Document Type
Article
Journal Title
International Journal of Molecular Sciences
Publication Date
5-21-2013
Volume
14
Abstract
Human prostatic acid phosphatase (PAcP) is a 100 kDa glycoprotein composed of two subunits. Recent advances demonstrate that cellular PAcP (cPAcP) functions as a protein tyrosine phosphatase by dephosphorylating ErbB-2/Neu/HER-2 at the phosphotyrosine residues in prostate cancer (PCa) cells, which results in reduced tumorigenicity. Further, the interaction of cPAcP and ErbB-2 regulates androgen sensitivity of PCa cells. Knockdown of cPAcP expression allows androgen-sensitive PCa cells to develop the castration-resistant phenotype, where cells proliferate under an androgen-reduced condition. Thus, cPAcP has a significant influence on PCa cell growth. Interestingly, promoter analysis suggests that PAcP expression can be regulated by NF-κB, via a novel binding sequence in an androgen-independent manner. Further understanding of PAcP function and regulation of expression will have a significant impact on understanding PCa progression and therapy.
ISSN
1422-0067
DOI Link
Creative Commons License
This work is licensed under a Creative Commons Attribution 3.0 License.
Recommended Citation
Muniyan, Sakthivel; Chaturvedi, Nagendra K.; Dwyer, Jennifer G.; LaGrange, Chad A.; Chaney, William G.; and Lin, Ming-Fong, "Human prostatic Acid phosphatase: structure, function and regulation." (2013). Journal Articles: Biochemistry & Molecular Biology. 46.
https://digitalcommons.unmc.edu/com_bio_articles/46