Protein amyloidose misfolding: mechanisms, detection, and pathological implications.

Published

Journal Article (Review)

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.

Full Text

Duke Authors

Cited Authors

  • Jeyashekar, NS; Sadana, A; Vo-Dinh, T

Published Date

  • January 2005

Published In

Volume / Issue

  • 300 /

Start / End Page

  • 417 - 435

PubMed ID

  • 15657495

Pubmed Central ID

  • 15657495

Electronic International Standard Serial Number (EISSN)

  • 1940-6029

International Standard Serial Number (ISSN)

  • 1064-3745

Digital Object Identifier (DOI)

  • 10.1385/1-59259-858-7:417

Language

  • eng