Peptidomic profiling of human cerebrospinal fluid identifies YPRPIHPA as a novel substrate for prolylcarboxypeptidase |
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| Authors: | Xuemei Zhao Katie Southwick Helene L. Cardasis Yi Du Michael E. Lassman Dan Xie Mohamed El‐Sherbeini Wayne M. Geissler KellyAnn D. Pryor Andreas Verras Margarita Garcia‐Calvo Dong‐Ming Shen Nathan A. Yates Shirly Pinto Ronald C. Hendrickon |
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| Affiliation: | 1. Department of Proteomics, Merck Research Laboratories, Rahway, NJ, USA;2. Department of Metabolic Disorders, Merck Research Laboratories, Rahway, NJ, USA;3. Department of Chemistry, Merck Research Laboratories, Rahway, NJ, USA;4. Department of In Vitro Sciences, Merck Research Laboratories, Rahway, NJ, USA |
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| Abstract: | 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. |
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| Keywords: | Biomedicine Cerebrospinal fluid dMS Endothelin B receptor‐like protein Prolylcarboxypeptidase |
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