Peptidomics of the Prolyl Peptidases

Journal Title: The AAPS Journal - Year 2010, Vol 12, Issue 4

Abstract

The prolyl peptidases are a family of enzymes characterized by a biochemical preference for cleaving proline-containing peptides. The members of this enzyme family include prolyl endopeptidase, prolyl endopeptidase-like, dipeptidyl peptidase 4 (DPP4), DPP7, DPP8, DPP9, and fibroblast activation protein. DPP4 is the best studied member of the family, due to its role in physiological glucose tolerance, exerted through the regulation of the insulinotropic peptide glucagon-like peptide-1. While other members of the prolyl peptidase family have also been implicated in various (patho)physiological processes, the underlying peptides and pathways regulated by these enzymes are less clear. The identification of endogenous substrates of the prolyl peptidases is an important step in elucidating the molecular mechanisms of these enzymes. Here, we highlight the utility of liquid chromatography–mass spectrometry-based peptidomics to enable the discovery of endogenous prolyl peptidase substrates directly from tissues, and demonstrate the utility of this information in understanding the biochemical and physiological functions of the prolyl peptidases.

Authors and Affiliations

Anna Mari Lone, Whitney M. Nolte, Arthur D. Tinoco, Alan Saghatelian

Keywords

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  • EP ID EP681406
  • DOI  10.1208/s12248-010-9208-y
  • Views 68
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How To Cite

Anna Mari Lone, Whitney M. Nolte, Arthur D. Tinoco, Alan Saghatelian (2010). Peptidomics of the Prolyl Peptidases. The AAPS Journal, 12(4), -. https://europub.co.uk/articles/-A-681406