Primary haemostasis: newer insights

Haemophilia. 2014 May:20 Suppl 4:15-22. doi: 10.1111/hae.12427.

Abstract

At the same time as biophysical and omics approaches are drilling deeper into the molecular details of platelets and other blood cells, as well as their receptors and mechanisms of regulation, there is also an increasing awareness of the functional overlap between human vascular systems. Together, these studies are redefining the intricate networks linking haemostasis and thrombosis with inflammation, infectious disease, cancer/metastasis and other vascular pathophysiology. The focus of this state-of-the-art review is some of the newer advances relevant to primary haemostasis. Of particular interest, platelet-specific primary adhesion-signalling receptors and associated activation pathways control platelet function in flowing blood and provide molecular links to other systems. Platelet glycoprotein (GP)Ibα of the GPIb-IX-V complex and GPVI not only initiate platelet aggregation and thrombus formation by primary interactions with von Willebrand factor and collagen, respectively, but are also involved in coagulation, leucocyte engagement, bacterial or viral interactions, and are relevant as potential risk markers in a range of human diseases. Understanding these systems in unprecedented detail promises significant advances in evaluation of individual risk, in new diagnostic or therapeutic possibilities and in monitoring the response to drugs or other treatment.

Keywords: Clec-2; arterial thrombosis; glycoprotein Ib; glycoptrotein VI; venous thrombosis; von Willebrand factor.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Blood Platelets / physiology
  • Cell Communication
  • Hemostasis / physiology*
  • Humans
  • Leukocytes / physiology
  • Ligands
  • Platelet Adhesiveness / physiology
  • Platelet Glycoprotein GPIb-IX Complex / metabolism
  • Protein Binding
  • Signal Transduction

Substances

  • Ligands
  • Platelet Glycoprotein GPIb-IX Complex
  • adhesion receptor
  • glycocalicin