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Differential alternative splicing of human transglutaminase 4 in benign prostate hyperplasia and prostate cancer

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dc.contributor.authorCho, Sung-Yup-
dc.contributor.authorChoi, Kyungho-
dc.contributor.authorKim, Chai-Wan-
dc.contributor.authorJeon, Ju-Hong-
dc.contributor.authorLee, Jong Bouk-
dc.contributor.authorKim, Choung-Soo-
dc.contributor.authorJeong, Eui Man-
dc.contributor.authorSong, Kye-Yong-
dc.contributor.authorKim, In-Gyu-
dc.contributor.authorJang, Gi-Yong-
dc.contributor.authorPark, Jeong-Soo-
dc.contributor.authorLee, Sang Eun-
dc.contributor.authorShin, Dong-Myung-
dc.date.accessioned2012-05-22T05:10:50Z-
dc.date.available2012-05-22T05:10:50Z-
dc.date.issued2010-04-30-
dc.identifier.citationEXPERIMENTAL AND MOLECULAR MEDICINE; Vol.42 4; 310-318ko_KR
dc.identifier.issn1226-3613-
dc.identifier.urihttps://hdl.handle.net/10371/76226-
dc.description.abstractTransglutaminase 4 is a member of enzyme family that catalyzes calcium-dependent posttranslational modification of proteins. Although transglutaminase 4 has been shown to have prostate-restricted expression pattern, little is known about the biological function of transglutaminase 4 in human. To gain insight into its role in prostate, we analyzed the expression status of human transglutaminase 4 in benign prostate hyperplasia (BPH) and prostate cancer (PCa). Unexpectedly, RT-PCR and nucleotide sequence analysis showed four alternative splicing variants of transglutaminase 4: transglutaminase 4-L, -M (-M1 and -M2) and -S. The difference between transglutaminase 4-M1 and -M2 is attributed to splicing sites, but not nucleotide size. The deduced amino acid sequences showed that transglutaminase 4-L, -M1 and -M2 have correct open reading frames, whereas transglutaminase 4-S has a truncated reading frame. RT-PCR analysis of clinical samples revealed that transglutaminase 4-M and -S were detected in all tested prostate tissue (80 BPH and 48 PCa). Interestingly, transglutaminase 4-L was found in 56% of BPH (45 out of 80) and only in 15% of PCa (7 out of 48). However, transglutaminase 4-L expression did not correlate with serum prostate-specific antigen (PSA) level, prostate volumes or PSA densities. These results will provide a clue to future investigation aiming at delineating physiological and pathological roles of human transglutaminase 4.ko_KR
dc.language.isoenko_KR
dc.publisherKOREAN SOC MED BIOCHEMISTRY MOLECULAR BIOLOGYko_KR
dc.subjectalternative splicingko_KR
dc.subjectprostate hyperplasiako_KR
dc.subjectprostatic neoplasmsko_KR
dc.subjecttransglutaminase 4ko_KR
dc.titleDifferential alternative splicing of human transglutaminase 4 in benign prostate hyperplasia and prostate cancerko_KR
dc.typeArticleko_KR
dc.contributor.AlternativeAuthor조성엽-
dc.contributor.AlternativeAuthor김채완-
dc.contributor.AlternativeAuthor최경호-
dc.contributor.AlternativeAuthor전주홍-
dc.contributor.AlternativeAuthor신동명-
dc.contributor.AlternativeAuthor이상은-
dc.contributor.AlternativeAuthor김인규-
dc.contributor.AlternativeAuthor송계용-
dc.contributor.AlternativeAuthor장기용-
dc.contributor.AlternativeAuthor정의만-
dc.contributor.AlternativeAuthor박정수-
dc.contributor.AlternativeAuthor김청수-
dc.contributor.AlternativeAuthor이종복-
dc.identifier.doi10.3858/emm.2010.42.4.031-
dc.citation.journaltitleEXPERIMENTAL AND MOLECULAR MEDICINE-
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College of Medicine/School of Medicine (의과대학/대학원)Dept. of Physiology (생리학교실)Journal Papers (저널논문_생리학교실)
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