NR ARQL
AU Jeyashekar,N.S.; Sadana,A.; Vo-Dinh,T.
TI Protein amyloidose misfolding: mechanisms, detection, and pathological implications.
QU Methods in Molecular Biology 2005; 300: 417-35
PT journal article; review; review, tutorial
AB A variety of diseases result because of misfolded protein that deposits in extracellular space in the body. These deposits can be amorphous (disordered) or fibrillar (ordered). Inclusion bodies are an example of amorphous aggregates, and amyloid fibril is an example of fibrillar or ordered aggregates. In this chapter, we discuss a class of diseases caused by fibrillar aggregate deposits or amyloid fibrils called amyloidosis. We also review mechanisms by which different proteins misfold to form amyloid fibrils. Each amyloid fibril formed from a different protein causes a different disease by affecting a different organ in the body. However, the characteristics of different amyloid fibrils, namely structure and morphology, observed by electron microscopy and X-ray fiber diffraction appear to be quite similar in nature. We present therapeutic strategies developed to eliminate amyloid fibril formation. These strategies could possibly avert a whole class of fatal diseases caused by amyloid fibril deposition owing to similar characteristics of the amyloid fibrils.
ZR 25
MH Alzheimer Disease/metabolism; Amyloid/chemistry/*metabolism/ultrastructure; Amyloid beta-Protein/metabolism; Animals; Humans; Microscopy, Electron; Muramidase/chemistry/metabolism/ultrastructure; Peptide Fragments/metabolism; Prealbumin/metabolism/ultrastructure; Prions/metabolism; *Protein Folding; X-Ray Diffraction
AD Chemical Engineering Department, University of Mississippi, Oak Ridge, TN, USA
SP englisch
PO USA