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Molecular and Cellular Biology, May 2002, p. 3345-3357, Vol. 22, No. 10
0270-7306/02/$04.00+0     DOI: 10.1128/MCB.22.10.3345-3357.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

mRTVP-1, a Novel p53 Target Gene with Proapoptotic Activities

Chengzhen Ren,1 Likun Li,1 Alexei A. Goltsov,1 Terry L. Timme,1 Salahaldin A. Tahir,1 Jianxiang Wang,1 Laura Garza,1 A. Craig Chinault,2 and Timothy C. Thompson1,3,4*

Scott Department of Urology,1 Department of Molecular and Human Genetics,2 Department of Molecular and Cellular Biology,3 Department of Radiology, Baylor College of Medicine, Houston, Texas 770304

Received 16 July 2001/ Returned for modification 5 September 2001/ Accepted 9 February 2002

We identified a novel mouse gene, mRTVP-1, as a p53 target gene using differential display PCR and extensive promoter analysis. The mRTVP-1 protein has 255 amino acids and differs from the human RTVP-1 (hRTVP-1) protein by two short in-frame deletions of two and nine amino acids. RTVP-1 mRNA was induced in multiple cancer cell lines by adenovirus-mediated delivery of p53 and by gamma irradiation or doxorubicin both in the presence and in the absence of endogenous p53. Analysis of RTVP-1 expression in nontransformed and transformed cells further supported p53-independent gene regulation. Using luciferase reporter and electrophoretic mobility shift assays we identified a p53 binding site within intron 1 of the mRTVP-1 gene. Overexpression of mRTVP-1 or hRTVP-1 induced apoptosis in multiple cancer cell lines including prostate cancer cell lines 148-1PA, 178-2BMA, PC-3, TSU-Pr1, and LNCaP, a human lung cancer cell line, H1299, and two isogenic human colon cancer cell lines, HCT116 p53+/+ and HCT116 p53-/-, as demonstrated by annexin V positivity, phase-contrast microscopy, and in selected cases 4',6'-diamidino-2-phenylindole staining and DNA fragmentation. Deletion of the signal peptide from the N terminus of RTVP-1 reduced its apoptotic activities, suggesting that a secreted and soluble form of RTVP-1 may mediate, in part, its proapoptotic activities.

* Corresponding author. Mailing address: Scott Department of Urology, Baylor College of Medicine, 6560 Fannin, Suite 2100, Houston, TX 77030. Phone: (713) 799-8718. Fax: (713) 794-7983. E-mail: timothyt{at}www.urol.bcm.tmc.edu.

Molecular and Cellular Biology, May 2002, p. 3345-3357, Vol. 22, No. 10
0022-538X/02/$04.00+0     DOI: 10.1128/MCB.22.10.3345-3357.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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