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10.3390/molecules26175344 http://scihub22266oqcxt.onion/10.3390/molecules26175344 34500777!8434204!34500777     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Molecules 2021 ; 26 (17): ä Nephropedia Template TP {{tp|p=34500777|t=2021. Discrimination of Methionine Sulfoxide and Sulfone by Human Neutrophil Elastase |pdf=|usr=}}{{34500777}} gab.com Text Discrimination of Methionine Sulfoxide and Sulfone by Human Neutrophil Elastase JO: Molecules http://www.kidney.de/pget.php?&tw=1&pmid=34500777 #FOAvip Human neutrophil elastase (HNE) is a uniquely destructive serine protease with the ability to unleash a wave of proteolytic activity by destroying the inhibitors of other proteases. Although this phenomenon forms an important part of the innate immune response to invading pathogens, it is responsible for the collateral host tissue damage observed in chronic conditions such as chronic obstructive pulmonary disease (COPD), and in more acute disorders such as the lung injuries associated with COVID-19 infection. Previously, a combinatorially selected activity-based probe revealed an unexpected substrate preference for oxidised methionine, which suggests a link to oxidative pathogen clearance by neutrophils. Here we use oxidised model substrates and inhibitors to confirm this observation and to show that neutrophil elastase is specifically selective for the di-oxygenated methionine sulfone rather than the mono-oxygenated methionine sulfoxide. We also posit a critical role for ordered solvent in the mechanism of HNE discrimination between the two oxidised forms methionine residue. Preference for the sulfone form of oxidised methionine is especially significant. While both host and pathogens have the ability to reduce methionine sulfoxide back to methionine, a biological pathway to reduce methionine sulfone is not known. Taken together, these data suggest that the oxidative activity of neutrophils may create rapidly cleaved elastase "super substrates" that directly damage tissue, while initiating a cycle of neutrophil oxidation that increases elastase tissue damage and further neutrophil recruitment. Twit Text FOAVip Discrimination of Methionine Sulfoxide and Sulfone by Human Neutrophil Elastase ????Molecules http://www.kidney.de/pget.php?&tw=1&pmid=34500777 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34500777 #FOAvip English Wikipedia <ref>{{Cite pmid|34500777}}</ref> Discrimination of Methionine Sulfoxide and Sulfone by Human Neutrophil Elastase #MMPMID34500777 Leahy D; Grant C; Jackson A; Duff A; Tardiota N; Van Haeften J; Chen X; Peake JM; Kruppa MD; Smith ET; Johnson DA; Lott WB; Harris JM Molecules 2021[Sep]; 26 (17): ä PMID34500777show ga Human neutrophil elastase (HNE) is a uniquely destructive serine protease with the ability to unleash a wave of proteolytic activity by destroying the inhibitors of other proteases. Although this phenomenon forms an important part of the innate immune response to invading pathogens, it is responsible for the collateral host tissue damage observed in chronic conditions such as chronic obstructive pulmonary disease (COPD), and in more acute disorders such as the lung injuries associated with COVID-19 infection. Previously, a combinatorially selected activity-based probe revealed an unexpected substrate preference for oxidised methionine, which suggests a link to oxidative pathogen clearance by neutrophils. Here we use oxidised model substrates and inhibitors to confirm this observation and to show that neutrophil elastase is specifically selective for the di-oxygenated methionine sulfone rather than the mono-oxygenated methionine sulfoxide. We also posit a critical role for ordered solvent in the mechanism of HNE discrimination between the two oxidised forms methionine residue. Preference for the sulfone form of oxidised methionine is especially significant. While both host and pathogens have the ability to reduce methionine sulfoxide back to methionine, a biological pathway to reduce methionine sulfone is not known. Taken together, these data suggest that the oxidative activity of neutrophils may create rapidly cleaved elastase "super substrates" that directly damage tissue, while initiating a cycle of neutrophil oxidation that increases elastase tissue damage and further neutrophil recruitment. |*Immunity, Innate[MESH] |Biocatalysis[MESH] |COVID-19/immunology/pathology/virology[MESH] |Catalytic Domain/genetics[MESH] |Enzyme Assays[MESH] |Host-Pathogen Interactions/immunology[MESH] |Humans[MESH] |Leukocyte Elastase/antagonists & inhibitors/genetics/*metabolism[MESH] |Lung/immunology/pathology/virology[MESH] |Methionine/*analogs & derivatives/metabolism[MESH] |Molecular Dynamics Simulation[MESH] |Neutrophil Infiltration[MESH] |Neutrophils/enzymology/*immunology[MESH] |Oxidation-Reduction/drug effects[MESH] |Proteolysis/drug effects[MESH] |Pulmonary Disease, Chronic Obstructive/immunology/pathology[MESH] |SARS-CoV-2/immunology[MESH]Discrimination of Methionine Sulfoxide and Sulfone by Human Neutrophil(epmc).pdf DeepDyve Pubget Overpricing