Regulation of S100P expression by androgen

Prostate. 1996 Dec;29(6):350-5. doi: 10.1002/(SICI)1097-0045(199612)29:6<350::AID-PROS2>3.0.CO;2-C.


Background: The growth and function the normal prostate is dependent on the presence of androgen. As prostate tumors progress there is a loss of androgen-dependent cell growth. The identification of the genes that are regulated by androgens may be of pathological and clinical significance.

Methods: In this study the differential display method was used to identify genes regulated by androgen in an androgen-responsive prostate cancer cell line, LNCaP-FGC.

Results: A gene whose expression is down-regulated in LNCaP-FGC cells after 30 hr of androgen deprivation has been identified. This gene is a previously identified member of the S100 gene family of calcium-binding proteins, namely S100P. Here we show that S100P expression is regulated by the synthetic androgen R1881, but not by serum growth factors. It is dysregulated in the androgen-independent prostate cancer cell lines LNCaP-R, DU145, and PC3.

Conclusions: The data indicate that S100P may play a role in the etiology of prostate cancer.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Androgens / pharmacology*
  • Base Sequence
  • Blotting, Northern
  • Calcium-Binding Proteins / genetics*
  • Calcium-Binding Proteins / physiology
  • DNA, Complementary / analysis
  • DNA, Complementary / chemistry
  • DNA, Complementary / genetics
  • DNA, Neoplasm / analysis
  • DNA, Neoplasm / chemistry
  • DNA, Neoplasm / genetics
  • Gene Expression Regulation, Neoplastic / drug effects
  • Gene Expression Regulation, Neoplastic / physiology
  • Humans
  • Male
  • Molecular Sequence Data
  • Neoplasm Proteins*
  • Polymerase Chain Reaction
  • Prostatic Neoplasms / etiology
  • Prostatic Neoplasms / pathology*
  • Prostatic Neoplasms / physiopathology
  • Tumor Cells, Cultured


  • Androgens
  • Calcium-Binding Proteins
  • DNA, Complementary
  • DNA, Neoplasm
  • Neoplasm Proteins
  • S100P protein, human