Transcription variants of the prostate-specific PrLZ gene and their interaction with 14-3-3 proteins

• Type of Material: Article
• Authors: Ruoxiang Wang, Emory University; Hui He, Xi’an Jiaotong University; Xiaojuan Sun, Emory University; Jianchun Xu, Emory University; Fray F. Marshall, Emory University; Haiyen Zhau, Emory University; Leland W. K. Chung, Emory University; Haian Fu, Emory University; Dalin He, Xi’an Jiaotong University
• Language: English
• Date: 2009-11-20
• Publisher: Elsevier: 12 months
• Publication Version: Author Accepted Manuscript (After Peer Review)
• Copyright Statement: © 2009 Elsevier Inc. All rights reserved.
• License: Creative Commons Attribution-NonCommercial-NoDerivs 4.0 International
• Final Published Version (URL): http://dx.doi.org/10.1016/j.bbrc.2009.08.165
• Title of Journal or Parent Work: Biochemical and Biophysical Research Communications
• ISSN: 0006-291X
• Volume: 389
• Issue: 3
• Start Page: 455
• End Page: 460
• Grant/Funding Information: This work is supported by esearch grants R21CA112330, PC040578, CA132388 (RXW), and CA98912-02 (LWKC).
• Keywords: Mammalian two-hybrid assay; THERAPY; Life Sciences & Biomedicine; Biophysics; SELECTION; EXPRESSION; TPD52L1; MODELS; BINDING; DISEASE; 14-3-3; Alternative splicing; Protein interaction; PrLZ gene; CANCER; Science & Technology; Prostate-specific gene; FAMILY; BREAST; Biochemistry & Molecular Biology
• Research Categories: Health Sciences, Oncology; Health Sciences, Medicine and Surgery

Abstract

We have reported isolation and characterization of the prostate-specific and androgen-regulated PrLZ gene abnormally expressed in prostate cancer. PrLZ is a potential biomarker for prostate cancer and a candidate oncogene promoting cell proliferation and survival in prostate cancer cells. A full delineation of the PrLZ gene and its gene products may provide clues to the mechanisms regulating its expression and function. In this report, we identified three additional exons in the PrLZ gene and recognized five transcript variants from alternative splicing that could be detected by RT-PCR and Western blotting. Structural comparison demonstrated that the PrLZ proteins are highly conserved among species. PrLZ contains multiple potential sites for interaction with other proteins. We used mammalian two-hybrid assays to demonstrate that PrLZ isoforms interact with 14-3-3 proteins, and multiple sites in the PrLZ may be involved in the interaction. Alternative splicing may contribute to abnormally enhanced PrLZ levels in prostate cancer, and interaction with 14-3-3 proteins may be a mechanism by which PrLZ promotes cell proliferation and survival during prostate cancer development and progression. This information is a valuable addition to the investigation of the oncogenic properties of the PrLZ gene.