Tissue factor: mechanisms of decryption.
It is generally believed that only a small fraction of the tissue factor (TF) found on cell surfaces is active whereas the vast majority is cryptic in coagulation. It is unclear how cryptic TF differs from the coagulant active TF or potential mechanisms involved in transformation of cryptic TF to the coagulant active form. Exposure of phosphatidylserine (PS) in response to various chemical or pathophysiological stimuli has been considered as the most potent inducer of TF decryption. In addition to PS, TF self-association and association with specialized membrane domains may also play a role in TF decryption. It has been suggested recently that protein disulfide isomerase regulates TF decryption through its oxidoreductase activity by targeting Cys186-Cys209 disulfide bond in TF extracellular domain or regulating the PS equilibrium at the plasma membrane. However, this hypothesis requires further validation to become an accepted mechanism. In this article, we critically review literature on TF encryption/decryption with specific emphasis on recently published data and provide our perspective on this subject.
Center for Biomedical Research, The University of Texas Health Science Center at Tyler, Tyler, Texas 75708, USA. vijay.rao@uthct.edu
L Vijaya Mohan
LV
Rao
Hema
H
Kothari
Usha R
UR
Pendurthi
D015942:Factor VIIa / Q000378:metabolism; D006801:Humans; D008565:Membrane Proteins / Q000502:physiology; D015398:Signal Transduction; D013925:Thromboplastin / Q000502:physiology*
D008565:Membrane Proteins; D013925:Thromboplastin; D015942:Factor VIIa