PXD005960 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Matrix-Assisted Laser Desorption Ionization Mass Spectrometry Imaging: a novel Tool for the Identification and Classification of Amyloidosis |
Description | 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 matrix-assisted laser desorption/ionization mass spectrometry imaging coupled with ion mobility separation (MALDI-IMS MSI) was used to investigate amyloid deposits in formalin-fixed and paraffin-embedded tissue samples. We designed a peptide filter method enabling the identification of tryptic peptides derived from amyloidogenic and amyloid-associated proteins without additional tandem mass spectrometry. Utilizing the filter we found a universal peptide signature for amyloidoses independent from amyloid type and histoanatomical localization. Examining a validation cohort of cardiac biopsies including 66 amyloid and 31 non-amyloid cases, amyloidosis was diagnosed with high sensitivity and specificity. Furthermore, differences in the peptide composition of AL-lambda 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 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. |
HostingRepository | PRIDE |
AnnounceDate | 2024-10-22 |
AnnouncementXML | Submission_2024-10-22_04:36:39.120.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Christoph Röcken |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | No PTMs are included in the dataset |
Instrument | MALDI Synapt G2-S MS |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2017-02-23 03:13:48 | ID requested | |
1 | 2017-10-16 06:16:06 | announced | |
⏵ 2 | 2024-10-22 04:36:42 | announced | 2024-10-22: Updated project metadata. |
Publication List
10.1002/pmic.201700236; |
Winter M, Tholey A, Kristen A, R, ö, cken C, MALDI Mass Spectrometry Imaging: A Novel Tool for the Identification and Classification of Amyloidosis. Proteomics, 17(22):(2017) [pubmed] |
Keyword List
curator keyword: Technical, Biomedical |
submitter keyword: formalin-fixed and paraffin-embedded, amyloidosis, ion mobility separation,MALDI MS imaging |
Contact List
Christoph Röcken |
contact affiliation | Department of Pathology, Christian-Albrechts-Universität, Germany |
contact email | christoph.roecken@uksh.de |
lab head | |
Christoph Röcken |
contact affiliation | Christian-Albrechts-University Kiel |
contact email | christoph.roecken@uksh.de |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD005960
- Label: PRIDE project
- Name: Matrix-Assisted Laser Desorption Ionization Mass Spectrometry Imaging: a novel Tool for the Identification and Classification of Amyloidosis