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A mouse model of cardiac immunoglobulin light chain amyloidosis reveals insights into tissue accumulation and toxicity of amyloid fibrils

The pathophysiology of Amyloid light-chain (AL) amyloidosis remains poorly understood due to the lack of reliable in vivo models. Here, the authors describe a transgenic mouse model that reproduces cardiac AL amyloidosis and provides new information on the formation of AL amyloid fibrils.

Gemma Martinez-Rivas
Maria Victoria Ayala
Christophe Sirac
ResearchOpen Access27 Mar 2025
Nature Communications

Volume: 16, P: 1-16
Cryo-EM structure of cardiac amyloid fibrils from an immunoglobulin light chain AL amyloidosis patient

Immunoglobulin Light Chain Amyloidosis (AL) is the most common systemic amyloidosis occurring in Western countries. Here the authors present the 4.0 Å cryo-EM structure of light chain AL55 fibrils that were isolated from the heart of an AL systemic amyloidosis patient.

Paolo Swuec
Francesca Lavatelli
Martino Bolognesi
ResearchOpen Access20 Mar 2019
Nature Communications

Volume: 10, P: 1-9
Indicators of profound hematologic response in AL amyloidosis: complete response remains the goal of therapy

Paolo Milani
Marco Basset
Giovanni Palladini
ResearchOpen Access01 Sept 2020
Blood Cancer Journal

Volume: 10, P: 1-8
Cryo-EM structure of ex vivo fibrils associated with extreme AA amyloidosis prevalence in a cat shelter

Here, the authors report the cryoEM structure of AA amyloid from a cat shelter with extreme disease prevalence and reveal the feline-specific sequence insert in the fibril core. The sequence is 99% identical to AA amyloid from cheetah with reported prion-like transmission in zoos.

Tim Schulte
Antonio Chaves-Sanjuan
Stefano Ricagno
ResearchOpen Access17 Nov 2022
Nature Communications

Volume: 13, P: 1-9
An N-glycosylation hotspot in immunoglobulin κ light chains is associated with AL amyloidosis

Alice Nevone
Maria Girelli
Mario Nuvolone
Research24 May 2022
Leukemia

Volume: 36, P: 2076-2085
Concurrent structural and biophysical traits link with immunoglobulin light chains amyloid propensity

Luca Oberti
Paola Rognoni
Stefano Ricagno
ResearchOpen Access01 Dec 2017
Scientific Reports

Volume: 7, P: 1-11
In situ characterization of protein aggregates in human tissues affected by light chain amyloidosis: a FTIR microspectroscopy study

Diletta Ami
Francesca Lavatelli
Giampaolo Merlini
ResearchOpen Access04 Jul 2016
Scientific Reports

Volume: 6, P: 1-12
Proteotoxicity in cardiac amyloidosis: amyloidogenic light chains affect the levels of intracellular proteins in human heart cells

Esther Imperlini
Massimiliano Gnecchi
Francesca Lavatelli
ResearchOpen Access15 Nov 2017
Scientific Reports

Volume: 7, P: 1-19

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