| http://purl.uniprot.org/citations/8215389 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/8215389 | http://www.w3.org/2000/01/rdf-schema#comment | "The biosynthesis and processing of a lysosomal cysteine proteinase, cathepsin C (dipeptidylaminopeptidase I), was investigated by pulse-chase experiments in cultured rat macrophages. Cathepsin C is first synthesized as procathepsin C with a molecular mass of 55 kDa. Procathepsin C is then cleaved and modified within 1 h into mature cathepsin C with two chains of 25 and 7.8 kDa. A combination of pulse-chase experiments and the subcellular fractionation analysis showed that procathepsin C and cathepsin C are located in low-buoyant-density organelles and lysosomes, respectively. The reactivity of endoglycosidase H and N-glycanase and analysis of phosphorylation indicated that both precursor and mature cathepsin C are phosphorylated and N-glycosylated to give a high-mannose-type. The addition of 300-kDa mannose 6-phosphate receptor antiserum to the chase medium caused extensive release of procathepsin C into the medium, whereas the addition of control serum did not. The membrane association of procathepsin C was tested by successive extraction of cells pulse labeled for 75 min with hypotonic buffer, alkaline solution, and Triton X-100. Procathepsin C was totally extracted by hypotonic solution, whereas procathepsin D was a membrane-associated form requiring Triton X-100 for its extraction. Gel-filtration chromatography analysis of the pulse-labeled products revealed that the precursor product exists as an oligomeric form. It is suggested that the oligomerization of cathepsin C occurs before its entry into lysosomes."xsd:string |
| http://purl.uniprot.org/citations/8215389 | http://purl.org/dc/terms/identifier | "doi:10.1006/abbi.1993.1486"xsd:string |
| http://purl.uniprot.org/citations/8215389 | http://purl.uniprot.org/core/author | "Ueno T."xsd:string |
| http://purl.uniprot.org/citations/8215389 | http://purl.uniprot.org/core/author | "Kominami E."xsd:string |
| http://purl.uniprot.org/citations/8215389 | http://purl.uniprot.org/core/author | "Ishidoh K."xsd:string |
| http://purl.uniprot.org/citations/8215389 | http://purl.uniprot.org/core/author | "Muno D."xsd:string |
| http://purl.uniprot.org/citations/8215389 | http://purl.uniprot.org/core/date | "1993"xsd:gYear |
| http://purl.uniprot.org/citations/8215389 | http://purl.uniprot.org/core/name | "Arch Biochem Biophys"xsd:string |
| http://purl.uniprot.org/citations/8215389 | http://purl.uniprot.org/core/pages | "103-110"xsd:string |
| http://purl.uniprot.org/citations/8215389 | http://purl.uniprot.org/core/title | "Processing and transport of the precursor of cathepsin C during its transfer into lysosomes."xsd:string |
| http://purl.uniprot.org/citations/8215389 | http://purl.uniprot.org/core/volume | "306"xsd:string |
| http://purl.uniprot.org/citations/8215389 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/8215389 |
| http://purl.uniprot.org/citations/8215389 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/8215389 |
| http://purl.uniprot.org/uniprot/#_A0A8I5ZZG1-mappedCitation-8215389 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/8215389 |
| http://purl.uniprot.org/uniprot/#_A0A8I6A0Q1-mappedCitation-8215389 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/8215389 |
| http://purl.uniprot.org/uniprot/#_P80067-mappedCitation-8215389 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/8215389 |
| http://purl.uniprot.org/uniprot/P80067 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/8215389 |
| http://purl.uniprot.org/uniprot/A0A8I5ZZG1 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/8215389 |
| http://purl.uniprot.org/uniprot/A0A8I6A0Q1 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/8215389 |