ArticleProteomics2017
MALDI Mass Spectrometry Imaging: A Novel Tool for the Identification and Classification of Amyloidosis.
Article in Proteomics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- In situ, antibody-independent, and multiplexed characterization of amyloid plaques by MALDI MS/MS imaging using iprm-PASEF.Analytical and bioanalytical chemistry · 2026Article
- Interpreting MALDI imaging data for rare types of ampullary cancer using machine learning.NPJ systems biology and applications · 2026Article
- Serum and Tissue Light-Chains as Disease Biomarkers in AL Amyloidosis.International journal of molecular sciences · 2025Review
- Proteomics-Based Analysis of Laser-Capture Micro-dissected, Formalin-Fixed Paraffin-Embedded Tissue Samples.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Monoclonal immunoglobulins on red blood cells: a potential supplementary diagnostic indicator for monoclonal gammopathies.Frontiers in immunology · 2025Article
- Quantitative mass spectrometry imaging: therapeutics & biomolecules.Chemical communications (Cambridge, England) · 2024Review
- Precise diagnosis and typing of early-stage renal immunoglobulin-derived amyloidosis by label-free quantification of parallel reaction monitoring-based targeted proteomics.BMC nephrology · 2023Article
- Monoclonal Gammopathy of Renal Significance: A Molecular Middle Earth between Oncology, Nephrology, and Pathology.Kidney diseases (Basel, Switzerland) · 2022Review
- N-terminal peptide fragment constitutes core of amyloid deposition of serum amyloid A: An imaging mass spectrometry study.PloS one · 2022Article
- Amyloidosis: What does pathology offer? The evolving field of tissue biopsy.Frontiers in cardiovascular medicine · 2022Review
- A systemic apolipoprotein A-IV-associated amyloidosis confirmed by proteome analysis.Virchows Archiv : an international journal of pathology · 2021Article
- Dissecting the Molecular Features of Systemic Light Chain (AL) Amyloidosis: Contributions from Proteomics.Medicina (Kaunas, Lithuania) · 2021Review
- Systemic amyloidosis: The skin as a clue of an unexpected diagnosis.International journal of women's dermatology · 2021Article
- Immunoglobulin light chain amyloidosis diagnosis and treatment algorithm 2021.Blood cancer journal · 2021Review
- Neurodegenerative Proteinopathies in the Proteoform Spectrum-Tools and Challenges.International journal of molecular sciences · 2021Review
- Gateway and journey of patients with cardiac amyloidosis.ESC heart failure · 2020Article
- Half a century of amyloids: past, present and future.Chemical Society reviews · 2020Review
- Systemic amyloidosis: moving into the spotlight.Leukemia · 2020Review
- Sudden death in lambda light chain AL cardiac amyloidosis: a review of literature and update for clinicians and pathologists.International journal of clinical and experimental pathology · 2020Review
- Towards resolving the spatial metabolome with unambiguous molecular annotations in complex biological systems by coupling mass spectrometry imaging with structures for lossless ion manipulations.Chemical communications (Cambridge, England) · 2019Article
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4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amyloidosis is a group of diseases caused by extracellular accumulation of fibrillar polypeptide aggregates. So far, diagnosis is performed by Congo red staining of tissue sections in combination with polarization microscopy. Subsequent identification of the causative protein by immunohistochemistry harbors some difficulties regarding sensitivity and specificity. Mass spectrometry based approaches have been demonstrated to constitute a reliable method to supplement typing of amyloidosis, but still depend on Congo red staining. In the present study, we used matrix-assisted laser desorption/ionization mass spectrometry imaging coupled with ion mobility separation (MALDI-IMS MSI) to investigate amyloid deposits in formalin-fixed and paraffin-embedded tissue samples. Utilizing a novel peptide filter method, we found a universal peptide signature for amyloidoses. Furthermore, differences in the peptide composition of ALλ and ATTR amyloid were revealed and used to build a reliable classification model. Integrating the peptide filter in MALDI-IMS MSI analysis, we developed a bioinformatics workflow facilitating the identification and classification of amyloidosis in a less time and sample-consuming experimental setup. Our findings demonstrate also the feasibility to investigate the amyloid's protein composition, thus paving the way to establish classification models for the diverse types of amyloidoses and to shed further light on the complex process of amyloidogenesis.
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