How our bodies fight amyloidosis: effects of physiological factors on pathogenic aggregation of amyloidogenic proteins.

Abstract

The process of protein aggregation from soluble amyloidogenic proteins to insoluble amyloid fibrils plays significant roles in the onset of over 30 human amyloidogenic diseases, such as Prion disease, Alzheimer's disease and type 2 diabetes mellitus. Amyloid deposits are commonly found in patients suffered from amyloidosis; however, such deposits are rarely seen in healthy individuals, which may be largely attributed to the self-regulation in vivo. A vast number of physiological factors have been demonstrated to directly affect the process of amyloid formation in vivo. In this review, physiological factors that influence amyloidosis, including biological factors (chaperones, natural antibodies, enzymes, lipids and saccharides) and physicochemical factors (metal ions, pH environment, crowding and pressure, etc.), together with the mechanisms underlying these proteostasis effects, are summarized.

• Authors: Lianqi Huang, Xinran Liu, Biao Cheng, Kun Huang
• Journal: Archives of biochemistry and biophysics (Arch Biochem Biophys) Vol. 568 Pg. 46-55 (Feb 15 2015) ISSN: 1096-0384 [Electronic] United States
• PMID: 25615529 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Review)
• Copyright: Copyright © 2015 Elsevier Inc. All rights reserved.

Chemical References

• Amyloid
• Amyloidogenic Proteins
• Metals
• Molecular Chaperones

Topics

• Alzheimer Disease (metabolism)
• Amyloid (analysis, metabolism)
• Amyloidogenic Proteins (analysis, metabolism)
• Amyloidosis (metabolism)
• Animals
• Diabetes Mellitus, Type 2 (metabolism)
• Humans
• Metals (analysis, metabolism)
• Models, Molecular
• Molecular Chaperones (analysis, metabolism)
• Prion Diseases (metabolism)
• Protein Aggregation, Pathological (metabolism)