Brief Communication abstract
Nature Chemical Biology 5, 23 - 25 (2008)
Published online: 16 November 2008 | doi:10.1038/nchembio.126
Peptidase substrates via global peptide profiling
Debarati M Tagore1, Whitney M Nolte1, John M Neveu2, Roberto Rangel3, Liliana Guzman-Rojas3, Renata Pasqualini3, Wadih Arap3, William S Lane2 & Alan Saghatelian1
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.
- Department of Chemistry and Chemical Biology, Harvard University, 12 Oxford Street, Cambridge, Massachusetts 02138, USA.
- Mass Spectrometry and Proteomics Resource Laboratory, FAS Center for Systems Biology, Harvard University, 52 Oxford Street, Cambridge, Massachusetts 02138, USA.
- The University of Texas M. D. Anderson Cancer Center, 1515 Holcombe Boulevard, Houston, Texas 77030, USA.
Correspondence to: Alan Saghatelian1 e-mail: saghatelian@chemistry.harvard.edu
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Peptidase substrates via global peptide profilingNature Chemical Biology Brief Communication (01 Jan 2009)
