Amyloid as a natural product
- PMID: 12743097
- PMCID: PMC2172945
- DOI: 10.1083/jcb.200304074
Amyloid as a natural product
Abstract
Amyloid fibrils, such as those found in Alzheimer's and the gelsolin amyloid diseases, result from the misassembly of peptides produced by either normal or aberrant intracellular proteolytic processing. A paper in this issue by Marks and colleagues (Berson et al., 2003) demonstrates that intra-melanosome fibrils are formed through normal biological proteolytic processing of an integral membrane protein. The resulting peptide fragment assembles into fibrils promoting the formation of melanin pigment granules. These results, along with the observation that amyloid fibril formation by bacteria is highly orchestrated, suggest that fibril formation is an evolutionary conserved biological pathway used to generate natural product nanostructures.
Comment on
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Proprotein convertase cleavage liberates a fibrillogenic fragment of a resident glycoprotein to initiate melanosome biogenesis.J Cell Biol. 2003 May 12;161(3):521-33. doi: 10.1083/jcb.200302072. Epub 2003 May 5. J Cell Biol. 2003. PMID: 12732614 Free PMC article.
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- Kim, S.H., J.W. Creemers, S. Chu, G. Thinakaran, and S.S. Sisodia. 2002. Proteolytic processing of familial British dementia-associated BRI variants: evidence for enhanced intracellular accumulation of amyloidogenic peptides. J. Biol. Chem. 277:1872–1877. - PubMed
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