ジャーナル: J Mol Biol / 年: 2023 タイトル: The Cryo-EM STRUCTURE of Renal Amyloid Fibril Suggests Structurally Homogeneous Multiorgan Aggregation in AL Amyloidosis. 著者: Sarita Puri / Tim Schulte / Antonio Chaves-Sanjuan / Giulia Mazzini / Serena Caminito / Carlo Pappone / Luigi Anastasia / Paolo Milani / Giampaolo Merlini / Martino Bolognesi / Mario Nuvolone ...著者: 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 / 要旨: 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.
分子量: 23326.557 Da / 分子数: 5 / 変異: No / 由来タイプ: 天然 / 由来: (天然) Homo sapiens (ヒト) / 器官: Kidney
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実験情報
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実験
実験
手法: 電子顕微鏡法
EM実験
試料の集合状態: FILAMENT / 3次元再構成法: らせん対称体再構成法
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試料調製
構成要素
名称: Renal AL55 amyloid fibrils / タイプ: COMPLEX 詳細: Light chain amyloid fibrils named AL55 extracted from the kidney of an AL amyloidosis patient Entity ID: all / 由来: NATURAL