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http://purl.uniprot.org/citations/33471263http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/33471263http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/33471263http://www.w3.org/2000/01/rdf-schema#comment"Serine hydrolases play crucial roles in many physiological and pathophysiological processes and a panel of these enzymes are targets of approved drugs. Despite this, most of the human serine hydrolases remain poorly characterized with respect to their biological functions and substrates and only a limited number of in vivo active inhibitors have been so far identified. Acylpeptide hydrolase (APEH) is a member of the prolyl-oligopeptidase class, with a unique substrate specificity, that has been suggested to have a potential oncogenic role. In this study, a set of peptides was rationally designed from the lead compound SsCEI 4 and in vitro screened for APEH inhibition. Out of these molecules, a dodecapeptide named Ala 3 showed the best inhibitory effects and it was chosen as a candidate for investigating the anti-cancer effects induced by inhibition of APEH in SAOS-2 cell lines. The results clearly demonstrated that Ala 3 markedly reduced cell viability via deregulation of the APEH-proteasome system. Furthermore, flow cytometric analysis revealed that Ala 3 anti-proliferative effects were closely related to the activation of a caspase-dependent apoptotic pathway. Our findings provide further evidence that APEH can play a crucial role in the pathogenesis of cancer, shedding new light on the great potential of this enzyme as an attractive target for the diagnosis and the quest for selective cancer therapies."xsd:string
http://purl.uniprot.org/citations/33471263http://purl.org/dc/terms/identifier"doi:10.1007/s11033-020-06129-4"xsd:string
http://purl.uniprot.org/citations/33471263http://purl.org/dc/terms/identifier"doi:10.1007/s11033-020-06129-4"xsd:string
http://purl.uniprot.org/citations/33471263http://purl.uniprot.org/core/author"Rossi M."xsd:string
http://purl.uniprot.org/citations/33471263http://purl.uniprot.org/core/author"Palmieri G."xsd:string
http://purl.uniprot.org/citations/33471263http://purl.uniprot.org/core/author"Sandomenico A."xsd:string
http://purl.uniprot.org/citations/33471263http://purl.uniprot.org/core/author"Cocca E."xsd:string
http://purl.uniprot.org/citations/33471263http://purl.uniprot.org/core/author"Calvanese L."xsd:string
http://purl.uniprot.org/citations/33471263http://purl.uniprot.org/core/author"Gogliettino M."xsd:string
http://purl.uniprot.org/citations/33471263http://purl.uniprot.org/core/author"Iaccarino E."xsd:string
http://purl.uniprot.org/citations/33471263http://purl.uniprot.org/core/author"Gratino L."xsd:string
http://purl.uniprot.org/citations/33471263http://purl.uniprot.org/core/date"2021"xsd:gYear
http://purl.uniprot.org/citations/33471263http://purl.uniprot.org/core/name"Mol Biol Rep"xsd:string
http://purl.uniprot.org/citations/33471263http://purl.uniprot.org/core/pages"1505-1519"xsd:string
http://purl.uniprot.org/citations/33471263http://purl.uniprot.org/core/title"Selective inhibition of acylpeptide hydrolase in SAOS-2 osteosarcoma cells: is this enzyme a viable anticancer target?"xsd:string
http://purl.uniprot.org/citations/33471263http://purl.uniprot.org/core/volume"48"xsd:string
http://purl.uniprot.org/citations/33471263http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/33471263
http://purl.uniprot.org/citations/33471263http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/33471263
http://purl.uniprot.org/citations/33471263http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/33471263
http://purl.uniprot.org/citations/33471263http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/33471263
http://purl.uniprot.org/enzyme/3.4.19.1http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/33471263
http://purl.uniprot.org/uniprot/#_P13798-mappedCitation-33471263http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/33471263
http://purl.uniprot.org/uniprot/P13798http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/33471263