{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Pruss CM"],"funding":["NHLBI NIH HHS","CIHR"],"pagination":["940-50"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5962034"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["10(5)"],"pubmed_abstract":["<h4>Background</h4>von Willebrand Factor (VWF) is tightly regulated by the metalloproteinase ADAMTS13, which cleaves VWF to reduce VWF multimer size and binding affinity for collagen and platelets.<h4>Objective</h4>This study examines two VWF mutations, R1597W (enhanced cleavage) and Y1605A-M1606A (decreased cleavage), to determine their impact on VWF, in addition to ADAMTS13-mediated cleavage.<h4>Methods</h4>In vitro mouse ADAMTS13 digestions were performed on recombinant proteins. VWF knockout mice received hydrodynamic injections of mouse Vwf cDNA, following which VWF antigen, multimer profile and VWF propeptide levels were determined. A ferric chloride injury model of thrombosis was also evaluated.<h4>Results</h4>In vitro ADAMTS13 digestion of full-length mouse VWF required > 97-fold h"],"journal":["Journal of thrombosis and haemostasis : JTH"],"pubmed_title":["Use of a mouse model to elucidate the phenotypic effects of the von Willebrand factor cleavage mutants, Y1605A/M1606A and R1597W."],"pmcid":["PMC5962034"],"funding_grant_id":["HL081588","P01 HL081588","MOP-97849"],"pubmed_authors":["Hegadorn C","Pruss CM","Bryant A","Golder M","Lillicrap D","Haberichter S"],"additional_accession":[]},"is_claimable":false,"name":"Use of a mouse model to elucidate the phenotypic effects of the von Willebrand factor cleavage mutants, Y1605A/M1606A and R1597W.","description":"<h4>Background</h4>von Willebrand Factor (VWF) is tightly regulated by the metalloproteinase ADAMTS13, which cleaves VWF to reduce VWF multimer size and binding affinity for collagen and platelets.<h4>Objective</h4>This study examines two VWF mutations, R1597W (enhanced cleavage) and Y1605A-M1606A (decreased cleavage), to determine their impact on VWF, in addition to ADAMTS13-mediated cleavage.<h4>Methods</h4>In vitro mouse ADAMTS13 digestions were performed on recombinant proteins. VWF knockout mice received hydrodynamic injections of mouse Vwf cDNA, following which VWF antigen, multimer profile and VWF propeptide levels were determined. A ferric chloride injury model of thrombosis was also evaluated.<h4>Results</h4>In vitro ADAMTS13 digestion of full-length mouse VWF required > 97-fold h","dates":{"release":"2012-01-01T00:00:00Z","publication":"2012 May","modification":"2025-04-25T18:25:47.149Z","creation":"2019-03-26T23:38:15Z"},"accession":"S-EPMC5962034","cross_references":{"pubmed":["22372972"],"doi":["10.1111/j.1538-7836.2012.04675.x"]}}