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Light chain amyloid fibrils from an AL amyloidosis patient (case 2), abdominal fat biopsy

ABSTRACT: In this study, we successfully extracted and resolved the high-resolution structure of amyloid fibrils from abdominal fat biopsy sample obtained from a living AL patient using cryo-EM.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Abdominal Adipose Tissue

SUBMITTER: Yuxuan Yao

LAB HEAD: Dan Li

PROVIDER: PXD065431 | Pride | 2025-12-23

REPOSITORIES: Pride

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			Action	DRS
	MS231585-fat-xu-ASP-N.raw	Raw
	MS231585-fat-xu-C.raw	Raw
	MS231585-fat-xu-PK.raw	Raw
	MS231585-fat-xu-T.raw	Raw
	MS231585-fat-xu-lytic.raw	Raw

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Light chain amyloid fibrils from an AL amyloidosis patient (case 1), abdominal fat biopsy

Project description:In this study, we successfully extracted and resolved the high-resolution structure of amyloid fibrils from biopsy sample obtained from a living AL patient using cryo-EM.

2025-12-23 | PXD065430 | Pride

Light chain amyloid fibrils from an AL amyloidosis patient (case 3), abdominal fat biopsy

Project description:In this study, we successfully extracted and resolved the high-resolution structure of amyloid fibrils from abdominal fat biopsy sample obtained from a living AL patient using cryo-EM.

2025-12-23 | PXD065432 | Pride

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Project description:In this study, we used minimally invasive abdominal fat biopsies routinely performed in clinical practice, to obtain amyloid fibrils from living MM patient. Using cryo-electron microscopy (cryo-EM) and mass spectrometry (MS), we successfully determined the sequence and high-resolution structure of light chain fibril polymorphs.

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Light chain amyloid fibrils from multiple myeloma patient (case 2), abdominal fat biopsy

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Protein identification in purified amyloid fibrils

Project description:We identified the protein in purified AL amyloid fibrils extracted from heart tissues from transgenic mice developing AL amyloidosis.

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Cryo-EM structure of ex vivo fibrils associated with extreme AA amyloidosis prevalence in a cat shelter

Project description:We present the 3.3 Å cryo-EM structure of an AA amyloid extracted post-mortem from the diseased kidney of a DSH cat with renal failure. The structure reveals a cross-beta architecture assembled from two 76-residue long proto-filaments. Despite >70% sequence homology to mouse and human SAA, the cat SAA variant adopts a unique amyloid fold exhibiting type-2 polymorphism. Based on shared disease profiles and almost identical sequences, we propose a similar amyloid fold of deposits identified previously in captive cheetah.

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Targeting Amyloid Fibrils by Passive Immunotherapy in Systemic Amyloidosis.

Project description:Systemic amyloidoses are characterized by the unrelenting deposition of autologous proteins as highly ordered fibrils in target organs. The ensuing, potentially fatal organ dysfunction is the result of the combined damage caused by the proteotoxic effect of prefibrillar species and by the cytotoxicity and the structural alterations produced by the amyloid fibrils. Current therapy is focused on eliminating the amyloid protein, thus extinguishing the amyloid cascade at its origin. While this approach may end the cell damage caused by prefibrillar aggregates and prevent further amyloid accumulation, the noxious effects of the amyloid fibrils persist and may hamper the recovery of organ function, which is the ultimate goal of therapy as it is necessary to improve the quality of life and extend survival. Preclinical studies indicate that the clearance of amyloid deposits can be accelerated by specific antibodies targeting amyloid fibrils that activate complement-mediated macrophages and giant cell phagocytosis, possibly promoting the recovery of organ function. Measuring the therapeutic effect of anti-amyloid agents is still a matter of research. In recent years, several monoclonal antibodies targeting amyloid deposits have been tested in clinical trials with mixed outcomes. Recent encouraging results from phase I/II trials, new anti-amyloid agents, and new antibody engineering offer hope that effective amyloid removal will be accomplished in the near future, accelerating organ recovery and improving quality of life and survival.

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Sequence of amyloid fibrils from renal AL amyloidosis

Project description:De novo sequencing of amyloid fibrils from renal AL amyloidosis based on LC-MS/MS

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Targeted mass spectrometry of Tau preparations purified from Alzheimer’s Disease brains plus either the deubiquitylase USP21 or its activity-dead mutant C221A.

Project description:To characterise the abundance of ubiquitylated Tau peptides in the presence of active or inactive variants (wt 196-565 vs. C221A) of the broad spectrum deubiquitylase USP21. Tau peptides are obtained from Tau fibrils purified from post mortem human brains diagnosed with Alzheimer’s. Their detection is facilitated by previous training of the mass spectrometer with in vitro ubiquitylated Tau. The same samples were used to evaluate the percentage of peptides modified with ubiquitin

2024-06-18 | PXD046645 | Pride

Diagnostic sensitivity of abdominal fat aspiration in cardiac amyloidosis.

Project description:AimsCongo red staining of an endomyocardial biopsy is the diagnostic gold-standard in suspected cardiac amyloidosis (CA), but the procedure is associated with the risk, albeit small, of serious complications, and delay in diagnosis due to the requirement for technical expertise. In contrast, abdominal fat pad fine needle aspiration (FPFNA) is a simple, safe and well-established procedure in systemic amyloidosis, but its diagnostic sensitivity in patients with suspected CA remains unclear.Methods and resultsWe assessed the diagnostic sensitivity of FPFNA in 600 consecutive patients diagnosed with CA [216 AL amyloidosis, 113 hereditary transthyretin (ATTRm), and 271 wild-type transthyretin (ATTRwt) amyloidosis] at our Centre. Amyloid was detected on Congo red staining of FPFNAs in 181/216 (84%) patients with cardiac AL amyloidosis, including 100, 97, and 78% of those with a large, moderate, and small whole-body amyloid burden, respectively, as assessed by serum amyloid P (SAP) component scintigraphy (P < 0.001); the deposits were successfully typed as AL by immunohistochemistry in 102/216 (47%) cases. Amyloid was detected in FPFNAs of 51/113 (45%) patients with ATTRm CA, and only 42/271 (15%) cases with ATTRwt CA.ConclusionsFPFNA has reasonable diagnostic sensitivity in cardiac AL amyloidosis, particularly in patients with a large whole-body amyloid burden. Although the diagnostic sensitivity of FPFNA is substantially lower in transthyretin CA, particularly ATTRwt, it may nevertheless sometimes obviate the need for endomyocardial biopsy.

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