Journal: Redox Biology

Article Title: ALDH1L2 induces resistance to chemotherapy in small cell lung cancer by inhibiting ferroptosis

doi: 10.1016/j.redox.2026.104098

Figure Lengend Snippet: ALDH1L2 promotes SCLC chemoresistance by negatively regulating the hyperoxidized PRDX3 and PRDX3 dimer content in the plasma membrane. (A) Immunofluorescence detection of the colocalization of ALDH1L2 and PRDX3 in SCLC cells. The cell nuclei are labeled with blue fluorescence, the ALDH1L2 protein is labeled with green fluorescence, and the PRDX3 protein is labeled with red fluorescence. Scale bar: 20 μm. (B) Coimmunoprecipitation assays revealed the interaction of the ALDH1L2 protein with the PRDX3 protein in chemoresistant SCLC cells. (C) Coimmunoprecipitation assays revealed the interaction of the TRX2 protein with the ALDH1L2 protein and the PRDX3 protein in chemoresistant SCLC cells. (D-E) The reaction of PRDX3 with hydroperoxides was analyzed by immunoblotting. Bar plots show the results of the semiquantitative analysis of the gray values of the protein bands by ImageJ software. (F–H) Analysis of the effect of ALDH1L2 knockdown on the content of hyperoxidized PRDXs protein in each fraction of H69AR and H446DDP cells. The results under no treatment, cisplatin treatment (10 μg/mL for 24 h) and erastin treatment (20 μM for 72 h) are shown in the graph. Bar plots show the results of the semiquantitative analysis of the gray values of the protein bands by ImageJ software. (I) Coimmunoprecipitation assays revealed that hyperoxidized PRDXs protein could be immunoprecipitated by anti-PRDX3 antibody. (J-N) Analysis of the effect of ALDH1L2 knockdown on the content of oxidized PRDX3 dimers in each fraction of H69AR and H446DDP cells. The results under no treatment, cisplatin treatment (10 μg/mL for 24 h) and erastin treatment (20 μM for 72 h) are shown in the graph. LE, long exposure; SE, short exposure. Bar plots show the results of the semiquantitative analysis of the gray values of the protein bands by ImageJ software. The data are expressed as mean ± standard deviation (n = 3). ns, not significant; ∗, p < 0.05; ∗∗, p < 0.01; ∗∗∗, p < 0.001; ∗∗∗∗, p < 0.0001.

Article Snippet: The purified PRDX3 protein was obtained from MedChemExpress (HY– P71147 , MCE, USA).

Techniques: Clinical Proteomics, Membrane, Immunofluorescence, Labeling, Fluorescence, Western Blot, Software, Knockdown, Immunoprecipitation, Standard Deviation

Journal: Redox Biology

Article Title: ALDH1L2 induces resistance to chemotherapy in small cell lung cancer by inhibiting ferroptosis

doi: 10.1016/j.redox.2026.104098

Figure Lengend Snippet: PRDX3 contributes to the ALDH1L2-mediated chemoresistance program in SCLC. (A-D) RT-qPCR was used to verify the knockdown and overexpression efficiency of PRDX3 in SCLC cells at the mRNA level. (E-L) Immunoblotting was performed to validate the knockdown and overexpression efficiency of PRDX3 in SCLC cells at the protein level. Bar plots show the results of the semiquantitative analysis of the gray values of the protein bands by ImageJ software. (M − P) CCK-8 assay to determine the role of PRDX3 in the regulation of chemoresistance elicited by ALDH1L2 in SCLC cells. IC50, half maximal inhibitory concentration. The data are expressed as mean ± standard deviation (n = 3). ns, not significant; ∗, p < 0.05; ∗∗, p < 0.01; ∗∗∗, p < 0.001; ∗∗∗∗, p < 0.0001.

Article Snippet: The purified PRDX3 protein was obtained from MedChemExpress (HY– P71147 , MCE, USA).

Techniques: Quantitative RT-PCR, Knockdown, Over Expression, Western Blot, Software, CCK-8 Assay, Concentration Assay, Standard Deviation

Journal: Redox Biology

Article Title: ALDH1L2 induces resistance to chemotherapy in small cell lung cancer by inhibiting ferroptosis

doi: 10.1016/j.redox.2026.104098

Figure Lengend Snippet: The PRDX3 inhibitor thiostrepton synergizes with chemotherapy to suppress tumor growth in SCLC. (A) CCK-8 assay to determine the IC50 values of thiostrepton in human normal bronchial epithelial BEAS-2B cells and SCLC cells (n = 3). (B–C) Verification of the inhibitory effect of thiostrepton on PRDX3 in SCLC cells by immunoblotting. Bar plots show the results of the semiquantitative analysis of the gray values of the protein bands by ImageJ software (n = 3). (D) The growth of tumors in the orthotopic SCLC model was recorded with the live animal imaging system (n = 5). (E) Line chart demonstrating the quantitative bioluminescence intensities for each group. (F) Growth curves of xenografted tumors derived from H69AR cells under different treatments are shown (n = 5). The tumor volume was calculated as follows: (longest diameter) × (shortest diameter) 2 /2. (G) Xenografted tumors derived from H69AR cells under different treatments were removed and photographed after the mice were euthanized. (H) Weights of xenografted tumors derived from H69AR cells under different treatments are shown. IC50, half maximal inhibitory concentration. The data are expressed as mean ± standard deviation. ns, not significant; ∗, p < 0.05; ∗∗, p < 0.01; ∗∗∗, p < 0.001; ∗∗∗∗, p < 0.0001.

Article Snippet: The purified PRDX3 protein was obtained from MedChemExpress (HY– P71147 , MCE, USA).

Techniques: CCK-8 Assay, Western Blot, Software, Imaging, Derivative Assay, Concentration Assay, Standard Deviation

Journal: Nature Communications

Article Title: Trifunctional sphingomyelin derivatives enable nanoscale resolution of sphingomyelin turnover in physiological and infection processes via expansion microscopy

doi: 10.1038/s41467-024-51874-w

Figure Lengend Snippet: a , b TFSMs are enriched within the Golgi and mitochondria. HeLa cells were treated with TFSM 1 for 2 h ( a ) or 24 h ( b ). Samples were fixed and clicked to BODIPY-FL-DBCO (backbone) or Atto647N-azide (headgroup). Golgi and mitochondria were visualized by an anti-Golgi matrix protein 130 (GM130) and anti-Peroxiredoxin (Prx3) antibody, respectively. n = 1. Scale bars: 25 µm ( a ) or 5 µm ( b ). c , d FRET measurement of TFSM conversion. HeLa or human umbilical vein endothelial cells (HuVEC) were incubated with TFSM 1, TFSM 2, or BODIPY-FL-C 12 -SM for 2 h. Then, the compounds were removed, and cells were either treated with bSMase or left untreated for 3 h. Samples treated with TFSMs were fixed, clicked with BODIPY-FL-DBCO (backbone) and AlexaFluor TM 546 (AF)546-azide (headgroup) and FRET efficiency was determined by acceptor bleaching. Cells treated with BODIPY-FL-C 12 -SM were detached, and lipids were extracted by CHCl 3 :MeOH. The proportion of unmetabolized SM was determined by thin-layer chromatography. Scale bars: 25 µm. n = 3. Statistics: Two-way ANOVA and Šídák’s multiple comparisons ( d ). Bars represent means ± SD. n corresponds to biological replicates. Source data and detailed statistics are provided as a Source Data file.

Article Snippet: 7163670), 1:50 anti-Prx3 antibody (OriGene, Cat. No. TA322472) or 4 μg/ml anti-chlamydial HSP60 antibody (SantaCruz, Cat. No. sc-57840, Lot.

Techniques: Incubation, Thin Layer Chromatography

Journal: Human molecular genetics

Article Title: Protein misfolding and clearance in the pathogenesis of a new infantile onset ataxia caused by mutations in PRDX3.

doi: 10.1093/hmg/ddac146

Figure Lengend Snippet: Figure 1. Brain MRI and pedigree of the proband. (A–F) Consecutive brain MRI of the patient from onset of ataxia at 19 months to 6.5 years of age. (A–E) Midsagittal T1-weighted images showing vermian atrophy over time. (F–K) Coronal FLAIR images revealing atrophy of cerebellar hemispheres and early appearance of cerebellar cortical hyperintensities (red arrow head). (L) Quantitative analysis using the midsagittal vermis relative diameter (MVRD). The vermis diameter/total posterior cranial fossa diameter ratio (%) was used to represent the proportion of both values. (M) Pedigree of the proband. The arrow indicates the proband MD-174. Mutation segregation PRDX3 c.489C > G (p.D163E) is below each symbol.

Article Snippet: The PRDX3 cDNA (NM_006793) was tagged with MycDDK in C-ter and cloned in pCMV6 (Origene Technologies, Inc., Rockville, MD, USA).

Techniques: Mutagenesis

Journal: Human molecular genetics

Article Title: Protein misfolding and clearance in the pathogenesis of a new infantile onset ataxia caused by mutations in PRDX3.

doi: 10.1093/hmg/ddac146

Figure Lengend Snippet: Figure 3. PRDX3 p.D163E expression in primary neurons. (A) Representative pictures of primary cortical neurons expressing at D5 either WT-PRDX3 or PRDX3 p.D163E. Boxed area shows the regions magnified and indicated as proximal and distal (solid and dashed lines, respectively). Arrowheads and red lines show the GFP positive regions that colocalized with PRDX3 protein in the neurites. Scale bar = 10 μm. (B) Schematic representation of the vector for the co-expression of PRDX3 and GFP linked by an internal ribosome entry site (IRES). (C) Upper graphs show either the ratio of the intensity of GFP and PRDX3 labeling. n = 20 control or mutant neurons. ∗P < 0.05, two-way ANOVA test. Average ± SEM. Lower graph shows the colocalization expressed as Manders’ Overlap Coefficient of PRDX3 over GFP labeling, overlapping areas are lined in red in (A). n ≥15 control or mutant neurons. ∗P < 0.05, two- way ANOVA test. Mean ± SEM. (D) Representative pictures of primary neurons at D5 expressing either PRDX3 WT or p.D163E mutant co-labeled with MitoTracker® Red. Full arrowheads indicate regions of co-localization. Scale bar = 10 μm. (E) Representative neurons at D12 expressing either PRDX3 WT or PRDX3 p.D163E mutant labeled with GFP. The box indicates the area of the neurite magnified or the right panels. Arrowheads indicate axonal swellings. Scale bar = 10 μm. (F) Quantification of neurite integrity based on the neuronal morphology. Ctrl, n = 50; PRDX3 WT, n = 109; PRDX3 mut, n = 109. ∗P < 0.05; Fisher’s exact test.

Article Snippet: The PRDX3 cDNA (NM_006793) was tagged with MycDDK in C-ter and cloned in pCMV6 (Origene Technologies, Inc., Rockville, MD, USA).

Techniques: Expressing, Plasmid Preparation, Labeling, Control, Mutagenesis

Journal: Human molecular genetics

Article Title: Protein misfolding and clearance in the pathogenesis of a new infantile onset ataxia caused by mutations in PRDX3.

doi: 10.1093/hmg/ddac146

Figure Lengend Snippet: Figure 4. Mitochondrial morphology in HeLa cells overexpressing WT-PRDX3 and mutated forms. (A) Distribution of cell percentage according to mitochondrial morphology and obtained percentages for WT and each mutation. (B–E) Quantitative analysis of mitochondrial network morphology by the ImageJ™Mito-Morphology macro. Quantification of the number of mitochondria (B), and the elongation and interconnectivity indices (C, D). (E, F) Quantitative analysis of mitochondrial network morphology by the ImageJ™plugin MiNA. Mean Branch Length is the average of the lengths of all lines used to represent the mitochondrial structures, and the footprint is the total area in the cell occupied by mitochondrial structures. Only statically significant comparatives are shown. Error bars represent SEM. ∗P < 0.05; ∗∗P < 0.01. One-way ANOVA and Tukey post hoc test.

Article Snippet: The PRDX3 cDNA (NM_006793) was tagged with MycDDK in C-ter and cloned in pCMV6 (Origene Technologies, Inc., Rockville, MD, USA).

Techniques: Mutagenesis

Journal: Human molecular genetics

Article Title: Protein misfolding and clearance in the pathogenesis of a new infantile onset ataxia caused by mutations in PRDX3.

doi: 10.1093/hmg/ddac146

Figure Lengend Snippet: Figure 5. Electron microscopy in transfected HeLa cells expressing PRDX3 p.D163E. HeLa cells were transiently transfected with plasmid DNA encoding PRDX3 p.D163E fused to Myc-DDK tag, immunostained and further processed for transmission electron microscopy (TEM) analysis. (A) Correlative light and electron microscopy (CLEM) to identify transfected cells and highlight the localization of the mutated protein (green fluorescence). (B) Enlarged picture of the square marked in (A), showing an overlay of p.D163E fluorescence signal and perinuclear clumped mitochondria at the ultrastructural level, observed in more detail in lower panels (C, D). Two additional analyzed transfected cells (E) and representative TEM high-magnification images (F– H) of the boxed regions in (E) displaying aberrant mitochondrial morphology and lipid droplets (LDs) absent in control cells. (I) Control non-transfected HeLa cells and successive higher resolution views (J–L) of the selected region in (I).

Article Snippet: The PRDX3 cDNA (NM_006793) was tagged with MycDDK in C-ter and cloned in pCMV6 (Origene Technologies, Inc., Rockville, MD, USA).

Techniques: Electron Microscopy, Transfection, Expressing, Plasmid Preparation, Transmission Assay, Fluorescence, Control

Journal: Human molecular genetics

Article Title: Protein misfolding and clearance in the pathogenesis of a new infantile onset ataxia caused by mutations in PRDX3.

doi: 10.1093/hmg/ddac146

Figure Lengend Snippet: Figure 6. PRDX3 p.D163E expression in fibroblasts and structural analysis. (A, B) PRDX3 expression in fibroblasts cultures derived from a healthy control and the patient (MD-174). (A) Immunofluorescence showing the subcellular location of WT-PRDX3 and PRDX3 p.D163E (green), the mitochondrial network with MitoTracker® Red and DAPI (blue). Scale bar = 50 μm. (B) WB analysis of the WT and mutated PRDX3 expression in both soluble and insoluble fractions. α-Tubulin was used to normalize the detected protein levels. (C) Filament organization of human PRDX3 observed in the crystal structure (PDB ID 5JCG). The subunits of each one of the stacked dodecamers are shown in different colors with different intensities for adjacent subunits. (D) Structural model of human ring-like PRDX3 dodecamer. The two subunits of each dimer are colored in light or dark blue, respectively. Localization of D163 is mapped with red spheres. (E) Detail of the intersubunit interface, where D163 is located. The side chain of D163 as well as that for the catalytic cysteine 47 is shown with stick representation and labeled.

Article Snippet: The PRDX3 cDNA (NM_006793) was tagged with MycDDK in C-ter and cloned in pCMV6 (Origene Technologies, Inc., Rockville, MD, USA).

Techniques: Expressing, Derivative Assay, Control, Immunofluorescence, Labeling

Journal: Human molecular genetics

Article Title: Protein misfolding and clearance in the pathogenesis of a new infantile onset ataxia caused by mutations in PRDX3.

doi: 10.1093/hmg/ddac146

Figure Lengend Snippet: Figure 7. Overexpression of mutated forms of PRDX3 in HeLa cells. (A) WB analysis of PRDX3 expression in transfected Hela cells with plasmids expressing WT PRDX3 and mutants. α-Tubulin was used as loading control. (B) Densitometric quantification of proteins detected by WB. Error bars represent SEM. ∗P < 0.05, ∗∗P < 0.01, one-way ANOVA followed by Dunnett’s test compared to WT. (C) Protein levels were normalized to calculate relative presence in both fractions for WT and mutated PRDX3 proteins. (D) WB analysis from transfected HeLa cells treated with MG-132 (proteasome inhibitor) or bafilomycin (autophagic inhibitor). The autophagic substrate p62 was used as a bafilomycin control and α-tubulin as loading control.

Article Snippet: The PRDX3 cDNA (NM_006793) was tagged with MycDDK in C-ter and cloned in pCMV6 (Origene Technologies, Inc., Rockville, MD, USA).

Techniques: Over Expression, Expressing, Transfection, Control

Journal: Advanced science (Weinheim, Baden-Wurttemberg, Germany)

Article Title: Kinome-Wide Synthetic Lethal Screen Identifies PANK4 as a Modulator of Temozolomide Resistance in Glioblastoma.

doi: 10.1002/advs.202306027

Figure Lengend Snippet: Figure 7. Continued DMSO, and siPANK4 TMZ (n = 3 biological replicates). Figure was created with BioRender.com. B) Volcano plot of differentially expressed proteins following PANK4 knockdown in T98GRes cells (siPANK4 DMSO), highlighting statistically significant changes (p ≤0.05) in protein abundance compared to control (siCTRL DMSO). The -Log10(p-values) versus the Log2(fold change) in protein abundance are plotted. Horizontal line represents the significant threshold (p = 0.05). Red and blue circles indicate significantly up- or down-regulated proteins, respectively. Grey circles indicate proteins with non- significant changes in abundance following PANK4 silencing; (ns, not significant). Validation of PANK4 protein levels by western blot using tubulin as loading control is shown. C) Dotplot showing the top 20 significantly enriched Gene Ontology (GO) Biological Processes (BP) of downregulated proteins following PANK4 knockdown (siPANK4 DMSO versus siCTRL DMSO). D) Violin plot showing abundance of the 14 significantly downregulated proteins following PANK4 knockdown involved in the GO BP terms: “cellular detoxification”, “cellular response to toxic substance”, and “detoxification”. E) Western blots showing expression of PANK4, PRDX3, ALDH1A1, NQO1, and AKR1B10 in control and PANK4-depleted T98GRes (left) and U87MGRes

Article Snippet: PRDX3 (#STJ115041, 1:1000), AKR1B10 (#STJ195042, 1:1000), and Cytochrome c (#STJ97419, 1:1000) were purchased from St. John’s Laboratory.

Techniques: Knockdown, Quantitative Proteomics, Control, Biomarker Discovery, Western Blot, Expressing

Journal: International journal of cancer

Article Title: Downregulation of the c-MYC target gene, peroxiredoxin III, contributes to arsenic trioxide-induced apoptosis in acute promyelocytic leukemia.

doi: 10.1002/ijc.24341

Figure Lengend Snippet: FIGURE 5 – Overexpression of Prx-III in U937 cells inhibits ATO- induced apoptosis. (a) Untransfected (UT) U-937 cells (Lane 1). U- 937 cells (1 3 106) were stably transfected by electroporation with 50 ng of control vector (Lane 2, pcDNA3.1/neo1) or with 50 ng of pcDNA3.1-Neo-Prdx3 vector (Lanes 3 and 4) as explained in the ‘‘Material and methods’’ section. Serial dilutions were performed to obtain individual clones with moderate (U937-14.1, Lane 3) or high (U937-13.13, Lane 4) levels of Prx III expression compared with non- transfected (U937-UT, Lane 1) U-937 cells. (b) Apoptosis was meas- ured by flow cytometry after staining with Annexin V-FITC/PI. Val- ues represent the percentage of apoptotic cells relative to the total cells. Values represent means 6 SD of triplicates.

Article Snippet: Full length human Prdx3 (OriGene, Rockville, MD) was cloned into the pcDNA3.1/neo1 mammalian expression vector (Invitrogen) using the EcoRI and NotI sites to generate the pcDNA3.1Neo- Prdx3 plasmid.

Techniques: Over Expression, Stable Transfection, Transfection, Electroporation, Control, Plasmid Preparation, Clone Assay, Expressing, Cytometry, Staining

Journal: International journal of cancer

Article Title: Downregulation of the c-MYC target gene, peroxiredoxin III, contributes to arsenic trioxide-induced apoptosis in acute promyelocytic leukemia.

doi: 10.1002/ijc.24341

Figure Lengend Snippet: FIGURE 7 – ATO treatment of NB4 cells reduces the levels of c-MYC binding to its canonical E-box in the Prdx3 gene. (a) Representative eth- idium bromide-stained agarose gels of PCR products: NB4 cells (2 3 106) were treated with 2 lM ATO for 4 and 24 hr. Samples were processed as described under ‘‘Material and methods’’. Equal volumes of soluble chromatin were used for IP with c-MYC, polymerase-II or IgG antibodies. Lane 1 corresponds to the IP with the c-MYC antibody and further PCR amplification with primers A, which encompass the c-MYC canonical recognition site in the Prdx3 gene. Lane 2 corresponds to the PCR product of the total input DNA amplified with primers A. Lane 3 corresponds to the IP with the c-MYC antibody and further PCR amplification with the primers B, which amplified a negative distal site of the Prdx3 gene. Lane 4 corresponds to the PCR product of the total input DNA amplified with the primers B. Lane 5 corresponds to the PCR products after IP with the Pol-II antibody followed by amplification with primers to GAPDH. Lane 6 corresponds to the IP with the IgG antibody followed by PCR amplification with primers A. (b) Densitometric analysis of the intensity of bands of IP/c-MYC (Lane 1) relative to input DNA (Lane 2) and of IP/c-MYC (Lane 1) relative to GAPDH (Lane 5). Percentages were calculated in relation to the untreated cells. (c) U-937 cells (1 3 106) were cotransfected with either a reporter plasmid containing the full-length (T-pGL4) Prdx3 promoter or a reporter plasmid (P-pGL4) containing only one Prdx3 canonical recognition site to c-MYC, together with a plasmid containing the human c-MYC (c-MYC-pCMV6-XL5) or with an empty vector (pCMV6-XL5). RLU were calculated as described in the ‘‘Material and methods’’. Each value represents means and 6 SD of three independent experiments.

Article Snippet: Full length human Prdx3 (OriGene, Rockville, MD) was cloned into the pcDNA3.1/neo1 mammalian expression vector (Invitrogen) using the EcoRI and NotI sites to generate the pcDNA3.1Neo- Prdx3 plasmid.

Techniques: Binding Assay, Staining, Plasmid Preparation

Journal: Oxidative Medicine and Cellular Longevity

Article Title: Azelaic Acid Exerts Antileukemia Effects against Acute Myeloid Leukemia by Regulating the Prdxs/ROS Signaling Pathway

doi: 10.1155/2020/1295984

Figure Lengend Snippet: AZA upregulated Prdx2 and Prdx3 expression. (a) Differentially expressed proteins (DEPs) were identified by LC-MS/MS after AZA treatment. Then, DEPs were annotated by WEGO analysis; the changes of DEPs involved in antioxidant activity and immune response were shown on a heat map. (b) The RNA expression levels of Prdx2 and Prdx3 in Molm-13 and THP-1 cells after AZA treatment and their detection by qPCR. (c) The interaction between Prdx3 and other proteins was analyzed by STRING. (d) The protein expression levels of Prdx2 and Prdx3 in Molm-13, THP-1, and AML patient primary cells (AML-PC) after AZA treatment and their detection by western blot.

Article Snippet: Antibodies to the following proteins were used: Prdx3 was from CUSABIO (Cat# CSB-PA003861, China); β -actin (Cat# 14395-1) and Prdx2 (Cat# 10545-2) were from ProteinTech (USA).

Techniques: Expressing, Liquid Chromatography with Mass Spectroscopy, Antioxidant Activity Assay, RNA Expression, Western Blot

Journal: Oxidative Medicine and Cellular Longevity

Article Title: Azelaic Acid Exerts Antileukemia Effects against Acute Myeloid Leukemia by Regulating the Prdxs/ROS Signaling Pathway

doi: 10.1155/2020/1295984

Figure Lengend Snippet: AZA suppressed AML tumorigenicity in vivo . (a) Flow chart of the PDX animal model construction and treatment. (b) AML patient cells could be observed on the peripheral blood (PB) and bone marrow (BM) smears under a microscope. Magnification: ×100. (c) Body weight change. (d) Survival. There were 8 mice in each group. (e) The expression of CD33 in mice BM after AZA treatment and its detection by immunohistochemistry. Magnification: ×40. (f) The levels of ROS-related indices MDA, SOD, GSH, and T-AOC in blood plasma after AZA treatment. (g) The expression of Prdx2 and Prdx3 in mice spleen after AZA treatment and their detection by immunohistochemistry. Magnification: ×40. ∗ P < 0.05, ∗∗ P < 0.01, and ∗∗∗ P < 0.001.

Article Snippet: Antibodies to the following proteins were used: Prdx3 was from CUSABIO (Cat# CSB-PA003861, China); β -actin (Cat# 14395-1) and Prdx2 (Cat# 10545-2) were from ProteinTech (USA).

Techniques: In Vivo, Animal Model, Microscopy, Expressing, Immunohistochemistry, Clinical Proteomics

Journal: Parasites & Vectors

Article Title: MiR-383-5p promotes schistosomiasis-induced liver fibrosis by targeting peroxiredoxin-3

doi: 10.1186/s13071-025-06824-w

Figure Lengend Snippet: The miR-383-5p or PRDX3 expression in the mice infected with schistosome. A Area of the single egg granuloma in the mouse liver at different stages of infection (HE staining, ratio = 200 µm) and statistical analysis. B Percentage of fibrotic area in the liver of the mice at different stages of infection (Masson staining, ratio = 200 µm) and statistical analysis. C The mRNA expression level of α-SMA , collagen I , collagen III , and TGF-β in the livers of mice at different stages of schistosome infection. D The protein expression levels of α-SMA and collagen I in the livers of mice infected with schistosomes at different stages. E The miRNA expression level of miR-383-5p in the livers of mice infected with schistosomes at different stages. F The mRNA expression level of PRDX3 in the livers of mice infected with schistosomes at different stages. G Levels of ROS in the livers of mice infected with schistosomes at different stages. * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001

Article Snippet: PRDX3 heterozygous mice (PRDX3 ± ) were purchased from Cyagen Biotechnology (Suzhou, China) and bred at the JIPD.

Techniques: Expressing, Infection, Staining

Journal: Parasites & Vectors

Article Title: MiR-383-5p promotes schistosomiasis-induced liver fibrosis by targeting peroxiredoxin-3

doi: 10.1186/s13071-025-06824-w

Figure Lengend Snippet: MiR-383-5p targeted PRDX3 and downregulated its expression. A Sequence alignment of miR-383-5p and the complementary region of the 3′UTR of PRDX3 . B Fluorescent enzyme activity detection of miR-383-5p binding to the 3′ UTR of PRDX3 . C The miRNA expression level of miR-383-5p in LX-2 cells transfected with miR-383-5p mimics or inhibitors. D The mRNA expression level of PRDX3 in LX-2 cells transfected with miR-383-5p mimics or inhibitors. E The mRNA expression level of α-SMA and TGF-β in LX-2 cells transfected with miR-383-5p mimics or inhibitors. F ROS fluorescence intensity in LX-2 cells transfected with miR-383-5p mimics or inhibitors. * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001

Article Snippet: PRDX3 heterozygous mice (PRDX3 ± ) were purchased from Cyagen Biotechnology (Suzhou, China) and bred at the JIPD.

Techniques: Expressing, Sequencing, Activity Assay, Binding Assay, Transfection, Fluorescence

Journal: Parasites & Vectors

Article Title: MiR-383-5p promotes schistosomiasis-induced liver fibrosis by targeting peroxiredoxin-3

doi: 10.1186/s13071-025-06824-w

Figure Lengend Snippet: The degree of liver lesions in mice infected with schistosomes injected with the mmu-miR-383-5p-AAV8 overexpression plasmid. A The miRNA expression of miR-383-5p in the livers of mice infected with schistosomes. B The mRNA expression level of PRDX3 in the livers of mice infected with schistosomes. C Area of single egg granulomas in the mouse liver (HE staining) and statistical analysis. D Percentage of fibrotic area in the livers of mice (Masson staining) and statistical analysis. E The mRNA expression level of α-SMA , collagen I , M M P 9 , T I M P 1 , and TGF-β in the livers of mice infected with schistosomes. F MiR-383-5p increased the level of ROS in the livers of mice infected with schistosomes. * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001

Article Snippet: PRDX3 heterozygous mice (PRDX3 ± ) were purchased from Cyagen Biotechnology (Suzhou, China) and bred at the JIPD.

Techniques: Infection, Injection, Over Expression, Plasmid Preparation, Expressing, Staining

Journal: Parasites & Vectors

Article Title: MiR-383-5p promotes schistosomiasis-induced liver fibrosis by targeting peroxiredoxin-3

doi: 10.1186/s13071-025-06824-w

Figure Lengend Snippet: Liver fibrotic lesions are exacerbated in PRDX3 knockout mice infected with schistosomes. A Pathological sections of liver granulomas (HE staining) and the area of a single egg granuloma in WT and PRDX3 knockout mice. B Pathological sections of liver fibrosis (Masson staining) in WT and PRDX3 knockout mice and the fibrotic area percentage. C The mRNA expression levels of α-SMA , TGF-β , collagen I , and collagen III in the livers of WT and PRDX3 knockout mice. D Knockout of PRDX3 increased ROS levels in the livers of schistosome-infected mice. * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001

Article Snippet: PRDX3 heterozygous mice (PRDX3 ± ) were purchased from Cyagen Biotechnology (Suzhou, China) and bred at the JIPD.

Techniques: Knock-Out, Infection, Staining, Expressing