淀粉样变性
载脂蛋白B
淀粉样蛋白(真菌学)
突变
载脂蛋白E
医学
淀粉样纤维
遗传学
发病机制
生物
疾病
生物信息学
病理
基因
内分泌学
淀粉样β
胆固醇
作者
Natasha Jeraj,Robert A. Hegele,Amanda J. Berberich
出处
期刊:Current Opinion in Lipidology
[Ovid Technologies (Wolters Kluwer)]
日期:2020-12-31
卷期号:32 (2): 132-140
被引量:4
标识
DOI:10.1097/mol.0000000000000736
摘要
Amyloidosis is caused by the deposition of misfolded aggregated proteins called amyloid fibrils that in turn cause organ damage and dysfunction. In this review, we aim to summarize the genetic, clinical, and histological findings in apolipoprotein-associated hereditary amyloidosis and the growing list of mutations and apolipoproteins associated with this disorder. We also endeavor to summarize the features of apolipoproteins that have led them to be overrepresented among amyloidogenic proteins. Additionally, we aim to distinguish mutations leading to amyloidosis from those that lead to inherited dyslipidemias.Apolipoproteins are becoming increasingly recognized in hereditary forms of amyloidosis. Although mutations in APOA1 and APOA2 have been well established in hereditary amyloidosis, new mutations are still being detected, providing further insight into the pathogenesis of apolipoprotein-related amyloidosis. Furthermore, amyloidogenic mutations in APOC2 and APOC3 have more recently been described. Although no hereditary mutations in APOE or APOA4 have been described to date, both protein products are amyloidogenic and frequently found within amyloid deposits.Understanding the underlying apolipoprotein mutations that contribute to hereditary amyloidosis may help improve understanding of this rare but serious disorder and could open the door for targeted therapies and the potential development of new treatment options.
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