Novel Small Molecule-Derived, Highly Selective Substrates for Fibroblast Activation Protein (FAP).

ABSTRACT: Fibroblast activation protein (FAP) is a proline-selective serine protease. It is hardly expressed in healthy adult tissue but upregulated in tissue remodeling sites associated with several diseases including epithelial cancer types, atherosclerosis, arthritis and fibrosis. Ongoing research aims at clinical implementation of FAP as a biomarker for these diseases. Several immunochemical methods that quantify FAP expression have been reported. An alternative/complementary approach focuses on quantification of FAP's enzymatic activity. Developing an activity-based assay for FAP has nonetheless proven challenging because of selectivity issues with respect to prolyl oligopeptidase (PREP). Here, we present substrate-type FAP probes that are structurally derived from a FAP-inhibitor (UAMC1110) th

SUBMITTER: De Decker A 

PROVIDER: S-EPMC6691567 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature