[HTML][HTML] Tissue factor coagulant function is enhanced by protein-disulfide isomerase independent of oxidoreductase activity
HH Versteeg, W Ruf - Journal of Biological Chemistry, 2007 - ASBMB
Protein-disulfide isomerase (PDI) switches tissue factor (TF) from coagulation to signaling by
targeting the allosteric Cys 186–Cys 209 disulfide. Here, we further characterize the
interaction of purified PDI with TF. We find that PDI enhances factor VIIa-dependent
substrate factor X activation 5–10-fold in the presence of wild-type, oxidized soluble TF but
not TF mutants that contain an unpaired Cys 186 or Cys 209. PDI-accelerated factor Xa
generation was blocked by bacitracin but not influenced by inhibition of vicinal thiols …
targeting the allosteric Cys 186–Cys 209 disulfide. Here, we further characterize the
interaction of purified PDI with TF. We find that PDI enhances factor VIIa-dependent
substrate factor X activation 5–10-fold in the presence of wild-type, oxidized soluble TF but
not TF mutants that contain an unpaired Cys 186 or Cys 209. PDI-accelerated factor Xa
generation was blocked by bacitracin but not influenced by inhibition of vicinal thiols …