The RFA regulatory sequence-binding protein in the promoter of prostate-specific antigen gene |
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Authors: | Weiwen?Chen Email author" target="_blank">Jianye?ZhangEmail author Charles?Y?F?Young Lianying?Zhang Liucun?Chen Jian?Zhao |
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Institution: | 1. Institute of Biochemistry and Molecular Biology, School of Medicine, Shandong University, Jinan 250012, China 2. Department of Urology Research of Mayo Clinic/Foundation, MN 55905,USA 3. Department of Thoracic Surgery, Qilu Hospital of Shandong University, Jinan 250012, China |
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Abstract: | To assure what sequence associated with the androgen regulation, a 15 bp region at the upstream of the ARE of prostate-specific
antigen (PSA) promoter, termed RFA, was found indispensable for androgen receptor (AR)-mediated transactivation of PSA promoter.
In transfection and CAT assays, some nucleotides substitution in RFA could significantly decrease the androgen inducibility
for PSA promoter. The in vitro DNA binding assay demonstrated that RFA bound specifically with some non-receptor protein factors in prostate cell nucleus,
but the mutant type of RFA lost this ability, so RFA might be a novel accessory cis-element. The RFA-binding proteins were
isolated and purified by affinity chromatography using RFA probes. SDS-PAGE and preliminary protein identification showed
these proteins possessed sequence high homology with multifunctional protein heterogeneous nuclear ribonucleoprotein A1, A2
(hnRNP A1, A2). RFA-binding proteins possibly cooperate with AR-mediated transactivation for PSA promoter as coactivator.
The study results will facilitate further understanding the mechanism and tissue specificity of PSA promoter. |
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Keywords: | prostate-specific antigen promoter heterogeneous nuclear ribonucleoprotein A1 A2 |
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