@prefix rdf: . @prefix ns1: . rdf:type ns1:RelevantPaper , ns1:ReferencePaper , ns1:CitationPaper . @prefix rdfs: . rdfs:seeAlso , , , . @prefix bibo: . bibo:cites , , , , , , , , , , , , , , , , , , , , , , , , ; ns1:cocitationWith , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , ; ns1:hasRelevantBibliographicResourceOf _:b308276504 , _:b308276505 , _:b308276506 , _:b308276507 , _:b308276508 , _:b308276509 , _:b308276510 , _:b308276511 , _:b308276496 , _:b308276497 , _:b308276498 , _:b308276499 , _:b308276500 , _:b308276501 , _:b308276502 , _:b308276503 , _:b308276488 , _:b308276489 , _:b308276490 , _:b308276491 , _:b308276492 , _:b308276493 , _:b308276494 , _:b308276495 , _:b308276480 , _:b308276481 , _:b308276482 , _:b308276483 , _:b308276484 , _:b308276485 , _:b308276486 , _:b308276487 , _:b308276536 , _:b308276537 , _:b308276538 , _:b308276539 , _:b308276540 , _:b308276541 , _:b308276542 , _:b308276528 , _:b308276529 , _:b308276530 , _:b308276531 , _:b308276532 , _:b308276533 , _:b308276534 , _:b308276535 , _:b308276520 , _:b308276521 , _:b308276522 , _:b308276523 , _:b308276524 , _:b308276525 , _:b308276526 , _:b308276527 , _:b308276512 , _:b308276513 , _:b308276514 , _:b308276515 , _:b308276516 , _:b308276517 , _:b308276518 , _:b308276519 , _:b308276440 , _:b308276441 , _:b308276442 , _:b308276443 , _:b308276444 , _:b308276445 , _:b308276446 , _:b308276447 , _:b308276432 , _:b308276433 , _:b308276434 , _:b308276435 , _:b308276436 , _:b308276437 , _:b308276438 , _:b308276439 , _:b308276424 , _:b308276425 , _:b308276426 , _:b308276427 , _:b308276428 , _:b308276429 , _:b308276430 , _:b308276431 , _:b308276416 , _:b308276417 , _:b308276418 , _:b308276419 , _:b308276420 , _:b308276421 , _:b308276422 , _:b308276423 , _:b308276472 , _:b308276473 , _:b308276474 , _:b308276475 , _:b308276476 , _:b308276477 , _:b308276478 , _:b308276479 , _:b308276464 , _:b308276465 , _:b308276466 , _:b308276467 , _:b308276468 , _:b308276469 , _:b308276470 , _:b308276471 , _:b308276456 , _:b308276457 , _:b308276458 , _:b308276459 , _:b308276460 , _:b308276461 , _:b308276462 , _:b308276463 , _:b308276448 , _:b308276449 , _:b308276450 , _:b308276451 , _:b308276452 , _:b308276453 , _:b308276454 , _:b308276455 , _:b308276408 , _:b308276409 , _:b308276410 , _:b308276411 , _:b308276412 , _:b308276413 , _:b308276414 , _:b308276415 , _:b308276400 , _:b308276401 , _:b308276402 , _:b308276403 , _:b308276404 , _:b308276405 , _:b308276406 , _:b308276407 , _:b308276392 , _:b308276393 , _:b308276394 , _:b308276395 , _:b308276396 , _:b308276397 , _:b308276398 , _:b308276399 , _:b308276391 ; ns1:pmcid "PMC0" ; bibo:doi "10.1084%2Fjem.20042041" . @prefix ns4: . ns4:contains _:b1101787 , _:b1101800 , _:b1101798 . _:b1101787 rdf:type ns4:Section . @prefix dc: . _:b1101787 dc:title "materials and methods" ; ns4:contains _:b1101788 , _:b1101789 , _:b1101790 , _:b1101791 , _:b1101792 , _:b1101793 , _:b1101794 , _:b1101795 , _:b1101796 , _:b1101797 . _:b1101788 rdf:type ns1:Context ; rdf:value "Staphopains were purified from the culture media supernatants of S. aureus strain V8-BC10 or 8325-4 as described previously (>>31<<). Purity of staphopains was assessed by SDS-PAGE, mass spectroscopy, and NH2-terminal amino acid sequence analysis." ; ns1:mentions . _:b1101789 rdf:type ns1:Context ; rdf:value "6, panel E); this matched the mass that was calculated from amino acid composition inferred from the gene structure and known processing site of proenzymes (>>32<<). The active site concentration of ScpA and SspB was determined by enzyme titration with E-64 and staphostatins, respectively (31, 33)." ; ns1:mentions . _:b1101790 rdf:type ns1:Context ; rdf:value "The active site concentration of ScpA and SspB was determined by enzyme titration with E-64 and staphostatins, respectively (>>31<<, 33)." ; ns1:mentions . _:b1101791 rdf:type ns1:Context ; rdf:value "The active site concentration of ScpA and SspB was determined by enzyme titration with E-64 and staphostatins, respectively (31, >>33<<)." ; ns1:mentions . _:b1101792 rdf:type ns1:Context ; rdf:value "The residual enzyme activity was assayed with azocoll or synthetic fluorogenic substrates as described previously (>>18<<, 20, 33)." ; ns1:mentions . _:b1101793 rdf:type ns1:Context ; rdf:value "The residual enzyme activity was assayed with azocoll or synthetic fluorogenic substrates as described previously (18, >>20<<, 33)." ; ns1:mentions . _:b1101794 rdf:type ns1:Context ; rdf:value "The residual enzyme activity was assayed with azocoll or synthetic fluorogenic substrates as described previously (18, 20, >>33<<)." ; ns1:mentions . _:b1101795 rdf:type ns1:Context ; rdf:value "The reaction was stopped by the addition of 2 \u03BCg of staphostatins, which are specific and very effective inhibitors of staphopains (>>33<<). Samples were boiled under reducing conditions and analyzed using SDS-PAGE (12% polyacrylamide gels; reference 34). Gels were silver stained." ; ns1:mentions . _:b1101796 rdf:type ns1:Context ; rdf:value "Samples were boiled under reducing conditions and analyzed using SDS-PAGE (12% polyacrylamide gels; reference >>34<<). Gels were silver stained." ; ns1:mentions . _:b1101797 rdf:type ns1:Context ; rdf:value "VL activity was determined by quantitatively measuring the extracted Evans blue by absorbance at 620 nm as described previously (>>21<<). Activity was expressed in terms of \u03BCg of dye extracted. The activity of the buffer was subtracted from the activity of each sample. HOE140 was injected subcutaneously to a guinea pig (10 nmol/kg body weight) 30 min before intradermal" ; ns1:mentions . _:b1101798 rdf:type ns4:Section ; dc:title "results" ; ns4:contains _:b1101799 . _:b1101799 rdf:type ns1:Context ; rdf:value "Although higher doses of BK and gingipain R, a bacterial proteinase that is known to elicit strong VL reaction (>>21<<), increased dye extravasation, the ratio of the blue spot area to the amount of dye was constant (\u223C2.5; Fig." ; ns1:mentions . _:b1101800 rdf:type ns4:Section ; dc:title "discussion" ; ns4:contains _:b1101804 , _:b1101805 , _:b1101806 , _:b1101807 , _:b1101801 , _:b1101802 , _:b1101803 , _:b1101812 , _:b1101813 , _:b1101814 , _:b1101815 , _:b1101808 , _:b1101809 , _:b1101810 , _:b1101811 , _:b1101816 . _:b1101801 rdf:type ns1:Context ; rdf:value "4), clearly showed that this pathogenic activity is exerted by kinin production, which is one of the prominent features of septic shock (>>3<<\u20138). Furthermore, because staphopains also can act on LK\u2014whose plasma molar concentration is threefold greater than HK (Fig. 5; reference 22)\u2014they also have more opportunity to interact with substrate than proteinases that generate BK only" ; ns1:mentions , , , , , . _:b1101802 rdf:type ns1:Context ; rdf:value "The premise gains further credence in light of a study that showed that heat-labile extracellular products of S. aureus, but not heat-treated bacterium, exerted lethal activity in a mouse sepsis model (>>14<<). This strongly argues against the importance of heat-stable components of the S. aureus cell wall, including teichoic acid and lipoteichoic acid as causative molecules of septic shock, despite the fact that they can activate the plasma" ; ns1:mentions . _:b1101803 rdf:type ns1:Context ; rdf:value "the importance of heat-stable components of the S. aureus cell wall, including teichoic acid and lipoteichoic acid as causative molecules of septic shock, despite the fact that they can activate the plasma kallikrein/kinin system (>>10<<). Moreover, in the mouse model, the lethal event was not dependent on toxins, such as toxic shock syndrome toxin 1, enterotoxins (A, B, and D), or hemolysins (\u03B1, \u03B2, and \u03B3; reference 14)." ; ns1:mentions . _:b1101804 rdf:type ns1:Context ; rdf:value "Moreover, in the mouse model, the lethal event was not dependent on toxins, such as toxic shock syndrome toxin 1, enterotoxins (A, B, and D), or hemolysins (\u03B1, \u03B2, and \u03B3; reference >>14<<). This implicates other proteins that are secreted by S. aureus\u2014especially proteolytic enzymes\u2014including epidermolytic toxins; the metalloproteinase, aureolysin; the V8 proteinase; and the two staphopains. The epidermolytic toxins, which" ; ns1:mentions . _:b1101805 rdf:type ns1:Context ; rdf:value "and prefer glutamic acid at the P1 site, cause epidermal dissociation, the pathologic hallmark of bullous impetigo and staphylococcal scalded-skin syndrome; however, they do not trigger edema when injected into newborn mouse skin (>>23<<) or guinea pig skin (unpublished data), so they are unlikely to cause lethal sepsis." ; ns1:mentions . _:b1101806 rdf:type ns1:Context ; rdf:value "Kinin-releasing cysteine proteinases have been reported from various sources, including cruzipain from Tripanosoma cruzi (>>24<<), clostripain from Clostridium histolyticum (25), and calpain from mammalian cells (26)." ; ns1:mentions . _:b1101807 rdf:type ns1:Context ; rdf:value "Kinin-releasing cysteine proteinases have been reported from various sources, including cruzipain from Tripanosoma cruzi (24), clostripain from Clostridium histolyticum (>>25<<), and calpain from mammalian cells (26)." ; ns1:mentions . _:b1101808 rdf:type ns1:Context ; rdf:value "Kinin-releasing cysteine proteinases have been reported from various sources, including cruzipain from Tripanosoma cruzi (24), clostripain from Clostridium histolyticum (25), and calpain from mammalian cells (>>26<<). Staphopains seem to be far more potent than the Streptococcus pyogenes cysteine proteinase (streptopain), which can also release kinins from human kininogens; however, the release of significant amount of kinins in plasma requires a" ; ns1:mentions . _:b1101809 rdf:type ns1:Context ; rdf:value "pyogenes cysteine proteinase (streptopain), which can also release kinins from human kininogens; however, the release of significant amount of kinins in plasma requires a streptopain concentration of 1 \u03BCM and 60 min incubation (>>27<<). In contrast, a submicromolar concentration of ScpA generates large amounts of kinin from human plasma in just 5 min (Fig." ; ns1:mentions . _:b1101810 rdf:type ns1:Context ; rdf:value "In this context, peptides that are released from kininogens by bacterial proteinases were shown to act like kinins by their VL activity and/or BK antigenicity\u2014in most cases without performing amino acid sequencing (>>16<<, 27). The fact that Leu-Met-Lys-BK was released in the presence of ScpA and SspB (Fig. 6) indicates that a combination of two proteinases can generate a kinin through synergistically cleaving kininogens at each terminal side of the kinin" ; ns1:mentions . _:b1101811 rdf:type ns1:Context ; rdf:value "In this context, peptides that are released from kininogens by bacterial proteinases were shown to act like kinins by their VL activity and/or BK antigenicity\u2014in most cases without performing amino acid sequencing (16, >>27<<). The fact that Leu-Met-Lys-BK was released in the presence of ScpA and SspB (Fig. 6) indicates that a combination of two proteinases can generate a kinin through synergistically cleaving kininogens at each terminal side of the kinin" ; ns1:mentions . _:b1101812 rdf:type ns1:Context ; rdf:value "Previously, we found that two cysteine proteinases from Porphyromonas gingivalis (gingipains: RgpA and Kgp) released BK from kininogens by cleaving the amino terminus by Kgp and the carboxy terminus by RgpA (>>28<<). The mixture of human neutrophil elastase and mast cell tryptase also produced BK from HK (29). Therefore, it may be a common event in vivo that two proteinases cooperatively generate a kinin, with one proteinase cleaving kininogen at" ; ns1:mentions . _:b1101813 rdf:type ns1:Context ; rdf:value "The mixture of human neutrophil elastase and mast cell tryptase also produced BK from HK (>>29<<). Therefore, it may be a common event in vivo that two proteinases cooperatively generate a kinin, with one proteinase cleaving kininogen at the amino terminus and the other at the carboxy terminus. The carboxy terminal residues of BK are" ; ns1:mentions . _:b1101814 rdf:type ns1:Context ; rdf:value "The carboxy terminal residues of BK are required for the binding to the B2-receptor on the cell (>>11<<), which is consistent with the finding that Leu-Met-Lys-BK is as active as BK in VL activity (Fig." ; ns1:mentions . _:b1101815 rdf:type ns1:Context ; rdf:value "kininogens by human neutrophil elastase, and the related peptides Ser-Leu-Met-Lys-BK-Ser-Ser and Ser-Leu-Met-Lys-BK can induce VL and lower blood pressure in a B2-receptor\u2013dependent manner, but cannot cause smooth muscle contraction (>>30<<). This suggests that additional residues at the carboxy-terminal side of these peptides are trimmed off immediately, presumably in the circulation, and convert the carboxy terminus to that found in BK." ; ns1:mentions . _:b1101816 rdf:type ns1:Context ; rdf:value "1 and 3) may be due to connective tissue damage through degradation of elastin (>>31<<), and possibly other extracellular matrix proteins by ScpA." ; ns1:mentions . _:b308276391 rdf:type ns1:RelevantBibliographicResource . @prefix xsd: . _:b308276391 ns1:RelevantScore "8"^^xsd:nonNegativeInteger ; ns1:hasRelevantPaperId . _:b308276392 rdf:type ns1:RelevantBibliographicResource ; ns1:RelevantScore "7"^^xsd:nonNegativeInteger ; ns1:hasRelevantPaperId . _:b308276393 rdf:type ns1:RelevantBibliographicResource ; ns1:RelevantScore "7"^^xsd:nonNegativeInteger ; ns1:hasRelevantPaperId . _:b308276394 rdf:type ns1:RelevantBibliographicResource ; ns1:RelevantScore "7"^^xsd:nonNegativeInteger ; ns1:hasRelevantPaperId . _:b308276395 rdf:type ns1:RelevantBibliographicResource ; 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