Journal: International Journal of Molecular Sciences

Article Title: The Protective Role of DUSP4 in Retinal Pigment Epithelium Senescence and Degeneration

doi: 10.3390/ijms26083735

Figure Lengend Snippet: The expression of DUSP4 in RPE of dry AMD model. ( A ). Diagram illustrating SI-induced RPE damage in mice. ( B ). The expression of DUSP4 in the RPE of mice with SI injection for 24 h ( n = 3). ( C ). Schematic diagram of ARPE-19 cells exposed to SI. ( D ). The mRNA expression of DUSP4 in ARPE-19 cells treated with SI (200 μg/mL; 500 μg/mL) for 24 h. ( E ). The protein expression of DUSP4 in ARPE-19 cells treated with SI at concentrations of 200 µg/mL or 500 µg/mL for 24 h. Band density was analyzed using ImageJ.

Article Snippet: Human DUSP4 overexpression plasmids and control plasmids (GeneCopoeia, EX-A0606-M98, Rockville, MD, USA) were used in this study.

Techniques: Expressing, Injection

Journal: International Journal of Molecular Sciences

Article Title: The Protective Role of DUSP4 in Retinal Pigment Epithelium Senescence and Degeneration

doi: 10.3390/ijms26083735

Figure Lengend Snippet: RPE senescence correlates with elevated DUSP4 expression. ( A ). APOE expression in mouse RPE 24 h after SI injection. ( B ). p16 and p21 expression in mouse RPE 24 h after SI injection. ( C ). APOE expression in ARPE-19 cells exposed to SI for 24 h. ( D ). p16 and p21 expression in ARPE-19 cells treated with SI for 24 h. ( E ). Protein expression of APOE, p16, and p21 in ARPE-19 cells 24 h after SI treatment. Band density was analyzed using ImageJ 1.48. ( F ). qPCR-quantified APOE expression in RPE from both young (10-week-old, n = 3) and old mice (15-month-old, n = 3). ( G ). qPCR-quantified DUSP4 expression in RPE of young and old mice.

Article Snippet: Human DUSP4 overexpression plasmids and control plasmids (GeneCopoeia, EX-A0606-M98, Rockville, MD, USA) were used in this study.

Techniques: Expressing, Injection

Journal: International Journal of Molecular Sciences

Article Title: The Protective Role of DUSP4 in Retinal Pigment Epithelium Senescence and Degeneration

doi: 10.3390/ijms26083735

Figure Lengend Snippet: DUSP4 knockdown correlates with severe visual impairment in dry AMD mice model. ( A ). Schematic of an SI-induced dry AMD model with DUSP4 knockdown in the RPE. ( B ). Visual function comparison between DUSP4_KD and control groups in AMD mice: DUSP4_KD ( n = 19) and control ( n = 17). ( C ). Retinal structural damage in DUSP4_KD and control groups: DUSP4_KD ( n = 6) and control ( n = 6). ( D ). ZO-1 staining of RPE/choroid flat mount showed the damage of RPE in both DUSP4_KD and control groups: DUSP4_KD ( n = 5) and control ( n = 5). The proportions of damage areas were calculated by ImageJ 1.48. Statistical significance was determined by using the unpaired t -test.

Article Snippet: Human DUSP4 overexpression plasmids and control plasmids (GeneCopoeia, EX-A0606-M98, Rockville, MD, USA) were used in this study.

Techniques: Knockdown, Comparison, Control, Staining

Journal: International Journal of Molecular Sciences

Article Title: The Protective Role of DUSP4 in Retinal Pigment Epithelium Senescence and Degeneration

doi: 10.3390/ijms26083735

Figure Lengend Snippet: DUSP4 depletion enhances senescence marker expression in RPE. ( A ). DUSP4 knockout upregulates APOE, p16, and p21 expression in ARPE-19 cells. ( B ). DUSP4 overexpression reverses senescence marker upregulation in DUSP4_KO-1 cells. ( C ). DUSP4 overexpression reverses senescence marker upregulation in DUSP4_KO-2 cells. Band density was quantified using ImageJ 1.48. Statistical significance was determined by using the unpaired t -test.

Article Snippet: Human DUSP4 overexpression plasmids and control plasmids (GeneCopoeia, EX-A0606-M98, Rockville, MD, USA) were used in this study.

Techniques: Marker, Expressing, Knock-Out, Over Expression

Journal: International Journal of Molecular Sciences

Article Title: The Protective Role of DUSP4 in Retinal Pigment Epithelium Senescence and Degeneration

doi: 10.3390/ijms26083735

Figure Lengend Snippet: DUSP4 downregulated the p38, p53, and NF-κB signaling pathways. ( A ). p-p38, p53, and p-NF-κB expression in DUSP4_KO cell lines. ( B ). DUSP4 overexpression attenuated p-p38, p53, and p-NF-κB expression in DUSP4_KO-1 cells. ( C ). DUSP4 overexpression attenuated p-p38, p53, and p-NF-κB expression in DUSP4_KO-2 cells. Band density was quantified using ImageJ 1.48. Statistical significance was determined by using the unpaired t -test.

Article Snippet: Human DUSP4 overexpression plasmids and control plasmids (GeneCopoeia, EX-A0606-M98, Rockville, MD, USA) were used in this study.

Techniques: Protein-Protein interactions, Expressing, Over Expression

Journal: PLoS ONE

Article Title: The Anti-Apoptotic and Cardioprotective Effects of Salvianolic Acid A on Rat Cardiomyocytes following Ischemia/Reperfusion by DUSP-Mediated Regulation of the ERK1/2/JNK Pathway

doi: 10.1371/journal.pone.0102292

Figure Lengend Snippet: In the SAA+I/R group, cardiomyocytes were cultivated for 1 h, and I/R was performed after pretreatment with 10 µM for 12 h. In the PD+SAA+I/R group, cardiomyocytes were pretreated with PD for 30 min prior to SAA pretreatment, after incubation with SAA, I/R was performed. In the SP+I/R groups, cardiomyocytes were pretreated with SP for 30 min prior to ischemia, after ischemia, reperfusion was followed. Bar graph a, b, c representative DUSP2, DUSP16, DUSP4 respectively. All data were expressed as mean ±SEM, n = 3, *P<0.05, **P<0.01 versus CON. $ P<0.05, $$ P<0.01versus I/R. # P<0.05 versus SAA+I/R. & P<0.05 versus PD+SAA+I/R.

Article Snippet: Equal protein loading was confirmed by probing for β-actin, and the membranes were probed overnight at 4°C with rabbit polyclonal primary antibodies or mouse monoclonal antibodies (at a dilution of 1∶1000) against the following proteins: ERK1/2, JNK, dual specificity protein phosphatase 2 (DUSP2), dual specificity protein phosphatase 4 (DUSP4), dual specificity protein phosphatase 16 (DUSP16), phospho-ERK1/2 (p-ERK1/2), phospho-JNK (p-JNK), phospho-DUSP2 (p-DUSP2), phospho-DUSP4 (p-DUSP4), phospho-DUSP16 (p-DUSP16) (1∶1000; Cell Signaling Technology, MA, USA), Bcl-2, Bax, caspase 3 (1∶500; Santa Cruz, USA) and β-actin (1∶1000; Zhongshan, Beijing, China).

Techniques: Incubation

Journal: PLoS ONE

Article Title: The Anti-Apoptotic and Cardioprotective Effects of Salvianolic Acid A on Rat Cardiomyocytes following Ischemia/Reperfusion by DUSP-Mediated Regulation of the ERK1/2/JNK Pathway

doi: 10.1371/journal.pone.0102292

Figure Lengend Snippet: (a) Effects of SAA and siRNA-DUSP4 on p-ERK(44 KDa, 42 KDa) and p-JNK(54 KDa, 46 KDa); (b) Effects of SAA and siRNA-DUSP16 on p-ERK and p-JNK; (C) Effects of SAA and siRNA-DUSP2 on p-ERK and p-JNK; Cardiomyocytes was transfected siRNA-DUSP2/4/16, then SAA pretreatment for 30 min before I/R. All data were expressed as mean ±SEM, n = 3, *P<0.05, **P<0.01 versus I/R group. # P<0.05, ## P<0.01 versus si-DUSP+I/R group. $ P<0.05, $$ P<0.01versus SAA+ I/R group.

Article Snippet: Equal protein loading was confirmed by probing for β-actin, and the membranes were probed overnight at 4°C with rabbit polyclonal primary antibodies or mouse monoclonal antibodies (at a dilution of 1∶1000) against the following proteins: ERK1/2, JNK, dual specificity protein phosphatase 2 (DUSP2), dual specificity protein phosphatase 4 (DUSP4), dual specificity protein phosphatase 16 (DUSP16), phospho-ERK1/2 (p-ERK1/2), phospho-JNK (p-JNK), phospho-DUSP2 (p-DUSP2), phospho-DUSP4 (p-DUSP4), phospho-DUSP16 (p-DUSP16) (1∶1000; Cell Signaling Technology, MA, USA), Bcl-2, Bax, caspase 3 (1∶500; Santa Cruz, USA) and β-actin (1∶1000; Zhongshan, Beijing, China).

Techniques: Transfection

Journal: PLoS ONE

Article Title: The Anti-Apoptotic and Cardioprotective Effects of Salvianolic Acid A on Rat Cardiomyocytes following Ischemia/Reperfusion by DUSP-Mediated Regulation of the ERK1/2/JNK Pathway

doi: 10.1371/journal.pone.0102292

Figure Lengend Snippet: SAA could play anti-apoptosis effect from myocardial IRI via the activation of ERK1/2 and inhibition of JNK, which resulted upregulation of ERK1/2 and downregulation of JNK, increased Bcl-2 and reduce Bax protein expression. JNK could inhibit the activation of ERK1/2 by DUSP2 mediating dephosphorylation of ERK1/2, and ERK1/2 mainly inhibits JNK activity by DUSP4/16-mediated dephosphorylation of JNK. SAA could activate ERK1/2 by inhibiting DUSP2-mediated JNK and inhibit JNK by activating DUSP4/16-mediated ERK1/2 to play anti-apoptosis from myocardial IRI.

Article Snippet: Equal protein loading was confirmed by probing for β-actin, and the membranes were probed overnight at 4°C with rabbit polyclonal primary antibodies or mouse monoclonal antibodies (at a dilution of 1∶1000) against the following proteins: ERK1/2, JNK, dual specificity protein phosphatase 2 (DUSP2), dual specificity protein phosphatase 4 (DUSP4), dual specificity protein phosphatase 16 (DUSP16), phospho-ERK1/2 (p-ERK1/2), phospho-JNK (p-JNK), phospho-DUSP2 (p-DUSP2), phospho-DUSP4 (p-DUSP4), phospho-DUSP16 (p-DUSP16) (1∶1000; Cell Signaling Technology, MA, USA), Bcl-2, Bax, caspase 3 (1∶500; Santa Cruz, USA) and β-actin (1∶1000; Zhongshan, Beijing, China).

Techniques: Activation Assay, Inhibition, Expressing, De-Phosphorylation Assay, Activity Assay

Journal: bioRxiv

Article Title: AMPK-independent LKB1 activity is required for efficient epithelial ovarian cancer metastasis

doi: 10.1101/591073

Figure Lengend Snippet: DUSP4 expression is increased due to sustained LKB1 loss. (A) Lysates from OVCAR8, OVCAR8- STK11 KO, HeyA8 and HeyA8- STK11 KO cells grown in adherent and spheroid culture were subjected to reverse-phase protein array analysis. Data is presented as a heat map of the log 2 -transformed fold-change in expression comparing STK11 KO cells to their respective parental cell controls. DUSP4 expression was consistently increased due to LKB1 loss in every sample analyzed. (B) Immunoblot analysis confirming DUSP4 expression is increased in all three EOC cell lines lacking LKB1 as compared with their respective controls. (C) Immunoblot analysis demonstrating increased DUSP4 protein in OVCAR8- STK11 KO tumour xenografts as compared with OVCAR8 tumours. LKB1 loss was confirmed, and tubulin used as a loading control. (D) Densitometric analysis of immunoblots in (C). Data are presented as the pixel intensity volume for DUSP4 normalized to tubulin with the mean value for OVCAR8 tumours set to 1. Statistical analysis was performed using a two-tailed Student’s t- test (*, p < 0.05). (E) Knockdown of DUSP4 in HeyA8 and HeyA8- STK11 KO cells as confirmed by immunoblot analysis. (F) Restoration of intact spheroid formation in HeyA8- STK11 KO cells resulting from DUSP4 knockdown. Scale bar represents 250 µm (G) Rescue of cell viability in HeyA8- STK11 KO spheroids due to DUSP4 knockdown as determined by Cell-Titer Glo assay in a 96-well ULA format. Two-way ANOVA and Tukey’s multiple comparisons test was performed (****, p < 0.0001).

Article Snippet: Antibodies against LKB1 (#3050S), phospho-AMPKα (T172) (#2535S), AMPKα (#5832S), phospho-p44/42 ERK (T202/Y204) (#9101S), phospho-JNK (T183/Y185) (#4668P), phospho-p38 (T180/Y182) (#4511S), and DUSP4 (#5149S) were purchased from Cell Signaling (Danvers, MA) and used at 1:1000 in 5% bovine serum albumin (BSA)/TBS-T. Antibody against CA9 (AF2188; 1 μg/mL) was purchased from R&D Systems (Minneapolis, MN).

Techniques: Expressing, Protein Array, Transformation Assay, Western Blot, Two Tailed Test, Glo Assay

Journal: Endocrinology

Article Title: In Utero Exposure to a High-Fat Diet Programs Hepatic Hypermethylation and Gene Dysregulation and Development of Metabolic Syndrome in Male Mice

doi: 10.1210/en.2017-00334

Figure Lengend Snippet: qRT-PCR of Genes Involved in Metabolism, Cell Signaling/Development, and Transcription Regulation in 5-Week-Old Liver

Article Snippet: Other canonical signaling pathways with significant numbers of differentially methylated and expressed genes include the aryl hydrocarbon receptor (four genes), extracellular signal–regulated kinase/mitogen-activated protein kinase (four genes), and sphingosine-1-phosphate (three genes). table ft1 table-wrap mode="anchored" t5 Table 2. caption a7 Metabolism and Cell Signaling/Development Control HF Pathway Aldh1l2 1.38 ± 0.57 3.84 ± 0.51 a Amino acid metabolism Mapkapk2 1.09 ± 0.20 2.92 ± 0.73 a Carbohydrate metabolism Dusp4 1.15 ± 0.27 3.72 ± 0.78 a Cell to cell signaling Tp53 (Trp53) 1.18 ± 0.40 2.38 ± 0.28 a Cellular development Ptprf 1.02 ± 0.10 3.13 ± 0.89 a Lipid metabolism Timp3 1.25 ± 0.46 5.06 ± 1.13 a Lipid metabolism Trio 1.16 ± 0.30 2.00 ± 0.18 a Lipid metabolism ILK pathway Control HF Pathway Itgb4 1.15 ± 0.28 2.49 ± 0.48 a ILK pathway Mmp9 1.34 ± 0.45 2.92 ± 0.43 a ILK pathway Sh2b2 1.07 ± 0.18 1.65 ± 0.17 a ILK pathway Tgfb1l1 1.04 ± 0.14 2.52 ± 0.60 a ILK pathway Transcription regulator Control HF Function Etv6 1.08 ± 0.21 2.59 ± 0.54 a Cell-to-cell signaling and interaction Tgfb1l1 1.04 ± 0.14 2.52 ± 0.60 a Cellular development, growth, and proliferation Jdp2 1.05 ± 0.18 4.19 ± 1.33 a Hereditary disorder Sox9 1.11 ± 0.25 6.34 ± 1.75 a Lipid metabolism Elf3 1.03 ± 0.13 2.21 ± 0.42 a Lipid metabolism, cell signaling Nfia 1.27 ± 0.49 3.04 ± 0.36 a Cellular development Open in a separate window Values are mean ± SEM or as otherwise indicated.

Techniques:

Journal: American Journal of Physiology - Gastrointestinal and Liver Physiology

Article Title: Genome-wide transcriptome analysis identifies novel gene signatures implicated in human chronic liver disease

doi: 10.1152/ajpgi.00077.2013

Figure Lengend Snippet: qPCR validation of new genes that are differentially expressed in Shp−/− mice, human liver steatosis, fibrosis, NASH, and alcohol and hepatitis C cirrhosis. A: from left to right, peptidoglycan recognition protein 2 (PGLYRP2), dual specific phosphatase-4 (DUSP4), and tetraspanin 4 (TSPAN4). B: from left to right, thrombospondin 1 (THBS1), SPARC-related modular calcium binding protein-2 (SMOC2), and SHP. Expression levels of each gene for each sample were normalized to the hypoxanthine phosphoribosyltransferase 1 expression level of that sample as an internal control. ¥P <0.001, ‡P <0.01, and *P <0.05. The no. of specimens in each group is as follows: HCV cirrhosis (n = 39), alcohol cirrhosis (n = 28), NASH cirrhosis (n = 13), fibrosis (n = 7), steatosis (n = 15), and control (n = 24). C: immunohistochemistry analysis of DUSP4 protein in human alcohol and hepatitis C cirrhosis compared with the normal liver. Two representative results from each group are shown. N, normal; AC, alcohol cirrhosis; HC, HCV cirrhosis. Top: DUSP4 protein expression. Bottom: DUSP4 overlay with DAPI staining. Magnification ×20.

Article Snippet: Detection of dual specific phosphatase-4 (DUSP4) protein levels was carried out using a DUSP4 mouse monoclonal antibody (SAB1403748-100UG; Sigma-Aldrich).

Techniques: Binding Assay, Expressing, Immunohistochemistry, Staining

Journal: Frontiers in Microbiology

Article Title: Echinococcus granulosus sensu lato promotes osteoclast differentiation through DUSP4-MAPK signaling in osseous echinococcosis

doi: 10.3389/fmicb.2025.1558603

Figure Lengend Snippet: PSC intervention downregulates DUSP4 and upregulates the MAPK signaling pathway. (A) mRNA expression levels of DUSP2 and DUSP4 following different doses of PSC intervention. (B) Protein expression levels of DUSP4 after different doses of PSC intervention. (C) Quantification of DUSP4 protein levels shown in (B) . (D) Visualization of F-actin ring formation and DUSP4 expression in osteoclasts after different doses of PSC intervention. Green: F-actin; red: DUSP4; blue: DAPI. Magnification ×40. (E) Quantification of the F-actin ring area and the absolute and relative fluorescence intensity of DUSP4 shown in (D) . Data represent three independent experiments. ns, not significant; * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001.

Article Snippet: The membrane was blocked with 5% bovine serum albumin (BSA) blocking solution (BIOTEK, China) for 2 h, and then incubated overnight at 4°C with primary antibodies: DUSP4 (1:1000; Boster, #OT17C11); GAPDH (1:2000; Boster, #BG-7) ERK (1:2,000; #4695), p-ERK (1:1,000; #4370), JNK (1:2,000; #9252), p-JNK (1:1,000; #4668), p38 (1:2,000; #8690), p-p38 (1:1,000; #4511) (Cell Signaling Technology, Inc.); MMP-9 (1:1000; #ab76003); c-Fos (1:2,000; #ab190289), TRAP (1:1,000; #ab191406), NFATc1 (4 μg/mL; #ab2796), Cathepsin K (1:2,000; #ab19027) (Abcam, Inc).

Techniques: Expressing, Fluorescence

Journal: Frontiers in Microbiology

Article Title: Echinococcus granulosus sensu lato promotes osteoclast differentiation through DUSP4-MAPK signaling in osseous echinococcosis

doi: 10.3389/fmicb.2025.1558603

Figure Lengend Snippet: Overexpression of DUSP4 affects osteoclast formation. (A) mRNA expression levels of DUSP4 in control, lentiviral-transfected null, and DUSP4-overexpression groups. (B) Protein levels of DUSP4 in the same groups. (C) Quantification of (B) . (D) Cell viability assay in the same groups. (E) TRAP staining of osteoclasts in control and DUSP4-overexpression groups after PSC intervention. Magnification ×40. (F) Quantification of the area occupied by TRAP-positive cells and the number of TRAP-positive cells shown in (E) . (G) F-actin ring staining in control and DUSP4-overexpression groups after PSC intervention green: F-actin; blue: DAPI. Magnification ×40. (H) Quantification of the F-actin ring area and fluorescence intensity shown in (G) . Data represent three independent experiments, and significance was determined using one-way ANOVA. ns, no significance; * p < 0.05, ** p < 0.01, and *** p < 0.001.

Article Snippet: The membrane was blocked with 5% bovine serum albumin (BSA) blocking solution (BIOTEK, China) for 2 h, and then incubated overnight at 4°C with primary antibodies: DUSP4 (1:1000; Boster, #OT17C11); GAPDH (1:2000; Boster, #BG-7) ERK (1:2,000; #4695), p-ERK (1:1,000; #4370), JNK (1:2,000; #9252), p-JNK (1:1,000; #4668), p38 (1:2,000; #8690), p-p38 (1:1,000; #4511) (Cell Signaling Technology, Inc.); MMP-9 (1:1000; #ab76003); c-Fos (1:2,000; #ab190289), TRAP (1:1,000; #ab191406), NFATc1 (4 μg/mL; #ab2796), Cathepsin K (1:2,000; #ab19027) (Abcam, Inc).

Techniques: Over Expression, Expressing, Control, Transfection, Viability Assay, Staining, Fluorescence

Journal: Frontiers in Microbiology

Article Title: Echinococcus granulosus sensu lato promotes osteoclast differentiation through DUSP4-MAPK signaling in osseous echinococcosis

doi: 10.3389/fmicb.2025.1558603

Figure Lengend Snippet: Effects of DUSP4 on the MAPK pathway and osteoclast-related genes. (A) Western blot analysis showing changes in MAPK signaling pathway components (p-JNK, p-ERK, and p-p38) in osteoclasts after PSC intervention in control and DUSP4-overexpression groups. (B) Quantification of MAPK pathway phosphorylation levels in osteoclasts from control and DUSP4-overexpression groups, as shown in (A) . (C) mRNA expression levels of osteoclast-related proteins (DUSP4, MMP9, NFATc1, TRAP, and CTSK) after PSC intervention in control and DUSP4-overexpression groups. (D) Western blot analysis of osteoclast-related proteins (DUSP4, MMP9, NFATc1, CTSK, and c-fos) after PSC intervention in control and overexpression groups. (E) Quantification of osteoclast-related proteins expression levels in (D) . Data represent three independent experiments, and significance was determined using one-way ANOVA. ns, no significance; * p < 0.05, ** p < 0.01, and *** p < 0.001.

Article Snippet: The membrane was blocked with 5% bovine serum albumin (BSA) blocking solution (BIOTEK, China) for 2 h, and then incubated overnight at 4°C with primary antibodies: DUSP4 (1:1000; Boster, #OT17C11); GAPDH (1:2000; Boster, #BG-7) ERK (1:2,000; #4695), p-ERK (1:1,000; #4370), JNK (1:2,000; #9252), p-JNK (1:1,000; #4668), p38 (1:2,000; #8690), p-p38 (1:1,000; #4511) (Cell Signaling Technology, Inc.); MMP-9 (1:1000; #ab76003); c-Fos (1:2,000; #ab190289), TRAP (1:1,000; #ab191406), NFATc1 (4 μg/mL; #ab2796), Cathepsin K (1:2,000; #ab19027) (Abcam, Inc).

Techniques: Western Blot, Control, Over Expression, Phospho-proteomics, Expressing

Journal: Frontiers in Microbiology

Article Title: Echinococcus granulosus sensu lato promotes osteoclast differentiation through DUSP4-MAPK signaling in osseous echinococcosis

doi: 10.3389/fmicb.2025.1558603

Figure Lengend Snippet: DUSP4 inhibits osteoclasts and attenuates bone destruction in osseous echinococcosis. (A) X-ray examination of long bones from mice treated with empty vector, lentiviral DUSP4, or left untreated in the affection of PSC after 6 months, with red rectangle indicating cyst. (B) Micro-CT images of long bones from each treatment group, with red arrows indicating bone defects. (C) HE staining of bone tissue sections from each treatment group. Magnification ×20. (D) Western blot analysis of osteoclast-related proteins (DUSP4 and CTSK) after PSC intervention in control and DUSP4-overexpression groups. (E) Quantification of osteoclast-related protein expression levels in osteoclasts from control and DUSP4-overexpression groups, as shown in (D) . Data are presented as mean ± SD from five mice per group. * p < 0.05, ** p < 0.01, and *** p < 0.001.

Article Snippet: The membrane was blocked with 5% bovine serum albumin (BSA) blocking solution (BIOTEK, China) for 2 h, and then incubated overnight at 4°C with primary antibodies: DUSP4 (1:1000; Boster, #OT17C11); GAPDH (1:2000; Boster, #BG-7) ERK (1:2,000; #4695), p-ERK (1:1,000; #4370), JNK (1:2,000; #9252), p-JNK (1:1,000; #4668), p38 (1:2,000; #8690), p-p38 (1:1,000; #4511) (Cell Signaling Technology, Inc.); MMP-9 (1:1000; #ab76003); c-Fos (1:2,000; #ab190289), TRAP (1:1,000; #ab191406), NFATc1 (4 μg/mL; #ab2796), Cathepsin K (1:2,000; #ab19027) (Abcam, Inc).

Techniques: Plasmid Preparation, Micro-CT, Staining, Western Blot, Control, Over Expression, Expressing

Journal: Frontiers in Microbiology

Article Title: Echinococcus granulosus sensu lato promotes osteoclast differentiation through DUSP4-MAPK signaling in osseous echinococcosis

doi: 10.3389/fmicb.2025.1558603

Figure Lengend Snippet:

Article Snippet: The membrane was blocked with 5% bovine serum albumin (BSA) blocking solution (BIOTEK, China) for 2 h, and then incubated overnight at 4°C with primary antibodies: DUSP4 (1:1000; Boster, #OT17C11); GAPDH (1:2000; Boster, #BG-7) ERK (1:2,000; #4695), p-ERK (1:1,000; #4370), JNK (1:2,000; #9252), p-JNK (1:1,000; #4668), p38 (1:2,000; #8690), p-p38 (1:1,000; #4511) (Cell Signaling Technology, Inc.); MMP-9 (1:1000; #ab76003); c-Fos (1:2,000; #ab190289), TRAP (1:1,000; #ab191406), NFATc1 (4 μg/mL; #ab2796), Cathepsin K (1:2,000; #ab19027) (Abcam, Inc).

Techniques:

Journal: Journal of Cancer

Article Title: miR-1226-3p Promotes Sorafenib Sensitivity of Hepatocellular Carcinoma via Downregulation of DUSP4 Expression.

doi: 10.7150/jca.31804

Figure Lengend Snippet: Fig. 3. miR-1226-3p downregulated DUSP4 expression. (A) The binding sites for miR-1226-3p in the 3’-UTRs of DUSP4 was determined. (B) HepG2 cells were co-transfected miR-1226-3p with pGL3-3’UTR DUSP4 (wild type or mutated) or pGL3-promoter vector (control), and the luciferase reporter assays were conducted to confirm the relationships between miR-1226-3p and DUSP4. (C, D) Relative expression of DUSP4 was measured respectively by qRT-PCR after HepG2 cells transfected with miRNA-1226-3p inhibitor/negative control and SK-HEP-1 cells transfected with miRNA-1226-3p mimic/negative control. (E) Western blot analysis of DUSP4 and β-tubulin were performed. (NC: negative control. IH: miRNA-1226-3p inhibitor. MIC: miRNA-1226-3p mimic) (*p < 0.05)

Article Snippet: The primary tumors were excised and analysed by immunohistochemistry of DUSP4 antibody (Proteintech Group, Wuhan, China) and PCNA antibody (Proteintech Group, Wuhan, China).

Techniques: Expressing, Binding Assay, Transfection, Plasmid Preparation, Control, Luciferase, Quantitative RT-PCR, Negative Control, Western Blot

Journal: Journal of Cancer

Article Title: miR-1226-3p Promotes Sorafenib Sensitivity of Hepatocellular Carcinoma via Downregulation of DUSP4 Expression.

doi: 10.7150/jca.31804

Figure Lengend Snippet: Fig. 4. Knockdown of DUSP4 increased sorafenib sensitivity and activated the JNK signaling pathway. (A) DUSP4 was knocked down in SK-HEP-1 cells by siRNA and qRT-PCR was performed to analyze DUSP4 expression. (B, C) The viability and apoptosis of SK-HEP-1 cells transfected with DUSP4 siRNA or negative control siRNA were respectively measured by CCK-8 assay and flow cytometric analysis after treating with 0 or 10 µM sorafenib for 48 h. (D) Western blot analysis of DUSP4, JNK, ERK, p38, Bcl-2, Bax and β-tubulin were performed. (NC: negative control. siDUSP4: DUSP4 siRNA. SR10: 10 µM sorafenib) (*p < 0.05)

Article Snippet: The primary tumors were excised and analysed by immunohistochemistry of DUSP4 antibody (Proteintech Group, Wuhan, China) and PCNA antibody (Proteintech Group, Wuhan, China).

Techniques: Knockdown, Quantitative RT-PCR, Expressing, Transfection, Negative Control, CCK-8 Assay, Western Blot

Journal: Journal of Cancer

Article Title: miR-1226-3p Promotes Sorafenib Sensitivity of Hepatocellular Carcinoma via Downregulation of DUSP4 Expression.

doi: 10.7150/jca.31804

Figure Lengend Snippet: Fig. 5. miR-1226-3p overexpression promoted the in vivo antitumor effects of sorafenib. (A) Representative photos of tumors at endpoint. Graph showing the weight of tumors generated in each group. (B) DUSP4 and PCNA expression levels were analysed by immunohistochemistry in SK-HEP-1/miR-1226-3p xenografts and SK-HEP-1/control xenografts with or without sorafenib treatment. Scale bars: 50 µm (200×) (NC: negative control) (*p < 0.05).

Article Snippet: The primary tumors were excised and analysed by immunohistochemistry of DUSP4 antibody (Proteintech Group, Wuhan, China) and PCNA antibody (Proteintech Group, Wuhan, China).

Techniques: Over Expression, In Vivo, Generated, Expressing, Immunohistochemistry, Control, Negative Control