Human Prostatic Acid Phosphatase: Structure, Function and Regulation

International Journal of Molecular Sciences

Sakthivel Muniyan³  Nagendra K. Chaturvedi³  Jennifer G. Dwyer²  Chad A. LaGrange¹  William G. Chaney³ 

[1] Department of Surgery/Urology, College of Medicine, University of Nebraska Medical Center, Omaha, NE 68198, USA; E-Mail:;College of Medicine, University of Nebraska Medical Center, Omaha, NE 68198, USA; E-Mail:;Department of Biochemistry and Molecular Biology, College of Medicine, University of Nebraska Medical Center, Omaha, NE 68198, USA; E-Mails:

关键词: prostate cancer;    prostatic acid phosphatase;    protein tyrosine phosphatase;    tumor suppressor;    ErbB-2;    epigenetic regulation;    immunotherapy;   

DOI  :  10.3390/ijms140510438

来源: mdpi

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2013 by the authors; licensee MDPI, Basel, Switzerland