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

Cited 39 time in Web of Science Cited 23 time in Scopus
Authors
Cho, Sung-Yup; Choi, Kyungho; Kim, Chai-Wan; Jeon, Ju-Hong; Lee, Jong Bouk; Kim, Choung-Soo; Jeong, Eui Man; Song, Kye-Yong; Kim, In-Gyu; Jang, Gi-Yong; Park, Jeong-Soo; Lee, Sang Eun; Shin, Dong-Myung
Issue Date
2010-04-30
Publisher
KOREAN SOC MED BIOCHEMISTRY MOLECULAR BIOLOGY
Citation
EXPERIMENTAL AND MOLECULAR MEDICINE; Vol.42 4; 310-318
Keywords
alternative splicingprostate hyperplasiaprostatic neoplasmstransglutaminase 4
Abstract
Transglutaminase 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.
ISSN
1226-3613
Language
English
URI
https://hdl.handle.net/10371/76226
DOI
https://doi.org/10.3858/emm.2010.42.4.031
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College of Medicine/School of Medicine (의과대학/대학원)Dept. of Physiology (생리학교실)Journal Papers (저널논문_생리학교실)
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