Spatial resolution of renal amyloid deposits through MALDI-MSI: a combined digital and molecular approach to monoclonal gammopathies

Autor: Greta Bindi, Andrew Smith, Glenda Oliveira, Albino Eccher, Simona Vatrano, Federico Alberici, Giorgio Cazzaniga, Stefania Galimberti, Giulia Capitoli, Fulvio Magni, Fabio Pagni, Vincenzo L'Imperio
Přispěvatelé: Bindi, G, Smith, A, Oliveira, G, Eccher, A, Vatrano, S, Alberici, F, Cazzaniga, G, Galimberti, S, Capitoli, G, Magni, F, Pagni, F, L'Imperio, V
Rok vydání: 2023
Předmět:
Zdroj: Journal of Clinical Pathology. :jcp-2023
ISSN: 1472-4146
0021-9746
DOI: 10.1136/jcp-2023-208790
Popis: AimsIdentification and characterisation of monoclonal gammopathies of renal significance (MGRS) is critical for therapeutic purposes. Amyloidosis represents one of the most common forms of MGRS, and renal biopsy remains the gold standard for their classification, although mass spectrometry has shown greater sensitivity in this area.MethodsIn the present study, a new in situ proteomic technique, matrix-assisted laser desorption/ionisation mass spectrometry imaging (MALDI-MSI), is investigated as an alternative to conventional laser capture microdissection MS for the characterisation of amyloids. MALDI-MSI was performed on 16 cases (3 lambda light chain amyloidosis (AL), 3 AL kappa, 3 serum amyloid A amyloidosis (SAA), 2 lambda light chain deposition disease (LCDD), 2 challenging amyloid cases and 3 controls). Analysis began with regions of interest labelled by the pathologist, and then automatic segmentation was performed.ResultsMALDI-MSI correctly identified and typed cases with known amyloid type (AL kappa, AL lambda and SAA). A ‘restricted fingerprint’ for amyloid detection composed of apolipoprotein E, serum amyloid protein and apolipoprotein A1 showed the best automatic segmentation performance (area under the curve >0.7).ConclusionsMALDI-MSI correctly assigned minimal/challenging cases of amyloidosis to the correct type (AL lambda) and identified lambda light chains in LCDD cases, highlighting the promising role of MALDI-MSI for amyloid typing.
Databáze: OpenAIRE