International Journal of Molecular Sciences | |
Human Prostatic Acid Phosphatase: Structure, Function and Regulation | |
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
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