Journal: Journal of Nanobiotechnology

Article Title: M2 microglia-derived migrasome-enriched extracellular vesicles restore mitochondrial homeostasis to orchestrate neurovascular unit recovery after ischemic stroke

doi: 10.1186/s12951-026-04643-4

Figure Lengend Snippet: M2 microglia-derived migrasome-enriched EVs activate the cAMP/EPAC1/Rap1 pathway to improve mitochondrial function in microglia. ( A ) Heatmap of differentially expressed genes in ipsilateral brain tissue between the MCAO and MIGs groups. ( B ) Volcano plot of DEGs between the MCAO and MIGs groups. ( C ) KEGG pathway enrichment analysis. The top enriched pathways are shown, with the cAMP signaling pathway and Rap1 signaling pathway highlighted. ( D ) cAMP levels in BV2 cells. ( E-G ) Representative immunofluorescence image and quantitative analysis of EPAC1 and Rap1 in BV2 cells. ( H, I ) Western blot analysis and quantification of EPAC1 and Rap1 protein expression in BV2 cells. ( J ) Representative TEM images of mitochondria in BV2 cells. ( K ) Representative images and quantification of mitochondrial mass. (L, M ) Representative images and quantification of mitochondrial superoxide levels. ( N, O ) Representative images and quantification of mitochondrial membrane potential (ΔΨm) assessed by JC-1 staining (red: J-aggregates, high ΔΨm; green: monomers, low ΔΨm). ( P ) Representative TTC-stained brain sections from MCAO mice treated with MIGs in the presence or absence of the Rap1 inhibitor GGTI298. ( Q ) Quantitative analysis of infarct volume. Data are presented as mean ± SD from at least three independent experiments (cells) or n = 6 mice per group. * p < 0.05, ** p < 0.01, *** p < 0.001

Article Snippet: For Rap1 inhibition experiments, mice received an intraperitoneal injection of GGTI298 (25 μM/kg; HY-100876, MCE, USA) 30 min prior to reperfusion.

Techniques: Derivative Assay, Immunofluorescence, Western Blot, Expressing, Membrane, Staining

Journal: Redox Biology

Article Title: Upregulated GBP2 exacerbates Parkinson's disease pathogenesis by impairing NIX-dependent mitophagy

doi: 10.1016/j.redox.2026.104029

Figure Lengend Snippet: Geranylgeranylation is essential for GBP2 mitochondrial localization and function, and its inhibition protects against neurotoxicity. (A) Triton X-114 phase partitioning assay in SH-SY5Y cells treated with or without MPP + . MPP + treatment shifted GBP2 toward the detergent phase, indicating increased hydrophobicity (n = 3 independent biological replicates). (B, C) SH-SY5Y cells were transfected with Flag-GBP2, Flag-GBP2-ΔCAAX, or treated with the geranylgeranylation inhibitor GGTI298 (10 μM) for 48 h (n = 3 independent biological replicates). (B) Immunofluorescence of GBP2 (green) and a Mitotracker (red) shows that disrupting geranylgeranylation reduces mitochondrial localization of GBP2. Scale bar, 10 μm. (C) Western blot of GBP2 in mitochondrial and cytosolic fractions confirms the reduction in mitochondrial targeting in Flag-GBP2-ΔCAAX group or GGTI298 group. (D) Co-IP assays in HEK293T cells show that GGTI298 treatment or expression of the GBP2-ΔCAAX mutant impairs the interaction between GBP2 and NIX. (E–G) MPTP-induced PD model mice were treated with GGTI298 or saline. (E) Behavioral tests (open field, pole, rotarod) demonstrate that GGTI298 treatment ameliorates MPTP-induced motor deficits (n = 8 mice per group). (F) Western blot and (G) representative IHC for TH in the substantia nigra and striatum show that GGTI298 treatment preserves dopaminergic neurons (n = 4 mice per group). Scale bar, 50 μm. Data are presented as mean ± SEM. ∗p < 0.05, ∗∗p < 0.01, ∗∗∗p < 0.001 for comparisons between the indicated groups.

Article Snippet: To further examine the role of protein geranylgeranylation in this process, a subset of mice was treated with the geranylgeranylation inhibitor GGTI298 via intraperitoneal injection (12 mg/kg daily for fourteen consecutive days; MedChemExpress, Cat#HY-15871) [ ].

Techniques: Inhibition, Transfection, Immunofluorescence, Western Blot, Co-Immunoprecipitation Assay, Expressing, Mutagenesis, Saline

Journal: Redox Biology

Article Title: Upregulated GBP2 exacerbates Parkinson's disease pathogenesis by impairing NIX-dependent mitophagy

doi: 10.1016/j.redox.2026.104029

Figure Lengend Snippet: Geranylgeranylation is essential for GBP2 mitochondrial localization and function, and its inhibition protects against neurotoxicity. (A) Triton X-114 phase partitioning assay in SH-SY5Y cells treated with or without MPP + . MPP + treatment shifted GBP2 toward the detergent phase, indicating increased hydrophobicity (n = 3 independent biological replicates). (B, C) SH-SY5Y cells were transfected with Flag-GBP2, Flag-GBP2-ΔCAAX, or treated with the geranylgeranylation inhibitor GGTI298 (10 μM) for 48 h (n = 3 independent biological replicates). (B) Immunofluorescence of GBP2 (green) and a Mitotracker (red) shows that disrupting geranylgeranylation reduces mitochondrial localization of GBP2. Scale bar, 10 μm. (C) Western blot of GBP2 in mitochondrial and cytosolic fractions confirms the reduction in mitochondrial targeting in Flag-GBP2-ΔCAAX group or GGTI298 group. (D) Co-IP assays in HEK293T cells show that GGTI298 treatment or expression of the GBP2-ΔCAAX mutant impairs the interaction between GBP2 and NIX. (E–G) MPTP-induced PD model mice were treated with GGTI298 or saline. (E) Behavioral tests (open field, pole, rotarod) demonstrate that GGTI298 treatment ameliorates MPTP-induced motor deficits (n = 8 mice per group). (F) Western blot and (G) representative IHC for TH in the substantia nigra and striatum show that GGTI298 treatment preserves dopaminergic neurons (n = 4 mice per group). Scale bar, 50 μm. Data are presented as mean ± SEM. ∗p < 0.05, ∗∗p < 0.01, ∗∗∗p < 0.001 for comparisons between the indicated groups.

Article Snippet: To further examine the role of protein geranylgeranylation in this process, a subset of mice was treated with the geranylgeranylation inhibitor GGTI298 via intraperitoneal injection (12 mg/kg daily for fourteen consecutive days; MedChemExpress, Cat#HY-15871) [ ].

Techniques: Inhibition, Transfection, Immunofluorescence, Western Blot, Co-Immunoprecipitation Assay, Expressing, Mutagenesis, Saline