Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Protein identification in purified amyloid fibrils

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

INSTRUMENT(S):

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Heart

SUBMITTER: Emilie Pinault

LAB HEAD: Christophe Sirac

PROVIDER: PXD059000 | Pride | 2025-01-17

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	Ex_vivo_fibrils_Heart_SAI_1187-7049_DDA_std_1ul_2003.d.zip	Other
	Ex_vivo_fibrils_Heart_SAI_1187-7049_DDA_std_1ul_2003.xlsx	Xlsx
	Ex_vivo_fibrils_Heart_SAI_1187-7049_DDA_std_1ul_2003_6.1.331.mgf	Mgf
	Ex_vivo_fibrils_Heart_SAI_4153-7519_DDA_std_1ul_2058.d.zip	Other
	Ex_vivo_fibrils_Heart_SAI_4153-7519_DDA_std_1ul_2058.xlsx	Xlsx

Items per page:

1 - 5 of 9

Similar Datasets

A mouse model of cardiac AL amyloidosis unveils mechanisms of tissue accumulation and toxicity of amyloid fibrils

Project description:Immunoglobulin light chain (LC) amyloidosis (AL) is one of the most common types of systemic amyloidosis. The lack of reliable in vivo models hinders the study of the disease in its physiological context. We developped a transgenic mouse model producing high amounts of a human AL free light chain (LC). While mice exceptionnaly develop spontaneous AL amyloidosis and do not exhibit organ toxicity due to the circulating amyloidogenic LC, a single injection of amyloid fibrils, made up of the variable domain (VL) of the human LC, or soluble VL led to amyloid deposits, mainly in heart. The biochemical composition and the fragmentation pattern of the LC in the fibrils are highly similar to that of human AL fibrils, arguing for a conserved mechanism of amyloid fibrils formation. Amyloidosis positive mice also develop an early cardiac dysfunction, with increased NT-proBNP, diastolic dysfunction and remodeling of the extracellular matrix. Overall, this transgenic mice closely reproduces human cardiac AL amyloidosis and shows that a partial degradation of the LC initiate amyloid fibril formations in vivo. Accumulation of AL amyloid fibrils, rather than the soluble LC, drive the initial cardiac dysfunction. This model fills an important gap for research on AL amyloidosis and preclinical evaluation of new therapies.

2025-01-17 | GSE286368 | GEO

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

2025-07-25 | PXD066587 |

A mouse model of cardiac AL amyloidosis unveils mechanisms of tissue accumulation and toxicity of amyloid fibrils

Project description:A mouse model of cardiac AL amyloidosis unveils mechanisms of tissue accumulation and toxicity of amyloid fibrils

2025-01-17 | PXD059046 | Pride

Helical superstructures between amyloid and collagen VI in heart derived fibrils from a patient with Light Chain Amyloidosis

Project description:we investigated the N-glycosylation of the amyloid fibrils extracted from the heart of a patient affected by AL amyloidosis, using a proteomic approach to evaluate indirectly the presence of glycans in immunoglobulin light chains.

2024-07-02 | PXD049369 | Pride

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 2), 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 | PXD065431 | Pride

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

2025-12-23 | PXD065432 | Pride

Helical superstructures between amyloid and collagen VI in heart derived fibrils from a patient with Light Chain Amyloidosis

Project description:We investigated the N- and C-terminome of the LCs proteoforms in fibrils extracted from the hearts of a patient affected by AL amyloidosis, using a proteomic approach based on N- and C-terminal residues derivatization, followed by mapping of fragmentation sites on the structures of fibrillar LCs

2024-07-02 | PXD049301 | Pride

Mass spectrometry-based proteomic analysis of virions and fibrils from Mimiviridae

Project description:Mimivirus 1.2Mb genome is organized into a 30 nm nucleocapsid-like structure made of two closely related GMC-oxidoreductases, also composing the fibrils decorating its virions. In this work, we used MS-proteomics to characterize the protein content of virions and fibrils from different members of the Mimiviridae family (clade A: Mimivirus reunion -Mr- and Mimivirus M4 -M4, clade B: Moumouvirus australiensis -Ma- and Moumouvirus maliensis -Mm, clade C: Megavirus chilensis -Mc- and Megavirus vitis -Mv). Furthermore, we analyzed fractions purified from Mr mutants devoid of one of the two GMC-oxidoreductases (Mr_KOqu_143 and Mr_KOqu_946), or of both GMC-oxidoreductases (Mr_2KO) with or without expression of the GFP fused to the N-terminus of one GMC-oxidoreductase (Mr_2KO-GFP). Our results show the versatility of the protein content of the fibrils, with fibrils composed of different proteins inter- and even intra-clade, clades B and C viruses presenting fibrils with a protein composition closer to each other than that of clade A viruses.

2024-06-16 | PXD041298 | Pride

Copy number analysis of plasma cells from AL amyloidosis patients

Project description:Immunoglobulin light chain (AL) amyloidosis is characterized by deposition of abnormal amyloid fibrils in multiple organs impairing their function. CD138-purified plasma cells producing these fibrils are investigated regarding chromosomal alterations by interphase fluorescence in situ hybridization (iFISH) using a multiple myeloma specific probe set for the IgH translocations as well as recurrent numerical aberrations. Aberrations genuine to AL amyloidosis cannot be detected due to the inherent limitation of this probe panel to known loci. We analyzed 118 AL amyloidosis patients by high-density copy number array to quantitatively detect genome-wide chromosomal imbalances. Most prevalent gains affected chromosomes 1q (37%), 9 (24%), 11q (24%), and 19 (16%). The most frequent deletion was monosomy 13 (28%) followed by partial deletions on 14q (21%), 16q (14%), and 13q (12%). The results were analyzed with respect to cytogenetic subgroups. In 88% of patients with translocation t(11;14) and concomitant gain of 11q22.3/11q23 detected by iFISH, the latter aberration was not due to trisomy of chromosome 11 but part of the unbalanced translocation der(14)t(11;14)(q13;q32) with breakpoint in the CCND1/MYEOV gene region. Partial loss of chromosomes 14q and 16q were significantly associated to patients with gain 1q. Our iFISH probe set is highly concordant with copy number results as it detects the most common cytogenetic aberrations present in AL amyloidosis. Beyond that, the probe panel is also the method of choice to detect translocations involving the IgH locus. In contrast to the results of our iFISH panel the frequency of hyperdiploidy detected by copy number array analysis is higher.

2017-03-29 | GSE89616 | GEO