Differential alternative splicing of human transglutaminase 4 in benign prostate hyperplasia and prostate cancer.
10.3858/emm.2010.42.4.031
- Author:
Sung Yup CHO
1
;
Kyungho CHOI
;
Ju Hong JEON
;
Chai Wan KIM
;
Dong Myung SHIN
;
Jong Bouk LEE
;
Sang Eun LEE
;
Choung Soo KIM
;
Jeong Soo PARK
;
Eui Man JEONG
;
Gi Yong JANG
;
Kye Yong SONG
;
In Gyu KIM
Author Information
1. Department of Biochemistry and Molecular Biology, Aging and Apoptosis Research Center (AARC), Seoul National University College of Medicine, Seoul 110-799, Korea. igkim@plaza.snu.ac.kr
- Publication Type:Original Article ; Research Support, Non-U.S. Gov't
- Keywords:
alternative splicing;
prostate hyperplasia;
prostatic neoplasms;
transglutaminase 4
- From:Experimental & Molecular Medicine
2010;42(4):310-318
- CountryRepublic of Korea
- Language:English
-
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.
