Physiological responses to protein aggregates: Fibrinolysis, coagulation and inflammation (new roles for old factors)

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 reco...

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Bibliographic Details
Published in:FEBS letters 2009-08, Vol.583 (16), p.2691-2699
Main Authors: Gebbink, Martijn F.B.G., Bouma, Barend, Maas, Coen, Bouma, Bonno N.
Format: Article
Language:English
Subjects:
Amyloid
Blood Coagulation
Bradykinin - metabolism
Crossbeta
Factor XII - metabolism
Fibrinolysis
Fibronectins - metabolism
Haemostasis
Hemostasis
Humans
Inflammation - metabolism
Kallikreins - metabolism
Kinins - metabolism
Misfolding
Protein Folding
Proteins - metabolism
Tissue Plasminogen Activator - metabolism
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/j.febslet.2009.06.013