Structural and functional analysis of human prostatic acid phosphatase

Expert Rev Anticancer Ther. 2010 Jul;10(7):1055-68. doi: 10.1586/era.10.46.

Abstract

Prostatic acid phosphatase (PAP) is the most abundant phosphatase in human prostate tissue/secretions. It is a clinically important protein for its relevance as a biomarker of prostate carcinoma. Furthermore, it has a potential role in fertilization. We describe here most of the features of PAP including gene regulation, gene/protein structure, functions, its role in tumor progression and evolutionary features. PAP has phosphatase activity and is an extensively studied biomarker of prostate cancer. The major action of PAP is to dephosphorylate macromolecules with the help of catalytic residues (His(12) and Asp(258)) that are located in the cleft between two domains. This article will be of great interest to all those scientists who are working in the area of prostate pathophysiology.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Acid Phosphatase
  • Adenocarcinoma / enzymology
  • Amino Acid Sequence
  • Androgens / physiology
  • Animals
  • Biomarkers, Tumor
  • Catalytic Domain
  • Enzyme Induction
  • Female
  • Fertilization
  • Humans
  • Male
  • Mammals / metabolism
  • Models, Molecular
  • Molecular Sequence Data
  • Placenta / enzymology
  • Pregnancy
  • Prostate / enzymology*
  • Prostatic Neoplasms / enzymology
  • Protein Conformation
  • Protein Structure, Tertiary
  • Protein Tyrosine Phosphatases / chemistry
  • Protein Tyrosine Phosphatases / physiology*
  • Semen / enzymology
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Structure-Activity Relationship

Substances

  • Androgens
  • Biomarkers, Tumor
  • Acid Phosphatase
  • prostatic acid phosphatase
  • Protein Tyrosine Phosphatases