Journal: bioRxiv

Article Title: Comparative analysis of wavelength-specific UV stress granule formation

doi: 10.64898/2026.03.15.711948

Figure Lengend Snippet: Representative images of SG formation by G3BP1 and TIA1 signals in wt U2OS cells treated as indicated. Cells were either untreated, treated with 250μM As III for 1h, or exposed to 15mJ/cm 2 of UV. UV samples were harvested and processed for imaging 4 hours after exposure. Yellow arrows indicate SGs. Scale bar = 20μm.

Article Snippet: The following antibodies were used in this study; G3BP1 (Proteintech® 13057 (rabbit) and 66486 (mouse)), S6 Ribosomal protein (RPS6) (ABclonal A6058), TIA1 (Proteintech® 12133), RACK1 (Proteintech® 66940), TRAF2 (Proteintech® 26846 (rabbit) 67315 (mouse)), Geminin (Proteintech® 10802), DHX9 (Proteintech®17721), cytokeratin 8 (Invitrogen, 06318), and eIF3n (Santa Cruz, 137214).

Techniques: Imaging

Journal: bioRxiv

Article Title: Comparative analysis of wavelength-specific UV stress granule formation

doi: 10.64898/2026.03.15.711948

Figure Lengend Snippet: (A) Representative images of SG formation by G3BP1 and TIA1 signals in HaCaT cells treated as indicated. Cells were either untreated, treated with 250μM As III for 1h, or exposed to 15mJ/cm 2 of UV. UV samples were harvested and processed for imaging 4 hours after exposure. (B) Quantification of SG formation by G3BP1 and TIA1 signals in wt U2OS, HaCaT, and wt MEF cells treated as indicated. Cells were either untreated, treated with 250μM As III for 1h, or exposed to 15mJ/cm 2 of UV. UV samples were harvested and processed for imaging 4 hours after exposure. At least 250 cells and 3 fields of view were scored to calculate percent SG formation. n =3; error bars are ±SD; ns P > 0.05, ** P ≤ 0.01, **** P ≤ 0.0001 by one-way ANOVA and Dunnett’s post-hoc test. (C) Quantification of SG formation by G3BP1 and TIA1 signals in wt U2OS cells treated as indicated. Cells were either untreated, treated with 250μM As III for 1h, or exposed to 150mJ/cm 2 of UV. UV samples were harvested and processed for imaging 4 hours after exposure. At least 250 cells and 3 fields of view were scored to calculate percent SG formation. n =3; error bars are ±SD; ns P > 0.05, **** P ≤ 0.0001 by one-way ANOVA and Dunnett’s post-hoc test. Scale bar = 20μm.

Article Snippet: The following antibodies were used in this study; G3BP1 (Proteintech® 13057 (rabbit) and 66486 (mouse)), S6 Ribosomal protein (RPS6) (ABclonal A6058), TIA1 (Proteintech® 12133), RACK1 (Proteintech® 66940), TRAF2 (Proteintech® 26846 (rabbit) 67315 (mouse)), Geminin (Proteintech® 10802), DHX9 (Proteintech®17721), cytokeratin 8 (Invitrogen, 06318), and eIF3n (Santa Cruz, 137214).

Techniques: Imaging

Journal: Cell Death & Disease

Article Title: Arginine dependency in omental metastasis of epithelial ovarian cancer reveals a therapeutic vulnerability

doi: 10.1038/s41419-026-08606-3

Figure Lengend Snippet: A Scheme of L -arginine-immobilized NHS magnetic beads and the enrichment strategy for arginine-binding proteins. B Volcano plot of arginine- and leucine-binding proteins. C , D GO analysis of arginine-binding proteins in A2780 cells. E Venn diagram showing arginine-binding proteins that were upregulated in both 500 μM arginine-treated A2780 ovarian cancer cells and omentum metastases. F Relative abundance of DDX3X protein captured by arginine or leucine-coupled magnetic beads. G WB detection of DDX3X in A2780 cells with arginine treatment, or lysate from omentum metastasis, and elution after purification with L -leucine- or L -arginine-immobilized NHS magnetic beads. H Molecular docking between DDX3X (HMDB ID: HMDB0000517) and L -arginine (PubChem CID: 6322) performed using Discovery Studio. I Molecular dynamics (MD) simulation was performed using Gromacs. The backbone root mean square deviation (RMSD) of the DDX3X- L -arginine complex over the 100 ns MD simulation was shown. J Surface plasmon resonance analysis for the binding of L -arginine to DDX3X. Data were shown as the mean ± SD. The p value was calculated using an unpaired two-tailed Student’s t -test ( F ). ** p < 0.01.

Article Snippet: Permeabilized cells were then sequentially incubated with a primary rabbit anti-DDX3X antibody (Cat. No. 11115-1-AP, Proteintech, Wuhan, China) and a secondary Goat Anti-Rabbit IgG antibody (Cat. No. AS070, ABclonal, Wuhan, China).

Techniques: Magnetic Beads, Binding Assay, Purification, SPR Assay, Two Tailed Test

Journal: Cell Death & Disease

Article Title: Arginine dependency in omental metastasis of epithelial ovarian cancer reveals a therapeutic vulnerability

doi: 10.1038/s41419-026-08606-3

Figure Lengend Snippet: A Representative confocal microscopy images and immunofluorescence analysis of DDX3X in A2780 cells treated with arginine at the indicated times. Scale bars, 10 μm. B WB analyses of DDX3X, histone H3, and tubulin protein levels in cytoplasmic and nuclear fractions of A2780 cells under the indicated treatments. C Representative confocal microscopy images of DDX3X immunofluorescence in A2780 cells treated as indicated. Scale bars, 10 μm. D WB analyses of DDX3X, CRM1, histone H3, and tubulin protein levels in the cytoplasmic and nuclear fractions of A2780 cells under the indicated treatments. E Representative confocal microscopy images of Flag immunofluorescence in A2780 shDDX3X cells treated as indicated. Scale bars, 10 μm. F WB analyses of Flag, histone H3, and tubulin protein levels in the cytoplasmic and nuclear fractions of A2780 shDDX3X cells under the indicated treatments. G Quantification of the nuclear-to-cytoplasmic ratio of DDX3X fluorescence intensity in A2780 cells treated with arginine as indicated. H Quantification of the nuclear-to-cytoplasmic ratio of DDX3X fluorescence intensity in A2780 shDDX3X cells treated with arginine as indicated. I Representative images and quantification of immunohistochemical staining of DDX3X in primary tumors and omentum metastases ( n = 20). Scale bars, 50 μm. J Immunohistochemical quantification of nuclear DDX3X in primary tumors and omentum metastases ( n = 20). Scale bars,50 μm. Data were shown as the mean ± SEM. The p value was calculated using one-way ANOVA ( A , G , H ), and unpaired two-tailed Student’s t -test ( I , J ). * p < 0.05, ** p < 0.01.

Article Snippet: Permeabilized cells were then sequentially incubated with a primary rabbit anti-DDX3X antibody (Cat. No. 11115-1-AP, Proteintech, Wuhan, China) and a secondary Goat Anti-Rabbit IgG antibody (Cat. No. AS070, ABclonal, Wuhan, China).

Techniques: Confocal Microscopy, Immunofluorescence, Fluorescence, Immunohistochemical staining, Staining, Two Tailed Test

Journal: Cell Death & Disease

Article Title: Arginine dependency in omental metastasis of epithelial ovarian cancer reveals a therapeutic vulnerability

doi: 10.1038/s41419-026-08606-3

Figure Lengend Snippet: A GO analysis of differentially expressed genes between DDX3X knockdown and control A2780 cells. B GO analysis of differentially expressed genes between A2780 cells with 100 and 500 μM arginine. C The relative levels of reactive oxygen species (ROS) were measured using the dihydroethidium (DHE) fluorescence method in fresh primary tumor and omental tissues ( n = 5). D Representative image and quantification of immunohistochemical staining of γH2AX and 8-OHdG in primary tumors and omentum metastases ( n = 20). Scale bars, 50 μm. E WB analyses of the protein levels of H2AX, γH2AX, and GAPDH in metastases from mice fed with the indicated diets. F Representative images and quantification of γH2AX immunofluorescence staining in A2780 cells treated with cisplatin and under the indicated treatments. Scale bars, 10 μm. G Representative images and quantification of the comet assay in A2780 cells treated with cisplatin and under the indicated treatments. Scale bars, 10 μm. H Representative images and quantification of immunofluorescence staining of γH2AX in A2780 cells treated with H 2 O 2 (1 mM final concentration) and under the indicated treatments. Scale bars, 10 μm. I Representative images and quantification of comet assay in A2780 cells treated with H 2 O 2 (1 mM final concentration) and under the indicated treatments. Scale bars, 10 μm. Data were shown as the mean ± SEM. The p value was calculated using one-way ANOVA ( F - I ), and unpaired two-tailed Student’s t -test ( C , D ). * p < 0.05, ** p < 0.01.

Article Snippet: Permeabilized cells were then sequentially incubated with a primary rabbit anti-DDX3X antibody (Cat. No. 11115-1-AP, Proteintech, Wuhan, China) and a secondary Goat Anti-Rabbit IgG antibody (Cat. No. AS070, ABclonal, Wuhan, China).

Techniques: Knockdown, Control, Fluorescence, Immunohistochemical staining, Staining, Immunofluorescence, Single Cell Gel Electrophoresis, Concentration Assay, Two Tailed Test

Journal: Cell Death & Disease

Article Title: Arginine dependency in omental metastasis of epithelial ovarian cancer reveals a therapeutic vulnerability

doi: 10.1038/s41419-026-08606-3

Figure Lengend Snippet: A The bar graph shows the fold changes in DDR gene expression following treatment with 500 μM arginine or DDX3X knockdown. B , C WB analyses for the protein level of ATM, Phospho-ATM (Ser 1981), ATR, Phospho-ATR, and GAPDH in metastasis of mice treated with the indicated diets. D , E WB showing the protein level of DDX3X, ATM, Phospho-ATM (Ser 1981), CHK2, Phospho-CHK2 (Thr68), P53, Phospho-P53 (Ser15), H2AX, γH2AX, and GAPDH in A2780 or HEY A8 cells with indicated treatments. F WB analyses for the protein level of ATM, Phospho-ATM (Ser 1981), H2AX, γH2AX, and GAPDH in A2780 cells with indicated treatments. G – I Representative images and quantification of immunofluorescence staining of γH2AX, comet assay in A2780 cells treated with cisplatin and ATM inhibitors (AZD0156[10 μM] and AZ31[5 μM]). Scale bars, 10 μm. J WB analyses for the protein level of CHK2, Phospho-CHK2 (Thr68), H2AX, γH2AX, and GAPDH in A2780 cells with the indicated treatments. K – M Representative images and quantification of immunofluorescence staining of γH2AX, comet assay in A2780 cells treated with cisplatin and CHK2 inhibitors (CCT241533 [5 μM] and PHI-101[1 μM]). Scale bars, 10 μm. Data were shown as the mean ± SEM from three independent experiments. The p value was calculated using one-way ANOVA ( H , I , L , M ). * p < 0.05, ** p < 0.01.

Article Snippet: Permeabilized cells were then sequentially incubated with a primary rabbit anti-DDX3X antibody (Cat. No. 11115-1-AP, Proteintech, Wuhan, China) and a secondary Goat Anti-Rabbit IgG antibody (Cat. No. AS070, ABclonal, Wuhan, China).

Techniques: Gene Expression, Knockdown, Immunofluorescence, Staining, Single Cell Gel Electrophoresis

Journal: Cell Death & Disease

Article Title: Arginine dependency in omental metastasis of epithelial ovarian cancer reveals a therapeutic vulnerability

doi: 10.1038/s41419-026-08606-3

Figure Lengend Snippet: A Experimental scheme illustrating orthotopic ovarian cancer and intraperitoneal ovarian cancer mice with arginase (10 μg/kg, intraperitoneal injection, three times a week) or DDX3X inhibitor (RK-33, 50 mg/kg, intraperitoneal injection, three times a week) administration. B Plasma arginine levels in arginase-injected mice were quantified using a biochemical assay kit at 24 h post-injection. C , D Representative IVIS bioluminescence images and quantitative luminescence analysis of mice with indicated treatments at 30 days after i.o. injection of ID8-Luc cells ( n = 5/group). E Representative images and weight of ovaries from orthotopic ovarian tumor mice with indicated treatments at 60 days after cell injection ( n = 5/group). Scale bars, 1 cm. F Representative IVIS bioluminescence images and quantitative luminescence analysis of mice with indicated treatments at 30 days after i.p. injection of ID8-Luc cells ( n = 5/group). G Kaplan–Meier analysis of mice with i.p. injection of ID8-Luc cells treated as indicated. ( n = 10/group). H – J Representative images of peritoneal metastasis ( H ), total number of metastatic deposits ( I ), and ascites volume ( J ) in mice with indicated treatments at 35 days after i.p. injection ( n = 5/group). K – M Representative images, tumor weight, and size of subcutaneous xenograft tumors in nude mice 30 days after injection of A2780 cisplatin-resistant cells, with the indicated treatments ( n = 5/group). Data were shown as the mean ± SD. The p value was calculated using unpaired two-tailed Student’s t -test ( A ), two-way ANOVA ( D – F , I , J , L ), and one-way ANOVA ( M ). Survival curves were generated with the Kaplan–Meier method and analyzed using the log-rank test ( G ). * p < 0.05, ** p < 0.01.

Article Snippet: Permeabilized cells were then sequentially incubated with a primary rabbit anti-DDX3X antibody (Cat. No. 11115-1-AP, Proteintech, Wuhan, China) and a secondary Goat Anti-Rabbit IgG antibody (Cat. No. AS070, ABclonal, Wuhan, China).

Techniques: Injection, Clinical Proteomics, Quantitative Luminescence, Two Tailed Test, Generated

Journal: The Journal of Biological Chemistry

Article Title: Versican binds collagen via its G3 domain and regulates the organization and mechanics of collagenous matrices

doi: 10.1016/j.jbc.2024.107968

Figure Lengend Snippet: Versican co-localizes with collagen fibers in mouse extrahepatic bile duct and collagen gels. A , schematic showing the different isoforms of versican. The antibody used for IEM binds to the β GAG domain in V0 and V1 (shown in green ). B and C , representative IEM images showing localization of versican ( black dots , indicated by teal arrows ) on collagen fibers ( blue arrows ) in postnatal day 3 ( B ) and adult ( C ) mouse bile ducts (N = 2). D , quantification of the number of gold particles, indicating versican, per total fiber area (manually selected and measured in ImageJ); p = 4.1e-14. E and F , representative IEM images showing the localization of versican in plugs of co-gelled collagen ( blue arrows ) and versican ( black dots indicated by teal arrows) ( E ) or collagen alone ( F ). Scale bar = 200 nm. Data represent mean ± SD and were analyzed by Mann–Whitney U test; ∗∗∗∗ p < 0.0001.

Article Snippet: Recombinant human versican isoform V3 and lumican were from R&D Systems.

Techniques: MANN-WHITNEY

Journal: The Journal of Biological Chemistry

Article Title: Versican binds collagen via its G3 domain and regulates the organization and mechanics of collagenous matrices

doi: 10.1016/j.jbc.2024.107968

Figure Lengend Snippet: Versican interacts with collagen via its G3 domain. A , Plates were coated with versican (Ver, red ) or the V3 isoform (V3, blue ) at 0.05, 0.1, 0.25, 0.5, and 1 μg/ml. The absorbance of collagen, added at 2.5 μg/ml and detected via a biotin-conjugated antibody, was measured colorimetrically. B , plates were coated with 0.25 μg/ml versican ( red ), V3 ( blue ) or versican after chondroitinase ABC digestion (Ver-ChABC, orange ). The binding of increasing concentrations of collagen (0.1, 0.5, 1.0, 2.5, and 5 μg/ml) was assayed. C , plates were coated with 0.25 μg/ml recombinant G1 ( pink ) or G3 ( teal ) and the binding of increasing concentrations of collagen (0.1, 0.5, 1.0, 2.5, and 5 μg/ml) was assayed. D , plates were coated with 0.25 μg/ml versican ( red ), V3 ( blue ), decorin (Dec, cyan ), lumican (Lum, orange dashed line ) or aggrecan (Agg, purple ), and the binding of increasing concentrations of collagen (0.1, 0.5, 1.0, 2.5, and 5 μg/ml) was measured. E , plates were coated with 0.25 μg/ml V3 to which was added collagen (1 μg/ml) mixed with increasing concentrations of HA (0.1, 0.5, 1, 5, and 10 ng/ml). F , plates were coated with 0.25 μg/ml V3 to which was added HA (10 ng/ml) mixed with increasing concentrations of collagen (0.1, 0.5, 1.0, 2.5, and 5 μg/ml). Three independent experiments were carried out for each panel in the figure and all data are shown. AU represents Absorbance Unit.

Article Snippet: Recombinant human versican isoform V3 and lumican were from R&D Systems.

Techniques: Binding Assay, Recombinant

Journal: The Journal of Biological Chemistry

Article Title: Versican binds collagen via its G3 domain and regulates the organization and mechanics of collagenous matrices

doi: 10.1016/j.jbc.2024.107968

Figure Lengend Snippet: The dissociation constant (K d ) and maximum absorbance (X-intercept) analyzed by the Scatchard equation: ΔA/C = ΔA max /K d -ΔA/K d (ΔA – measured value of absorbance, C – collagen concentration)

Article Snippet: Recombinant human versican isoform V3 and lumican were from R&D Systems.

Techniques: Concentration Assay, Binding Assay

Journal: The Journal of Biological Chemistry

Article Title: Versican binds collagen via its G3 domain and regulates the organization and mechanics of collagenous matrices

doi: 10.1016/j.jbc.2024.107968

Figure Lengend Snippet: Potential versican binding sites on collagen identified using the CLC II. A and B , Binding between CLC II peptides and 10 μg/ml recombinant V3 ( A ) or G3 ( B ) was tested using a solid-phase binding assay. Empty wells in the CLC-coated plate contained full-length collagen as a positive control and data were normalized to the positive control (see dashed red lines ). Three independent experiments were carried out and all data are shown. C , binding motifs (in color and shaded) identified by the alignment of versican-binding CLC peptides (where O represents hydroxyproline). Note that peptide II-5 has two instances of the potential motif.

Article Snippet: Recombinant human versican isoform V3 and lumican were from R&D Systems.

Techniques: Binding Assay, Recombinant, Positive Control

Journal: The Journal of Biological Chemistry

Article Title: Versican binds collagen via its G3 domain and regulates the organization and mechanics of collagenous matrices

doi: 10.1016/j.jbc.2024.107968

Figure Lengend Snippet: Versican and its V3 isoform upregulated the deposition of collagen-rich matrices by fibroblasts and led to increased fiber alignment. A – C , representative SHG imaging of the fibroblast-deposited matrices: control plate, with vitronectin coating ( A ), versican-coated plate ( B ), V3-coated plate ( C ). D , quantification of the intensity of the SHG signals, normalized to the value for the control group ( p < 1.0e-15 for Control vs. Ver and Control vs. V3; p = 0.0313 for Ver vs. V3). E , the distribution of collagen fiber orientation was analyzed using OrientationJ. The data were normalized to the dominant angle of each SHG image. For each condition, SD is represented by dotted lines. The statistical significance of differences between conditions is shown in Table S3 . F – H , representative confocal imaging of immunostaining for fibronectin in fibroblast-deposited matrices ( red - fibronectin, blue - DAPI): vitronectin coated plate as a control ( F ), versican-coated plate ( G ), V3-coated plate ( H ). I , quantification of the intensity of fibronectin staining ( p = 0.0426 for Control vs. V3). J , quantification of cell numbers after 7 days in culture. Four independent experiments were carried out with two technical repeats for each coating condition per experiment and 9 SHG images were obtained and analyzed for each technical repeat. Scale bar = 100 μm. Data represent mean ± SD; D was analyzed using the Kruskal-Wallis test with Dunn’s multiple comparisons, I and J were analyzed using one-way ANOVA with Tukey’s multiple comparisons, E was analyzed using two-way ANOVA with repeated measurements with Tukey’s multiple comparisons; ∗ p < 0.05 and ∗∗∗∗ p < 0.0001.

Article Snippet: Recombinant human versican isoform V3 and lumican were from R&D Systems.

Techniques: Imaging, Control, Immunostaining, Staining

Journal: The Journal of Biological Chemistry

Article Title: Versican binds collagen via its G3 domain and regulates the organization and mechanics of collagenous matrices

doi: 10.1016/j.jbc.2024.107968

Figure Lengend Snippet: Different matrix proteoglycans have distinct effects on the mechanics of collagen networks. A , gelation times for collagen-proteoglycan co-gels, with rheological measurements taken during gelation. Col: 2.5 mg/ml pure collagen gel; Col-Ver: 2.5 mg/ml collagen with 0.167 mg/ml versican; Col-V3: 2.5 mg/ml collagen gel with 0.167 mg/ml V3; Col-Agg: 2.5 mg/ml collagen gel with 0.167 mg/ml aggrecan; Col-Dec: 2.5 mg/ml collagen gel with 0.167 mg/ml decorin ( p = 2.4e-8 for Col vs. Col-Ver; p = 1.6e-9 for Col vs. Col-V3; p = 1.6e-7 for Col-Ver vs. Col-Agg; p = 2.5e-6 for Col-Ver vs. Col-Dec; p = 1.1e-8 for Col-V3 vs. Col-Agg; p = 1.9e-7 for Col-V3 vs. Col-Dec). B , the shear storage modulus (G′) for the gels in ( A ), measured after complete gelation ( p = 1.6e-5 for Col vs. Col-Ver; p = 2.0e-5 for Col vs. Col-V3; p = 1.3e-5 for Col-Ver vs. Col-Agg; p = 0.0021 for Col-Ver vs. Col-Dec; p = 1.7e-5 for Col-V3 vs. Col-Agg; p = 0.0022 for Col-V3 vs. Col-Dec). C , G′ for collagen gelled with the addition of high molecular weight (1.5 MDa) HA or both HA and V3. Col-0.1HA: 2.5 mg/ml collagen gel containing 0.1 mg/ml HA; Col-0.1HA-V3: 2.5 mg/ml collagen gel containing 0.1 mg/ml HA and 0.167 mg/ml V3 ( p = 0.0248 for Col vs. Col-0.1HA). D , G′ of different collagen-proteoglycan co-gels measured by shear rheometry under increasing strain stiffening after full gelation (see Table S4 ). E , G′ of different collagen-proteoglycan co-gels measured with the gap remaining at 1 mm and under compression to 10% (gap changed to 0.9 mm) (at non-compression, p = 0.0001 for Col vs. Col-Ver, p = 0.026 for Col vs. Col-V3, p = 0.0073 for Col-Agg vs. Col-V3, p = 2.3e-5 for Col-Agg vs. Col-Ver, p = 0.0237 for Col-Dec vs. Col-V3, p = 9.9e-5 for Col-Dec vs Col-Ver; at 10% compression, p = 0.0081 for Col-Agg vs. Col-Ver). F, G′ values at 10% compression for the different co-gels in (E) were normalized to the G′ in the non-compressed state ( p = 0.0056 for Col vs. Col-Agg, p = 0.0004 for Col-Ver vs. Col-Agg, p = 0.0031 for Col-Agg vs. Col-V3). For measuring G′ during gelation in A and B, N = 17 for Col, N = 12 for Col-Ver, N = 11 for Col-V3, N = 15 for Col-Agg and N = 11 for Col-Dec; in C, N = 13 for Col, N = 12 for Col-0.1HA and N = 10 for Col-0.1HA-V3. These gels were tested with either strain sweep (N = 3 for Col, N = 3 for Col-Ver, N = 3 for Col-V3, N = 4 for Col-Agg and N = 3 for Col-Dec) or compression (N = 3 for Col, N = 3 for Col-Ver, N = 4 for Col-V3, N = 4 for Col-Agg and N = 3 for Col-Dec); each gel was subject to only one test. The dotted lines in ( D ) represent SD. Data represent mean ± SD; A and B were analyzed using one-way ANOVA with Tukey multiple comparison, C was analyzed by Kruskal-Wallis test with Dunn’s multiple comparison, D , E , and F were analyzed using two-way ANOVA with repeated measurements with Tukey’s multiple comparison; ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001 and ∗∗∗∗ p < 0.0001.

Article Snippet: Recombinant human versican isoform V3 and lumican were from R&D Systems.

Techniques: Shear, High Molecular Weight, Comparison

Journal: The Journal of Biological Chemistry

Article Title: Versican binds collagen via its G3 domain and regulates the organization and mechanics of collagenous matrices

doi: 10.1016/j.jbc.2024.107968

Figure Lengend Snippet: ADAMTS5 and ChABC treatment of rat livers alters compression stiffening behavior. A , sulfated GAG quantification after perfusion with either enzyme, compared to control (Hank’s Balanced Salt Solution; HBSS) ( p = 0.0123 for HBSS vs. ADAMTS5 and p = 0.0019 for HBSS vs. ChABC). B , representative confocal imaging of immunostaining using an antibody against DPEAAE, the epitope exposed by ADAMTS5 cleavage of versican. DPEAAE ( green ), DAPI ( blue ). C , G′ was measured under 0%, 10%, 15%, 20% and 25% compression (with HBSS perfusion as a control). There is a significant difference at 25% compression ( p = 0.0171 for HBSS vs. ChABC at 25% compression). D , Young’s modulus ( E ) was calculated from normal force and gap changes and plotted at 5%, 12.5%, 17.5% and 22.5% compression ( p = 0.003 for HBSS vs. ADAMTS5 and p = 1.8e-5 for HBSS vs. ChABC at 22.5% compression). E , G′ measured at increasing strain from 1% to 50% (data did not show statistical differences.). N = 3 for HBSS, N = 4 for ADAMTS5, and N = 4 for ChABC-perfused livers. Compression and strain sweep experiments were done on the same liver samples, as was the assay for sulfated GAGs ( A ). Scale bar = 200 μm. Data represent mean ± SD; A was analyzed using one-way ANOVA, C , D , and E using two-way ANOVA with repeated measurements; post hoc test by Tukey’s multiple comparisons; ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001 and ∗∗∗∗ p < 0.0001.

Article Snippet: Recombinant human versican isoform V3 and lumican were from R&D Systems.

Techniques: Control, Imaging, Immunostaining

Journal: The Journal of Biological Chemistry

Article Title: Versican binds collagen via its G3 domain and regulates the organization and mechanics of collagenous matrices

doi: 10.1016/j.jbc.2024.107968

Figure Lengend Snippet: Model of interactions between HA, collagen, and versican. A , collagen and HA binding sites on different versican isoforms. B , versican may serve as a linker between collagen fibers and HA chains in collagen fibrous networks. The median diameter of a collagen fibril is approximately 200 nm , and the size of isolated versican, measured by dynamic light scattering (data not shown), is 203.4 nm. In this schematic model, the collagen fibril diameter and length of versican are therefore represented as being roughly the same size.

Article Snippet: Recombinant human versican isoform V3 and lumican were from R&D Systems.

Techniques: Binding Assay, Isolation

Journal: Nucleic acid therapeutics

Article Title: Pyrene-Modified DNA Aptamers with High Affinity to Wild-Type EGFR and EGFRvIII.

doi: 10.1089/nat.2019.0830

Figure Lengend Snippet: FIG. 6. Association (A, C) and dissociation (B, D) curves for complex of GR200 aptamer with EGFR vIII for two immobilization strategies: (A, B) biotinylated aptamer was immobilized onto streptavidin sensors, (C, D) protein was conjugated to sensors via EDC/s-NHS-mediated amine coupling. Thick lines are experimental signal after subtraction of signal from reference sensors; thin lines correspond to approximation of the curves.

Article Snippet: The recombinant extracellular domain of human EGFR vIII was also purchased from R&D Systems, catalog number 9565-ER, lot number PIC0118041.

Techniques:

Journal: Journal of Cellular and Molecular Medicine

Article Title: Electroacupuncture Pretreatment Ameliorates Perioperative Neurocognitive Disorder in Aged Mice by Inhibiting Ferroptosis Through the SIRT1 / NRF2 / GPX4 Pathway

doi: 10.1111/jcmm.71021

Figure Lengend Snippet: SIRT1/NRF2/GPX4 pathway is involved in hippocampal ferroptosis in aged mice. (A) WB images and quantification analysis of SIRT1, NRF2 and GPX4 in the hippocampus of aged mice. (B) WB images and quantification analysis of SLC7A11, TFR1, IRP2 and ferritin in the hippocampus of aged mice ( n = 3 per group). (C) qRT‐PCR expression of SIRT1, NRF2, GPX4, SLC7A11, TFR1, IRP2 and ferritin mRNA in the hippocampus of aged mice ( n = 3 per group). Values are presented as mean ± SEM. ** p < 0.01 compared with the C group; # p < 0.05 and ## p < 0.01 compared with the M group; + p < 0.05 and ++ p < 0.01 and compared with the EX group.

Article Snippet: The membrane was then incubated overnight at 4°C with primary antibodies: SIRT1 (1:850; Lot‐19G10A10; BOSTER), NRF2 (1:1500; Cat#YT3189; Immunoway), iron regulatory protein 2 (IRP2) (1:3000; Cat#YN3307; Immunoway), transferrin receptor 1 (TFR1) (1:750; LotNo‐23BP65E1; BOSTER), GPX4 (1:1500; Cat#YN3047; Immunoway), ferritin (1:3000; Cat#YT1692; Immunoway) and SLC7A11 (1:2000; Cat#YT8130; Immunoway).

Techniques: Quantitative RT-PCR, Expressing