pone.0250276.ref022","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/1742-9994-5-11","article-title":"Outlining eicosanoid biosynthesis in the crustacean Daphnia","volume":"5","author":"LH Heckmann","year":"2008","journal-title":"Front Zool"},{"key":"pone.0250276.ref023","article-title":"Direct evidence of the cyclooxygenase pathway of prostaglandin synthesis in arthropods: Genetic and biochemical characterization of two crustacean cyclooxygenases","author":"K Varvas","year":"2009","journal-title":"Insect Biochem Mol Biol"},{"key":"pone.0250276.ref024","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0076934","article-title":"Insights into the prostanoid pathway in the ovary development of the penaeid shrimp Penaeus monodon","volume":"8","author":"W Wimuttisuk","year":"2013","journal-title":"PLoS One"},{"key":"pone.0250276.ref025","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1007\/s00239-015-9670-3","article-title":"Reconstruction of cyclooxygenase evolution in animals suggests variable, lineage-specific duplications, and homologs with low sequence identity","volume":"80","author":"JC Havird","year":"2015","journal-title":"J Mol Evol"},{"key":"pone.0250276.ref026","doi-asserted-by":"crossref","first-page":"1602","DOI":"10.1111\/are.14508","article-title":"Stress response and lipid composition in shrimp Litopenaeus vannamei fed diets enriched with squid or scallop viscera meal","volume":"51","author":"C Navarro","year":"2020","journal-title":"Aquac Res"},{"key":"pone.0250276.ref027","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/j.ygcen.2015.04.019","article-title":"Variation of prostaglandin E2 concentrations in ovaries and its effects on ovarian maturation and oocyte proliferation in the giant fresh water prawn, Macrobrachium rosenbergii","volume":"223","author":"C Sumpownon","year":"2015","journal-title":"Gen Comp Endocrinol"},{"key":"pone.0250276.ref028","doi-asserted-by":"crossref","first-page":"128","DOI":"10.1016\/j.applanim.2009.02.018","article-title":"Pain and stress in crustaceans?","volume":"118","author":"RW Elwood","year":"2009","journal-title":"Appl Anim Behav Sci"},{"key":"pone.0250276.ref029","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pbio.1000412","article-title":"Improving bioscience research reporting: the ARRIVE guidelines for reporting animal research","volume":"8","author":"C Kilkenny","year":"2010","journal-title":"PLOS Biol"},{"key":"pone.0250276.ref030","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1016\/S0022-2836(05)80360-2","article-title":"Basic local alignment search tool","volume":"215","author":"SF Altschul","year":"1990","journal-title":"J Mol Biol"},{"key":"pone.0250276.ref031","article-title":"Prediction of polyadenylation signals in human DNA sequences using nucleotide frequencies","author":"F Ahmed","year":"2009","journal-title":"In Silico Biol"},{"key":"pone.0250276.ref032","article-title":"CDART: Protein homology by domain architecture","author":"LY Geer","year":"2002","journal-title":"Genome Res"},{"key":"pone.0250276.ref033","first-page":"7","article-title":"Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega","author":"F Sievers","year":"2011","journal-title":"Mol Syst Biol"},{"key":"pone.0250276.ref034","article-title":"MEGA X: Molecular evolutionary genetics analysis across computing platforms","author":"S Kumar","year":"2018","journal-title":"Mol Biol Evol"},{"key":"pone.0250276.ref035","article-title":"NetNGlyc: Prediction of N-glycosylation sites in human proteins","author":"R Gupta","year":"2004","journal-title":"Prep"},{"key":"pone.0250276.ref036","doi-asserted-by":"crossref","first-page":"596","DOI":"10.1093\/nar\/24.4.596","article-title":"Transfecting mammalian cells: optimization of critical parameters affecting calcium-phosphate precipitate formation","volume":"24","author":"M Jordan","year":"1996","journal-title":"Nucleic Acids Res"},{"key":"pone.0250276.ref037","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1016\/S0021-9258(19)52451-6","article-title":"Protein measurement with the Folin phenol reagent","volume":"193","author":"OH Lowry","year":"1951","journal-title":"J Biol Chem"},{"key":"pone.0250276.ref038","article-title":"Role of arachidonic acid and COX inhibitors in the regulation of reproduction in freshwater crab Oziothelphusa senex senex","author":"K Prameswari","year":"2017","journal-title":"J Aquac Res Dev"},{"key":"pone.0250276.ref039","article-title":"Reproduction recovery of the crustacean Daphnia magna after chronic exposure to ibuprofen","author":"Y Hayashi","year":"2008","journal-title":"Ecotoxicology"},{"key":"pone.0250276.ref040","article-title":"Toxicity of the Non-Steroidal Anti-Inflammatory Drugs (NSAIDs) acetylsalicylic acid, paracetamol, diclofenac, ibuprofen and naproxen towards freshwater invertebrates: A review","author":"M Parolini","year":"2020","journal-title":"Science of the Total Environment"},{"key":"pone.0250276.ref041","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1016\/j.ygcen.2003.08.002","article-title":"The synthesis and effects of prostaglandins on the ovary of the crab Oziotelphusa senex senex","volume":"135","author":"PRS Reddy","year":"2004","journal-title":"Gen Comp Endocrinol"},{"key":"pone.0250276.ref042","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1016\/j.cbpb.2003.12.005","article-title":"Maturation-related variations in prostaglandin and fatty acid content of ovary in the kuruma prawn (Marsupenaeus japonicus)","volume":"137","author":"D Tahara","year":"2004","journal-title":"Comp Biochem Physiol\u2014A Mol Integr Physiol"},{"key":"pone.0250276.ref043","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1016\/j.aquaculture.2011.09.037","article-title":"Molecular characterization and expression of the prostaglandin reductase 1 gene and protein during ovarian development of the giant tiger shrimp Penaeus monodon","volume":"322\u2013323","author":"S Prasertlux","year":"2011","journal-title":"Aquaculture"},{"key":"pone.0250276.ref044","article-title":"Prostaglandin E2 in previtellogenic ovaries of the prawn Macrobrachium rosenbergii: synthesis and effect on the level of cAMP","author":"A Sagi","year":"1995","journal-title":"Gen Comp Endocrinol"},{"key":"pone.0250276.ref045","article-title":"A combined computational strategy of sequence and structural analysis predicts the existence of a functional eicosanoid pathway in Drosophila melanogaster","author":"M Scarpati","year":"2019","journal-title":"PLoS One"},{"key":"pone.0250276.ref046","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1242\/dev.017590","article-title":"Drosophila Pxt: a cyclooxygenase-like facilitator of follicle maturation","volume":"135","author":"TL Tootle","year":"2008","journal-title":"Development"},{"key":"pone.0250276.ref047","article-title":"The X-ray crystal structure of the membrane protein prostaglandin H 2 synthase-1","author":"D Picot","year":"1994","journal-title":"Nature"},{"key":"pone.0250276.ref048","article-title":"The cyclooxygenase reaction mechanism","author":"WA Van der Donk","year":"2002","journal-title":"Biochemistry"},{"key":"pone.0250276.ref049","article-title":"Structural analysis of NSAID binding by prostaglandin H2 synthase: Time-dependent and time-independent inhibitors elicit identical enzyme conformations","author":"BS Selinsky","year":"2001","journal-title":"Biochemistry"},{"key":"pone.0250276.ref050","article-title":"Dynamics of prostaglandin H synthases. Studies with prostaglandin H synthase 2 Y355F unmask mechanisms of time-dependent inhibition and allosteric activation","author":"OY So","year":"1998","journal-title":"J Biol Chem"},{"key":"pone.0250276.ref051","article-title":"Arginine 120 of prostaglandin G\/H synthase-1 is required for the inhibition by nonsteroidal anti-inflammatory drugs containing a carboxylic acid moiety","author":"JA Mancini","year":"1995","journal-title":"J Biol Chem"},{"key":"pone.0250276.ref052","doi-asserted-by":"crossref","first-page":"6616","DOI":"10.1021\/bi0002333","article-title":"Peroxidase Activity in Prostaglandin Endoperoxide H Synthase-1 Occurs with a Neutral Histidine Proximal Heme Ligand","volume":"39","author":"SA Seibold","year":"2000","journal-title":"Biochemistry"},{"key":"pone.0250276.ref053","article-title":"Cyclooxygenase isozymes: The biology of prostaglandin synthesis and inhibition","author":"DL Simmons","year":"2004","journal-title":"Pharmacological Reviews"},{"key":"pone.0250276.ref054","article-title":"Characterization of the glycosylation sites in cyclooxygenase-2 using mass spectrometry","author":"JF Nemeth","year":"2001","journal-title":"Biochemistry"},{"key":"pone.0250276.ref055","doi-asserted-by":"crossref","DOI":"10.1186\/2193-1801-3-436","volume-title":"N-glycosylation site occupancy in human prostaglandin H synthases expressed in Pichia pastoris","author":"K Kukk","year":"2014"},{"key":"pone.0250276.ref056","article-title":"Developmental expression of functional cyclooxygenases in zebrafish","author":"T Grosser","year":"2002","journal-title":"Proc Natl Acad Sci U S A"},{"key":"pone.0250276.ref057","article-title":"Glycosylation of human cyclooxygenase-2 (COX-2) decreases the efficacy of certain COX-2 inhibitors","author":"MB Sevigny","year":"2012","journal-title":"Pharmacol Res"},{"key":"pone.0250276.ref058","first-page":"lb79","article-title":"Effect of glycosylation of cyclooxygenase-2 (COX-2) on homodimerization","volume":"31","author":"DDC Vann-Victorino","year":"2017","journal-title":"FASEB J"},{"key":"pone.0250276.ref059","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1111\/are.12163","article-title":"The effect of Ibuprofen on female and male reproduction of the open thelyca marine shrimp, Litopenaeus","volume":"46","author":"J Alfaro-Montoya","year":"2015","journal-title":"Aquac Res"},{"key":"pone.0250276.ref060","article-title":"Metabolism of prostaglandin glycerol esters and prostaglandin ethanolamides in vitro and in vivo","author":"KR Kozak","year":"2001","journal-title":"J Biol Chem"},{"key":"pone.0250276.ref061","article-title":"Why there are two cyclooxygenase isozymes","author":"WL Smith","year":"2001","journal-title":"Journal of Clinical Investigation"},{"key":"pone.0250276.ref062","article-title":"Divergent cyclooxygenase responses to fatty acid structure and peroxide level in fish and mammalian prostaglandin H synthases","author":"W Liu","year":"2006","journal-title":"FASEB J"},{"key":"pone.0250276.ref063","doi-asserted-by":"crossref","first-page":"541","DOI":"10.1007\/BF00302112","article-title":"Changes in prostaglandin E2 and F2\u03b1 during vitellogenesis in the florida crayfish Procambarus paeninsulanus","volume":"163","author":"EP Spaziani","year":"1993","journal-title":"J Comp Physiol B"},{"key":"pone.0250276.ref064","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1007\/s12562-009-0208-8","article-title":"Detection of prostaglandin E2 in polychaete Perinereis sp. and its effect on Penaeus monodon oocyte development in vitro","volume":"76","author":"O Meunpol","year":"2010","journal-title":"Fish Sci"},{"key":"pone.0250276.ref065","article-title":"Smith WL. Different fatty acids compete with arachidonic acid for binding to the allosteric or catalytic subunits of cyclooxygenases to regulate prostanoid synthesis","author":"L Dong","year":"2016","journal-title":"J Biol Chem"},{"key":"pone.0250276.ref066","article-title":"The role of cyclooxygenase in n-6 and n-3 polyunsaturated fatty acid mediated effects on cell proliferation, PGE2 synthesis and cytotoxicity in human colorectal carcinoma cell lines","author":"YEM Dommels","year":"2003","journal-title":"Carcinogenesis"}],"container-title":["PLOS ONE"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pone.0250276","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,4,22]],"date-time":"2021-04-22T20:03:07Z","timestamp":1619121787000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pone.0250276"}},"subtitle":[],"editor":[{"given":"Andreas","family":"Hofmann","sequence":"first","affiliation":[],"role":[{"role":"editor","vocabulary":"crossref"}]}],"short-title":[],"issued":{"date-parts":[[2021,4,22]]},"references-count":66,"journal-issue":{"issue":"4","published-online":{"date-parts":[[2021,4,22]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pone.0250276","relation":{},"ISSN":["1932-6203"],"issn-type":[{"type":"electronic","value":"1932-6203"}],"subject":[],"published":{"date-parts":[[2021,4,22]]}}}