The cleavage site specificity of human prostate specific antigen for insulin-like growth factor binding protein-3

FEBS Lett. 1999 Mar 19;447(1):87-90. doi: 10.1016/s0014-5793(99)00275-6.

Abstract

The cleavage site of human insulin-like growth factor binding protein-3 by urinary prostate specific antigen was examined. Human insulin-like growth factor binding protein-3 was incubated with urinary prostate specific antigen at 37 degrees C and its proteolyzed fragments were separated by a reversed phase HPLC followed by N-terminal amino acid sequence analysis, demonstrating that the cleavage mainly occurred at Tyr-159. The synthetic peptide including Tyr-159 was also cleaved at the same site, although its reaction rate was relatively low. These results indicate that human insulin-like growth factor binding protein-3 is specifically cleaved at Tyr-159 by prostate specific antigen. Human insulin-like growth factor binding protein-3 was previously reported to be cleaved at five sites including Arg-97, Arg-132, Tyr-159, Phe-173 and Arg-179 by another group, however, prostate specific antigen preparation is possibly contaminated by trypsin-like protease. In contrast, our purified urinary prostate specific antigen had only a chymotrypsin-like activity, demonstrating that prostate specific antigen has the high substrate specificity for human insulin-like growth factor binding protein-3.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Chymotrypsin / metabolism*
  • Humans
  • Insulin-Like Growth Factor Binding Protein 3 / metabolism*
  • Male
  • Molecular Sequence Data
  • Prostate-Specific Antigen / isolation & purification*
  • Prostate-Specific Antigen / metabolism*
  • Prostate-Specific Antigen / urine
  • Semen / enzymology
  • Substrate Specificity

Substances

  • Insulin-Like Growth Factor Binding Protein 3
  • Chymotrypsin
  • Prostate-Specific Antigen