Peptidase substrates via global peptide profiling

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Abstract

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. © 2009 Nature America, Inc. All rights reserved.

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Tagore, D. M., Nolte, W. M., Neveu, J. M., Rangel, R., Guzman-Rojas, L., Pasqualini, R., … Saghatelian, A. (2009). Peptidase substrates via global peptide profiling. Nature Chemical Biology, 5(1), 23–25. https://doi.org/10.1038/nchembio.126

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