Control of Von Willebrand Factor Multimer Size by Thrombospondin-1

@article{Xie2001ControlOV,
  title={Control of Von Willebrand Factor Multimer Size by Thrombospondin-1},
  author={Lijuan Xie and Colin N. Chesterman and Philip J Hogg},
  journal={The Journal of Experimental Medicine},
  year={2001},
  volume={193},
  pages={1341 - 1350}
}
Plasma von Willebrand factor (vWF) is a multimeric protein that mediates adhesion of platelets to sites of vascular injury. Only the very large vWF multimers are effective in promoting platelet adhesion in flowing blood. A protein disulfide bond reductase in plasma reduces the average multimer size of vWF secreted by endothelial cells. This activity has been isolated from human endothelial cell conditioned medium and shown to be the trimeric glycoprotein, thrombospondin-1 (TSP-1). Incubation of… CONTINUE READING
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The protein disulfideisomerase family: unravelling a string of folds

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