{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,22]],"date-time":"2025-10-22T10:34:20Z","timestamp":1761129260836},"reference-count":36,"publisher":"Cambridge University Press (CUP)","issue":"13","license":[{"start":{"date-parts":[[2015,8,18]],"date-time":"2015-08-18T00:00:00Z","timestamp":1439856000000},"content-version":"unspecified","delay-in-days":0,"URL":"https:\/\/www.cambridge.org\/core\/terms"}],"content-domain":{"domain":["journals.cambridge.org"],"crossmark-restriction":true},"short-container-title":["Parasitology"],"published-print":{"date-parts":[[2015,11]]},"abstract":"<jats:title>SUMMARY<\/jats:title><jats:p>Phospholipid hydroperoxide glutathione peroxidase (PHGPx, GPx4) is a major antioxidant enzyme, which plays unique roles in the protection of cells against oxidative stress by catalysing reduction of lipid hydroperoxides. We isolated and characterized a full-length cDNA sequence encoding<jats:italic>GPx<\/jats:italic>gene from a blood fluke,<jats:italic>Schistosoma japonicum<\/jats:italic>(designated<jats:italic>SjGPx<\/jats:italic>), which contained an in-frame TGA codon for selenocysteine (Sec) and a concurrent Sec insertion sequence in its 3\u2032-untranslated region. Protein encoded by<jats:italic>SjGPx<\/jats:italic>demonstrated a primary structure characteristic to the PHGPx family, including preservation of catalytic domains and absence of the subunit interaction domains. Semi-quantitative reverse transcription PCR and Western blotting showed that the SjGPx was mainly expressed in the female adults and eggs. RNA interference approach was employed to investigate the effects of knockdown of<jats:italic>SjGPx<\/jats:italic>. SjGPx expression level was significantly reduced on the 5th day post-RNAi. Significantly reduction in GPx enzyme activities, as well as obvious changes in morphology of intrauterine eggs followed the reduction in<jats:italic>SjGPx<\/jats:italic>transcript level. We observed a 63\u00b704% reduction in GPx activity and the eggs severely deformed. Our results revealed that SjGPx protein might be involved in the provision of enzyme activity during egg production.<\/jats:p>","DOI":"10.1017\/s0031182015001055","type":"journal-article","created":{"date-parts":[[2015,8,18]],"date-time":"2015-08-18T05:41:22Z","timestamp":1439876482000},"page":"1595-1604","update-policy":"http:\/\/dx.doi.org\/10.1017\/policypage","source":"Crossref","is-referenced-by-count":2,"title":["Expression and characterization of a phospholipid hydroperoxide glutathione peroxidase gene in<i>Schistosoma japonicum<\/i>"],"prefix":"10.1017","volume":"142","author":[{"given":"YING","family":"ZHANG","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"YUAN","family":"HE","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"LI","family":"HE","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"HONGYING","family":"ZONG","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"GUOBIN","family":"CAI","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"56","published-online":{"date-parts":[[2015,8,18]]},"reference":[{"key":"S0031182015001055_ref22","doi-asserted-by":"publisher","DOI":"10.1016\/0020-7519(88)90101-4"},{"key":"S0031182015001055_ref13","doi-asserted-by":"publisher","DOI":"10.1016\/j.exppara.2012.10.001"},{"key":"S0031182015001055_ref7","doi-asserted-by":"publisher","DOI":"10.1002\/jgm.1314"},{"key":"S0031182015001055_ref33","doi-asserted-by":"publisher","DOI":"10.1016\/0166-6851(92)90042-I"},{"key":"S0031182015001055_ref29","doi-asserted-by":"publisher","DOI":"10.1126\/science.282.5388.430"},{"key":"S0031182015001055_ref5","doi-asserted-by":"publisher","DOI":"10.1016\/j.ijpara.2008.05.011"},{"key":"S0031182015001055_ref20","doi-asserted-by":"publisher","DOI":"10.1006\/expr.1995.1038"},{"key":"S0031182015001055_ref36","doi-asserted-by":"publisher","DOI":"10.1017\/S0031182004004895"},{"key":"S0031182015001055_ref28","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.bi.65.070196.000503"},{"key":"S0031182015001055_ref23","doi-asserted-by":"publisher","DOI":"10.1016\/j.molbiopara.2007.10.009"},{"key":"S0031182015001055_ref16","doi-asserted-by":"publisher","DOI":"10.1016\/j.molbiopara.2007.03.006"},{"key":"S0031182015001055_ref15","doi-asserted-by":"publisher","DOI":"10.1017\/S0031182009005654"},{"key":"S0031182015001055_ref2","doi-asserted-by":"publisher","DOI":"10.1017\/S0031182014001942"},{"key":"S0031182015001055_ref1","doi-asserted-by":"publisher","DOI":"10.1007\/PL00000664"},{"key":"S0031182015001055_ref4","doi-asserted-by":"publisher","DOI":"10.1007\/s00436-008-1236-5"},{"key":"S0031182015001055_ref3","doi-asserted-by":"crossref","first-page":"7342","DOI":"10.1016\/S0021-9258(17)37290-3","article-title":"Phospholipid-hydroperoxide glutathione peroxidase. 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