http://purl.uniprot.org/citations/11932257 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/11932257 | http://www.w3.org/2000/01/rdf-schema#comment | "The lysosomal cysteine protease cathepsin B is thought to play a central role in intrapancreatic trypsinogen activation and the onset of experimental pancreatitis. Recent in vitro studies have suggested that this mechanism might be of pathophysiological relevance in hereditary pancreatitis, a human inborn disorder associated with mutations in the cationic trypsinogen gene. In the present study evidence is presented that cathepsin B is abundantly present in the secretory compartment of the human exocrine pancreas, as judged by immunogold electron microscopy. Moreover, pro-cathepsin B and mature cathepsin B are both secreted together with trypsinogen and active trypsin into the pancreatic juice of patients with sporadic pancreatitis or hereditary pancreatitis. Finally, cathepsin B-catalyzed activation of recombinant human cationic trypsinogen with hereditary pancreatitis-associated mutations N29I, N29T, or R122H were characterized. In contrast to a previous report, cathepsin B-mediated activation of wild type and all three mutant trypsinogen forms was essentially identical under a wide range of experimental conditions. These observations confirm the presence of active cathepsin B in the human pancreatic secretory pathway and are consistent with the notion that cathepsin B-mediated trypsinogen activation might play a pathogenic role in human pancreatitis. On the other hand, the results clearly demonstrate that hereditary pancreatitis-associated mutations do not lead to increased or decreased trypsinogen activation by cathepsin B. Therefore, mutation-dependent alterations in cathepsin B-induced trypsinogen activation are not the cause of hereditary pancreatitis."xsd:string |
http://purl.uniprot.org/citations/11932257 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m200878200"xsd:string |
http://purl.uniprot.org/citations/11932257 | http://purl.uniprot.org/core/author | "Toth M."xsd:string |
http://purl.uniprot.org/citations/11932257 | http://purl.uniprot.org/core/author | "Sahin-Toth M."xsd:string |
http://purl.uniprot.org/citations/11932257 | http://purl.uniprot.org/core/author | "Kruger B."xsd:string |
http://purl.uniprot.org/citations/11932257 | http://purl.uniprot.org/core/author | "Halangk W."xsd:string |
http://purl.uniprot.org/citations/11932257 | http://purl.uniprot.org/core/author | "Lerch M.M."xsd:string |
http://purl.uniprot.org/citations/11932257 | http://purl.uniprot.org/core/author | "Steed P.M."xsd:string |
http://purl.uniprot.org/citations/11932257 | http://purl.uniprot.org/core/author | "Kukor Z."xsd:string |
http://purl.uniprot.org/citations/11932257 | http://purl.uniprot.org/core/author | "Mayerle J."xsd:string |
http://purl.uniprot.org/citations/11932257 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
http://purl.uniprot.org/citations/11932257 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
http://purl.uniprot.org/citations/11932257 | http://purl.uniprot.org/core/pages | "21389-21396"xsd:string |
http://purl.uniprot.org/citations/11932257 | http://purl.uniprot.org/core/title | "Presence of cathepsin B in the human pancreatic secretory pathway and its role in trypsinogen activation during hereditary pancreatitis."xsd:string |
http://purl.uniprot.org/citations/11932257 | http://purl.uniprot.org/core/volume | "277"xsd:string |
http://purl.uniprot.org/citations/11932257 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11932257 |
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