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Peptidomic profiling of human cerebrospinal fluid identifies YPRPIHPA as a novel substrate for prolylcarboxypeptidase
Author(s) -
Zhao Xuemei,
Southwick Katie,
Cardasis Helene L.,
Du Yi,
Lassman Michael E.,
Xie Dan,
ElSherbeini Mohamed,
Geissler Wayne M.,
Pryor KellyAnn D.,
Verras Andreas,
GarciaCalvo Margarita,
Shen DongMing,
Yates Nathan A.,
Pinto Shirly,
Hendrickon Ronald C.
Publication year - 2010
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.201000145
Subject(s) - serine protease , cerebrospinal fluid , proteases , peptide , serine , biology , protease , extracellular , in vitro , amino acid , biochemistry , microbiology and biotechnology , chemistry , enzyme , neuroscience
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.