Peptidomic profiling of human cerebrospinal fluid identifies YPRPIHPA as a novel substrate for prolylcarboxypeptidase
Prolylcarboxypeptidase (PRCP) is a serine protease that catalyzes the cleavage of C-terminal amino acids linked to proline in peptides. It is ubiquitously expressed and is involved in regulating blood pressure, proliferation, inflammation, angiogenesis, and weight maintenance. To identify the candidate proximal target engagement markers for PRCP inhibition in the central nervous system, we profiled the peptidome of human cerebrospinal fluid to look for PRCP substrates using a MS-based in vitro substrate profiling assay. These experiments identified a single peptide, with the sequence YPRPIHPA, as a novel substrate for PRCP in human cerebrospinal fluid. The peptide YPRPIHPA is from the extracellular portion of human endothelin B receptor-like protein 2. © 2010 Wiley-VCH Verlag GmbH & Co. KGaA.
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Zhao, Xuemei; Southwick, Katie; Cardasis, Helene L.; Du, Yi; Lassman, Michael E.; Xie, Dan; El-Sherbeini, Mohamed; Geissler, Wayne M.; Pryor, Kelly Ann D.; Verras, Andreas; Garcia-Calvo, Margarita; Shen, Dong Ming; Yates, Nathan A.; Pinto, Shirly; and Hendrickon, Ronald C., "Peptidomic profiling of human cerebrospinal fluid identifies YPRPIHPA as a novel substrate for prolylcarboxypeptidase" (2010). Kean Publications. 2336.