Dipeptidyl-peptidase IV (CD26)-role in the inactivation of regulatory peptides

@article{Mentlein1999DipeptidylpeptidaseI,
  title={Dipeptidyl-peptidase IV (CD26)-role in the inactivation of regulatory peptides},
  author={Rolf Mentlein},
  journal={Regulatory Peptides},
  year={1999},
  volume={85},
  pages={9-24}
}
  • R. Mentlein
  • Published 1999
  • Biology, Medicine
  • Regulatory Peptides
Dipeptidyl-peptidase IV (DPP IV/CD26) has a dual function as a regulatory protease and as a binding protein. Its role in the inactivation of bioactive peptides was recognized 20 years ago due to its unique ability to liberate Xaa-Pro or Xaa-Ala dipeptides from the N-terminus of regulatory peptides, but further examples are now emerging from in vitro and vivo experiments. Despite the minimal N-terminal truncation by DPP IV, many mammalian regulatory peptides are inactivated--either totally or… Expand
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