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Head-to-Head Comparison of Aptamer- and Antibody-Based Proteomic Platforms in Human Cerebrospinal Fluid Samples from a Real-World Memory Clinic Cohort.

Authors :
Puerta, Raquel
Cano, Amanda
García-González, Pablo
García-Gutiérrez, Fernando
Capdevila, Maria
de Rojas, Itziar
Olivé, Clàudia
Blázquez-Folch, Josep
Sotolongo-Grau, Oscar
Miguel, Andrea
Montrreal, Laura
Martino-Adami, Pamela
Khan, Asif
Orellana, Adelina
Sung, Yun Ju
Frikke-Schmidt, Ruth
Marchant, Natalie
Lambert, Jean Charles
Rosende-Roca, Maitée
Alegret, Montserrat
Source :
International Journal of Molecular Sciences; Jan2025, Vol. 26 Issue 1, p286, 23p
Publication Year :
2025

Abstract

High-throughput proteomic platforms are crucial to identify novel Alzheimer's disease (AD) biomarkers and pathways. In this study, we evaluated the reproducibility and reliability of aptamer-based (SomaScan<superscript>®</superscript> 7k) and antibody-based (Olink<superscript>®</superscript> Explore 3k) proteomic platforms in cerebrospinal fluid (CSF) samples from the Ace Alzheimer Center Barcelona real-world cohort. Intra- and inter-platform reproducibility were evaluated through correlations between two independent SomaScan<superscript>®</superscript> assays analyzing the same samples, and between SomaScan<superscript>®</superscript> and Olink<superscript>®</superscript> results. Association analyses were performed between proteomic measures, CSF biological traits, sample demographics, and AD endophenotypes. Our 12-category metric of reproducibility combining correlation analyses identified 2428 highly reproducible SomaScan CSF measures, with over 600 proteins well reproduced on another proteomic platform. The association analyses among AD clinical phenotypes revealed that the significant associations mainly involved reproducible proteins. The validation of reproducibility in these novel proteomics platforms, measured using this scarce biomaterial, is essential for accurate analysis and proper interpretation of innovative results. This classification metric could enhance confidence in multiplexed proteomic platforms and improve the design of future panels. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
16616596
Volume :
26
Issue :
1
Database :
Complementary Index
Journal :
International Journal of Molecular Sciences
Publication Type :
Academic Journal
Accession number :
182451389
Full Text :
https://doi.org/10.3390/ijms26010286