Hasam Madarati, Veronica DeYoung, Kanwal Singh, Taylor Sparring, Andrew C Kwong, James C Fredenburgh, Cherie Teney, Marlys L Koschinsky, Michael B Boffa, Jeffrey I Weitz, Colin A Kretz
ADAMTS13, a disintegrin and metalloprotease with a thrombospondin type 1 motif, member 13, regulates the length of Von Willebrand factor (VWF) multimers and their platelet-binding activity. ADAMTS13 is constitutively secreted as an active protease and is not inhibited by circulating protease inhibitors. Therefore, the mechanisms that regulate ADAMTS13 protease activity are unknown. We performed an unbiased proteomics screen to identify ligands of ADAMTS13 by optimizing the application of BioID to plasma. Plasma BioID identified 5 plasma proteins significantly labeled by the ADAMTS13-birA* fusion, including VWF and plasminogen...
April 20, 2024: Scientific Reports