Dipeptidyl peptidase IV (CD 26) and aminopeptidase N (CD 13) catalyzed hydrolysis of cytokines and peptides with N-terminal cytokine sequences

FEBS Lett. 1993 Dec 20;336(1):61-4. doi: 10.1016/0014-5793(93)81609-4.

Abstract

A number of natural cytokines are characterized as having dipeptidyl peptidase (DP) IV susceptible N-terminal peptide sequences. Here we demonstrate that oligopeptides with sequences analogous to the N-terminal part of human IL-1 beta, IL-2, TNF-beta and murine IL-6 were hydrolyzed by purified DP IV and aminopeptidase N (AP-N). The rate of DP IV-catalyzed hydrolysis of these peptides was negatively correlated with their chain length. In contrast to these results, no degradation was found under our conditions for the intact recombinant cytokines, IL-1 alpha, IL-1 beta, IL-2, G-CSF and for natural IL-2, independent of whether DP IV and AP-N were used separately or in combination.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Aminopeptidases / metabolism*
  • Animals
  • CD13 Antigens
  • Catalysis
  • Cytokines / chemistry
  • Cytokines / metabolism*
  • Dipeptidyl Peptidase 4
  • Dipeptidyl-Peptidases and Tripeptidyl-Peptidases / metabolism*
  • Humans
  • Hydrolysis
  • Mice
  • Molecular Sequence Data
  • Peptides / chemistry
  • Peptides / metabolism*

Substances

  • Cytokines
  • Peptides
  • Aminopeptidases
  • CD13 Antigens
  • Dipeptidyl-Peptidases and Tripeptidyl-Peptidases
  • Dipeptidyl Peptidase 4