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10.1074/jbc.RA120.014525 http://scihub22266oqcxt.onion/10.1074/jbc.RA120.014525 32675285!7476710!32675285     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=32675285&cmd=llinks): Failed to open stream: HTTP request failed! 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Intracellular autoactivation of TMPRSS11A, an airway epithelial transmembrane serine protease |pdf=|usr=}}{{32675285}} gab.com Text Intracellular autoactivation of TMPRSS11A, an airway epithelial transmembrane serine protease JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=32675285 #FOAvip Type II transmembrane serine proteases (TTSPs) are a group of enzymes participating in diverse biological processes. Some members of the TTSP family are implicated in viral infection. TMPRSS11A is a TTSP expressed on the surface of airway epithelial cells, which has been shown to cleave and activate spike proteins of the severe acute respiratory syndrome (SARS) and the Middle East respiratory syndrome coronaviruses (CoVs). In this study, we examined the mechanism underlying the activation cleavage of TMPRSS11A that converts the one-chain zymogen to a two-chain enzyme. By expression in human embryonic kidney 293, esophageal EC9706, and lung epithelial A549 and 16HBE cells, Western blotting, and site-directed mutagenesis, we found that the activation cleavage of human TMPRSS11A was mediated by autocatalysis. Moreover, we found that TMPRSS11A activation cleavage occurred before the protein reached the cell surface, as indicated by studies with trypsin digestion to remove cell surface proteins, treatment with cell organelle-disturbing agents to block intracellular protein trafficking, and analysis of a soluble form of TMPRSS11A without the transmembrane domain. We also showed that TMPRSS11A was able to cleave the SARS-CoV-2 spike protein. These results reveal an intracellular autocleavage mechanism in TMPRSS11A zymogen activation, which differs from the extracellular zymogen activation reported in other TTSPs. These findings provide new insights into the diverse mechanisms in regulating TTSP activation. Twit Text FOAVip Intracellular autoactivation of TMPRSS11A, an airway epithelial transmembrane serine protease ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=32675285 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32675285 #FOAvip English Wikipedia <ref>{{Cite pmid|32675285}}</ref> Intracellular autoactivation of TMPRSS11A, an airway epithelial transmembrane serine protease #MMPMID32675285 Zhang C; Zhang Y; Zhang S; Wang Z; Sun S; Liu M; Chen Y; Dong N; Wu Q J Biol Chem 2020[Sep]; 295 (36): 12686-12696 PMID32675285show ga Type II transmembrane serine proteases (TTSPs) are a group of enzymes participating in diverse biological processes. Some members of the TTSP family are implicated in viral infection. TMPRSS11A is a TTSP expressed on the surface of airway epithelial cells, which has been shown to cleave and activate spike proteins of the severe acute respiratory syndrome (SARS) and the Middle East respiratory syndrome coronaviruses (CoVs). In this study, we examined the mechanism underlying the activation cleavage of TMPRSS11A that converts the one-chain zymogen to a two-chain enzyme. By expression in human embryonic kidney 293, esophageal EC9706, and lung epithelial A549 and 16HBE cells, Western blotting, and site-directed mutagenesis, we found that the activation cleavage of human TMPRSS11A was mediated by autocatalysis. Moreover, we found that TMPRSS11A activation cleavage occurred before the protein reached the cell surface, as indicated by studies with trypsin digestion to remove cell surface proteins, treatment with cell organelle-disturbing agents to block intracellular protein trafficking, and analysis of a soluble form of TMPRSS11A without the transmembrane domain. We also showed that TMPRSS11A was able to cleave the SARS-CoV-2 spike protein. These results reveal an intracellular autocleavage mechanism in TMPRSS11A zymogen activation, which differs from the extracellular zymogen activation reported in other TTSPs. These findings provide new insights into the diverse mechanisms in regulating TTSP activation. |*Proteolysis[MESH] |A549 Cells[MESH] |Cells, Cultured[MESH] |Epithelial Cells/*metabolism[MESH] |HEK293 Cells[MESH] |Humans[MESH] |Membrane Proteins/chemistry/genetics/*metabolism[MESH] |Mutation[MESH] |Protein Domains[MESH] |Protein Transport[MESH] |Respiratory Mucosa/cytology[MESH] |Serine Proteases/chemistry/genetics/*metabolism[MESH] |Spike Glycoprotein, Coronavirus/metabolism[MESH]Intracellular autoactivation of TMPRSS11A, an airway epithelial transm(epmc).pdf DeepDyve Pubget Overpricing