FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2029702015> ?p ?o ?g. }

• W2029702015 endingPage "709" @default.
• W2029702015 startingPage "697" @default.
• W2029702015 abstract "Bovine corneal endothelial cells in culture bind internalize and degrade [125I]-trypsin. Binding involves the active site of trypsin and increases as a function of [125I]-trypsin concentration. Saturation is observed at a concentration of 0.5-1.0 micrograms ml-1. The cell surface binding of [125I]-trypsin is specific: a seven-fold excess of unlabeled trypsin abolishes about 60% of the total cell surface-associated radioactivity. In addition, thrombin competes poorly with [125I]-trypsin cell surface binding and only 20% of the specific cell surface binding of [125I]-trypsin is subjected to competition with thrombin. This fraction of the cell surface-bound [125I]-trypsin which is accessible to competition with thrombin appears in a covalent complex of [125I]-trypsin X protease-nexin with a molecular weight of 64000 daltons. The cells, when incubated at 37 degrees C, appear to internalize the cell surface-bound [125I]-trypsin at a rate of 0.15-0.25 ng (10(6) cells)-1 min-1. Both the non-covalently cell surface-bound and the protease-nexin (PN) mediated-bound [125I]-trypsin are internalized by the cells, but the [125I]-trypsin X PN complexes contribute about 75% of the total amount of [125I]-trypsin internalized by the cells. The internalized [125I]-trypsin is degraded by the cultures at a rate of about 0.05 ng (10(6) cells)-1 min-1 and the degradation products are released by the cells into the incubation medium as a trichloroacetic acid non-precipitable material. Chloroquine inhibits about 60% of the internalization of [125I]-trypsin by the cells, and inhibits more than 80% of the degradation process of [125I]-trypsin, which indicates that the degradation of the ligand is taking place in lysosomes. Bovine corneal endothelial cells in culture have demonstrated the binding and metabolism of the serine protease trypsin. This described process may indicate the ability of corneal endothelial cells to control the activity of serine proteases in their microenvironment." @default.
• W2029702015 created "2016-06-24" @default.
• W2029702015 creator A5077139130 @default.
• W2029702015 creator A5089742626 @default.
• W2029702015 date "1985-05-01" @default.
• W2029702015 modified "2023-09-27" @default.
• W2029702015 title "Binding and processing of trypsin by cultured bovine corneal endothelial cells" @default.
• W2029702015 cites W109443676 @default.
• W2029702015 cites W1502488284 @default.
• W2029702015 cites W1522487436 @default.
• W2029702015 cites W1537294977 @default.
• W2029702015 cites W1589339079 @default.
• W2029702015 cites W2013750006 @default.
• W2029702015 cites W2017749217 @default.
• W2029702015 cites W2017946397 @default.
• W2029702015 cites W2021219843 @default.
• W2029702015 cites W2028744742 @default.
• W2029702015 cites W2084797477 @default.
• W2029702015 cites W2100837269 @default.
• W2029702015 cites W2107924955 @default.
• W2029702015 cites W2412575900 @default.
• W2029702015 doi "https://doi.org/10.1016/0014-4835(85)90139-3" @default.
• W2029702015 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/4007080" @default.
• W2029702015 hasPublicationYear "1985" @default.
• W2029702015 type Work @default.
• W2029702015 sameAs 2029702015 @default.
• W2029702015 citedByCount "3" @default.
• W2029702015 crossrefType "journal-article" @default.
• W2029702015 hasAuthorship W2029702015A5077139130 @default.
• W2029702015 hasAuthorship W2029702015A5089742626 @default.
• W2029702015 hasConcept C1491633281 @default.
• W2029702015 hasConcept C153911025 @default.
• W2029702015 hasConcept C181199279 @default.
• W2029702015 hasConcept C185592680 @default.
• W2029702015 hasConcept C203014093 @default.
• W2029702015 hasConcept C2776714187 @default.
• W2029702015 hasConcept C2777292125 @default.
• W2029702015 hasConcept C2780340462 @default.
• W2029702015 hasConcept C54355233 @default.
• W2029702015 hasConcept C55493867 @default.
• W2029702015 hasConcept C81885089 @default.
• W2029702015 hasConcept C86803240 @default.
• W2029702015 hasConcept C89560881 @default.
• W2029702015 hasConceptScore W2029702015C1491633281 @default.
• W2029702015 hasConceptScore W2029702015C153911025 @default.
• W2029702015 hasConceptScore W2029702015C181199279 @default.
• W2029702015 hasConceptScore W2029702015C185592680 @default.
• W2029702015 hasConceptScore W2029702015C203014093 @default.
• W2029702015 hasConceptScore W2029702015C2776714187 @default.
• W2029702015 hasConceptScore W2029702015C2777292125 @default.
• W2029702015 hasConceptScore W2029702015C2780340462 @default.
• W2029702015 hasConceptScore W2029702015C54355233 @default.
• W2029702015 hasConceptScore W2029702015C55493867 @default.
• W2029702015 hasConceptScore W2029702015C81885089 @default.
• W2029702015 hasConceptScore W2029702015C86803240 @default.
• W2029702015 hasConceptScore W2029702015C89560881 @default.
• W2029702015 hasIssue "5" @default.
• W2029702015 hasLocation W20297020151 @default.
• W2029702015 hasLocation W20297020152 @default.
• W2029702015 hasOpenAccess W2029702015 @default.
• W2029702015 hasPrimaryLocation W20297020151 @default.
• W2029702015 hasRelatedWork W17428494 @default.
• W2029702015 hasRelatedWork W1976369551 @default.
• W2029702015 hasRelatedWork W1984160343 @default.
• W2029702015 hasRelatedWork W2022672510 @default.
• W2029702015 hasRelatedWork W2024082801 @default.
• W2029702015 hasRelatedWork W2078595220 @default.
• W2029702015 hasRelatedWork W2410036357 @default.
• W2029702015 hasRelatedWork W2491451478 @default.
• W2029702015 hasRelatedWork W4231761976 @default.
• W2029702015 hasRelatedWork W4239935025 @default.
• W2029702015 hasVolume "40" @default.
• W2029702015 isParatext "false" @default.
• W2029702015 isRetracted "false" @default.
• W2029702015 magId "2029702015" @default.
• W2029702015 workType "article" @default.