Proteomics

Dataset Information

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Protease-sensitive regions in amyloid light chains: what a common pattern of fragmentation across organs suggests about aggregation


ABSTRACT: In this study we aimed to provide a detailed comparative description of the fragmentation sites of amyloid LCs in multiple organs of an individual patient.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Kidney, Subcutaneous Adipose Tissue

DISEASE(S): Amyloidosis

SUBMITTER: Giulia Mazzini  

LAB HEAD: Giovanni Palladini

PROVIDER: PXD025185 | Pride | 2022-08-12

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
AL55_fat.mgf Mgf
AL55_fat.pep.xml Pepxml
AL55_fat.raw Raw
AL55_fat.zip Other
AL55_fat_Cterm.mgf Mgf
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Publications

Protease-sensitive regions in amyloid light chains: what a common pattern of fragmentation across organs suggests about aggregation.

Mazzini Giulia G   Ricagno Stefano S   Caminito Serena S   Rognoni Paola P   Milani Paolo P   Nuvolone Mario M   Basset Marco M   Foli Andrea A   Russo Rosaria R   Merlini Giampaolo G   Palladini Giovanni G   Lavatelli Francesca F  

The FEBS journal 20210915 2


Light-chain (AL) amyloidosis is characterized by deposition of immunoglobulin light chains (LC) as fibrils in target organs. Alongside the full-length protein, abundant LC fragments are always present in AL deposits. Herein, by combining gel-based and mass spectrometry analyses, we identified and compared the fragmentation sites of amyloid LCs from multiple organs of an AL λ amyloidosis patient (AL-55). The positions pinpointed here in kidney and subcutaneous fat, alongside those previously dete  ...[more]

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