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10.1016/j.ebiom.2017.01.032 http://scihub22266oqcxt.onion/10.1016/j.ebiom.2017.01.032 C5474509!5474509 !28139439     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28139439 &cmd=llinks): Failed to open stream: HTTP request failed! 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Neutrophil Protease Cleavage of Von Willebrand Factor in Glomeruli - An Anti-thrombotic Mechanism in the Kidney |pdf=|usr=}}{{28139439 }} gab.com Text Neutrophil Protease Cleavage of Von Willebrand Factor in Glomeruli - An Anti-thrombotic Mechanism in the Kidney JO: EBioMedicine http://www.kidney.de/pget.php?&tw=1&pmid=28139439 #FOAvip Adequate cleavage of von Willebrand factor (VWF) prevents formation of thrombi. ADAMTS13 is the main VWF-cleaving protease and its deficiency results in development of thrombotic microangiopathy. Besides ADAMTS13 other proteases may also possess VWF-cleaving activity, but their physiological importance in preventing thrombus formation is unknown. This study investigated if, and which, proteases could cleave VWF in the glomerulus. The content of the glomerular basement membrane (GBM) was studied as a reflection of processes occurring in the subendothelial glomerular space. VWF was incubated with human GBMs and VWF cleavage was assessed by multimer structure analysis, immunoblotting and mass spectrometry. VWF was cleaved into the smallest multimers by the GBM, which contained ADAMTS13 as well as neutrophil proteases, elastase, proteinase 3 (PR3), cathepsin-G and matrix-metalloproteinase 9. The most potent components of the GBM capable of VWF cleavage were in the serine protease or metalloprotease category, but not ADAMTS13. Neutralization of neutrophil serine proteases inhibited GBM-mediated VWF-cleaving activity, demonstrating a marked contribution of elastase and/or PR3. VWF-platelet strings formed on the surface of primary glomerular endothelial cells, in a perfusion system, were cleaved by both elastase and the GBM, a process blocked by elastase inhibitor. Ultramorphological studies of the human kidney demonstrated neutrophils releasing elastase into the GBM. Neutrophil proteases may contribute to VWF cleavage within the subendothelium, adjacent to the GBM, and thus regulate thrombus size. This anti-thrombotic mechanism would protect the normal kidney during inflammation and could also explain why most patients with ADAMTS13 deficiency do not develop severe kidney failure. Twit Text FOAVip Neutrophil Protease Cleavage of Von Willebrand Factor in Glomeruli - An Anti-thrombotic Mechanism in the Kidney ????EBioMedicine http://www.kidney.de/pget.php?&tw=1&pmid=28139439 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28139439 #FOAvip English Wikipedia <ref>{{Cite pmid|28139439 }}</ref> Neutrophil Protease Cleavage of Von Willebrand Factor in Glomeruli - An Anti-thrombotic Mechanism in the Kidney #MMPMID28139439 Tati R ; Kristoffersson AC ; Manea Hedström M ; Mörgelin M ; Wieslander J ; van Kooten C ; Karpman D EBioMedicine 2017[Feb]; 16 (ä): 302-311 PMID28139439 show ga Adequate cleavage of von Willebrand factor (VWF) prevents formation of thrombi. ADAMTS13 is the main VWF-cleaving protease and its deficiency results in development of thrombotic microangiopathy. Besides ADAMTS13 other proteases may also possess VWF-cleaving activity, but their physiological importance in preventing thrombus formation is unknown. This study investigated if, and which, proteases could cleave VWF in the glomerulus. The content of the glomerular basement membrane (GBM) was studied as a reflection of processes occurring in the subendothelial glomerular space. VWF was incubated with human GBMs and VWF cleavage was assessed by multimer structure analysis, immunoblotting and mass spectrometry. VWF was cleaved into the smallest multimers by the GBM, which contained ADAMTS13 as well as neutrophil proteases, elastase, proteinase 3 (PR3), cathepsin-G and matrix-metalloproteinase 9. The most potent components of the GBM capable of VWF cleavage were in the serine protease or metalloprotease category, but not ADAMTS13. Neutralization of neutrophil serine proteases inhibited GBM-mediated VWF-cleaving activity, demonstrating a marked contribution of elastase and/or PR3. VWF-platelet strings formed on the surface of primary glomerular endothelial cells, in a perfusion system, were cleaved by both elastase and the GBM, a process blocked by elastase inhibitor. Ultramorphological studies of the human kidney demonstrated neutrophils releasing elastase into the GBM. Neutrophil proteases may contribute to VWF cleavage within the subendothelium, adjacent to the GBM, and thus regulate thrombus size. This anti-thrombotic mechanism would protect the normal kidney during inflammation and could also explain why most patients with ADAMTS13 deficiency do not develop severe kidney failure. |ADAMTS13 Protein/metabolism [MESH] |Adult [MESH] |Blood Platelets/metabolism [MESH] |Cathepsin G/metabolism [MESH] |Endothelial Cells/metabolism [MESH] |Glomerular Basement Membrane/drug effects/metabolism [MESH] |Humans [MESH] |Immunoblotting [MESH] |Kidney Glomerulus/drug effects/*metabolism/ultrastructure [MESH] |Kidney/blood supply/*metabolism/ultrastructure [MESH] |Leukocyte Elastase/antagonists & inhibitors/metabolism [MESH] |Male [MESH] |Matrix Metalloproteinase 9/metabolism [MESH] |Microscopy, Electron, Transmission [MESH] |Myeloblastin/metabolism [MESH] |Neutrophils/*enzymology [MESH] |Peptide Hydrolases/*metabolism [MESH] |Proteinase Inhibitory Proteins, Secretory/pharmacology [MESH] |Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization [MESH] |Thrombosis/*metabolism/prevention & control [MESH]Neutrophil Protease Cleavage of Von Willebrand Factor in Glomeruli - A(epmc).pdf DeepDyve Pubget Overpricing