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Physiological responses to protein aggregates: Fibrinolysis, coagulation and inflammation (new roles for old factors)
Author(s) -
Gebbink Martijn F.B.G.,
Bouma Barend,
Maas Coen,
Bouma Bonno N.
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.06.013
Subject(s) - protein aggregation , protein folding , fibrinolysis , proteases , inflammation , coagulation , immunogenicity , chemistry , biology , microbiology and biotechnology , biochemistry , immunology , medicine , immune system , psychiatry , enzyme
Misfolding is an inherent and potentially problematic propensity of proteins. Misfolded proteins tend to aggregate and the deposition of aggregated proteins is associated with a variety of highly debilitating diseases known as amyloidoses. Protein misfolding and aggregation is also increasingly recognized as the underlying cause of other health problems, including atherosclerosis and immunogenicity of biopharmaceuticals. This raises the question how nature deals with the removal of obsolete proteins in order to avoid their accumulation and disease. In recent years two proteases, tPA and factor XII, have been identified that specifically recognize aggregates of misfolded proteins. We here review these discoveries that have uncovered new roles for the fibrinolytic system and the contact activation system beyond haemostasis.