| http://purl.uniprot.org/citations/12185078 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12185078 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12185078 | http://www.w3.org/2000/01/rdf-schema#comment | "The prophenoloxidase (proPO) activation pathway, like the vertebrate complement system, consists of a protease cascade and functions as a non-self-recognition system in these animals. Determining the molecular mechanism by which pattern recognition molecules differentiate non-self from self and transduce signals that stimulate defense responses is a key for understanding the ways in which innate immune systems are regulated. However, the proPO system is poorly defined at the molecular level. The proPO-activating system of the insect Holotrichia diomphalia comprises several components, some of which have been cloned and characterized, such as the novel 27-kDa proPO-activating factor-III (PPAF-III) from the plasma of H. diomphalia larvae and two prophenoloxidases. The PPAF-III gene encodes an easter-type serine protease zymogen consisting of 351 amino acid residues with a mass of 40 kDa. The purified 27-kDa PPAF-III specifically cleaved a 55-kDa proPPAF-II to generate a 45-kDa PPAF-II with or without Ca2+ present. Furthermore, two Holotrichia prophenoloxidases (proPO-I and -II) have been characterized, and their structural changes during activation were examined by in vitro reconstitution experiments. When the proPOs were incubated with PPAF-I, the 79-kDa proPOs were converted to 76-kDa proPOs, which did not exhibit any phenoloxidase (PO) activity. However, when the proPOs were incubated simultaneously with PPAF-I, proPPAF-II, and PPAF-III in the presence of Ca2+, a 60-kDa protein (PO-1) with PO activity was detected in addition to the 76-kDa proPO-II protein. These results indicate that the conversion of Holotrichia proPOs to enzymatically active phenoloxidase is accomplished by PPAF-I, PAF-II, and PPAF-III through a two-step limited proteolysis in the presence of Ca2+."xsd:string |
| http://purl.uniprot.org/citations/12185078 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m205508200"xsd:string |
| http://purl.uniprot.org/citations/12185078 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m205508200"xsd:string |
| http://purl.uniprot.org/citations/12185078 | http://purl.uniprot.org/core/author | "Lee S.Y."xsd:string |
| http://purl.uniprot.org/citations/12185078 | http://purl.uniprot.org/core/author | "Lee S.Y."xsd:string |
| http://purl.uniprot.org/citations/12185078 | http://purl.uniprot.org/core/author | "Lee M.H."xsd:string |
| http://purl.uniprot.org/citations/12185078 | http://purl.uniprot.org/core/author | "Lee M.H."xsd:string |
| http://purl.uniprot.org/citations/12185078 | http://purl.uniprot.org/core/author | "Park J.W."xsd:string |
| http://purl.uniprot.org/citations/12185078 | http://purl.uniprot.org/core/author | "Park J.W."xsd:string |
| http://purl.uniprot.org/citations/12185078 | http://purl.uniprot.org/core/author | "Lee B.L."xsd:string |
| http://purl.uniprot.org/citations/12185078 | http://purl.uniprot.org/core/author | "Lee B.L."xsd:string |
| http://purl.uniprot.org/citations/12185078 | http://purl.uniprot.org/core/author | "Kim M.S."xsd:string |
| http://purl.uniprot.org/citations/12185078 | http://purl.uniprot.org/core/author | "Kim M.S."xsd:string |
| http://purl.uniprot.org/citations/12185078 | http://purl.uniprot.org/core/author | "Soderhall K."xsd:string |
| http://purl.uniprot.org/citations/12185078 | http://purl.uniprot.org/core/author | "Soderhall K."xsd:string |
| http://purl.uniprot.org/citations/12185078 | http://purl.uniprot.org/core/author | "Baek M.J."xsd:string |
| http://purl.uniprot.org/citations/12185078 | http://purl.uniprot.org/core/author | "Baek M.J."xsd:string |
| http://purl.uniprot.org/citations/12185078 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/12185078 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/12185078 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/12185078 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/12185078 | http://purl.uniprot.org/core/pages | "39999-40004"xsd:string |
| http://purl.uniprot.org/citations/12185078 | http://purl.uniprot.org/core/pages | "39999-40004"xsd:string |