The Cryo-EM structure of renal amyloid fibril suggests structurally homogeneous multiorgan aggregation in AL amyloidosis
Articolo
Data di Pubblicazione:
2023
Citazione:
The Cryo-EM structure of renal amyloid fibril suggests structurally homogeneous multiorgan aggregation in AL amyloidosis / S. Sarita, T. Schulte, A. Chaves-Sanjuan, G. Mazzini, S. Caminito, C. Pappone, L. Anastasia, P. Milani, G. Merlini, M. Bolognesi, M. Nuvolone, G. Palladini, S. Ricagno. - In: JOURNAL OF MOLECULAR BIOLOGY. - ISSN 0022-2836. - 435:18(2023 Sep 15), pp. 168215.1-168215.8. [10.1016/j.jmb.2023.168215]
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 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 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.
Tipologia IRIS:
01 - Articolo su periodico
Keywords:
AL amyloidosis; Light chains; amyloid-fibril structure; cryo-electron microscopy; multiorgan fibril deposition
Elenco autori:
S. Sarita, T. Schulte, A. Chaves-Sanjuan, G. Mazzini, S. Caminito, C. Pappone, L. Anastasia, P. Milani, G. Merlini, M. Bolognesi, M. Nuvolone, G. Palladini, S. Ricagno
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