<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Ding Q</submitter><funding>National Heart, Lung, and Blood Institute of the National Institute of Health</funding><funding>NHLBI NIH HHS</funding><pagination>614-24</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3634890</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>109(4)</volume><pubmed_abstract>Protein C is a vitamin K-dependent serine protease zymogen in plasma which upon activation to activated protein C (APC) by thrombin down-regulates the clotting cascade by limited proteolysis of the procoagulant cofactors Va and VIIIa. In addition to its anticoagulant activity, APC also exhibits potent cytoprotective and anti-inflammatory activities. While the anticoagulant activity of APC is enhanced by the cofactor function of protein S on membrane phospholipids, the cytoprotective intracellular signalling activity of APC requires complex formation with endothelial protein C receptor (EPCR) expressed on the vascular endothelium. Two natural variants of APC [Arg-147 to Trp substitution (R147W) and Lys-150 deletion (K150del)] have been identified in the Chinese population as hotspot mutants</pubmed_abstract><journal>Thrombosis and haemostasis</journal><pubmed_title>Expression and functional characterisation of natural R147W and K150del variants of protein C in the Chinese population.</pubmed_title><pmcid>PMC3634890</pmcid><funding_grant_id>R01 HL101917</funding_grant_id><funding_grant_id>R01 HL062565</funding_grant_id><funding_grant_id>(HL 101917 and HL 62565 to ARR)</funding_grant_id><pubmed_authors>Yang L</pubmed_authors><pubmed_authors>Hassanian SM</pubmed_authors><pubmed_authors>Ding Q</pubmed_authors><pubmed_authors>Rezaie AR</pubmed_authors></additional><is_claimable>false</is_claimable><name>Expression and functional characterisation of natural R147W and K150del variants of protein C in the Chinese population.</name><description>Protein C is a vitamin K-dependent serine protease zymogen in plasma which upon activation to activated protein C (APC) by thrombin down-regulates the clotting cascade by limited proteolysis of the procoagulant cofactors Va and VIIIa. In addition to its anticoagulant activity, APC also exhibits potent cytoprotective and anti-inflammatory activities. While the anticoagulant activity of APC is enhanced by the cofactor function of protein S on membrane phospholipids, the cytoprotective intracellular signalling activity of APC requires complex formation with endothelial protein C receptor (EPCR) expressed on the vascular endothelium. Two natural variants of APC [Arg-147 to Trp substitution (R147W) and Lys-150 deletion (K150del)] have been identified in the Chinese population as hotspot mutants</description><dates><release>2013-01-01T00:00:00Z</release><publication>2013 Apr</publication><modification>2025-04-19T09:06:16.92Z</modification><creation>2019-03-27T01:07:49Z</creation></dates><accession>S-EPMC3634890</accession><cross_references><pubmed>23389250</pubmed><doi>10.1160/TH12-10-0760</doi><doi>10.1160/th12-10-0760</doi></cross_references></HashMap>