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10.1038/s41598-021-91231-1 http://scihub22266oqcxt.onion/10.1038/s41598-021-91231-1 34108510!8190434!34108510     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=34108510&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Sci+Rep 2021 ; 11 (1): 12157 Nephropedia Template TP {{tp|p=34108510|t=2021. Endothelial glycocalyx shields the interaction of SARS-CoV-2 spike protein with ACE2 receptors |pdf=|usr=}}{{34108510}} gab.com Text Endothelial glycocalyx shields the interaction of SARS-CoV-2 spike protein with ACE2 receptors JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=34108510 #FOAvip Endothelial cells (ECs) play a crucial role in the development and propagation of the severe COVID-19 stage as well as multiorgan dysfunction. It remains, however, controversial whether COVID-19-induced endothelial injury is caused directly by the infection of ECs with SARS-CoV-2 or via indirect mechanisms. One of the major concerns is raised by the contradictory data supporting or denying the presence of ACE2, the SARS-CoV-2 binding receptor, on the EC surface. Here, we show that primary human pulmonary artery ECs possess ACE2 capable of interaction with the viral Spike protein (S-protein) and demonstrate the crucial role of the endothelial glycocalyx in the regulation of the S-protein binding to ACE2 on ECs. Using force spectroscopy method, we directly measured ACE2- and glycocalyx-dependent adhesive forces between S-protein and ECs and characterized the nanomechanical parameters of the cells exposed to S-protein. We revealed that the intact glycocalyx strongly binds S-protein but screens its interaction with ACE2. Reduction of glycocalyx layer exposes ACE2 receptors and promotes their interaction with S-protein. These results indicate that the susceptibility of ECs to COVID-19 infection may depend on the glycocalyx condition. Twit Text FOAVip Endothelial glycocalyx shields the interaction of SARS-CoV-2 spike protein with ACE2 receptors ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=34108510 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34108510 #FOAvip English Wikipedia <ref>{{Cite pmid|34108510}}</ref> Endothelial glycocalyx shields the interaction of SARS-CoV-2 spike protein with ACE2 receptors #MMPMID34108510 Targosz-Korecka M; Kubisiak A; Kloska D; Kopacz A; Grochot-Przeczek A; Szymonski M Sci Rep 2021[Jun]; 11 (1): 12157 PMID34108510show ga Endothelial cells (ECs) play a crucial role in the development and propagation of the severe COVID-19 stage as well as multiorgan dysfunction. It remains, however, controversial whether COVID-19-induced endothelial injury is caused directly by the infection of ECs with SARS-CoV-2 or via indirect mechanisms. One of the major concerns is raised by the contradictory data supporting or denying the presence of ACE2, the SARS-CoV-2 binding receptor, on the EC surface. Here, we show that primary human pulmonary artery ECs possess ACE2 capable of interaction with the viral Spike protein (S-protein) and demonstrate the crucial role of the endothelial glycocalyx in the regulation of the S-protein binding to ACE2 on ECs. Using force spectroscopy method, we directly measured ACE2- and glycocalyx-dependent adhesive forces between S-protein and ECs and characterized the nanomechanical parameters of the cells exposed to S-protein. We revealed that the intact glycocalyx strongly binds S-protein but screens its interaction with ACE2. Reduction of glycocalyx layer exposes ACE2 receptors and promotes their interaction with S-protein. These results indicate that the susceptibility of ECs to COVID-19 infection may depend on the glycocalyx condition. |Angiotensin-Converting Enzyme 2/*metabolism[MESH] |Endothelial Cells/*cytology/metabolism[MESH] |Glycocalyx/*metabolism[MESH] |Humans[MESH] |Protein Binding[MESH] |Pulmonary Artery/cytology[MESH]Endothelial glycocalyx shields the interaction of SARS-CoV-2 spike pro(epmc).pdf DeepDyve Pubget Overpricing