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From Proteopedia
Amyloid fibril from human systemic AA amyloidosis (vascular variant)
Structural highlights
DiseaseSAA1_HUMAN Secondary amyloidosis. Reactive, secondary amyloidosis is characterized by the extracellular accumulation in various tissues of the SAA1 protein. These deposits are highly insoluble and resistant to proteolysis; they disrupt tissue structure and compromise function. Elevated serum SAA1 protein levels may be associated with lung cancer. FunctionSAA1_HUMAN Major acute phase reactant. Apolipoprotein of the HDL complex. Publication Abstract from PubMedSystemic AA amyloidosis is a debilitating protein misfolding disease in humans and animals. In humans, it occurs in two variants that are called 'vascular' and 'glomerular', depending on the main amyloid deposition site in the kidneys. Using cryo electron microscopy, we here show the amyloid fibril structure underlying the vascular disease variant. Fibrils purified from the tissue of such patients are mainly left-hand twisted and contain two non-equal stacks of fibril proteins. They contrast in these properties to the fibrils from the glomerular disease variant which are right-hand twisted and consist of two structurally equal stacks of fibril proteins. Our data demonstrate that the different disease variants in systemic AA amyloidosis are associated with different fibril morphologies. Amyloid fibril structure from the vascular variant of systemic AA amyloidosis.,Banerjee S, Baur J, Daniel C, Pfeiffer PB, Hitzenberger M, Kuhn L, Wiese S, Bijzet J, Haupt C, Amann KU, Zacharias M, Hazenberg BPC, Westermark GT, Schmidt M, Fandrich M Nat Commun. 2022 Nov 25;13(1):7261. doi: 10.1038/s41467-022-34636-4. PMID:36433936[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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