Iron-enhanced coagulation is attenuated by chelation: A thrombelastographic and ultrastructural analysis

Vance G. Nielsen, Etheresia Pretorius

Research output: Contribution to journalArticlepeer-review

28 Scopus citations


Increased circulating ferritin and free iron have been found in a variety of disease states associated with thrombophilia. When blood or plasma is exposed to iron addition, characteristic changes in thrombus formation are observed by scanning electron microscopy, which include fusion of fibrin polymers, matting, and even sheeting of fibrin. A primary mechanism posited to explain iron-mediated hypercoagulability is hydroxyl radical formation and modification of fibrinogen; however, iron has also been demonstrated to bind to fibrinogen. We have recently demonstrated that iron enhances coagulation, manifested as a decrease in the time of onset of coagulation. Using clinically encountered concentrations of iron created by addition of FeCl3 to human plasma, we demonstrated that iron-mediated changes in reaction time determined by thrombelastography or changes in thrombus ultrastructure were significantly, but not completely, reversed by iron chelation with deferoxamine. Thus, reversible iron binding to fibrinogen mechanistically explains a significant portion of coagulation kinetic and ultrastructural hypercoagulability. Further investigation is needed to determine whether residual iron binding or other iron-mediated effects is responsible for hypercoagulability observed after chelation.

Original languageEnglish (US)
Pages (from-to)845-850
Number of pages6
JournalBlood Coagulation and Fibrinolysis
Issue number8
StatePublished - 2014


  • Coagulation
  • Electron microscopy
  • Iron
  • Thrombelastography

ASJC Scopus subject areas

  • Hematology


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