Could Some Nonhemostatic Plasma Proteins Serve as Refuse Collectors for Fibrin(ogen)?

  title={Could Some Nonhemostatic Plasma Proteins Serve as Refuse Collectors for Fibrin(ogen)?},
  author={Rustem I. Litvinov and John W. Weisel},
  journal={Thrombosis and haemostasis},
In the October issue of Thrombosis and Haemostasis, Talens et al1 proposed a general physiological role for certain plasma proteins previously shown to bind strongly but noncovalently to fibrinogen and/or fibrin. After excluding the proteins with known hemostatic activities, the authors recognized that some of the remainingfibrin-bound proteins (clusterin, haptoglobin,α2-macroglobulin, apolipoproteins E and AI, albumin, serum amyloid P, and α1-antitrypsin) belong to a familyof “extracellular… 

Rupture of blood clots: Mechanics and pathophysiology

Toughness, i.e., resistance to rupture, quantified by the critical energy release rate of physiologically relevant fibrin gels was determined to be 7.6 ± 0.45 J/m2, and it was shown that breaking of fibers ahead the crack at a critical stretch is the mechanism of rupture of blood clots, including thrombotic embolization.



Decoration of Fibrin with Extracellular Chaperones.

Fibrin clots generated in plasma are decorated with extracellular chaperones, which indicates that cross-β structures in unfolded fibrin(ogen) are involved in clot binding of the proteins, which supports the chaperone hypothesis.

Extracellular chaperones and proteostasis.

It is critically important to further increase the understanding of the mechanisms that operate to effect extracellular proteostasis, as this is essential knowledge upon which to base the development of effective therapies for some of the world's most debilitating, costly, and intractable diseases.