FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1874668543> ?p ?o ?g. }

• W1874668543 endingPage "762" @default.
• W1874668543 startingPage "756" @default.
• W1874668543 abstract "It has been shown that Porphyromonas gingivalis 381, a suspected periodontopathogen, possesses fimbriae on its cell surface. The organism is also known to produce proteases which can degrade the host cell surface matrix proteins. In this study, we investigated the effect of protease on the binding of the purified P. gingivalis fimbriae to cultured fibroblasts or matrix proteins. A protease that can hydrolyze benzoyl-L-arginine p-nitroanilide was obtained from P. gingivalis 381 cells by sonication in phosphate-buffered 0.2% Triton X-100 and was purified by column chromatography. The molecular size of the protease was estimated to be 55 kDa by gel filtration or 47 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis. The enzyme activity was markedly inhibited by sulfhydryl reagents, antipain, and leupeptin. The protease degraded various host proteins, including collagen and fibronectin, and cleaved the COOH terminus of the arginine residue in peptides such as benzoyl-L-arginine p-nitroanilide. However, P. gingivalis fimbriae were not degraded by protease activity. The enzyme activity was enhanced in the presence of reducing agents or CaCl2. When cultured fibroblasts were partially treated with the protease, the binding of the purified P. gingivalis fimbriae to the fibroblast monolayer was increased significantly. However, this enhancing effect was suppressed upon the addition of antipain and leupeptin. Similarly, binding of the fimbriae to the collagen or fibronectin immobilized on the microtiter wells was also enhanced. Addition of these host matrix proteins efficiently inhibited the binding of fimbriae to the fibroblast monolayer. The binding assay of fimbriae using dipeptidyl ligand affinity column chromatography demonstrated a clear interaction between fimbriae and the arginine residue. Taken together, these results indicate that the P. gingivalis protease at least partially degrades the host matrix proteins, which, in turn, may lead to an increased exposure of the cryptic ligands that can result in enhanced fimbria-mediated binding of this organism to periodontal tissues." @default.
• W1874668543 created "2016-06-24" @default.
• W1874668543 creator A5012268704 @default.
• W1874668543 creator A5023165797 @default.
• W1874668543 creator A5035457147 @default.
• W1874668543 creator A5050387199 @default.
• W1874668543 creator A5055801894 @default.
• W1874668543 creator A5057771677 @default.
• W1874668543 creator A5059015629 @default.
• W1874668543 creator A5073188851 @default.
• W1874668543 date "1996-03-01" @default.
• W1874668543 modified "2023-09-26" @default.
• W1874668543 title "Cysteine protease of Porphyromonas gingivalis 381 enhances binding of fimbriae to cultured human fibroblasts and matrix proteins" @default.
• W1874668543 cites W1514298611 @default.
• W1874668543 cites W1535481983 @default.
• W1874668543 cites W1538268336 @default.
• W1874668543 cites W1595536772 @default.
• W1874668543 cites W1821270395 @default.
• W1874668543 cites W1822585528 @default.
• W1874668543 cites W1851348219 @default.
• W1874668543 cites W1859540183 @default.
• W1874668543 cites W1938414864 @default.
• W1874668543 cites W1956236905 @default.
• W1874668543 cites W1961692317 @default.
• W1874668543 cites W1966468462 @default.
• W1874668543 cites W1970434698 @default.
• W1874668543 cites W1987844494 @default.
• W1874668543 cites W1997539836 @default.
• W1874668543 cites W2002472577 @default.
• W1874668543 cites W2025607505 @default.
• W1874668543 cites W2031592714 @default.
• W1874668543 cites W2034604829 @default.
• W1874668543 cites W2045634593 @default.
• W1874668543 cites W2061081100 @default.
• W1874668543 cites W2061469613 @default.
• W1874668543 cites W2069545891 @default.
• W1874668543 cites W2070371129 @default.
• W1874668543 cites W2071451674 @default.
• W1874668543 cites W2074420943 @default.
• W1874668543 cites W2076743261 @default.
• W1874668543 cites W2095436997 @default.
• W1874668543 cites W2100837269 @default.
• W1874668543 cites W2102117283 @default.
• W1874668543 cites W2113552067 @default.
• W1874668543 cites W2113643753 @default.
• W1874668543 cites W2120316045 @default.
• W1874668543 cites W2122456003 @default.
• W1874668543 cites W2127864555 @default.
• W1874668543 cites W2137266684 @default.
• W1874668543 cites W2150260980 @default.
• W1874668543 cites W2150525106 @default.
• W1874668543 cites W2154270070 @default.
• W1874668543 cites W2159383556 @default.
• W1874668543 cites W2253279010 @default.
• W1874668543 cites W2300511507 @default.
• W1874668543 cites W2415701729 @default.
• W1874668543 cites W603314494 @default.
• W1874668543 doi "https://doi.org/10.1128/iai.64.3.756-762.1996" @default.
• W1874668543 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/173834" @default.
• W1874668543 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8641778" @default.
• W1874668543 hasPublicationYear "1996" @default.
• W1874668543 type Work @default.
• W1874668543 sameAs 1874668543 @default.
• W1874668543 citedByCount "75" @default.
• W1874668543 countsByYear W18746685432012 @default.
• W1874668543 countsByYear W18746685432013 @default.
• W1874668543 countsByYear W18746685432014 @default.
• W1874668543 countsByYear W18746685432017 @default.
• W1874668543 countsByYear W18746685432020 @default.
• W1874668543 countsByYear W18746685432021 @default.
• W1874668543 countsByYear W18746685432023 @default.
• W1874668543 crossrefType "journal-article" @default.
• W1874668543 hasAuthorship W1874668543A5012268704 @default.
• W1874668543 hasAuthorship W1874668543A5023165797 @default.
• W1874668543 hasAuthorship W1874668543A5035457147 @default.
• W1874668543 hasAuthorship W1874668543A5050387199 @default.
• W1874668543 hasAuthorship W1874668543A5055801894 @default.
• W1874668543 hasAuthorship W1874668543A5057771677 @default.
• W1874668543 hasAuthorship W1874668543A5059015629 @default.
• W1874668543 hasAuthorship W1874668543A5073188851 @default.
• W1874668543 hasBestOaLocation W18746685431 @default.
• W1874668543 hasConcept C104317684 @default.
• W1874668543 hasConcept C116084860 @default.
• W1874668543 hasConcept C153911025 @default.
• W1874668543 hasConcept C181199279 @default.
• W1874668543 hasConcept C182220744 @default.
• W1874668543 hasConcept C2775883766 @default.
• W1874668543 hasConcept C2776714187 @default.
• W1874668543 hasConcept C2777283782 @default.
• W1874668543 hasConcept C2780183776 @default.
• W1874668543 hasConcept C2781378782 @default.
• W1874668543 hasConcept C39103817 @default.
• W1874668543 hasConcept C523546767 @default.
• W1874668543 hasConcept C54355233 @default.
• W1874668543 hasConcept C547475151 @default.
• W1874668543 hasConcept C55493867 @default.
• W1874668543 hasConcept C86803240 @default.
• W1874668543 hasConceptScore W1874668543C104317684 @default.

• next