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Title | The Cryo-EM STRUCTURE of Renal Amyloid Fibril Suggests Structurally Homogeneous Multiorgan Aggregation in AL Amyloidosis. |
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Journal, issue, pages | J Mol Biol, Vol. 435, Issue 18, Page 168215, Year 2023 |
Publish date | Jul 27, 2023 |
Authors | Sarita Puri / Tim Schulte / Antonio Chaves-Sanjuan / Giulia Mazzini / Serena Caminito / Carlo Pappone / Luigi Anastasia / Paolo Milani / Giampaolo Merlini / Martino Bolognesi / Mario Nuvolone / Giovanni Palladini / Stefano Ricagno / |
PubMed Abstract | Immunoglobulin light chain amyloidosis (AL) is caused by the aberrant production of amyloidogenic light chains (LC) that accumulate as amyloid deposits in vital organs. Distinct LC sequences in each ...Immunoglobulin light chain amyloidosis (AL) is caused by the aberrant production of amyloidogenic light chains (LC) that accumulate as amyloid deposits in vital organs. Distinct LC sequences in each patient yield distinct amyloid structures. However different tissue microenvironments may also cause identical protein precursors to adopt distinct amyloid structures. To address the impact of the tissue environment on the structural polymorphism of amyloids, we extracted fibrils from the kidney of an AL patient (AL55) whose cardiac amyloid structure was previously determined by our group. Here we show that the 4.0 Å resolution cryo-EM structure of the renal fibril is virtually identical to that reported for the cardiac fibril. These results provide the first structural evidence that LC amyloids independently deposited in different organs of the same AL patient share a common fold. |
External links | J Mol Biol / PubMed:37516426 |
Methods | EM (helical sym.) |
Resolution | 4.0 Å |
Structure data | EMDB-16780, PDB-8cpe: |
Source |
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Keywords | PROTEIN FIBRIL / Light chains / Amyloid fibrils / AL amyloidosis. |