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http://purl.uniprot.org/citations/20655338http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20655338http://www.w3.org/2000/01/rdf-schema#comment"Carboxypeptidase E (CPE) is an exopeptidase that removes C-terminal basic amino acids from a variety of bioactive peptides. In addition to this role, data obtained in recent years has supported a potential function for CPE as a sorting receptor, helping direct peptides destined for regulated secretion from the trans-Golgi to granules in preparation for release. This possible sorting function was assessed using mouse AtT-20 cells, a well-established corticotroph cell line that synthesizes and releases POMC/ACTH in regulated fashion. Cells that were treated with siRNA to Cpe effectively suppressed CPE expression. ACTH was released in a regulated fashion from CPE-depleted cells in response to two secretagogues, 8-bromo-cyclic AMP and corticotrophin-releasing hormone. POMC/ACTH content of CPE-depleted cells was higher than that of control cells, but both released a similar percentage of ACTH content in response to secretagogue addition. Cells depleted of CPE generally secreted more high-molecular weight forms of POMC/ACTH under basal conditions than control cells; however, the CPE-depleted cells responded to a secretagogue by releasing newly synthesized ACTH 1-39 in a manner similar to controls. These results, whereby RNAi was used to acutely suppress CPE, do not support a role for this protein as necessary for or central to sorting of POMC/ACTH to the regulated secretory pathway in AtT-20 cells."xsd:string
http://purl.uniprot.org/citations/20655338http://purl.org/dc/terms/identifier"doi:10.1016/j.regpep.2010.07.162"xsd:string
http://purl.uniprot.org/citations/20655338http://purl.uniprot.org/core/author"Behrend E.N."xsd:string
http://purl.uniprot.org/citations/20655338http://purl.uniprot.org/core/author"Kemppainen R.J."xsd:string
http://purl.uniprot.org/citations/20655338http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20655338http://purl.uniprot.org/core/name"Regul Pept"xsd:string
http://purl.uniprot.org/citations/20655338http://purl.uniprot.org/core/pages"174-179"xsd:string
http://purl.uniprot.org/citations/20655338http://purl.uniprot.org/core/title"Acute inhibition of carboxypeptidase E expression in AtT-20 cells does not affect regulated secretion of ACTH."xsd:string
http://purl.uniprot.org/citations/20655338http://purl.uniprot.org/core/volume"165"xsd:string
http://purl.uniprot.org/citations/20655338http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20655338
http://purl.uniprot.org/citations/20655338http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/20655338
http://purl.uniprot.org/uniprot/#_Q00493-mappedCitation-20655338http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20655338
http://purl.uniprot.org/uniprot/#_Q543R4-mappedCitation-20655338http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20655338
http://purl.uniprot.org/uniprot/Q00493http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/20655338
http://purl.uniprot.org/uniprot/Q543R4http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/20655338