纤维
淀粉样变性
淀粉样蛋白(真菌学)
发病机制
淀粉样纤维
血清淀粉样蛋白A
淀粉样变性
蛋白质折叠
化学
医学
疾病
炎症
生物化学
病理
免疫学
淀粉样β
家族性地中海热
作者
Gunilla T. Westermark,Marcus Fändrich,Per Westermark
出处
期刊:Annual Review of Pathology-mechanisms of Disease
[Annual Reviews]
日期:2014-11-11
卷期号:10 (1): 321-344
被引量:227
标识
DOI:10.1146/annurev-pathol-020712-163913
摘要
The understanding of why and how proteins misfold and aggregate into amyloid fibrils has increased considerably during recent years. Central to amyloid formation is an increase in the frequency of the β-sheet structure, leading to hydrogen bonding between misfolded monomers and creating a fibril that is comparably resistant to degradation. Generation of amyloid fibrils is nucleation dependent, and once formed, fibrils recruit and catalyze the conversion of native molecules. In AA amyloidosis, the expression of cytokines, particularly interleukin 6, leads to overproduction of serum amyloid A (SAA) by the liver. A chronically high plasma concentration of SAA results in the aggregation of amyloid into cross-β-sheet fibrillar deposits by mechanisms not fully understood. Therefore, AA amyloidosis can be thought of as a consequence of long-standing inflammatory disease. This review summarizes current knowledge about AA amyloidosis. The systemic amyloidoses have been regarded as intractable conditions, but improvements in the understanding of fibril composition and pathogenesis over the past decade have led to the development of a number of different therapeutic approaches with promising results.
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