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zo 1  (Proteintech)


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    Proteintech zo 1
    Effects of MMC and CDDP on Barrier Junction, Proliferation, and Tube Formation in Primarily Cultured Rat PAECs, PVECs, and PMVECs. (A, B) Immunofluorescence staining and quantification of ZO‑1 expression in PAECs, PVECs, and PMVECs treated with MMC (0.5 µg/mL) or CDDP (12 µM) for 24 or 48 h. n = 7 independent experiments for PAECs and n = 10 for PVECs and PMVECs. (C, D) Edu incorporation and quantification in PAECs, PVECs and PMVECs treated with MMC (0.5 µg/mL) or CDDP (12 µM) for 24 or 48 h. n = 5 independent experiments per group. (E, F) Tube formation images and quantification of the angiogenic capacity in PAECs, PVECs, and PMVECs treated with MMC (0.5 µg/mL) or CDDP (12 µM) for 24 or 48 h. n = 6 independent experiments per group. Data are presented as mean ± SD. Differences for B <t>(ZO‐1</t> signal intensity) and D (EdU‐positive cell percentage) were analyzed by one‐way ANOVA with Tukey's HSD post hoc test. Differences between two groups in F were analyzed by unpaired t ‐test, except for the comparison of total segment length between Veh‐ and MMC‐treated PMVECs, for which the Mann–Whitney U‐test was used. A value of P < 0.05 is considered statistically significant, n.s. indicates no statistical significance. Scale bar = 50 µm in A and C, and 100 µm in E. Veh: vehicle control.
    Zo 1, supplied by Proteintech, used in various techniques. Bioz Stars score: 97/100, based on 2554 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 97 stars, based on 2554 article reviews
    zo 1 - by Bioz Stars, 2026-10
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    1) Product Images from "Alkylating Agent–Induced FANCL Impairment Damages Pulmonary Arterial, Venous, and Microvascular Endothelial Cells and Predisposes to PAH/PVOD"

    Article Title: Alkylating Agent–Induced FANCL Impairment Damages Pulmonary Arterial, Venous, and Microvascular Endothelial Cells and Predisposes to PAH/PVOD

    Journal: Advanced Science

    doi: 10.1002/advs.78081

    Effects of MMC and CDDP on Barrier Junction, Proliferation, and Tube Formation in Primarily Cultured Rat PAECs, PVECs, and PMVECs. (A, B) Immunofluorescence staining and quantification of ZO‑1 expression in PAECs, PVECs, and PMVECs treated with MMC (0.5 µg/mL) or CDDP (12 µM) for 24 or 48 h. n = 7 independent experiments for PAECs and n = 10 for PVECs and PMVECs. (C, D) Edu incorporation and quantification in PAECs, PVECs and PMVECs treated with MMC (0.5 µg/mL) or CDDP (12 µM) for 24 or 48 h. n = 5 independent experiments per group. (E, F) Tube formation images and quantification of the angiogenic capacity in PAECs, PVECs, and PMVECs treated with MMC (0.5 µg/mL) or CDDP (12 µM) for 24 or 48 h. n = 6 independent experiments per group. Data are presented as mean ± SD. Differences for B (ZO‐1 signal intensity) and D (EdU‐positive cell percentage) were analyzed by one‐way ANOVA with Tukey's HSD post hoc test. Differences between two groups in F were analyzed by unpaired t ‐test, except for the comparison of total segment length between Veh‐ and MMC‐treated PMVECs, for which the Mann–Whitney U‐test was used. A value of P < 0.05 is considered statistically significant, n.s. indicates no statistical significance. Scale bar = 50 µm in A and C, and 100 µm in E. Veh: vehicle control.
    Figure Legend Snippet: Effects of MMC and CDDP on Barrier Junction, Proliferation, and Tube Formation in Primarily Cultured Rat PAECs, PVECs, and PMVECs. (A, B) Immunofluorescence staining and quantification of ZO‑1 expression in PAECs, PVECs, and PMVECs treated with MMC (0.5 µg/mL) or CDDP (12 µM) for 24 or 48 h. n = 7 independent experiments for PAECs and n = 10 for PVECs and PMVECs. (C, D) Edu incorporation and quantification in PAECs, PVECs and PMVECs treated with MMC (0.5 µg/mL) or CDDP (12 µM) for 24 or 48 h. n = 5 independent experiments per group. (E, F) Tube formation images and quantification of the angiogenic capacity in PAECs, PVECs, and PMVECs treated with MMC (0.5 µg/mL) or CDDP (12 µM) for 24 or 48 h. n = 6 independent experiments per group. Data are presented as mean ± SD. Differences for B (ZO‐1 signal intensity) and D (EdU‐positive cell percentage) were analyzed by one‐way ANOVA with Tukey's HSD post hoc test. Differences between two groups in F were analyzed by unpaired t ‐test, except for the comparison of total segment length between Veh‐ and MMC‐treated PMVECs, for which the Mann–Whitney U‐test was used. A value of P < 0.05 is considered statistically significant, n.s. indicates no statistical significance. Scale bar = 50 µm in A and C, and 100 µm in E. Veh: vehicle control.

    Techniques Used: Cell Culture, Immunofluorescence, Staining, Expressing, EdU Assay, Comparison, MANN-WHITNEY, Control

    Effects of MMC and CDDP on Functional Marker Protein Expression in Primary Cultured Rat PAECs, PVECs, and PMVECs. (A–L) Immunoblots and analyzed graphs showing the protein expression of ZO‐1, VEGFR2, FANCL, PCNA, Slug, Bcl2, Bax, and γ‐H2AX in PAECs, PVECs, and PMVECs treated with MMC (0.5 µg/mL) or CDDP (12 µM) for 24 or 48 h. Data are presented as mean ± SD, n = 5 rats per group. Data are presented as mean ± SD. Differences between two groups were analyzed by unpaired t ‐test, except for D (ZO1 at 48 h and VEGFR2 at 24 and 48 h), F (Bax/Bcl2 and γ‐H2AX at 24 h and Slug at 48 h), H (ZO1 at 24 h and PCNA at 48 h), and J (γ‐H2AX at 24 h), for which the Mann–Whitney U‐test was used. A value of P < 0.05 is considered statistically significant, n.s. indicates no statistical significance. (M, N) Heatmap of RNA‑seq data depicting gene‑ and pathway‑level changes in cultured rat PMVECs treated with MMC (0.5 µg/mL) or CDDP (12 µM) for 24 or 48 h. Veh: vehicle control.
    Figure Legend Snippet: Effects of MMC and CDDP on Functional Marker Protein Expression in Primary Cultured Rat PAECs, PVECs, and PMVECs. (A–L) Immunoblots and analyzed graphs showing the protein expression of ZO‐1, VEGFR2, FANCL, PCNA, Slug, Bcl2, Bax, and γ‐H2AX in PAECs, PVECs, and PMVECs treated with MMC (0.5 µg/mL) or CDDP (12 µM) for 24 or 48 h. Data are presented as mean ± SD, n = 5 rats per group. Data are presented as mean ± SD. Differences between two groups were analyzed by unpaired t ‐test, except for D (ZO1 at 48 h and VEGFR2 at 24 and 48 h), F (Bax/Bcl2 and γ‐H2AX at 24 h and Slug at 48 h), H (ZO1 at 24 h and PCNA at 48 h), and J (γ‐H2AX at 24 h), for which the Mann–Whitney U‐test was used. A value of P < 0.05 is considered statistically significant, n.s. indicates no statistical significance. (M, N) Heatmap of RNA‑seq data depicting gene‑ and pathway‑level changes in cultured rat PMVECs treated with MMC (0.5 µg/mL) or CDDP (12 µM) for 24 or 48 h. Veh: vehicle control.

    Techniques Used: Functional Assay, Marker, Expressing, Cell Culture, Western Blot, MANN-WHITNEY, Control

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    Incubation:

    Article Title: The effects and mechanisms of corn zein hydrolysate on intestinal inflammation in mouse and organoid models
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    Staining:

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    Article Title: Alkylating Agent–Induced FANCL Impairment Damages Pulmonary Arterial, Venous, and Microvascular Endothelial Cells and Predisposes to PAH/PVOD
    Article Snippet: The commercial sources of major reagents and chemicals include: Mitomycin C (MMC, S8146, Selleck, Shanghai, China), Cisplatin (CDDP, MB1055, Meilunbio, Dalian, China), SU5416 (HY‐10374, MedChemExpress, Monmouth Junction, NJ, USA), Amifostine trihydrate (S4298, Selleck, Shanghai, China). .. Primary antibodies for fibronectin (FN, #15613‐I‐AP, Proteintech, Rosemont, IL, USA), Twist (ab50887, Abcam, Cambridge, MA, USA), Vimentin (#5741, Cell Signaling Technology, Danvers, MA, USA), Snail (#ab53519, Abcam, Cambridge, MA, USA), ZO‐1 (21773‐1‐AP, proteintech, Wuhan, China), VEGFR2 (9698, CST, Boston, USA), Slug (YM8357, Immunoway, California, USA), proliferating cell nuclear antigen (PCNA, ab29, Abcam, Cambridge, MA, USA), CD31 (AF3628, R&D Systems, Minneapolis, MN, USA), Cleaved caspase3 (#9664, Cell Signaling Technology, Danvers, MA, USA), Bax (#2772S, Cell Signaling Technology, Danvers, MA, USA), B‐cell lymphoma/leukemia 2 (Bcl‐2, 13–8800, Thermo Fisher Scientific, Rockford, IL, USA), γ‐H2AX (#05‐635, EMD Millipore/Merck, USA), α‐smooth muscle actin (α‐SMA, ab124964 and ab7817, Abcam, Cambridge, MA, USA), FANCL (LS‐C807939, LifeSpan BioSciences, Seattle, WA, USA), FANCD2 (NB100‐182, Novus Biologicals, USA), general control nonderepressible 2 (GCN2, #46041, Cell Signaling Technology, Danvers, MA, USA), and β‐actin (66009‐1‐Ig, Proteintech, Rosemont, IL, USA) were used for immunoblotting, immunofluorescence (IF), and immunohistochemistry (IHC) staining. ..

    Article Title: Spatiotemporally engineered microneedle for microenvironment remodeling propels mucosal regeneration after tracheal mucosal injury
    Article Snippet: .. Immunofluorescence staining of CK14 (Abcam, ab181595), AC-Tub (Proteintech, 66200-1-Ig), ZO-1 (Proteintech, 21773-1-AP), and Immunohistochemical (IHC) staining for CD31 (Servicebio, S1002) were conducted to reveal the conditions of mucosal regeneration, according to previous literature [ ]. ..

    Cell-Signaling:

    Article Title: Alkylating Agent–Induced FANCL Impairment Damages Pulmonary Arterial, Venous, and Microvascular Endothelial Cells and Predisposes to PAH/PVOD
    Article Snippet: The commercial sources of major reagents and chemicals include: Mitomycin C (MMC, S8146, Selleck, Shanghai, China), Cisplatin (CDDP, MB1055, Meilunbio, Dalian, China), SU5416 (HY‐10374, MedChemExpress, Monmouth Junction, NJ, USA), Amifostine trihydrate (S4298, Selleck, Shanghai, China). .. Primary antibodies for fibronectin (FN, #15613‐I‐AP, Proteintech, Rosemont, IL, USA), Twist (ab50887, Abcam, Cambridge, MA, USA), Vimentin (#5741, Cell Signaling Technology, Danvers, MA, USA), Snail (#ab53519, Abcam, Cambridge, MA, USA), ZO‐1 (21773‐1‐AP, proteintech, Wuhan, China), VEGFR2 (9698, CST, Boston, USA), Slug (YM8357, Immunoway, California, USA), proliferating cell nuclear antigen (PCNA, ab29, Abcam, Cambridge, MA, USA), CD31 (AF3628, R&D Systems, Minneapolis, MN, USA), Cleaved caspase3 (#9664, Cell Signaling Technology, Danvers, MA, USA), Bax (#2772S, Cell Signaling Technology, Danvers, MA, USA), B‐cell lymphoma/leukemia 2 (Bcl‐2, 13–8800, Thermo Fisher Scientific, Rockford, IL, USA), γ‐H2AX (#05‐635, EMD Millipore/Merck, USA), α‐smooth muscle actin (α‐SMA, ab124964 and ab7817, Abcam, Cambridge, MA, USA), FANCL (LS‐C807939, LifeSpan BioSciences, Seattle, WA, USA), FANCD2 (NB100‐182, Novus Biologicals, USA), general control nonderepressible 2 (GCN2, #46041, Cell Signaling Technology, Danvers, MA, USA), and β‐actin (66009‐1‐Ig, Proteintech, Rosemont, IL, USA) were used for immunoblotting, immunofluorescence (IF), and immunohistochemistry (IHC) staining. ..

    Control:

    Article Title: Alkylating Agent–Induced FANCL Impairment Damages Pulmonary Arterial, Venous, and Microvascular Endothelial Cells and Predisposes to PAH/PVOD
    Article Snippet: The commercial sources of major reagents and chemicals include: Mitomycin C (MMC, S8146, Selleck, Shanghai, China), Cisplatin (CDDP, MB1055, Meilunbio, Dalian, China), SU5416 (HY‐10374, MedChemExpress, Monmouth Junction, NJ, USA), Amifostine trihydrate (S4298, Selleck, Shanghai, China). .. Primary antibodies for fibronectin (FN, #15613‐I‐AP, Proteintech, Rosemont, IL, USA), Twist (ab50887, Abcam, Cambridge, MA, USA), Vimentin (#5741, Cell Signaling Technology, Danvers, MA, USA), Snail (#ab53519, Abcam, Cambridge, MA, USA), ZO‐1 (21773‐1‐AP, proteintech, Wuhan, China), VEGFR2 (9698, CST, Boston, USA), Slug (YM8357, Immunoway, California, USA), proliferating cell nuclear antigen (PCNA, ab29, Abcam, Cambridge, MA, USA), CD31 (AF3628, R&D Systems, Minneapolis, MN, USA), Cleaved caspase3 (#9664, Cell Signaling Technology, Danvers, MA, USA), Bax (#2772S, Cell Signaling Technology, Danvers, MA, USA), B‐cell lymphoma/leukemia 2 (Bcl‐2, 13–8800, Thermo Fisher Scientific, Rockford, IL, USA), γ‐H2AX (#05‐635, EMD Millipore/Merck, USA), α‐smooth muscle actin (α‐SMA, ab124964 and ab7817, Abcam, Cambridge, MA, USA), FANCL (LS‐C807939, LifeSpan BioSciences, Seattle, WA, USA), FANCD2 (NB100‐182, Novus Biologicals, USA), general control nonderepressible 2 (GCN2, #46041, Cell Signaling Technology, Danvers, MA, USA), and β‐actin (66009‐1‐Ig, Proteintech, Rosemont, IL, USA) were used for immunoblotting, immunofluorescence (IF), and immunohistochemistry (IHC) staining. ..

    Western Blot:

    Article Title: Alkylating Agent–Induced FANCL Impairment Damages Pulmonary Arterial, Venous, and Microvascular Endothelial Cells and Predisposes to PAH/PVOD
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    Immunofluorescence:

    Article Title: Alkylating Agent–Induced FANCL Impairment Damages Pulmonary Arterial, Venous, and Microvascular Endothelial Cells and Predisposes to PAH/PVOD
    Article Snippet: The commercial sources of major reagents and chemicals include: Mitomycin C (MMC, S8146, Selleck, Shanghai, China), Cisplatin (CDDP, MB1055, Meilunbio, Dalian, China), SU5416 (HY‐10374, MedChemExpress, Monmouth Junction, NJ, USA), Amifostine trihydrate (S4298, Selleck, Shanghai, China). .. Primary antibodies for fibronectin (FN, #15613‐I‐AP, Proteintech, Rosemont, IL, USA), Twist (ab50887, Abcam, Cambridge, MA, USA), Vimentin (#5741, Cell Signaling Technology, Danvers, MA, USA), Snail (#ab53519, Abcam, Cambridge, MA, USA), ZO‐1 (21773‐1‐AP, proteintech, Wuhan, China), VEGFR2 (9698, CST, Boston, USA), Slug (YM8357, Immunoway, California, USA), proliferating cell nuclear antigen (PCNA, ab29, Abcam, Cambridge, MA, USA), CD31 (AF3628, R&D Systems, Minneapolis, MN, USA), Cleaved caspase3 (#9664, Cell Signaling Technology, Danvers, MA, USA), Bax (#2772S, Cell Signaling Technology, Danvers, MA, USA), B‐cell lymphoma/leukemia 2 (Bcl‐2, 13–8800, Thermo Fisher Scientific, Rockford, IL, USA), γ‐H2AX (#05‐635, EMD Millipore/Merck, USA), α‐smooth muscle actin (α‐SMA, ab124964 and ab7817, Abcam, Cambridge, MA, USA), FANCL (LS‐C807939, LifeSpan BioSciences, Seattle, WA, USA), FANCD2 (NB100‐182, Novus Biologicals, USA), general control nonderepressible 2 (GCN2, #46041, Cell Signaling Technology, Danvers, MA, USA), and β‐actin (66009‐1‐Ig, Proteintech, Rosemont, IL, USA) were used for immunoblotting, immunofluorescence (IF), and immunohistochemistry (IHC) staining. ..

    Article Title: Spatiotemporally engineered microneedle for microenvironment remodeling propels mucosal regeneration after tracheal mucosal injury
    Article Snippet: .. Immunofluorescence staining of CK14 (Abcam, ab181595), AC-Tub (Proteintech, 66200-1-Ig), ZO-1 (Proteintech, 21773-1-AP), and Immunohistochemical (IHC) staining for CD31 (Servicebio, S1002) were conducted to reveal the conditions of mucosal regeneration, according to previous literature [ ]. ..

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    Article Snippet: Irritable bowel syndrome (IBS) is a common gut-brain axis disorder characterized by visceral hypersensitivity, abdominal pain, and anxiety.. Although probiotics have emerged as a promising strategy for IBS management, the specific metabolite-driven mechanisms and their role in gut-brain axis modulation remain largely unclear.. In this study, 18 Lactiplantibacillus plantarum strains were screened for conjugated linoleic acid (CLA) production, and strain MNN1 was identified as a high-CLA producer, with a yield of 426 μmol/L, approximately threefold higher than that of the reference strain WCFS1.

    Immunohistochemistry:

    Article Title: Alkylating Agent–Induced FANCL Impairment Damages Pulmonary Arterial, Venous, and Microvascular Endothelial Cells and Predisposes to PAH/PVOD
    Article Snippet: The commercial sources of major reagents and chemicals include: Mitomycin C (MMC, S8146, Selleck, Shanghai, China), Cisplatin (CDDP, MB1055, Meilunbio, Dalian, China), SU5416 (HY‐10374, MedChemExpress, Monmouth Junction, NJ, USA), Amifostine trihydrate (S4298, Selleck, Shanghai, China). .. Primary antibodies for fibronectin (FN, #15613‐I‐AP, Proteintech, Rosemont, IL, USA), Twist (ab50887, Abcam, Cambridge, MA, USA), Vimentin (#5741, Cell Signaling Technology, Danvers, MA, USA), Snail (#ab53519, Abcam, Cambridge, MA, USA), ZO‐1 (21773‐1‐AP, proteintech, Wuhan, China), VEGFR2 (9698, CST, Boston, USA), Slug (YM8357, Immunoway, California, USA), proliferating cell nuclear antigen (PCNA, ab29, Abcam, Cambridge, MA, USA), CD31 (AF3628, R&D Systems, Minneapolis, MN, USA), Cleaved caspase3 (#9664, Cell Signaling Technology, Danvers, MA, USA), Bax (#2772S, Cell Signaling Technology, Danvers, MA, USA), B‐cell lymphoma/leukemia 2 (Bcl‐2, 13–8800, Thermo Fisher Scientific, Rockford, IL, USA), γ‐H2AX (#05‐635, EMD Millipore/Merck, USA), α‐smooth muscle actin (α‐SMA, ab124964 and ab7817, Abcam, Cambridge, MA, USA), FANCL (LS‐C807939, LifeSpan BioSciences, Seattle, WA, USA), FANCD2 (NB100‐182, Novus Biologicals, USA), general control nonderepressible 2 (GCN2, #46041, Cell Signaling Technology, Danvers, MA, USA), and β‐actin (66009‐1‐Ig, Proteintech, Rosemont, IL, USA) were used for immunoblotting, immunofluorescence (IF), and immunohistochemistry (IHC) staining. ..

    Article Title: Spatiotemporally engineered microneedle for microenvironment remodeling propels mucosal regeneration after tracheal mucosal injury
    Article Snippet: .. Immunofluorescence staining of CK14 (Abcam, ab181595), AC-Tub (Proteintech, 66200-1-Ig), ZO-1 (Proteintech, 21773-1-AP), and Immunohistochemical (IHC) staining for CD31 (Servicebio, S1002) were conducted to reveal the conditions of mucosal regeneration, according to previous literature [ ]. ..

    other:

    Article Title: Zhuche Pill alleviates DSS-induced colonic epithelial injury in mice: involvement of IL-17/NF-κB and Wnt/β-catenin signaling pathways.
    Article Snippet: Ethnopharmacological relevance: Zhuche Pill (ZCP), a traditional Chinese medicine formula first documented in Qianjin Yaofang during the Tang Dynasty, has been used for centuries to treat dysentery-associated gastrointestinal disorders, including abdominal pain, diarrhea, hematochezia, and tenesmus.. Despite the long-standing clinical application of ZCP, the pharmacological basis underlying its therapeutic effects remains incompletely understood.. Aim of the study: This study aims to evaluate the protective effects of ZCP against colitis and explore its potential underlying mechanisms.

    Immunohistochemical staining:

    Article Title: Spatiotemporally engineered microneedle for microenvironment remodeling propels mucosal regeneration after tracheal mucosal injury
    Article Snippet: .. Immunofluorescence staining of CK14 (Abcam, ab181595), AC-Tub (Proteintech, 66200-1-Ig), ZO-1 (Proteintech, 21773-1-AP), and Immunohistochemical (IHC) staining for CD31 (Servicebio, S1002) were conducted to reveal the conditions of mucosal regeneration, according to previous literature [ ]. ..



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    B: Analysis of the height of intestinal villi and the depth of intestinal crypts and their ratios among the six groups.C: RT-qPCR was used to analyze the expression levels of barrier and inflammation-related genes in the intestinal tissues of mice. Statistical significance is indicated as *p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001. Data are presented as mean ± SEM. Abbreviations: HE, hematoxylin and eosin; RT-qPCR, reverse transcription quantitative polymerase chain reaction; <t>ZO-1,</t> zonula occludens-1; SEM, standard error of the mean.
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    B: Analysis of the height of intestinal villi and the depth of intestinal crypts and their ratios among the six groups.C: RT-qPCR was used to analyze the expression levels of barrier and inflammation-related genes in the intestinal tissues of mice. Statistical significance is indicated as *p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001. Data are presented as mean ± SEM. Abbreviations: HE, hematoxylin and eosin; RT-qPCR, reverse transcription quantitative polymerase chain reaction; <t>ZO-1,</t> zonula occludens-1; SEM, standard error of the mean.
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    Image Search Results


    Effects of MMC and CDDP on Barrier Junction, Proliferation, and Tube Formation in Primarily Cultured Rat PAECs, PVECs, and PMVECs. (A, B) Immunofluorescence staining and quantification of ZO‑1 expression in PAECs, PVECs, and PMVECs treated with MMC (0.5 µg/mL) or CDDP (12 µM) for 24 or 48 h. n = 7 independent experiments for PAECs and n = 10 for PVECs and PMVECs. (C, D) Edu incorporation and quantification in PAECs, PVECs and PMVECs treated with MMC (0.5 µg/mL) or CDDP (12 µM) for 24 or 48 h. n = 5 independent experiments per group. (E, F) Tube formation images and quantification of the angiogenic capacity in PAECs, PVECs, and PMVECs treated with MMC (0.5 µg/mL) or CDDP (12 µM) for 24 or 48 h. n = 6 independent experiments per group. Data are presented as mean ± SD. Differences for B (ZO‐1 signal intensity) and D (EdU‐positive cell percentage) were analyzed by one‐way ANOVA with Tukey's HSD post hoc test. Differences between two groups in F were analyzed by unpaired t ‐test, except for the comparison of total segment length between Veh‐ and MMC‐treated PMVECs, for which the Mann–Whitney U‐test was used. A value of P < 0.05 is considered statistically significant, n.s. indicates no statistical significance. Scale bar = 50 µm in A and C, and 100 µm in E. Veh: vehicle control.

    Journal: Advanced Science

    Article Title: Alkylating Agent–Induced FANCL Impairment Damages Pulmonary Arterial, Venous, and Microvascular Endothelial Cells and Predisposes to PAH/PVOD

    doi: 10.1002/advs.78081

    Figure Lengend Snippet: Effects of MMC and CDDP on Barrier Junction, Proliferation, and Tube Formation in Primarily Cultured Rat PAECs, PVECs, and PMVECs. (A, B) Immunofluorescence staining and quantification of ZO‑1 expression in PAECs, PVECs, and PMVECs treated with MMC (0.5 µg/mL) or CDDP (12 µM) for 24 or 48 h. n = 7 independent experiments for PAECs and n = 10 for PVECs and PMVECs. (C, D) Edu incorporation and quantification in PAECs, PVECs and PMVECs treated with MMC (0.5 µg/mL) or CDDP (12 µM) for 24 or 48 h. n = 5 independent experiments per group. (E, F) Tube formation images and quantification of the angiogenic capacity in PAECs, PVECs, and PMVECs treated with MMC (0.5 µg/mL) or CDDP (12 µM) for 24 or 48 h. n = 6 independent experiments per group. Data are presented as mean ± SD. Differences for B (ZO‐1 signal intensity) and D (EdU‐positive cell percentage) were analyzed by one‐way ANOVA with Tukey's HSD post hoc test. Differences between two groups in F were analyzed by unpaired t ‐test, except for the comparison of total segment length between Veh‐ and MMC‐treated PMVECs, for which the Mann–Whitney U‐test was used. A value of P < 0.05 is considered statistically significant, n.s. indicates no statistical significance. Scale bar = 50 µm in A and C, and 100 µm in E. Veh: vehicle control.

    Article Snippet: Primary antibodies for fibronectin (FN, #15613‐I‐AP, Proteintech, Rosemont, IL, USA), Twist (ab50887, Abcam, Cambridge, MA, USA), Vimentin (#5741, Cell Signaling Technology, Danvers, MA, USA), Snail (#ab53519, Abcam, Cambridge, MA, USA), ZO‐1 (21773‐1‐AP, proteintech, Wuhan, China), VEGFR2 (9698, CST, Boston, USA), Slug (YM8357, Immunoway, California, USA), proliferating cell nuclear antigen (PCNA, ab29, Abcam, Cambridge, MA, USA), CD31 (AF3628, R&D Systems, Minneapolis, MN, USA), Cleaved caspase3 (#9664, Cell Signaling Technology, Danvers, MA, USA), Bax (#2772S, Cell Signaling Technology, Danvers, MA, USA), B‐cell lymphoma/leukemia 2 (Bcl‐2, 13–8800, Thermo Fisher Scientific, Rockford, IL, USA), γ‐H2AX (#05‐635, EMD Millipore/Merck, USA), α‐smooth muscle actin (α‐SMA, ab124964 and ab7817, Abcam, Cambridge, MA, USA), FANCL (LS‐C807939, LifeSpan BioSciences, Seattle, WA, USA), FANCD2 (NB100‐182, Novus Biologicals, USA), general control nonderepressible 2 (GCN2, #46041, Cell Signaling Technology, Danvers, MA, USA), and β‐actin (66009‐1‐Ig, Proteintech, Rosemont, IL, USA) were used for immunoblotting, immunofluorescence (IF), and immunohistochemistry (IHC) staining.

    Techniques: Cell Culture, Immunofluorescence, Staining, Expressing, EdU Assay, Comparison, MANN-WHITNEY, Control

    Effects of MMC and CDDP on Functional Marker Protein Expression in Primary Cultured Rat PAECs, PVECs, and PMVECs. (A–L) Immunoblots and analyzed graphs showing the protein expression of ZO‐1, VEGFR2, FANCL, PCNA, Slug, Bcl2, Bax, and γ‐H2AX in PAECs, PVECs, and PMVECs treated with MMC (0.5 µg/mL) or CDDP (12 µM) for 24 or 48 h. Data are presented as mean ± SD, n = 5 rats per group. Data are presented as mean ± SD. Differences between two groups were analyzed by unpaired t ‐test, except for D (ZO1 at 48 h and VEGFR2 at 24 and 48 h), F (Bax/Bcl2 and γ‐H2AX at 24 h and Slug at 48 h), H (ZO1 at 24 h and PCNA at 48 h), and J (γ‐H2AX at 24 h), for which the Mann–Whitney U‐test was used. A value of P < 0.05 is considered statistically significant, n.s. indicates no statistical significance. (M, N) Heatmap of RNA‑seq data depicting gene‑ and pathway‑level changes in cultured rat PMVECs treated with MMC (0.5 µg/mL) or CDDP (12 µM) for 24 or 48 h. Veh: vehicle control.

    Journal: Advanced Science

    Article Title: Alkylating Agent–Induced FANCL Impairment Damages Pulmonary Arterial, Venous, and Microvascular Endothelial Cells and Predisposes to PAH/PVOD

    doi: 10.1002/advs.78081

    Figure Lengend Snippet: Effects of MMC and CDDP on Functional Marker Protein Expression in Primary Cultured Rat PAECs, PVECs, and PMVECs. (A–L) Immunoblots and analyzed graphs showing the protein expression of ZO‐1, VEGFR2, FANCL, PCNA, Slug, Bcl2, Bax, and γ‐H2AX in PAECs, PVECs, and PMVECs treated with MMC (0.5 µg/mL) or CDDP (12 µM) for 24 or 48 h. Data are presented as mean ± SD, n = 5 rats per group. Data are presented as mean ± SD. Differences between two groups were analyzed by unpaired t ‐test, except for D (ZO1 at 48 h and VEGFR2 at 24 and 48 h), F (Bax/Bcl2 and γ‐H2AX at 24 h and Slug at 48 h), H (ZO1 at 24 h and PCNA at 48 h), and J (γ‐H2AX at 24 h), for which the Mann–Whitney U‐test was used. A value of P < 0.05 is considered statistically significant, n.s. indicates no statistical significance. (M, N) Heatmap of RNA‑seq data depicting gene‑ and pathway‑level changes in cultured rat PMVECs treated with MMC (0.5 µg/mL) or CDDP (12 µM) for 24 or 48 h. Veh: vehicle control.

    Article Snippet: Primary antibodies for fibronectin (FN, #15613‐I‐AP, Proteintech, Rosemont, IL, USA), Twist (ab50887, Abcam, Cambridge, MA, USA), Vimentin (#5741, Cell Signaling Technology, Danvers, MA, USA), Snail (#ab53519, Abcam, Cambridge, MA, USA), ZO‐1 (21773‐1‐AP, proteintech, Wuhan, China), VEGFR2 (9698, CST, Boston, USA), Slug (YM8357, Immunoway, California, USA), proliferating cell nuclear antigen (PCNA, ab29, Abcam, Cambridge, MA, USA), CD31 (AF3628, R&D Systems, Minneapolis, MN, USA), Cleaved caspase3 (#9664, Cell Signaling Technology, Danvers, MA, USA), Bax (#2772S, Cell Signaling Technology, Danvers, MA, USA), B‐cell lymphoma/leukemia 2 (Bcl‐2, 13–8800, Thermo Fisher Scientific, Rockford, IL, USA), γ‐H2AX (#05‐635, EMD Millipore/Merck, USA), α‐smooth muscle actin (α‐SMA, ab124964 and ab7817, Abcam, Cambridge, MA, USA), FANCL (LS‐C807939, LifeSpan BioSciences, Seattle, WA, USA), FANCD2 (NB100‐182, Novus Biologicals, USA), general control nonderepressible 2 (GCN2, #46041, Cell Signaling Technology, Danvers, MA, USA), and β‐actin (66009‐1‐Ig, Proteintech, Rosemont, IL, USA) were used for immunoblotting, immunofluorescence (IF), and immunohistochemistry (IHC) staining.

    Techniques: Functional Assay, Marker, Expressing, Cell Culture, Western Blot, MANN-WHITNEY, Control

    B: Analysis of the height of intestinal villi and the depth of intestinal crypts and their ratios among the six groups.C: RT-qPCR was used to analyze the expression levels of barrier and inflammation-related genes in the intestinal tissues of mice. Statistical significance is indicated as *p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001. Data are presented as mean ± SEM. Abbreviations: HE, hematoxylin and eosin; RT-qPCR, reverse transcription quantitative polymerase chain reaction; ZO-1, zonula occludens-1; SEM, standard error of the mean.

    Journal: PLOS Neglected Tropical Diseases

    Article Title: Novel inhibitors against Cryptosporidium parvum through blocking its energy metabolism

    doi: 10.1371/journal.pntd.0014742

    Figure Lengend Snippet: B: Analysis of the height of intestinal villi and the depth of intestinal crypts and their ratios among the six groups.C: RT-qPCR was used to analyze the expression levels of barrier and inflammation-related genes in the intestinal tissues of mice. Statistical significance is indicated as *p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001. Data are presented as mean ± SEM. Abbreviations: HE, hematoxylin and eosin; RT-qPCR, reverse transcription quantitative polymerase chain reaction; ZO-1, zonula occludens-1; SEM, standard error of the mean.

    Article Snippet: The membranes were submerged in 5% skim milk at room temperature for 2 h, and incubated overnight at 4 °C with primary antibodies against GAPDH, Occludin, Cleaved Caspase-1, Claudin-1 or ZO-1 (ABclonal).

    Techniques: Analysis, Quantitative RT-PCR, Expressing, Reverse Transcription, Real-time Polymerase Chain Reaction

    B: The content of inflammatory factors in calf serum. C: RT-qPCR was used to analyze the expression levels of barrier and inflammation-related genes in calf intestinal tissues. D: Western Blot was used to analyze the expression levels of barrier and inflammation-related proteins in calf intestinal tissues. Statistical significance is indicated as *p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001. Data are presented as mean ± SEM. Abbreviations: HE, hematoxylin and eosin; RT-qPCR, reverse transcription quantitative polymerase chain reaction; ZO-1, zonula occludens-1; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; IL-6, interleukin-6; IL-10, interleukin-10; IL-1β, interleukin-1 beta; TNF-α, tumor necrosis factor-alpha; SEM, standard error of the mean.

    Journal: PLOS Neglected Tropical Diseases

    Article Title: Novel inhibitors against Cryptosporidium parvum through blocking its energy metabolism

    doi: 10.1371/journal.pntd.0014742

    Figure Lengend Snippet: B: The content of inflammatory factors in calf serum. C: RT-qPCR was used to analyze the expression levels of barrier and inflammation-related genes in calf intestinal tissues. D: Western Blot was used to analyze the expression levels of barrier and inflammation-related proteins in calf intestinal tissues. Statistical significance is indicated as *p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001. Data are presented as mean ± SEM. Abbreviations: HE, hematoxylin and eosin; RT-qPCR, reverse transcription quantitative polymerase chain reaction; ZO-1, zonula occludens-1; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; IL-6, interleukin-6; IL-10, interleukin-10; IL-1β, interleukin-1 beta; TNF-α, tumor necrosis factor-alpha; SEM, standard error of the mean.

    Article Snippet: The membranes were submerged in 5% skim milk at room temperature for 2 h, and incubated overnight at 4 °C with primary antibodies against GAPDH, Occludin, Cleaved Caspase-1, Claudin-1 or ZO-1 (ABclonal).

    Techniques: Quantitative RT-PCR, Expressing, Western Blot, Reverse Transcription, Real-time Polymerase Chain Reaction

    Abbreviations: CpLDH, Cryptosporidium parvum lactate dehydrogenase; TCA, tricarboxylic acid; ROS, reactive oxygen species; TJ, tight junction; ZO-1, zonula occludens-1; GSDMD, gasdermin D; IL-1β, interleukin-1 beta; IL-18, interleukin-18. Created in BioRender. Kun, L. (2026) https://BioRender.com/vs16jmb .

    Journal: PLOS Neglected Tropical Diseases

    Article Title: Novel inhibitors against Cryptosporidium parvum through blocking its energy metabolism

    doi: 10.1371/journal.pntd.0014742

    Figure Lengend Snippet: Abbreviations: CpLDH, Cryptosporidium parvum lactate dehydrogenase; TCA, tricarboxylic acid; ROS, reactive oxygen species; TJ, tight junction; ZO-1, zonula occludens-1; GSDMD, gasdermin D; IL-1β, interleukin-1 beta; IL-18, interleukin-18. Created in BioRender. Kun, L. (2026) https://BioRender.com/vs16jmb .

    Article Snippet: The membranes were submerged in 5% skim milk at room temperature for 2 h, and incubated overnight at 4 °C with primary antibodies against GAPDH, Occludin, Cleaved Caspase-1, Claudin-1 or ZO-1 (ABclonal).

    Techniques:

    Primer sequences for target genes and the reference gene.

    Journal: Frontiers in Microbiology

    Article Title: Tight junction suppression by candidalysin promotes gut-to-blood dissemination of Candida albicans

    doi: 10.3389/fmicb.2026.1919478

    Figure Lengend Snippet: Primer sequences for target genes and the reference gene.

    Article Snippet: The membranes were blocked with 5% bovine serum albumin in Tris-buffered saline containing 0.1% Tween-20 for 1 h at room temperature and subsequently incubated overnight at 4 °C with primary antibodies against ZO-1 (rabbit, Proteintech, Cat. No. 21773-1-AP, 1:1000), occludin (rabbit, Proteintech, Cat. No. 27260-1-AP, 1:1000), claudin-1 (rabbit, Proteintech, Cat. No. 28674-1-AP, 1:1000), Dsg2 (rabbit, Proteintech, Cat. No. [21880-1-AP], 1:1000), β-actin (rabbit, Proteintech, Cat. No. 20536-1-AP, 1:1000 in NCM-460) and GAPDH (glyceraldehyde-3-phosphate dehydrogenase) (rabbit, Proteintech, Cat. No. 10494-1-AP, 1:1000 in mice tissues).

    Techniques:

    Candidalysin disrupts intestinal tight junction proteins. (A) Western blot analysis of intestinal tissues at 48 h post-infection showing expression levels of tight junction proteins ZO-1, Occludin, and Claudin-1. Protein levels were reduced in tissues from mice infected with WT and ECE1-reconstituted strains, whereas expression in ece1Δ/Δ-infected mice was relatively preserved. (B) Immunohistochemical staining of intestinal mucosa for ZO-1, Occludin, and Claudin-1. Loss of protein expression and disrupted mucosal structure were observed in WT (1477) and ECE1-reconstituted (2059) infections, whereas continuous and well-distributed staining was maintained in ece1Δ/Δ (2057)-infected tissues, similar to negative control mice. The staining pattern was consistent with strain-dependent TJ disruption during intestinal infection.

    Journal: Frontiers in Microbiology

    Article Title: Tight junction suppression by candidalysin promotes gut-to-blood dissemination of Candida albicans

    doi: 10.3389/fmicb.2026.1919478

    Figure Lengend Snippet: Candidalysin disrupts intestinal tight junction proteins. (A) Western blot analysis of intestinal tissues at 48 h post-infection showing expression levels of tight junction proteins ZO-1, Occludin, and Claudin-1. Protein levels were reduced in tissues from mice infected with WT and ECE1-reconstituted strains, whereas expression in ece1Δ/Δ-infected mice was relatively preserved. (B) Immunohistochemical staining of intestinal mucosa for ZO-1, Occludin, and Claudin-1. Loss of protein expression and disrupted mucosal structure were observed in WT (1477) and ECE1-reconstituted (2059) infections, whereas continuous and well-distributed staining was maintained in ece1Δ/Δ (2057)-infected tissues, similar to negative control mice. The staining pattern was consistent with strain-dependent TJ disruption during intestinal infection.

    Article Snippet: The membranes were blocked with 5% bovine serum albumin in Tris-buffered saline containing 0.1% Tween-20 for 1 h at room temperature and subsequently incubated overnight at 4 °C with primary antibodies against ZO-1 (rabbit, Proteintech, Cat. No. 21773-1-AP, 1:1000), occludin (rabbit, Proteintech, Cat. No. 27260-1-AP, 1:1000), claudin-1 (rabbit, Proteintech, Cat. No. 28674-1-AP, 1:1000), Dsg2 (rabbit, Proteintech, Cat. No. [21880-1-AP], 1:1000), β-actin (rabbit, Proteintech, Cat. No. 20536-1-AP, 1:1000 in NCM-460) and GAPDH (glyceraldehyde-3-phosphate dehydrogenase) (rabbit, Proteintech, Cat. No. 10494-1-AP, 1:1000 in mice tissues).

    Techniques: Western Blot, Analysis, Infection, Expressing, Immunohistochemical staining, Staining, Negative Control, Disruption

    Biphasic modulation of tight junction proteins by candidalysin in NCM-460 colonic epithelial cells. Immunofluorescence analysis of ZO-1, Occludin, and Claudin-1 (200× magnification) following exposure of intestinal epithelial cells to different concentrations of candidalysin. Representative immunofluorescence images are shown for vehicle and candidalysin at the indicated concentrations. At 3.125 μg/mL, junction-associated signals were relatively preserved. At 12.5 and 50 μg/mL, junction-associated signals were reduced and showed altered localization, with Occludin and Claudin-1 particularly affected. Primary antibodies against each individual TJ protein were used at 1:500 dilution, followed by FITC-conjugated goat anti-rabbit secondary antibodies for detection. Nuclei were counterstained with DAPI.

    Journal: Frontiers in Microbiology

    Article Title: Tight junction suppression by candidalysin promotes gut-to-blood dissemination of Candida albicans

    doi: 10.3389/fmicb.2026.1919478

    Figure Lengend Snippet: Biphasic modulation of tight junction proteins by candidalysin in NCM-460 colonic epithelial cells. Immunofluorescence analysis of ZO-1, Occludin, and Claudin-1 (200× magnification) following exposure of intestinal epithelial cells to different concentrations of candidalysin. Representative immunofluorescence images are shown for vehicle and candidalysin at the indicated concentrations. At 3.125 μg/mL, junction-associated signals were relatively preserved. At 12.5 and 50 μg/mL, junction-associated signals were reduced and showed altered localization, with Occludin and Claudin-1 particularly affected. Primary antibodies against each individual TJ protein were used at 1:500 dilution, followed by FITC-conjugated goat anti-rabbit secondary antibodies for detection. Nuclei were counterstained with DAPI.

    Article Snippet: The membranes were blocked with 5% bovine serum albumin in Tris-buffered saline containing 0.1% Tween-20 for 1 h at room temperature and subsequently incubated overnight at 4 °C with primary antibodies against ZO-1 (rabbit, Proteintech, Cat. No. 21773-1-AP, 1:1000), occludin (rabbit, Proteintech, Cat. No. 27260-1-AP, 1:1000), claudin-1 (rabbit, Proteintech, Cat. No. 28674-1-AP, 1:1000), Dsg2 (rabbit, Proteintech, Cat. No. [21880-1-AP], 1:1000), β-actin (rabbit, Proteintech, Cat. No. 20536-1-AP, 1:1000 in NCM-460) and GAPDH (glyceraldehyde-3-phosphate dehydrogenase) (rabbit, Proteintech, Cat. No. 10494-1-AP, 1:1000 in mice tissues).

    Techniques: Immunofluorescence, Analysis

    Candidalysin regulates tight junction proteins at both protein and transcript levels in colonic epithelial cells. (A) Representative Western blot analysis of ZO-1, Occludin, Claudin-1, and desmoglein-2 (Dsg2) in NCM-460 cells treated with 3.125 μg/mL or 50 μg/mL candidalysin. GAPDH was used as the loading control, whereas Dsg2 was included as a desmosomal comparison protein. (B–E) Densitometric quantification of TJ proteins from n = 3 independent biological experiments. ZO-1 expression was significantly increased at 3.125 μg/mL but markedly reduced at 50 μg/mL. Claudin-1 showed significant reduction at 50 μg/mL, while Occludin levels remained unchanged at both concentrations. (F) Scanning electron microscopy images showing intact polygonal morphology with preserved junctions in untreated cells versus marked structural collapse of cell structures and junctional disintegration after 50 μg/mL candidalysin exposure. (G) qPCR analysis of ZO-1, Occludin, and Claudin-1 transcripts showing significant downregulation at both low and high candidalysin concentrations, with greatest reduction observed at 50 μg/mL.* p < 0.05; ** p < 0.01.

    Journal: Frontiers in Microbiology

    Article Title: Tight junction suppression by candidalysin promotes gut-to-blood dissemination of Candida albicans

    doi: 10.3389/fmicb.2026.1919478

    Figure Lengend Snippet: Candidalysin regulates tight junction proteins at both protein and transcript levels in colonic epithelial cells. (A) Representative Western blot analysis of ZO-1, Occludin, Claudin-1, and desmoglein-2 (Dsg2) in NCM-460 cells treated with 3.125 μg/mL or 50 μg/mL candidalysin. GAPDH was used as the loading control, whereas Dsg2 was included as a desmosomal comparison protein. (B–E) Densitometric quantification of TJ proteins from n = 3 independent biological experiments. ZO-1 expression was significantly increased at 3.125 μg/mL but markedly reduced at 50 μg/mL. Claudin-1 showed significant reduction at 50 μg/mL, while Occludin levels remained unchanged at both concentrations. (F) Scanning electron microscopy images showing intact polygonal morphology with preserved junctions in untreated cells versus marked structural collapse of cell structures and junctional disintegration after 50 μg/mL candidalysin exposure. (G) qPCR analysis of ZO-1, Occludin, and Claudin-1 transcripts showing significant downregulation at both low and high candidalysin concentrations, with greatest reduction observed at 50 μg/mL.* p < 0.05; ** p < 0.01.

    Article Snippet: The membranes were blocked with 5% bovine serum albumin in Tris-buffered saline containing 0.1% Tween-20 for 1 h at room temperature and subsequently incubated overnight at 4 °C with primary antibodies against ZO-1 (rabbit, Proteintech, Cat. No. 21773-1-AP, 1:1000), occludin (rabbit, Proteintech, Cat. No. 27260-1-AP, 1:1000), claudin-1 (rabbit, Proteintech, Cat. No. 28674-1-AP, 1:1000), Dsg2 (rabbit, Proteintech, Cat. No. [21880-1-AP], 1:1000), β-actin (rabbit, Proteintech, Cat. No. 20536-1-AP, 1:1000 in NCM-460) and GAPDH (glyceraldehyde-3-phosphate dehydrogenase) (rabbit, Proteintech, Cat. No. 10494-1-AP, 1:1000 in mice tissues).

    Techniques: Western Blot, Analysis, Control, Comparison, Expressing, Scanning Electron Microscopy, Morphology