Journal
NATURE CHEMICAL BIOLOGY
Volume 5, Issue 1, Pages 23-25Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nchembio.126
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Funding
- US National Institutes of Health [1DP2OD002374]
- Burroughs Wellcome Fund Career Award in the Biomedical Sciences
- OFFICE OF THE DIRECTOR, NATIONAL INSTITUTES OF HEALTH [DP2OD002374] Funding Source: NIH RePORTER
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Peptide metabolism is a complex process that involves many proteins working in concert. Mass spectrometry-based global peptide profiling of mice lacking dipeptidyl peptidase 4 (DPP4) identified endogenous DPP4 substrates and revealed an unrecognized pathway during proline peptide catabolism that interlinks aminopeptidase and DPP4 activities. Together, these studies elucidate specific aspects of DPP4-regulated metabolism and, more generally, highlight the utility of global peptide profiling for studying peptide metabolism in vivo.
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