Apolipoprotein A‐I induced amyloidosis

FEBS Letters

Genschel, Janine¹  Schmidt, Hartmut H.-J¹  Pröpsting, Marcus J¹  Haas, Regina¹ 

[1] Abteilung Gastroenterologie und Hepatologie, OE 6852, Medizinische Hochschule Hannover, D-30623 Hannover, Germany

关键词: Apolipoprotein A-I;    Mutation;    Amyloidosis;    Lipoprotein;    In vivo metabolism;    Proteolysis;   

DOI  :  10.1016/S0014-5793(98)00668-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Amyloidosis is characterized by extracellular deposits of protein fibrils with a high content of β-sheets in secondary structure. The protein forms together with proteoglycans amyloid fibrils causing organ damage and serious morbidity. Intact apolipoprotein A-I (apoA-I) is an important protein in lipid metabolism regulating the synthesis and catabolism of high density lipoproteins (HDL). Usually, apoA-I is not associated with amyloidosis. However, four naturally occuring mutant forms of apoA-I are known so far resulting in amyloidosis. The most important feature of all variants is the very similar formation of N-terminal fragments which were found in the amyloid deposits (residues 1–83 to 1–94). The new insights in the understanding of the association of apoA-I with HDL, its metabolism, and its hypothesized structural findings may explain a common mechanism for the genesis of apoA-I induced amyloidosis. Here we summarized the specific features of all known amyloidogenic variants of apoA-I and speculate about its metabolic pathway, which may have general implications for the metabolism of apoA-I.

【 授权许可】

Unknown