Complete abolishment of coagulant activity in monomeric disulfide-deficient tissue factor.

نویسندگان

  • Lisa G van den Hengel
  • Begüm Kocatürk
  • Pieter H Reitsma
  • Wolfram Ruf
  • Henri H Versteeg
چکیده

previous PV diagnosis, achieved at least CCyR. In summary, in this larger cohort of CML patients compared with that studied by Makishima et al,1 we found 2.55% of cases presenting concomitant BCR/ABL rearrangement and JAK2V617F mutation, indicating that the simultaneous occurrence of these mutations is rare event but it is not a phoenix; however, while the pathophysiologic significance of this double mutated phenotype remains to be clarified, it seems clear that the predominant clinical phenotype is, in most cases, that of a typical BCR-ABL rearranged CML.

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Tissue factor coagulant function is enhanced by protein-disulfide isomerase independent of oxidoreductase activity.

Protein-disulfide isomerase (PDI) switches tissue factor (TF) from coagulation to signaling by targeting the allosteric Cys186-Cys209 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...

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عنوان ژورنال:
  • Blood

دوره 118 12  شماره 

صفحات  -

تاریخ انتشار 2011