期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 421, 期 2-3, 页码 142-159出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2012.01.024
关键词
protein aggregation; fibrillogenesis; protein folding diseases; amyloid; amyloidoses
资金
- National Institute on Aging [AG 1925901, AG 030027]
The molecular investigation of the amyloidoses began in the mid-19th century with the observation of areas in human tissues obtained at autopsy that were homogeneous and eosinophilic with conventional stains but became blue when exposed to mixtures of iodine and sulfuric acid. The foci corresponded to regions formerly identified as waxy or lardaceous. Subsequent identification of the characteristic staining of the same tissues with metachromatic dyes such as crystal violet or with the cotton dye Congo red (particularly under polarized light) and thioflavins allowed the pathological classification of those tissues as belonging to a set of disorders known as the amyloidoses. Not unexpectedly, progress has reflected evolving technology and parallel advances in all fields of biological science. Investigation using contemporary methods has expanded our notions of amyloid proteins from being simply agents or manifestations of systemic, largely extracellular diseases to include protein-only infection, the concept that normal functional amyloids might exist in eukaryotes and prokaryotes and that aggregatability may be an intrinsic structural price to be paid for some functional protein domains. We now distinguish between the amyloidoses, that is, diseases caused by the deposition of amyloid fibrils and amyloid proteins (i.e., purified or recombinant proteins that form amyloid fibrils in vitro), which may or may not be associated with disease in vivo. (C) 2012 Elsevier Ltd. All rights reserved.
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