Rapid communications in mass spectrometry : RCM · 2025
Exploring the Mechanisms of Cyclosporine Therapy in Aplastic Anemia: A Data-Independent Acquisition Proteomics Approach.
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Guo Mingxin, Dai Ting, Wan Lin, Sun Xiang, Hu Zhiqiang, Chen Yanchun
Аннотация
RATIONALE: Clinically, cyclosporine (CsA) plays a crucial role in the treatment of aplastic anemia (AA) and has demonstrated significant therapeutic efficacy. We applied DIA-based quantitative proteomics to analyze plasma protein profiles in AA patients, aiming to identify proteins and pathways modulated by CsA, thereby elucidating its therapeutic mechanisms.
METHODS: Plasma samples from three AA patients pre- and post-CsA treatment underwent data-independent acquisition proteomics. DEPs were identified using fold-change thresholds. Gene Ontology, KEGG, and STRING analyses revealed functional pathways and hub proteins, which were validated by ELISA in 13 AA patients. Molecular docking assessed CsA-core protein binding affinities.
RESULTS: Compared to healthy people, AA patients exhibited 303 differential proteins, enriched in pathways related to oxidative stress, cellular adhesion, and energy dysregulation. Post-CsA treatment, 107 DEPs were identified, linked to redox balance and structural remodeling. Forty-eight proteins overlapped, with GAPDH, SOD1, CFL1, and ACTG1 as core targets. ELISA confirmed expression differences, and molecular docking showed strong CsA binding affinities to these proteins.
CONCLUSIONS: Significant protein expression differences between AA patients and healthy controls suggest immune-related pathways, including metabolism, oxidative stress, and cell structure, as key treatment targets. CsA may regulate these to intervene in AA progression.
METHODS: Plasma samples from three AA patients pre- and post-CsA treatment underwent data-independent acquisition proteomics. DEPs were identified using fold-change thresholds. Gene Ontology, KEGG, and STRING analyses revealed functional pathways and hub proteins, which were validated by ELISA in 13 AA patients. Molecular docking assessed CsA-core protein binding affinities.
RESULTS: Compared to healthy people, AA patients exhibited 303 differential proteins, enriched in pathways related to oxidative stress, cellular adhesion, and energy dysregulation. Post-CsA treatment, 107 DEPs were identified, linked to redox balance and structural remodeling. Forty-eight proteins overlapped, with GAPDH, SOD1, CFL1, and ACTG1 as core targets. ELISA confirmed expression differences, and molecular docking showed strong CsA binding affinities to these proteins.
CONCLUSIONS: Significant protein expression differences between AA patients and healthy controls suggest immune-related pathways, including metabolism, oxidative stress, and cell structure, as key treatment targets. CsA may regulate these to intervene in AA progression.