Human prostatic acid phosphatase: Structure, function and regulation

Sakthivel Muniyan, Nagendra K. Chaturvedi, Jennifer G. Dwyer, Chad A LaGrange, William G Chaney, Ming-Fong Lin

Research output: Contribution to journalReview articlepeer-review

63 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)10438-10464
Number of pages27
JournalInternational journal of molecular sciences
Issue number5
StatePublished - May 2013


  • Epigenetic regulation
  • ErbB-2
  • Immunotherapy
  • Prostate cancer
  • Prostatic acid phosphatase
  • Protein tyrosine phosphatase
  • Tumor suppressor

ASJC Scopus subject areas

  • Catalysis
  • Molecular Biology
  • Spectroscopy
  • Computer Science Applications
  • Physical and Theoretical Chemistry
  • Organic Chemistry
  • Inorganic Chemistry


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