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10.1074/jbc.RA120.015303 http://scihub22266oqcxt.onion/10.1074/jbc.RA120.015303 33122196!7833600!33122196     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Biol+Chem 2020 ; 295 (52): 18579-18588 Nephropedia Template TP {{tp|p=33122196|t=2020. High affinity binding of SARS-CoV-2 spike protein enhances ACE2 carboxypeptidase activity |pdf=|usr=}}{{33122196}} gab.com Text High affinity binding of SARS-CoV-2 spike protein enhances ACE2 carboxypeptidase activity JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=33122196 #FOAvip The novel severe acute respiratory syndrome coronavirus (SARS-CoV-2) has emerged to a pandemic and caused global public health crisis. Human angiotensin-converting enzyme 2(ACE2) was identified as the entry receptor for SARS-CoV-2. As a carboxypeptidase, ACE2 cleaves many biological substrates besides angiotensin II to control vasodilatation and vascular permeability. Given the nanomolar high affinity between ACE2 and SARS-CoV-2 spike protein, we investigated how this interaction would affect the enzymatic activity of ACE2. Surprisingly, SARS-CoV-2 trimeric spike protein increased ACE2 proteolytic activity approximately 3-10 fold against model peptide substrates, such as caspase-1 substrate and Bradykinin-analog. The enhancement in ACE2 enzymatic function was mediated by the binding of SARS-CoV-2 spike RBD domain. These results highlighted the potential for SARS-CoV-2 infection to enhance ACE2 activity, which may be relevant to the cardiovascular symptoms associated with COVID-19. Twit Text FOAVip High affinity binding of SARS-CoV-2 spike protein enhances ACE2 carboxypeptidase activity ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=33122196 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33122196 #FOAvip English Wikipedia <ref>{{Cite pmid|33122196}}</ref> High affinity binding of SARS-CoV-2 spike protein enhances ACE2 carboxypeptidase activity #MMPMID33122196 Lu J; Sun PD J Biol Chem 2020[Dec]; 295 (52): 18579-18588 PMID33122196show ga The novel severe acute respiratory syndrome coronavirus (SARS-CoV-2) has emerged to a pandemic and caused global public health crisis. Human angiotensin-converting enzyme 2(ACE2) was identified as the entry receptor for SARS-CoV-2. As a carboxypeptidase, ACE2 cleaves many biological substrates besides angiotensin II to control vasodilatation and vascular permeability. Given the nanomolar high affinity between ACE2 and SARS-CoV-2 spike protein, we investigated how this interaction would affect the enzymatic activity of ACE2. Surprisingly, SARS-CoV-2 trimeric spike protein increased ACE2 proteolytic activity approximately 3-10 fold against model peptide substrates, such as caspase-1 substrate and Bradykinin-analog. The enhancement in ACE2 enzymatic function was mediated by the binding of SARS-CoV-2 spike RBD domain. These results highlighted the potential for SARS-CoV-2 infection to enhance ACE2 activity, which may be relevant to the cardiovascular symptoms associated with COVID-19. |Angiotensin-Converting Enzyme 2/*metabolism[MESH] |COVID-19/enzymology/*metabolism/virology[MESH] |Humans[MESH] |Protein Binding[MESH] |Protein Domains[MESH] |Proteolysis[MESH] |SARS-CoV-2/*metabolism[MESH] |Spike Glycoprotein, Coronavirus/*metabolism[MESH]High affinity binding of SARS-CoV-2 spike protein enhances ACE2 carbox(epmc).pdf DeepDyve Pubget Overpricing