{"refrec":{"BRefID":110877,"RR":"Wang, L.-Q.; James, M.O. (2007). Sulfonation of 17ß-estradiol and inhibition of sulfotransferase activity by polychlorobiphenylols and celecoxib in channel catfish, Ictalurus punctatus. Aquat. Toxicol. 81(3): 286-292. https://dx.doi.org/10.1016/j.aquatox.2006.12.011","BEntID":105521,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":0,"RefStringPartII":". Aquat. Toxicol. 81(3): 286-292. https://dx.doi.org/10.1016/j.aquatox.2006.12.011","DocTypID":8,"DocType":"Journal article","MarineFlag":0,"FreshFlag":1,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Wang, L.-Q.; James, M.O.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Wang, L.-Q.; James, M.O.","Englishabstract":"The sulfonation of 17β-estradiol (E2) by human liver and recombinant sulfotransferases is influenced by environmental contaminants such as hydroxylated metabolites of polychlorinated biphenyls (OH-PCBs), which are potent inhibitors, and the therapeutic drug, celecoxib, which affects positional sulfonation of E2. In some locations, the aquatic environment is contaminated by PCBs, OH-PCBs and widely used therapeutic drugs. The objectives of this study were to investigate the sulfonation kinetics of E2 in liver cytosol from channel catfish (Ictalurus punctatus); to examine the effect of OH-PCBs on E2 sulfonation; and to determine if celecoxib altered the position of E2 sulfonation, as it does with human liver cytosol. E2 was converted to both 3- and 17-sulfates by catfish liver cytosol. At E2 concentrations below 1 μM, formation of E2-3-sulfate (E2-3-S) predominated, but substrate inhibition was observed at higher concentrations. Rates of E2-3-S formation at different E2 concentrations were fit to a substrate inhibition model, with K′m and Vmax values of 0.40 ± 0.10 μM and 91.0 ± 4.7 pmol/min/mg protein, respectively and KI of 1.08 ± 0.09μM. The formation of E2-17-S fit Michaelis-Menten kinetics over the concentration range 25nM to 2.5μM, with Km and Vmax values of 1.07 ± 0.23μM and 25.7 ± 4.43 pmol/min/mg protein, respectively. The efficiency (Vmax/Km) of formation of E2-3-S was 9.8-fold higher than that of E2-17-S. Several OH-PCBs inhibited E2 3-sulfonation, measured at an E2 concentration of 1nM. Of those tested, the most potent inhibitor was 4′-OH-CB79, with two chlorine atoms flanking the OH group (IC50: 94nM). The inhibition of estrogen sulfonation by OH-PCBs may disrupt the endocrine system and thus contribute to the known toxic effects of these compounds. Celecoxib did not stimulate E2-17-S formation, as is the case with human liver cytosol, but did inhibit the formation of E2-3-S (IC50: 44μM) and to a lesser extent, E2-17-S (IC50: >160μM), suggesting the previously found effect of celecoxib on E2-17-S formation may be specific to human SULT2A1.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"Sulfonation of 17ß-estradiol and inhibition of sulfotransferase activity by polychlorobiphenylols and celecoxib in channel catfish, Ictalurus punctatus","OrigTitleLangCode":"en","OrigTitleLangCodeExtended":"eng","OrigTitleLangID":15,"DateLastModified":{"date":"2026-06-09 01:31:16.780638","timezone_type":1,"timezone":"+02:00"},"UserAccessRight":null,"UserAccID":null,"AuthorKeywords":"sulfotransferase; sulfonation; channel catfish; inhibition; OH-PCBs;celecoxib","OtherDescriptors":null,"Notes":null,"AnaPub":2007,"MonPub":null,"DateUpdate":"2020-10-22","DateCreate":"2007-06-06","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000245069500006","VABBcode":null,"OpenAcc":0,"DOI":"10.1016/j.aquatox.2006.12.011"},"refs":null,"anarec":{"AnaID":110877,"PubliDate":2007,"Pagination":"286-292","XtraPublOfAnaID":null,"ISBN":null,"Volume":"81","Issue":"3","BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":42203,"SerRR":"Aquatic Toxicology. Elsevier Science: Tokyo; New York; London; Amsterdam. ISSN 0166-445X; e-ISSN 1879-1514","StandardTitleSer":"Aquatic Toxicology","ISSN":"0166-445X","AbbrevSer":"Aquat. Toxicol.","StandardTitleMon":null,"StartPage":286,"Pages":7,"ToPubliDate":null,"BRefBibLvlCode":"S","SerNotes":null},"monrec":null,"serrec":null,"relations":null,"relationsRev":null,"addrec":{"Line1":"University of Florida, Gainesville, FL 32610, USA","Email":"mojames@ufl.edu","Line2":null,"EnvName":"USA"},"othpubs":null,"ownerships":null,"authors":[{"AutName":"Wang","Firstname":"Li-Quan","Initials":"L.-Q.","Affiliation":null,"Discriminator":null,"CorporateFlag":0,"BEntID":105521,"AutID":73735,"OrderNr":1,"DegrID":null,"EditorFlag":0,"CorrespFlag":0,"IllustratorFlag":0,"ReviserFlag":0,"TranslatorFlag":0,"InsAcronym":null,"InsFSN":null,"ORCID":null,"PersID":null,"InsID":null},{"AutName":"James","Firstname":"Margaret","Initials":"M.O.","Affiliation":null,"Discriminator":null,"CorporateFlag":0,"BEntID":105521,"AutID":52760,"OrderNr":2,"DegrID":null,"EditorFlag":0,"CorrespFlag":0,"IllustratorFlag":0,"ReviserFlag":0,"TranslatorFlag":0,"InsAcronym":null,"InsFSN":null,"ORCID":null,"PersID":null,"InsID":null}],"mapdetails":null,"datasets":null,"monographs":null,"monparts":null,"serparts":null,"BEntOpen":null,"BEntPrivate":null,"availability":[{"BInstID":353165,"LibID":36,"BRefID":110877,"EmbargoDate":null,"FullEmbargoDate":null,"PhysMedID":16,"hasOCRd":null,"ShelfLocCode":"353165","RFID":null,"PaidValue":null,"Medium":"Server","Description":"Interne VLIZ documenten","Acronym":"VLIZ","Library":"Vlaams Instituut voor de Zee","DutchTerm":"Non-open access","URL":null,"ClassifID":228,"Classification":"Non-open access","ReqLink":1,"ClassifTypID":3,"URLLocation":"https://www.vliz.be/imisdocs/publications/","SubDir":1,"InternalReq":1,"LoggedInReq":1,"Disclaimer":"Disclaimer_VLIZ_Intern","DutchDisclaimer":"
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