IMR Press / FBE / Volume 4 / Issue 1 / DOI: 10.2741/e385

Frontiers in Bioscience-Elite (FBE) is published by IMR Press from Volume 13 Issue 2 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on as a courtesy and upon agreement with Frontiers in Bioscience.

Open Access Review

Posttranslational modifications of tissue factor

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1 Department of Biochemistry, College of Medicine, University of Vermont, Burlington, VT, USA

*Author to whom correspondence should be addressed.

Academic Editor: L. Vijaya Mohan Rao

Front. Biosci. (Elite Ed) 2012, 4(1), 381–391;
Published: 1 January 2012

Tissue factor (TF), a membrane protein, is an initiator of blood coagulation in vivo. In this review we discuss how posttranslational modifications affect activity and other properties of TF. Glycosylation of the extracellular domain and the composition of carbohydrates at three glycosylation sites have an influence on TF activity in the extrinsic FXase by increasing the rate of FX proteolysis. No influence of TF glycosylation on the activity of the FVIIa/TF complex towards small synthetic substrates was observed, suggesting that glycosylation has no effect on TF interaction with FVIIa. There are no published data suggesting a direct influence of phosphorylation or palmitoylation in the cytoplasmic domain on TF procoagulant activity. There has been a debate in the recent literature related to the role and formation of the Cys186-Cys209 disulfide bond. Published opinions from various laboratories range from this bond being essential for the expression of cell TF activity to having no role in it. Overall, it is clear that some modifications of TF have an effect on TF procoagulant activity, signaling functions and trafficking. The influences of other modifications are debatable.

Tissue Factor
Factor VIIa
Factor X activation
Carbohydrate composition
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