Topic
Antipain
About: Antipain is a research topic. Over the lifetime, 471 publications have been published within this topic receiving 15864 citations.
Papers published on a yearly basis
Papers
TL;DR: It is tentatively concluded that rumen bacteria possess, primarily, serine, cysteine, and metalloproteinases.
Abstract: Proteolytic activity of the bovine rumen microflora was studied with azocasein as the substrate. Approximately 25% of the proteolytic activity of rumen contents was recovered in the strained rumen fluid fraction, and the balance of the activity was associated with the particulate fraction. The proportion of proteinase activity associated with particulate material decreased when the quantity of particulate material in rumen contents was reduced. The specific activity of the proteinase from the bacterial fraction was 6 to 10 times higher than that from the protozoal fraction. Proteinase inhibitors of synthetic, plant, and microbial origin were tested on proteolytic activity of the separated bacteria. Synthetic proteinase inhibitors that caused significant inhibition of proteolysis included phenylmethylsulfonyl fluoride, N-tosyl-1-lysine chloromethyl ketone, N-tosylphenylalanine chloromethyl ketone, EDTA, cysteine, dithiothreitol, iodoacetate, and Merthiolate. Plant proteinase inhibitors that had an inhibitory effect included soybean trypsin inhibitors types I-S and II-S and the lima bean trypsin inhibitor. Proteinase inhibitors of microbial origin that showed an inhibitory effect included antipain, leupeptin, and chymostatin; phosphoramidon and pepstatin had little effect. We tentatively concluded that rumen bacteria possess, primarily, serine, cysteine, and metalloproteinases.
294 citations
TL;DR: The results suggest that the enzyme Tryptase Clara is a possible activator of inactive viral fusion glycoprotein in the respiratory tract and thus responsible for pneumopathogenicity of the virus.
282 citations
TL;DR: The results suggest that the perturbation of intracellular Ca2+ homeostasis by cystamine is caused by the inhibition ofCa2+ efflux associated with the formation of cystamines-protein mixed disulfides in the plasma membrane and that subsequent cytotoxicity results from Ca2-activation of a nonlysosomal proteolytic system.
264 citations
TL;DR: The results suggest that Pseudoalteromonas sp.
Abstract: The marine bacterium Pseudoalteromonas sp. strain A28 was able to kill the diatom Skeletonema costatum strain NIES-324. The culture supernatant of strain A28 showed potent algicidal activity when it was applied to a paper disk placed on a lawn of S. costatum NIES-324. The condensed supernatant, which was prepared by subjecting the A28 culture supernatant to ultrafiltration with a 10,000-M(w)-cutoff membrane, showed algicidal activity, suggesting that strain A28 produced extracellular substances capable of killing S. costatum cells. The condensed supernatant was then found to have protease and DNase activities. Two Pseudoalteromonas mutants lacking algicidal activity, designated NH1 and NH2, were selected after N-methyl-N'-nitrosoguanidine mutagenesis. The culture supernatants of NH1 and NH2 showed less than 15% of the protease activity detected with the parental strain, A28. The protease was purified to homogeneity from A28 culture supernatants by using ion-exchange chromatography followed by preparative gel electrophoresis. Paper-disk assays revealed that the purified protease had potent algicidal activity. The purified protease had a molecular mass for 50 kDa, and the N-terminal amino acid sequence was determined to be Ala-Thr-Pro-Asn-Asp-Pro. The optimum pH and temperature of the protease were found to be 8.8 and 30 degrees C, respectively, by using succinyl-Ala-Ala-Pro-Phe-p-nitroanilide as a substrate. The protease activity was strongly inhibited by phenylmethylsulfonyl fluoride, diisopropyl fluorophosphate, antipain, chymostatin, and leupeptin. No significant inhibition was detected with EDTA, EGTA, phenanthroline or tetraethylenepentamine. These results suggest that Pseudoalteromonas sp. strain A28 produced an extracellular serine protease which was responsible for the algicidal activity of this marine bacterium.
227 citations
TL;DR: It was shown that fungal serine protease activity induced the production of interleukin (IL)-8 and IL-6 and monocyte chemotactic protein-1 and caused cell detachment in a dose-dependent fashion and by eliciting a cytokine response, the epithelium may signal the mucosal inflammatory response against A. fumigatus.
Abstract: Aspergillus fumigatus is a pathogen causing diverse respiratory disorders. Several studies have suggested that fungal proteases may play a role in the pathogenicity of fungi. Since the airways are the most common route for entry of A. fumigatus, this study focused on the ability of fungal proteases to induce the release of proinflammatory cytokines and to cause cell detachment in human pulmonary epithelial cell lines. It was shown that fungal serine protease activity induced the production of interleukin (IL)-8 and IL-6 and monocyte chemotactic protein-1 and caused cell detachment in a dose-dependent fashion. Chymostatin, antipain, phenylmethylsulfonyl fluoride, and heat treatment completely inhibited fungal protease activity, cytokine production and cell detachment; antileukoprotease partially inhibited these activities. By causing cell detachment, fungal proteases may decrease the physical barrier function of the epithelium; however, by eliciting a cytokine response, the epithelium may signal the mucosal inflammatory response against A. fumigatus.
205 citations
Related Topics (5)
Performance Metrics
| Year | Papers |
|---|---|
| 2022 | 1 |
| 2021 | 3 |
| 2018 | 1 |
| 2017 | 2 |
| 2016 | 31 |
| 2015 | 1 |