Molecular cloning and characterization of the mouse Peroxiredoxin V gene

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dc.contributor.authorTae Hoon Lee-
dc.contributor.authorSun Jung Kim-
dc.contributor.authorSang Won Kang-
dc.contributor.authorKyung Kwang Lee-
dc.contributor.authorSue Goo Rhee-
dc.contributor.authorDae Yeul Yu-
dc.date.accessioned2017-04-19T08:56:58Z-
dc.date.available2017-04-19T08:56:58Z-
dc.date.issued2000-
dc.identifier.issn0006-291X-
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/5052-
dc.description.abstractWe have cloned two cDNA isoforms as well as genomic sequences of the mouse Prx V gene and characterized their molecular genetic features. Two isoforms of the mouse Prx V cDNA were identified from liver and testis. The testis-originated long transcripts had extra 1164-bp 5'-UTR sequences compared to the liver-originated short transcripts. Primer extension and sequence analyses revealed that the two isoforms were presumably transcribed at the same gene locus. The gene was composed of six exons spanning 3.2 kb. The short transcript was abundantly expressed in the kidney, liver, and heart of the adult mouse tissues and in the extra-membrane of the 10.5 dpc embryos. The long transcript of 1985 bp was abundantly detected in testis with trace amounts in other tissues. Interestingly, in testis and fetus, only mRNA expression of the long form was identified. However, the protein expression was not found in testis, implying that the long form could not properly direct the protein expression. The long Prx V cDNA has eight uORFs in the extra 5'-UTR, which proceed the major ORF. The inability of protein expression for the long-form cDNA in testis suggests that the uORFs might inhibit translation of the major ORF and thereby confer the tissue-specific regulation of the mouse Prx V gene.-
dc.publisherElsevier-
dc.titleMolecular cloning and characterization of the mouse Peroxiredoxin V gene-
dc.title.alternativeMolecular cloning and characterization of the mouse Peroxiredoxin V gene-
dc.typeArticle-
dc.citation.titleBiochemical and Biophysical Research Communications-
dc.citation.number2-
dc.citation.endPage362-
dc.citation.startPage356-
dc.citation.volume270-
dc.contributor.affiliatedAuthorTae Hoon Lee-
dc.contributor.affiliatedAuthorSun Jung Kim-
dc.contributor.affiliatedAuthorKyung Kwang Lee-
dc.contributor.affiliatedAuthorDae Yeul Yu-
dc.contributor.alternativeName이태훈-
dc.contributor.alternativeName김선정-
dc.contributor.alternativeName강상원-
dc.contributor.alternativeName이경광-
dc.contributor.alternativeName이서구-
dc.contributor.alternativeName유대열-
dc.identifier.bibliographicCitationBiochemical and Biophysical Research Communications, vol. 270, no. 2, pp. 356-362-
dc.identifier.doi10.1006/bbrc.2000.2430-
dc.subject.keywordperoxiredoxin V-
dc.subject.keywordantioxidant enzyme-
dc.subject.keywordbacterial artificial chromosome-
dc.subject.keywordupstream open reading frame-
dc.subject.localPeroxiredoxin 5-
dc.subject.localPeroxiredoxin V-
dc.subject.localperoxiredoxin 5-
dc.subject.localperoxiredoxin V-
dc.subject.localAnti-oxidant enzyme-
dc.subject.localAntioxidant Enzymes-
dc.subject.localAntioxidant enzyme-
dc.subject.localAntioxidant enzymes-
dc.subject.localantioxidant enzyme-
dc.subject.localantioxidant enzymes-
dc.subject.localBacterial artificial chromosome-
dc.subject.localbacterial artificial chromosome-
dc.subject.localbacterial artificial chromosome (BAC)-
dc.subject.localupstream open reading frame-
dc.description.journalClassY-
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