Please wait a minute...
Shopping Cart Email List Chinese
Advanced Search Fig/Tab
Frontiers of Medicine

ISSN 2095-0217

ISSN 2095-0225(Online)

CN 11-5983/R

Postal Subscription Code 80-967

2018 Impact Factor: 1.847

Featured Articles  |  Most Downloaded  |  Most Reading
Online Submission Subscribe to Our RSS Content Feed
Front Med Chin    2009, Vol. 3 Issue (2) : 197-203    https://doi.org/10.1007/s11684-009-0036-3
RESEARCH ARTICLE
Expression and clinical implication of PRL-1 and PRL-3 in transitional cell carcinoma of bladder
Bin HAO1,2(), Changwei LIU2, Huixiang LI3
1. Department of Urology, Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology, Wuhan 430030, China; 2. The Second Affiliated Hospital, Zhengzhou University, Zhengzhou 450014, China; 3. The First Affiliated Hospital, Zhengzhou University, Zhengzhou 450003, China
 Download: PDF(178 KB)   HTML
 Export: BibTeX | EndNote | Reference Manager | ProCite | RefWorks
Abstract

The mRNA and protein expression of phosphatase of regenerating liver 1 (PRL-1) and phosphatase of regenerating liver 3 (PRL-3) in transitional cell carcinoma of bladder (BTCC) and normal epithelia of bladder was investigated, and the relationship between the BTCC and pathological changes was clarified. The expression of PRL-1 and PRL-3 mRNA was detected by using reverse transcription polymerase chain reaction (RT-PCR) in 30 cases of BTCC and 10 cases of normal bladder, and the expression of PRL-1 and PRL-3 protein was checked by using immunohistochemistry in 30 cases of BTCC and 15 cases of normal bladder. The expression levels of PRL-1 and PRL-3 mRNA and protein were higher in BTCC than those in normal bladder epithelia (P<0.05). The increased expression of PRL-1 and PRL-3 mRNA and protein was detectable in deep invasion and metastasis of BTCC (P<0.05). There was no correlation between the expression of PRL-1 and PRL-3 and gender, age or recurrence of BTCC (all P>0.05). A significantly positive correlation was found between PRL-1 and PRL-3 in BTCC (P<0.05). PRL-1 and PRL-3 are expressed consistently and may contribute to the growth, differentiation, invasion and metastasis of BTCC.
Keywords transitional cell carcinoma of bladder      phosphatase of regenerating liver 1      phosphatase of regenerating liver 3      reverse transcription polymerase chain reaction      immunohistochemistry     
Corresponding Author(s): HAO Bin,Email:binhao68@hotmail.com   
Issue Date: 05 June 2009
 Cite this article:   
Bin HAO,Changwei LIU,Huixiang LI. Expression and clinical implication of PRL-1 and PRL-3 in transitional cell carcinoma of bladder[J]. Front Med Chin, 2009, 3(2): 197-203.
 URL:  
https://academic.hep.com.cn/fmd/EN/10.1007/s11684-009-0036-3
https://academic.hep.com.cn/fmd/EN/Y2009/V3/I2/197
Fig.1  Expression of PRL-1 protein in BTCC (Immunohistochemistry SP, ×200). PRL-1: phosphatase of regenerating liver 1; BTCC: transitional cell carcinoma of bladder.
variablen PRL-1 proteinP value PRL-3 proteinP’ value
+-positive rate/%+-positive rate/%
normal156940.00.030a31220.00.020a’
tumor3022873.3171356.7
WHO grade
I52340.00.608*2340.01.000*
II106460.00.121**5550.00.442**
III1514193.30.032***10566.70.347***
TNM
Tis-T193633.30.0032722.20.020
T2-T42119290.515671.4
Recurrence
yes54180.01.0002340.00.628
no2518772.0151060.0
gender
male2114766.70.374101147.60.229
female98188.97277.8
age
&lt;6085362.50.6433537.50.242
≥602217577.314863.6
Tab.1  Expression of PRL-1 and PRL-3 protein in BTCC and normal urothelia, and the relation with clinicopathological parameters
Fig.2  Expression of PRL-3 protein in BTCC (Immunohistochemistry SP, ×200). PRL-3: phosphatase of regenerating liver 3; BTCC: transitional cell carcinoma of bladder.
Fig.3  Expression of PRL-1 and PRL-3 in transitional cell carcinoma of bladder (RT-PCR). Product of PRL-1 was a 490 bp fluorescent light, PRL-3 was a 473 bp fluorescent light, and β-actin was a 330 bp fluorescent light. PRL-1: phosphatase of regenerating liver 1; PRL-3: phosphatase of regenerating liver 3.
variablenPRL-1 mRNAsP valuePRL-3 mRNAsP’ value
+-positive rate/%+–positive rate/%
normal101910.00.010a0100.00.035a’
tumor30171356.7102033.3
clinical stage
I51420.00.308*1420.01.000*
II116554.50.434**4736.41.000**
III1410471.40.111***5935.71.000***
TNM
Tis-T171614.30.0251614.30.372
T2-T42316769.691439.1
recurrence
yes330100.00.2380300.532
no 27141351.9101737.0
gender
male2011955.01.00051525.00.231
female106460.05550.0
age/yr
&lt;60118372.70.2596554.50.108
≥601991047.441521.1
Tab.2  mRNA expression of PRL-1 and PRL-3 in BTCC and normal urothelia, and the relation with clinicopathological parameters
PRL-3 proteinPRL-1 proteinnrsP valueP’ value
+–
+152170.3850.0350.180
–7613
Tab.3  The correlation and difference between PRL-1 protein and PRL-3 protein in BTCC
PRL-3 mRNAPRL-1 mRNAnrsP valueP’ value
+–
+91100.4760.0080.678
–81220
Tab.4  The correlation and difference between PRL-1 mRNA and PRL-3 mRNA in BTCC
1 Hunter T. Signaling — 2000 and beyond. Cell , 2000, 100(1): 113-127
2 Lyon M A, Ducruet A P, Wipf P, Lazo J S. Dual-specificity phosphatases as targets for antineoplastic agents. Nat Rev Drug Discov , 2002, 1(12): 961-976
doi: 10.1038/nrd963
3 Zeng Q, Si X, Horstmann H, Xu Y, Hong W, Pallen C J. Prenylation dependent association of protein-tyrosine phosphatases PRL-1, -2, and-3 with the plasma membrane and the early endosome. J Biol Chem , 2000, 275(28): 21444-21452
doi: 10.1074/jbc.M000453200
4 Diamond R H, Cressman D E, Laz T M, Abrams C S, Taub R. PRL-1, a unique nuclear protein tyrosine phosphatase, affects cell growth. Mol Cell Biol , 1994, 14(6): 3752-3762
5 Zeng Q, Dong J M, Guo K, Li J, Koh V, Pallen C J, Manser E, Hong W. PRL-3 and PRL-1 promote cell migration, invasion, and metastasis. Cancer Res , 2003, 63(11): 2716-2722
6 Wang Q, Holmes D I, Powell S M, Lu Q L, Waxman J. Analysis of stromal-epithelial interactions in prostate cancer identifies PTPCAAX2 as a potential oncogene. Cancer Lett , 2002, 175(1): 63-69
doi: 10.1016/S0304-3835(01)00703-0
7 Saha S, Bardelli A, Buckhaults P, Velculescu V E, Rago C, St Croix B, Romans K E, Choti M A, Lengauer C, Kinzler K W, Vogelstein B. A phosphatase associated with metastasis of colorectal cancer. Science , 2001, 294(5545): 1343-1346
doi: 10.1126/science.1065817
8 Miskad U A, Semba S, Kato H, Yokozaki H. Expression of PRL-3 phosphatase in human gastric carcinomas: close correlation with invasion and metastasis. Pathobiology , 2004, 71(4): 176-184
doi: 10.1159/000078671
9 Radke I, G?tte M, Kersting C, Mattsson B, Kiesel L, Wülfing P. Expression and prognostic impact of the protein tyrosine phophatases PRL-1, PRL-2 and PRL-3 in breast cancer. Brit J Cancer , 2006, 95(3): 347-354
doi: 10.1038/sj.bjc.6603261
10 Zhang Z Y, Zhou B, Xie L. Modulation of protein kinase signaling by protein phosphatases and inhibitor. Pharmacol Ther , 2002, 93(2,3): 307-317
11 Dumaual C M, Sandusky G E, Crowell P L, Randall S K. Cellular localization of PRL-1 and PRL-2 gene expression in normal adult human tissues. J Histochem Cytochem , 2006, 54(12): 1401-1412
doi: 10.1369/jhc.6A7019.2006
12 Matter W F, Estridge T, Zhang C, Belagaje R, Stancato L, Dixon J, Johnson B, Bloem L, Pickard T, Donaqhue M, Acton S, Jeyaseelan R, Kadambi V, Vlahos C J. Role of PRL-3, a human muscle-specific tyrosine phosphatase, in angiotensin-II signaling. Biochem Biophys Res Commun , 2001, 283(5): 1061-1068
doi: 10.1006/bbrc.2001.4881
13 Cates C A, Michael R L, Stayrook K R, Harvey K A, Burke Y D, Randall S K, Crowell P L, Crowell D N. Prenylation of oncogenic human PTP (CAAX) protein tyrosine phosphatases. Cancer Lett , 1996, 110(1,2): 49-55
14 Miskad U A, Semba S, Kato H, Matsukawa Y, Kodama Y, Mizuuchi E, Maeda N, Yanagihara K, Yokozaki H. High PRL-3 expression in human gastric cancer is a marker of metastasis and grades of malignancies: an in situ hybridization study. Virchows Arch . 2007, 450(3): 303-310
doi: 10.1007/s00428-006-0361-8
15 Polato F, Codegoni A, Fruscio R, Perego P, Manqioni C, Saha S, Bardelli A, Broqqini M. PRL-3 phosphatase is implicated in ovarian cancer growth. Clin Cancer Res , 2005, 11(9 Pt 1): 6835-6839
doi: 10.1158/1078-0432.CCR-04-2357
16 Wu X, Zeng H, Zhang X, Zhao Y, Sha H, Ge X, Zhang M, Gao X, Xu Q. Phosphatase of regenerating liver-3 promotes motility and metastasis of mouse melanoma cells. Am J Pathol , 2004, 164(6): 2039-2054
17 Peng L, Ning J, Meng L, Shou C. The association of the expression level of protein tyrosine phosphatase PRL-3 protein with liver metastasis and prognosis of patients with colorectal cancer. J Cancer Res Clin Oncol , 2004, 130(9): 521-526
doi: 10.1007/s00432-004-0563-x
18 Bardelli A, Saha S, Sager J A, Romans K E, Xin B, Markowitz S D, Lengauer C, Velculescu V E, Kinzler K W, Voqelstein B. PRL-3 expression in metastatic cancers. Clin Cancer Res , 2003, 9(15): 5607-5615
19 Guo K, Li J, Tang J P, Koh V, Gan B Q, Zeng Q. Catalytic domain of PRL-3 plays an essential role in tumor metastasis: formation of PRL-3 tumors inside the blood vessels. Cancer Biol Ther , 2004, 3(10): 945-951
20 Sager J, Benvenuti S, Bardelli A. PRL-3: a phosphatase for metastasis? Cancer Biol Ther , 2004, 3(10): 952-953
[1] Wenjing Wang, Shigang Ding, Hejun Zhang, Jun Li, Jun Zhan, Hongquan Zhang. G protein-coupled receptor LGR6 is an independent risk factor for colon adenocarcinoma[J]. Front. Med., 2019, 13(4): 482-491.
[2] GUO Weichun, CHEN Anmin. Expression of heat shock protein gp96 in osteosarcoma and its clinical significance[J]. Front. Med., 2008, 2(2): 200-203.
[3] XU Jun, HU Yong, WANG Jian, ZHANG Taiping, ZHOU Ji, YU Hongyu. Immunohistochemical characterization of hepatic stem cell-related cells in developing human liver[J]. Front. Med., 2007, 1(3): 264-268.
Viewed
Full text


Abstract

Cited
  Shared   
  Discussed