Apolipoprotein A-I induced amyloidosis |
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Authors: | Janine Genschel Regina Haas Marcus J Prpsting Hartmut H -J Schmidt |
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Institution: | Janine Genschel, Regina Haas, Marcus J. Pröpsting,Hartmut H. -J. Schmidt |
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Abstract: | 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. |
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Keywords: | Apolipoprotein A-I Mutation Amyloidosis Lipoprotein In vivo metabolism Proteolysis |
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