Fbxw11 regulates macrophage polarization and enhances the anti-leukemia activity
Ontology highlight
ABSTRACT:
ORGANISM(S): Mus musculus
PROVIDER: GSE316297 | GEO | 2026/01/21
REPOSITORIES: GEO
Similar Datasets
Project description:Fbxw11 regulates macrophage polarization and enhances the anti-leukemia activity
| PRJNA1402246 | ENA
Project description:Modulation of macrophage polarization by HMB [macrophage]
| PRJNA739181 | ENA
Project description:Extramedullary infiltration (EMI) is a concomitant manifestation indicating poor prognosis of acute myeloid leukemia (AML), yet the underlying mechanism remains poorly understood and therapeutic options are limited. Here, we employed single-cell RNA sequencing on bone marrow (BM) and EMI samples from an AML patient presenting pervasive leukemia cutis. A complement C1Q + macrophage-like leukemia subset which is enriched within cutis and existed in BM prior to EMI manifestations was identified and further verified in multiple AML patients. RNA-sequencing and quantitative proteomics profiling revealed adverse prognosis of patients bearing C1Q + population. C1Q expression endowed leukemia cells with tissue-infiltration ability which could establish prominent cutaneous or gastrointestinal EMI nodules in patient-derived xenograft (PDX) and CDX models. Fibroblasts attracted migration of the C1Q + leukemia cells through surface C1Q-gC1QR recognition and subsequent stimulation of MAFB-TGF-β signaling. Thus, C1Q orchestrates cancer infiltration pathways through communicating with fibroblasts and represents a compelling therapeutic target for EMI.
2022-08-03 | PXD035784 |
Project description:The experiments were done using an Orbitrap Fusion or an Orbitrap Fusion Lumos mass spectrometer. Multiplexing was achieved using either TMT10 or TMT11 reagents and the SPS-MS3 method. Basic pH reversed-phase chromatography (bRPLC) was used for off-line pre-fractionation; 12 fractions were analyzed for proteome mappings (PMID: 26700037) and 24 fractions plus a phosphotyrosine-enriched sample for phosphoproteome mappings (PMID: 31606085). Phosphoproteome mappings were done using both HCD fragmentation with Orbitrap fragment ion detection and CID fragmentation with ion trap fragment ion detection (PMID: 29487189, PMID: 31606085). If multiple TMT sets were required to analyze all samples from an experiment two bridge channels pooled from all samples was used to connect the data from the individual TMT sets (PMID: 28892078).
Five proteomics experiments are described in the paper:
(i) 1. Quantitative proteomics of fully polarized macrophages after 4 days of treatment with IL4 or IFNgamma/LPS to determine global proteome landscape of fully polarized THP-1-derived M1-type versus M2a-type macrophages:
Proteome mapping on Orbitrap Fusion (one TMT set)
RAW files: Marneros_4DayTreatment_proteome_fraction01 to ...fraction12
8 samples
Labeling: PMA.1 (126), PMA.2 (127n), IL4.1 (127c), IL4.2 (128n), ILJQ1.1 (128c), ILJQ1.2 (129n), IFNgamma.1 (129c), IFNgamma.2 (130n)
(ii) Time-course quantitative proteomics during the first 24 hours after induction of macrophage polarization in THP-1-derived macrophages to identify protein changes associated with M1-type (IFNgamma/LPS-induced) versus M2a-type (IL-4-induced) polarization:
Proteome mapping on Orbitrap Fusion (three TMT sets: set01, set02, set03)
RAW files:
Marneros_timecourse_proteome_TMTset01_fraction01 to ...fraction12
Marneros_timecourse_proteome_TMTset02_fraction01 to ...fraction12
Marneros_timecourse_proteome_TMTset03_fraction01 to ...fraction12
22 samples
Labeling:
set01; bridge 1 (126), PMA 0min (127n), PMA 10min (127c), PMA 30min (128n), PMA 1h (128c), PMA 2h (129n), PMA 4h (129c), PMA 8h (130n), PMA 24h (130c), bridge 2 (131n)
set02; bridge 1 (126), IL4 10min (127n), IL4 30min (127c), IL4 1h (128n), IL4 2h (128c), IL4 4h (129n), IL4 8h (129c), IL4 24h (130n), IFN 10min (130c), bridge 2 (131n)
set03; bridge 1 (126), IFN 30min (127n), IFN 1h (127c), IFN 2h (128n), IFN 4h (128c), IFN 8h (129n), IFN 24h (129c), bridge 2 (131n)
(iii) Time-course quantitative phosphoproteomics during the first 24 hours after induction of macrophage polarization in THP-1-derived macrophages to identify phosphorylation events associated with M1-type (IFNgamma/LPS-induced) versus M2a-type (IL-4-induced) polarization (same time points as in group 2):
Phosphoproteome mapping on Orbitrap Fusion (three TMT sets: set01, set02, set03)
RAW files:
Marneros_timecourse_phospho_TMTset01_fraction01 to ...fraction06, ...fraction08 to ...fraction24, ...pY
Marneros_timecourse_phospho_TMTset02_fraction01 to ...fraction12, ...fraction16 to ...fraction24, ...pY
Marneros_timecourse_phospho_TMTset03_fraction01 to ...fraction24, ...pY
The following RAW files gave no phosphopeptide quantifications (they are no included in the group of provided RAW files): set01_fraction07, set02_fraction13, set02_fraction14, set02_fraction15.
22 samples
Labeling: as in (ii)
(iv) Quantitative proteomics to assess the effects of the B-Raf inhibitor GDC-0879 or of the MEK inhibitor trametinib on IL-4-induced M2-type polarization and IFNgamma/LPS-induced M1-type polarization on THP-1-derived macrophages after 24 hours of treatment:
Proteome mapping on Orbitrap Fusion (one TMT set)
RAW files: Marneros_BRAF_inhibitor_proteine_fraction01 to ...fraction12
11 samples
Labeling: IL4 1 (131c), IL4 2 (127n), IL4+GDC 1 (131n), IL4+GDC 2 (128n), IL4+TRAM 1 (130c), IL4+TRAM 2 (129n), IFNgamma+LPS 1 (130n), IFNgamma+LPS 2 (127c), IFNgamma+LPS+TRAM 1 (126), IFNgamma+LPS+TRAM 2(129c), IFNgamma+LPS+GDC (128c)
(v) Quantitative phosphoproteomics to assess the effects of the B-Raf inhibitor GDC-0879 on IL-4-induced M2-type polarization and IFNgamma/LPS-induced M1-type polarization on THP-1-derived macrophages after 24 hours of treatment:
Phosphoproteome mapping on Orbitrap Fusion Lumos (one TMT set)
RAW files: Marneros_BRAF_inhibitor_phospho_fraction01 to ...fraction24, ...pY
7 samples
Labeling: IL4 1 (131c), IL4 2 (127n), IL4+GDC 1 (130n), IL4+GDC 2 (128n), IFNgamma+LPS 1 (128c), IFNgamma+LPS 2 (127c), IFNgamma+LPS+GDC (130c)
2019-12-10 | MSV000084672 | MassIVE
Project description: Not available
| S-EPMC5724266 | biostudies-literature
Project description:In this study, using the RNAomic approach we revealed the dose-dependent macrophage polarization of tissue-resident macrophages using cationic nanocellulose in vivo. This study will envision a new approach for nanocellulose as a therapeutic vehicle for tissue engineering and regeneration medicine.
2025-08-01 | E-MTAB-14734 | biostudies-arrayexpress
Project description:Allergic rhinitis (AR) is a prevalent inflammatory condition characterized by an overactive immune response to allergens. Recent studies have highlighted the role of macrophage polarization in modulating immune responses. This study investigates the role of Follistatin-like 1 (FSTL1) in promoting macrophage M2 polarization and its implications in AR. Using in vitro and in vivo models, we demonstrate that FSTL1 significantly enhances the expression of M2 macrophage markers, including Arg1, CD206, and IL-10, while concurrently reducing M1 markers such as iNOS and TNF-α. Furthermore, FSTL1-treated macrophages exhibited increased anti-inflammatory properties, contributing to the attenuation of allergic inflammation in a murine model of AR. Our findings suggest that FSTL1-mediated M2 polarization plays a crucial role in mitigating allergic responses, providing a potential therapeutic target for AR management.
2025-11-01 | GSE281116 | GEO
Project description:TIPE1 regulation on macrophage polarization
| PRJNA759608 | ENA
Project description:Macrophages play crucial roles in inflammation and tissue homeostasis, exhibiting phenotypic and functional plasticity that enables them to initiate, sustain, or resolve inflammation. To support the evidence-based selection of biomedically relevant preclinical models, this study comprehensively characterized ovine macrophage differentiation and polarization by integrating morphological assessments with in-depth proteomic profiling of cellular lysates and secretomes. Monocytes isolated from peripheral blood were differentiated into macrophages using GM-CSF (GMØ) or M-CSF (MMØ), then polarized into M1 and M2 phenotypes. Mass spectrometry identified 4804 proteins in cell lysates and 901 in secretomes, including 42 CD antigens, enabling the establishment of CD marker profiles for monocytes and the distinct macrophage differentiation and polarization states. Proteomic analyses revealed significant upregulation of inflammatory markers in M1 and elevated tissue repair markers in M2 macrophages. Enrichment analysis confirmed activation of antimicrobial and matrix-degrading pathways in M1 macrophages, and regenerative, proteolysis-inhibiting functions in M2 macrophages. In conclusion, this study addresses the limitations of currently available immunological tools by providing an antibody-independent alternative for the classification of ovine macrophages, facilitating more precise phenotypic characterization and functional insight in ovine immunology research.
2026-01-12 | PXD068541 | Pride
Project description: Not available
| S-EPMC12271640 | biostudies-literature