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hela human cervical cancer cells  (ATCC)


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    ATCC hela human cervical cancer cells
    (a) Fluorescence confocal images of <t>HeLa,</t> <t>4T1,</t> MCF-7, and NIH 3T3 cells after incubation with Pro-BDP-3 (5.0 μM) for 2 h with or without further incubation with RuL2 or RuL3 (2.5 μM) for a further 4 h (red fluorescence; λ ex = 633 nm, λ em = 650–900 nm). The cells being incubated with BDP-COOH (5.0 μM) for 2 h were used as the positive control. The cell nuclei were stained with Hoechst (1.0 μM) for 15 min (blue fluorescence; λ ex = 405 nm, λ em = 420–500 nm). Scale bar = 20 μm. (b) Corresponding mean red fluorescence intensities quantified by ImageJ. Data are reported as the mean ± standard error of the mean (SEM) for three independent experiments (∗∗∗∗p < 0.0001). (c) Fluorescence confocal images of HeLa, 4T1, MCF-7, and NIH 3T3 cells after the aforementioned treatments and further incubation with H 2 DCFDA (10 μM) for 30 min, followed by light irradiation (λ > 610 nm, 25.8 mW/cm 2 ) for 8 min to give a total fluence of 12 J/cm 2 (green fluorescence; λ ex = 488 nm, λ em = 493–550 nm). Scale bar = 20 μm. (d) Corresponding mean green fluorescence intensities of DCF quantified by ImageJ. Data are reported as the mean ± SEM for three independent experiments (∗∗∗∗p < 0.0001). (e) Dark and photo (λ > 610 nm, 25.8 mW/cm 2 , 12 J/cm 2 ) cytotoxicity of BDP-COOH , Pro-BDP-3 , RuL2 , Pro-BDP-3 + RuL2 , RuL3 , and Pro-BDP-3 + RuL3 against HeLa, 4T1, MCF-7, and NIH 3T3 cells. The cells were incubated with BDP-COOH , Pro-BDP-3 , RuL2 , or RuL3 for 2 h. For Pro-BDP-3 + RuL2 and Pro-BDP-3 + RuL3 , the cells were first incubated with Pro-BDP-3 for 2 h and then with RuL2 or RuL3 (0.5 equiv.) for a further 4 h. Data are expressed as the mean ± SEM of three independent experiments, each performed in quadruplicate. (f) Photocytotoxicity of these agents at 5.0 μM and the combination treatments at 5.0 μM of Pro-BDP-3 against the four cell lines. The rightmost figure compiles the results for Pro-BDP-3 + RuL3 (∗∗∗∗p < 0.0001). Data are expressed as the mean ± SEM of three independent experiments, each performed in quadruplicate. (g) Live/dead cell viability assay using calcein-AM and PI. The cells were treated as described above, followed by incubation with calcein-AM (1 μM) and PI (2 μM) in binding buffer (2 mL) at 37 °C for 30 min. The live cells were indicated by the green fluorescence of calcein-AM (λ ex = 488 nm, λ em = 493–550 nm), while the dead cells were indicated by the red fluorescence of PI (λ ex = 561 nm, λ em = 600–800 nm). Scale bar = 50 μm. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)
    Hela Human Cervical Cancer Cells, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 29028 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "Expanding the toolbox of bioorthogonal activation of photosensitizers for precise photodynamic therapy through transition metal-mediated deallylation"

    Article Title: Expanding the toolbox of bioorthogonal activation of photosensitizers for precise photodynamic therapy through transition metal-mediated deallylation

    Journal: Materials Today Bio

    doi: 10.1016/j.mtbio.2026.102797

    (a) Fluorescence confocal images of HeLa, 4T1, MCF-7, and NIH 3T3 cells after incubation with Pro-BDP-3 (5.0 μM) for 2 h with or without further incubation with RuL2 or RuL3 (2.5 μM) for a further 4 h (red fluorescence; λ ex = 633 nm, λ em = 650–900 nm). The cells being incubated with BDP-COOH (5.0 μM) for 2 h were used as the positive control. The cell nuclei were stained with Hoechst (1.0 μM) for 15 min (blue fluorescence; λ ex = 405 nm, λ em = 420–500 nm). Scale bar = 20 μm. (b) Corresponding mean red fluorescence intensities quantified by ImageJ. Data are reported as the mean ± standard error of the mean (SEM) for three independent experiments (∗∗∗∗p < 0.0001). (c) Fluorescence confocal images of HeLa, 4T1, MCF-7, and NIH 3T3 cells after the aforementioned treatments and further incubation with H 2 DCFDA (10 μM) for 30 min, followed by light irradiation (λ > 610 nm, 25.8 mW/cm 2 ) for 8 min to give a total fluence of 12 J/cm 2 (green fluorescence; λ ex = 488 nm, λ em = 493–550 nm). Scale bar = 20 μm. (d) Corresponding mean green fluorescence intensities of DCF quantified by ImageJ. Data are reported as the mean ± SEM for three independent experiments (∗∗∗∗p < 0.0001). (e) Dark and photo (λ > 610 nm, 25.8 mW/cm 2 , 12 J/cm 2 ) cytotoxicity of BDP-COOH , Pro-BDP-3 , RuL2 , Pro-BDP-3 + RuL2 , RuL3 , and Pro-BDP-3 + RuL3 against HeLa, 4T1, MCF-7, and NIH 3T3 cells. The cells were incubated with BDP-COOH , Pro-BDP-3 , RuL2 , or RuL3 for 2 h. For Pro-BDP-3 + RuL2 and Pro-BDP-3 + RuL3 , the cells were first incubated with Pro-BDP-3 for 2 h and then with RuL2 or RuL3 (0.5 equiv.) for a further 4 h. Data are expressed as the mean ± SEM of three independent experiments, each performed in quadruplicate. (f) Photocytotoxicity of these agents at 5.0 μM and the combination treatments at 5.0 μM of Pro-BDP-3 against the four cell lines. The rightmost figure compiles the results for Pro-BDP-3 + RuL3 (∗∗∗∗p < 0.0001). Data are expressed as the mean ± SEM of three independent experiments, each performed in quadruplicate. (g) Live/dead cell viability assay using calcein-AM and PI. The cells were treated as described above, followed by incubation with calcein-AM (1 μM) and PI (2 μM) in binding buffer (2 mL) at 37 °C for 30 min. The live cells were indicated by the green fluorescence of calcein-AM (λ ex = 488 nm, λ em = 493–550 nm), while the dead cells were indicated by the red fluorescence of PI (λ ex = 561 nm, λ em = 600–800 nm). Scale bar = 50 μm. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)
    Figure Legend Snippet: (a) Fluorescence confocal images of HeLa, 4T1, MCF-7, and NIH 3T3 cells after incubation with Pro-BDP-3 (5.0 μM) for 2 h with or without further incubation with RuL2 or RuL3 (2.5 μM) for a further 4 h (red fluorescence; λ ex = 633 nm, λ em = 650–900 nm). The cells being incubated with BDP-COOH (5.0 μM) for 2 h were used as the positive control. The cell nuclei were stained with Hoechst (1.0 μM) for 15 min (blue fluorescence; λ ex = 405 nm, λ em = 420–500 nm). Scale bar = 20 μm. (b) Corresponding mean red fluorescence intensities quantified by ImageJ. Data are reported as the mean ± standard error of the mean (SEM) for three independent experiments (∗∗∗∗p < 0.0001). (c) Fluorescence confocal images of HeLa, 4T1, MCF-7, and NIH 3T3 cells after the aforementioned treatments and further incubation with H 2 DCFDA (10 μM) for 30 min, followed by light irradiation (λ > 610 nm, 25.8 mW/cm 2 ) for 8 min to give a total fluence of 12 J/cm 2 (green fluorescence; λ ex = 488 nm, λ em = 493–550 nm). Scale bar = 20 μm. (d) Corresponding mean green fluorescence intensities of DCF quantified by ImageJ. Data are reported as the mean ± SEM for three independent experiments (∗∗∗∗p < 0.0001). (e) Dark and photo (λ > 610 nm, 25.8 mW/cm 2 , 12 J/cm 2 ) cytotoxicity of BDP-COOH , Pro-BDP-3 , RuL2 , Pro-BDP-3 + RuL2 , RuL3 , and Pro-BDP-3 + RuL3 against HeLa, 4T1, MCF-7, and NIH 3T3 cells. The cells were incubated with BDP-COOH , Pro-BDP-3 , RuL2 , or RuL3 for 2 h. For Pro-BDP-3 + RuL2 and Pro-BDP-3 + RuL3 , the cells were first incubated with Pro-BDP-3 for 2 h and then with RuL2 or RuL3 (0.5 equiv.) for a further 4 h. Data are expressed as the mean ± SEM of three independent experiments, each performed in quadruplicate. (f) Photocytotoxicity of these agents at 5.0 μM and the combination treatments at 5.0 μM of Pro-BDP-3 against the four cell lines. The rightmost figure compiles the results for Pro-BDP-3 + RuL3 (∗∗∗∗p < 0.0001). Data are expressed as the mean ± SEM of three independent experiments, each performed in quadruplicate. (g) Live/dead cell viability assay using calcein-AM and PI. The cells were treated as described above, followed by incubation with calcein-AM (1 μM) and PI (2 μM) in binding buffer (2 mL) at 37 °C for 30 min. The live cells were indicated by the green fluorescence of calcein-AM (λ ex = 488 nm, λ em = 493–550 nm), while the dead cells were indicated by the red fluorescence of PI (λ ex = 561 nm, λ em = 600–800 nm). Scale bar = 50 μm. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

    Techniques Used: Fluorescence, Incubation, Positive Control, Staining, Irradiation, Viability Assay, Binding Assay



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    (a) Fluorescence confocal images of <t>HeLa,</t> <t>4T1,</t> MCF-7, and NIH 3T3 cells after incubation with Pro-BDP-3 (5.0 μM) for 2 h with or without further incubation with RuL2 or RuL3 (2.5 μM) for a further 4 h (red fluorescence; λ ex = 633 nm, λ em = 650–900 nm). The cells being incubated with BDP-COOH (5.0 μM) for 2 h were used as the positive control. The cell nuclei were stained with Hoechst (1.0 μM) for 15 min (blue fluorescence; λ ex = 405 nm, λ em = 420–500 nm). Scale bar = 20 μm. (b) Corresponding mean red fluorescence intensities quantified by ImageJ. Data are reported as the mean ± standard error of the mean (SEM) for three independent experiments (∗∗∗∗p < 0.0001). (c) Fluorescence confocal images of HeLa, 4T1, MCF-7, and NIH 3T3 cells after the aforementioned treatments and further incubation with H 2 DCFDA (10 μM) for 30 min, followed by light irradiation (λ > 610 nm, 25.8 mW/cm 2 ) for 8 min to give a total fluence of 12 J/cm 2 (green fluorescence; λ ex = 488 nm, λ em = 493–550 nm). Scale bar = 20 μm. (d) Corresponding mean green fluorescence intensities of DCF quantified by ImageJ. Data are reported as the mean ± SEM for three independent experiments (∗∗∗∗p < 0.0001). (e) Dark and photo (λ > 610 nm, 25.8 mW/cm 2 , 12 J/cm 2 ) cytotoxicity of BDP-COOH , Pro-BDP-3 , RuL2 , Pro-BDP-3 + RuL2 , RuL3 , and Pro-BDP-3 + RuL3 against HeLa, 4T1, MCF-7, and NIH 3T3 cells. The cells were incubated with BDP-COOH , Pro-BDP-3 , RuL2 , or RuL3 for 2 h. For Pro-BDP-3 + RuL2 and Pro-BDP-3 + RuL3 , the cells were first incubated with Pro-BDP-3 for 2 h and then with RuL2 or RuL3 (0.5 equiv.) for a further 4 h. Data are expressed as the mean ± SEM of three independent experiments, each performed in quadruplicate. (f) Photocytotoxicity of these agents at 5.0 μM and the combination treatments at 5.0 μM of Pro-BDP-3 against the four cell lines. The rightmost figure compiles the results for Pro-BDP-3 + RuL3 (∗∗∗∗p < 0.0001). Data are expressed as the mean ± SEM of three independent experiments, each performed in quadruplicate. (g) Live/dead cell viability assay using calcein-AM and PI. The cells were treated as described above, followed by incubation with calcein-AM (1 μM) and PI (2 μM) in binding buffer (2 mL) at 37 °C for 30 min. The live cells were indicated by the green fluorescence of calcein-AM (λ ex = 488 nm, λ em = 493–550 nm), while the dead cells were indicated by the red fluorescence of PI (λ ex = 561 nm, λ em = 600–800 nm). Scale bar = 50 μm. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)
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    99
    ATCC human cells lines hela
    a. Top, schematic of engineered GshF construct targeted to ER ( ER-GshF ), with signal peptide (SP) from ERP44 at N-terminus, V5 tag and ER retention signal KDEL at C-terminus. Bottom left, schematic of GSH synthesis in ER catalyzed by ER-GshF. Bottom right, immunoblot analysis of ER-GshF expression <t>from</t> <t>HEK293T</t> cells expressing inducible ER-GshF (iER-GshF HEK293T) treated with 1 µg/ml doxycycline for 24 hours. b. Immunofluorescence analysis of ER-GshF (V5, red) and calnexin (CANX, green) in iER-GshF HEK293T cells treated with 1 µg/ml doxycycline for 48 hours. Micrographs are representative of two independent experiments. c. Percent labeled glutathione from HEK293T cells expressing a vector control or inducible ER-GshF pre-treated with or without BSO and doxycycline. Cells pretreated with or without 1 mM BSO and 1 µg/ml doxycycline for 24 hours, were switched to cystine free media with 200 µM isotope labeled cystine (³CL, ¹LNL) for 8 hours before harvesting the cells, BSO and doxycycline were kept the same as pretreatment during labeling. d. Schematic of the ER-focused CRISPR genetic screens in iER-GshF HEK293T cells cultured in the presence or absence of 1 µg/ml doxycycline for 14 doublings. e. Left, CRISPR gene scores in iER-GshF HEK293T cells cultured in the presence or absence of 1 µg/ml doxycycline for 14 doublings. Top scoring hits color-coded. Pearson correlation coefficient, two-sided. Right, differential gene score from iER-GshF HEK293T cells cultured with doxycycline compared to untreated. Top genes sensitizing iER-GshF HEK293T cells under doxycycline treatment are shown. f. Left, percent cell number from SLC33A1 knockout HEK293T cells expressing inducible ER-GshF complemented with a vector control or SLC33A1 cDNA under different concentrations of doxycycline for 4 days. Numbers under doxycycline treated are normalized to untreated. Right, representative images of the indicated cells. g. Left, volcano plot showing relative fold change (log 2 ) in ER metabolite abundance versus −log (P values) from SLC33A1 knockout ER-tag HEK293T cells expressing a vector control or SLC33A1 cDNA. Statistical significance was determined by multiple two-tailed unpaired t-tests. The dotted line represents P =0.01. Right, volcano plot showing relative fold change (log 2 ) in whole-cell metabolite abundance versus −log (P values) from SLC33A1 knockout ER-tag HEK293T cells expressing a vector control or SLC33A1 cDNA. Statistical significance was determined by multiple two-tailed unpaired t-tests. The dotted line represents P =0.01. h. Left, volcano plot showing relative fold change (log 2 ) in ER metabolite abundance versus −log (P values) from Slc33a1 knockout ER-tag KPK cells expressing a vector control or SLC33A1 cDNA. Statistical significance was determined by multiple two-tailed unpaired t-tests. The dotted line represents P =0.01. Right, volcano plot showing relative fold change (log 2 ) in whole-cell metabolite abundance versus −log (P values) from Slc33a1 knockout ER-tag KPK cells expressing a vector control or SLC33A1 cDNA. Statistical significance was determined by multiple two-tailed unpaired t-tests. The dotted line represents P =0.01. i. Relative metabolite abundance of indicated whole cell or ER metabolites from SLC33A1 knockout ER-tag HEK293T, <t>HeLa</t> and KPK cells expressing a vector control compared to those expressing SLC33A1 cDNA. ER UDP-GlcNAc abundance is shown to indicate ER amount.
    Human Cells Lines Hela, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    human cervical carcinoma cell line hela  (ATCC)
    99
    ATCC human cervical carcinoma cell line hela
    HIV-1 Tat <t>and</t> <t>EBV</t> Zta physically interact in B cells and human serum. (A) Immunoprecipitation of Tat in B cells. The RPMI8866 lymphoblastoid cell line inducibly expressing unconjugated HIV-1 Tat (RPMI8866 Tat i cell line) upon treatment with Doxycycline (Tat) was treated or not with 1 µg/ml recombinant Zta protein. Cell lysates were subjected to immunoprecipitation using anti-Tat antibodies. Input and immunoprecipitated fractions were analysed by western blotting staining for Tat, Zta, Galectin 9 (negative control) and β-actin (control of protein load). (B) Immunoprecipitation of Zta in B cells. The RPMI8866 lymphoblastoid cells were transfected with YFP (lane 1), YFP-Tat (Tat, lane 2), mCherry-Zta (Zta, lane 3), YFP-Tat and mCherry-Zta (lane 4), YFP-Zta and mCherry-Tat (lane 5), followed by immunoprecipitation of Zta using anti-Zta antibodies after 24 h. Input and immunoprecipitated fractions were analysed by western blotting staining for Tat, Zta, Galectin 9 (negative control) and GAPDH (control of protein load). ( C) A healthy donor (HIV-negative) serum sample supplemented with Tat and Zta (at 250 ng/ml and 1000 ng/ml, respectively, HIV-neg. + Tat + Zta) and a serum sample from an HIV-positive individual (HIV-pos.) were immunoprecipitated using Protein G magnetic beads cross-linked with anti-Zta or anti-Tat antibodies. Immunoprecipitated (IP) and non-immunoprecipitated flowthrough (FT) fractions were analysed by Western blotting staining for Zta, Tat, transferrin (negative control) and transthyretin (negative control). (D , E) Analysis of Tat and Zta interaction by an in vitro binding assay. Equal amounts of recombinant HIV-1 Tat protein linked to AminoLink agarose beads or BSA control agarose beads were incubated with increasing amounts of recombinant Zta protein. (D) Bound protein was separated on SDS-PAGE gel and bound Zta was then analysed by Western blotting staining. A representative image is shown. (E) The non-linear fit of Zta binding to Tat (densitometry analysis of western blotting band intensity of bound Zta) against Zta concentration in solution with one site-specific binding model. Zta binding at a concentration of 0.2 µM was set as 1 (fraction bound). (F , G) Tat and Zta interaction analysed by YFP reconstitution. (F) The modular composition of the fusion proteins used in this study (above). A representative image of <t>HeLa</t> cells after transfection with YFP1-Tat and YFP2-Zta plasmids, nuclei were counterstained with DAPI, scale bar 10 μm (below). (G) The percentage of YFP-positive cells in HeLa, RPMI8866 or Jurkat cells transfected with YFP1-Tat + YFP2-Zta or YFP1-ERGIC-53 and YFP2-MCFD2 (positive control) as analysed by flow cytometry. (H-J) The analysis of Tat and Zta interaction by FRET with the acceptor photobleaching method. (H) Representative images of RPMI8866 cells, transfected with different combinations of CFP, YFP, Tat-CFP and YFP-Zta. Scale bar 10 μm. (I-J) FRET efficiencies for each combination in RPMI8866 (I) and HeLa (J) cells. Data are presented as mean ± SEM
    Human Cervical Carcinoma Cell Line Hela, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    (a) Fluorescence confocal images of HeLa, 4T1, MCF-7, and NIH 3T3 cells after incubation with Pro-BDP-3 (5.0 μM) for 2 h with or without further incubation with RuL2 or RuL3 (2.5 μM) for a further 4 h (red fluorescence; λ ex = 633 nm, λ em = 650–900 nm). The cells being incubated with BDP-COOH (5.0 μM) for 2 h were used as the positive control. The cell nuclei were stained with Hoechst (1.0 μM) for 15 min (blue fluorescence; λ ex = 405 nm, λ em = 420–500 nm). Scale bar = 20 μm. (b) Corresponding mean red fluorescence intensities quantified by ImageJ. Data are reported as the mean ± standard error of the mean (SEM) for three independent experiments (∗∗∗∗p < 0.0001). (c) Fluorescence confocal images of HeLa, 4T1, MCF-7, and NIH 3T3 cells after the aforementioned treatments and further incubation with H 2 DCFDA (10 μM) for 30 min, followed by light irradiation (λ > 610 nm, 25.8 mW/cm 2 ) for 8 min to give a total fluence of 12 J/cm 2 (green fluorescence; λ ex = 488 nm, λ em = 493–550 nm). Scale bar = 20 μm. (d) Corresponding mean green fluorescence intensities of DCF quantified by ImageJ. Data are reported as the mean ± SEM for three independent experiments (∗∗∗∗p < 0.0001). (e) Dark and photo (λ > 610 nm, 25.8 mW/cm 2 , 12 J/cm 2 ) cytotoxicity of BDP-COOH , Pro-BDP-3 , RuL2 , Pro-BDP-3 + RuL2 , RuL3 , and Pro-BDP-3 + RuL3 against HeLa, 4T1, MCF-7, and NIH 3T3 cells. The cells were incubated with BDP-COOH , Pro-BDP-3 , RuL2 , or RuL3 for 2 h. For Pro-BDP-3 + RuL2 and Pro-BDP-3 + RuL3 , the cells were first incubated with Pro-BDP-3 for 2 h and then with RuL2 or RuL3 (0.5 equiv.) for a further 4 h. Data are expressed as the mean ± SEM of three independent experiments, each performed in quadruplicate. (f) Photocytotoxicity of these agents at 5.0 μM and the combination treatments at 5.0 μM of Pro-BDP-3 against the four cell lines. The rightmost figure compiles the results for Pro-BDP-3 + RuL3 (∗∗∗∗p < 0.0001). Data are expressed as the mean ± SEM of three independent experiments, each performed in quadruplicate. (g) Live/dead cell viability assay using calcein-AM and PI. The cells were treated as described above, followed by incubation with calcein-AM (1 μM) and PI (2 μM) in binding buffer (2 mL) at 37 °C for 30 min. The live cells were indicated by the green fluorescence of calcein-AM (λ ex = 488 nm, λ em = 493–550 nm), while the dead cells were indicated by the red fluorescence of PI (λ ex = 561 nm, λ em = 600–800 nm). Scale bar = 50 μm. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

    Journal: Materials Today Bio

    Article Title: Expanding the toolbox of bioorthogonal activation of photosensitizers for precise photodynamic therapy through transition metal-mediated deallylation

    doi: 10.1016/j.mtbio.2026.102797

    Figure Lengend Snippet: (a) Fluorescence confocal images of HeLa, 4T1, MCF-7, and NIH 3T3 cells after incubation with Pro-BDP-3 (5.0 μM) for 2 h with or without further incubation with RuL2 or RuL3 (2.5 μM) for a further 4 h (red fluorescence; λ ex = 633 nm, λ em = 650–900 nm). The cells being incubated with BDP-COOH (5.0 μM) for 2 h were used as the positive control. The cell nuclei were stained with Hoechst (1.0 μM) for 15 min (blue fluorescence; λ ex = 405 nm, λ em = 420–500 nm). Scale bar = 20 μm. (b) Corresponding mean red fluorescence intensities quantified by ImageJ. Data are reported as the mean ± standard error of the mean (SEM) for three independent experiments (∗∗∗∗p < 0.0001). (c) Fluorescence confocal images of HeLa, 4T1, MCF-7, and NIH 3T3 cells after the aforementioned treatments and further incubation with H 2 DCFDA (10 μM) for 30 min, followed by light irradiation (λ > 610 nm, 25.8 mW/cm 2 ) for 8 min to give a total fluence of 12 J/cm 2 (green fluorescence; λ ex = 488 nm, λ em = 493–550 nm). Scale bar = 20 μm. (d) Corresponding mean green fluorescence intensities of DCF quantified by ImageJ. Data are reported as the mean ± SEM for three independent experiments (∗∗∗∗p < 0.0001). (e) Dark and photo (λ > 610 nm, 25.8 mW/cm 2 , 12 J/cm 2 ) cytotoxicity of BDP-COOH , Pro-BDP-3 , RuL2 , Pro-BDP-3 + RuL2 , RuL3 , and Pro-BDP-3 + RuL3 against HeLa, 4T1, MCF-7, and NIH 3T3 cells. The cells were incubated with BDP-COOH , Pro-BDP-3 , RuL2 , or RuL3 for 2 h. For Pro-BDP-3 + RuL2 and Pro-BDP-3 + RuL3 , the cells were first incubated with Pro-BDP-3 for 2 h and then with RuL2 or RuL3 (0.5 equiv.) for a further 4 h. Data are expressed as the mean ± SEM of three independent experiments, each performed in quadruplicate. (f) Photocytotoxicity of these agents at 5.0 μM and the combination treatments at 5.0 μM of Pro-BDP-3 against the four cell lines. The rightmost figure compiles the results for Pro-BDP-3 + RuL3 (∗∗∗∗p < 0.0001). Data are expressed as the mean ± SEM of three independent experiments, each performed in quadruplicate. (g) Live/dead cell viability assay using calcein-AM and PI. The cells were treated as described above, followed by incubation with calcein-AM (1 μM) and PI (2 μM) in binding buffer (2 mL) at 37 °C for 30 min. The live cells were indicated by the green fluorescence of calcein-AM (λ ex = 488 nm, λ em = 493–550 nm), while the dead cells were indicated by the red fluorescence of PI (λ ex = 561 nm, λ em = 600–800 nm). Scale bar = 50 μm. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)

    Article Snippet: The HeLa human cervical cancer cells (ATCC, CCL-2), 4T1 murine mammary carcinoma cells (ATCC, CRL-2539), MCF-7 human breast cancer cells (ATCC, HTB-22), and NIH 3T3 murine embryonic fibroblast cells were maintained in Dulbecco's modified Eagle's medium (DMEM, ThermoFisher, cat. no. 11965092) supplemented with fetal calf serum (10 %) and penicillin-streptomycin (100 unit/mL and 100 μg/mL, respectively).

    Techniques: Fluorescence, Incubation, Positive Control, Staining, Irradiation, Viability Assay, Binding Assay

    a. Top, schematic of engineered GshF construct targeted to ER ( ER-GshF ), with signal peptide (SP) from ERP44 at N-terminus, V5 tag and ER retention signal KDEL at C-terminus. Bottom left, schematic of GSH synthesis in ER catalyzed by ER-GshF. Bottom right, immunoblot analysis of ER-GshF expression from HEK293T cells expressing inducible ER-GshF (iER-GshF HEK293T) treated with 1 µg/ml doxycycline for 24 hours. b. Immunofluorescence analysis of ER-GshF (V5, red) and calnexin (CANX, green) in iER-GshF HEK293T cells treated with 1 µg/ml doxycycline for 48 hours. Micrographs are representative of two independent experiments. c. Percent labeled glutathione from HEK293T cells expressing a vector control or inducible ER-GshF pre-treated with or without BSO and doxycycline. Cells pretreated with or without 1 mM BSO and 1 µg/ml doxycycline for 24 hours, were switched to cystine free media with 200 µM isotope labeled cystine (³CL, ¹LNL) for 8 hours before harvesting the cells, BSO and doxycycline were kept the same as pretreatment during labeling. d. Schematic of the ER-focused CRISPR genetic screens in iER-GshF HEK293T cells cultured in the presence or absence of 1 µg/ml doxycycline for 14 doublings. e. Left, CRISPR gene scores in iER-GshF HEK293T cells cultured in the presence or absence of 1 µg/ml doxycycline for 14 doublings. Top scoring hits color-coded. Pearson correlation coefficient, two-sided. Right, differential gene score from iER-GshF HEK293T cells cultured with doxycycline compared to untreated. Top genes sensitizing iER-GshF HEK293T cells under doxycycline treatment are shown. f. Left, percent cell number from SLC33A1 knockout HEK293T cells expressing inducible ER-GshF complemented with a vector control or SLC33A1 cDNA under different concentrations of doxycycline for 4 days. Numbers under doxycycline treated are normalized to untreated. Right, representative images of the indicated cells. g. Left, volcano plot showing relative fold change (log 2 ) in ER metabolite abundance versus −log (P values) from SLC33A1 knockout ER-tag HEK293T cells expressing a vector control or SLC33A1 cDNA. Statistical significance was determined by multiple two-tailed unpaired t-tests. The dotted line represents P =0.01. Right, volcano plot showing relative fold change (log 2 ) in whole-cell metabolite abundance versus −log (P values) from SLC33A1 knockout ER-tag HEK293T cells expressing a vector control or SLC33A1 cDNA. Statistical significance was determined by multiple two-tailed unpaired t-tests. The dotted line represents P =0.01. h. Left, volcano plot showing relative fold change (log 2 ) in ER metabolite abundance versus −log (P values) from Slc33a1 knockout ER-tag KPK cells expressing a vector control or SLC33A1 cDNA. Statistical significance was determined by multiple two-tailed unpaired t-tests. The dotted line represents P =0.01. Right, volcano plot showing relative fold change (log 2 ) in whole-cell metabolite abundance versus −log (P values) from Slc33a1 knockout ER-tag KPK cells expressing a vector control or SLC33A1 cDNA. Statistical significance was determined by multiple two-tailed unpaired t-tests. The dotted line represents P =0.01. i. Relative metabolite abundance of indicated whole cell or ER metabolites from SLC33A1 knockout ER-tag HEK293T, HeLa and KPK cells expressing a vector control compared to those expressing SLC33A1 cDNA. ER UDP-GlcNAc abundance is shown to indicate ER amount.

    Journal: bioRxiv

    Article Title: SLC33A1 exports oxidized glutathione to maintain endoplasmic reticulum redox homeostasis

    doi: 10.64898/2026.02.01.703113

    Figure Lengend Snippet: a. Top, schematic of engineered GshF construct targeted to ER ( ER-GshF ), with signal peptide (SP) from ERP44 at N-terminus, V5 tag and ER retention signal KDEL at C-terminus. Bottom left, schematic of GSH synthesis in ER catalyzed by ER-GshF. Bottom right, immunoblot analysis of ER-GshF expression from HEK293T cells expressing inducible ER-GshF (iER-GshF HEK293T) treated with 1 µg/ml doxycycline for 24 hours. b. Immunofluorescence analysis of ER-GshF (V5, red) and calnexin (CANX, green) in iER-GshF HEK293T cells treated with 1 µg/ml doxycycline for 48 hours. Micrographs are representative of two independent experiments. c. Percent labeled glutathione from HEK293T cells expressing a vector control or inducible ER-GshF pre-treated with or without BSO and doxycycline. Cells pretreated with or without 1 mM BSO and 1 µg/ml doxycycline for 24 hours, were switched to cystine free media with 200 µM isotope labeled cystine (³CL, ¹LNL) for 8 hours before harvesting the cells, BSO and doxycycline were kept the same as pretreatment during labeling. d. Schematic of the ER-focused CRISPR genetic screens in iER-GshF HEK293T cells cultured in the presence or absence of 1 µg/ml doxycycline for 14 doublings. e. Left, CRISPR gene scores in iER-GshF HEK293T cells cultured in the presence or absence of 1 µg/ml doxycycline for 14 doublings. Top scoring hits color-coded. Pearson correlation coefficient, two-sided. Right, differential gene score from iER-GshF HEK293T cells cultured with doxycycline compared to untreated. Top genes sensitizing iER-GshF HEK293T cells under doxycycline treatment are shown. f. Left, percent cell number from SLC33A1 knockout HEK293T cells expressing inducible ER-GshF complemented with a vector control or SLC33A1 cDNA under different concentrations of doxycycline for 4 days. Numbers under doxycycline treated are normalized to untreated. Right, representative images of the indicated cells. g. Left, volcano plot showing relative fold change (log 2 ) in ER metabolite abundance versus −log (P values) from SLC33A1 knockout ER-tag HEK293T cells expressing a vector control or SLC33A1 cDNA. Statistical significance was determined by multiple two-tailed unpaired t-tests. The dotted line represents P =0.01. Right, volcano plot showing relative fold change (log 2 ) in whole-cell metabolite abundance versus −log (P values) from SLC33A1 knockout ER-tag HEK293T cells expressing a vector control or SLC33A1 cDNA. Statistical significance was determined by multiple two-tailed unpaired t-tests. The dotted line represents P =0.01. h. Left, volcano plot showing relative fold change (log 2 ) in ER metabolite abundance versus −log (P values) from Slc33a1 knockout ER-tag KPK cells expressing a vector control or SLC33A1 cDNA. Statistical significance was determined by multiple two-tailed unpaired t-tests. The dotted line represents P =0.01. Right, volcano plot showing relative fold change (log 2 ) in whole-cell metabolite abundance versus −log (P values) from Slc33a1 knockout ER-tag KPK cells expressing a vector control or SLC33A1 cDNA. Statistical significance was determined by multiple two-tailed unpaired t-tests. The dotted line represents P =0.01. i. Relative metabolite abundance of indicated whole cell or ER metabolites from SLC33A1 knockout ER-tag HEK293T, HeLa and KPK cells expressing a vector control compared to those expressing SLC33A1 cDNA. ER UDP-GlcNAc abundance is shown to indicate ER amount.

    Article Snippet: Human cells lines HeLa, HEK293T cells were purchased from the ATCC.

    Techniques: Construct, Western Blot, Expressing, Immunofluorescence, Labeling, Plasmid Preparation, Control, CRISPR, Cell Culture, Knock-Out, Two Tailed Test

    HIV-1 Tat and EBV Zta physically interact in B cells and human serum. (A) Immunoprecipitation of Tat in B cells. The RPMI8866 lymphoblastoid cell line inducibly expressing unconjugated HIV-1 Tat (RPMI8866 Tat i cell line) upon treatment with Doxycycline (Tat) was treated or not with 1 µg/ml recombinant Zta protein. Cell lysates were subjected to immunoprecipitation using anti-Tat antibodies. Input and immunoprecipitated fractions were analysed by western blotting staining for Tat, Zta, Galectin 9 (negative control) and β-actin (control of protein load). (B) Immunoprecipitation of Zta in B cells. The RPMI8866 lymphoblastoid cells were transfected with YFP (lane 1), YFP-Tat (Tat, lane 2), mCherry-Zta (Zta, lane 3), YFP-Tat and mCherry-Zta (lane 4), YFP-Zta and mCherry-Tat (lane 5), followed by immunoprecipitation of Zta using anti-Zta antibodies after 24 h. Input and immunoprecipitated fractions were analysed by western blotting staining for Tat, Zta, Galectin 9 (negative control) and GAPDH (control of protein load). ( C) A healthy donor (HIV-negative) serum sample supplemented with Tat and Zta (at 250 ng/ml and 1000 ng/ml, respectively, HIV-neg. + Tat + Zta) and a serum sample from an HIV-positive individual (HIV-pos.) were immunoprecipitated using Protein G magnetic beads cross-linked with anti-Zta or anti-Tat antibodies. Immunoprecipitated (IP) and non-immunoprecipitated flowthrough (FT) fractions were analysed by Western blotting staining for Zta, Tat, transferrin (negative control) and transthyretin (negative control). (D , E) Analysis of Tat and Zta interaction by an in vitro binding assay. Equal amounts of recombinant HIV-1 Tat protein linked to AminoLink agarose beads or BSA control agarose beads were incubated with increasing amounts of recombinant Zta protein. (D) Bound protein was separated on SDS-PAGE gel and bound Zta was then analysed by Western blotting staining. A representative image is shown. (E) The non-linear fit of Zta binding to Tat (densitometry analysis of western blotting band intensity of bound Zta) against Zta concentration in solution with one site-specific binding model. Zta binding at a concentration of 0.2 µM was set as 1 (fraction bound). (F , G) Tat and Zta interaction analysed by YFP reconstitution. (F) The modular composition of the fusion proteins used in this study (above). A representative image of HeLa cells after transfection with YFP1-Tat and YFP2-Zta plasmids, nuclei were counterstained with DAPI, scale bar 10 μm (below). (G) The percentage of YFP-positive cells in HeLa, RPMI8866 or Jurkat cells transfected with YFP1-Tat + YFP2-Zta or YFP1-ERGIC-53 and YFP2-MCFD2 (positive control) as analysed by flow cytometry. (H-J) The analysis of Tat and Zta interaction by FRET with the acceptor photobleaching method. (H) Representative images of RPMI8866 cells, transfected with different combinations of CFP, YFP, Tat-CFP and YFP-Zta. Scale bar 10 μm. (I-J) FRET efficiencies for each combination in RPMI8866 (I) and HeLa (J) cells. Data are presented as mean ± SEM

    Journal: Cellular and Molecular Life Sciences: CMLS

    Article Title: Interaction between HIV-1 Tat and EBV Zta favours immune escape of B cells by downregulating HLA-ABC expression

    doi: 10.1007/s00018-025-06029-5

    Figure Lengend Snippet: HIV-1 Tat and EBV Zta physically interact in B cells and human serum. (A) Immunoprecipitation of Tat in B cells. The RPMI8866 lymphoblastoid cell line inducibly expressing unconjugated HIV-1 Tat (RPMI8866 Tat i cell line) upon treatment with Doxycycline (Tat) was treated or not with 1 µg/ml recombinant Zta protein. Cell lysates were subjected to immunoprecipitation using anti-Tat antibodies. Input and immunoprecipitated fractions were analysed by western blotting staining for Tat, Zta, Galectin 9 (negative control) and β-actin (control of protein load). (B) Immunoprecipitation of Zta in B cells. The RPMI8866 lymphoblastoid cells were transfected with YFP (lane 1), YFP-Tat (Tat, lane 2), mCherry-Zta (Zta, lane 3), YFP-Tat and mCherry-Zta (lane 4), YFP-Zta and mCherry-Tat (lane 5), followed by immunoprecipitation of Zta using anti-Zta antibodies after 24 h. Input and immunoprecipitated fractions were analysed by western blotting staining for Tat, Zta, Galectin 9 (negative control) and GAPDH (control of protein load). ( C) A healthy donor (HIV-negative) serum sample supplemented with Tat and Zta (at 250 ng/ml and 1000 ng/ml, respectively, HIV-neg. + Tat + Zta) and a serum sample from an HIV-positive individual (HIV-pos.) were immunoprecipitated using Protein G magnetic beads cross-linked with anti-Zta or anti-Tat antibodies. Immunoprecipitated (IP) and non-immunoprecipitated flowthrough (FT) fractions were analysed by Western blotting staining for Zta, Tat, transferrin (negative control) and transthyretin (negative control). (D , E) Analysis of Tat and Zta interaction by an in vitro binding assay. Equal amounts of recombinant HIV-1 Tat protein linked to AminoLink agarose beads or BSA control agarose beads were incubated with increasing amounts of recombinant Zta protein. (D) Bound protein was separated on SDS-PAGE gel and bound Zta was then analysed by Western blotting staining. A representative image is shown. (E) The non-linear fit of Zta binding to Tat (densitometry analysis of western blotting band intensity of bound Zta) against Zta concentration in solution with one site-specific binding model. Zta binding at a concentration of 0.2 µM was set as 1 (fraction bound). (F , G) Tat and Zta interaction analysed by YFP reconstitution. (F) The modular composition of the fusion proteins used in this study (above). A representative image of HeLa cells after transfection with YFP1-Tat and YFP2-Zta plasmids, nuclei were counterstained with DAPI, scale bar 10 μm (below). (G) The percentage of YFP-positive cells in HeLa, RPMI8866 or Jurkat cells transfected with YFP1-Tat + YFP2-Zta or YFP1-ERGIC-53 and YFP2-MCFD2 (positive control) as analysed by flow cytometry. (H-J) The analysis of Tat and Zta interaction by FRET with the acceptor photobleaching method. (H) Representative images of RPMI8866 cells, transfected with different combinations of CFP, YFP, Tat-CFP and YFP-Zta. Scale bar 10 μm. (I-J) FRET efficiencies for each combination in RPMI8866 (I) and HeLa (J) cells. Data are presented as mean ± SEM

    Article Snippet: Human cervical carcinoma cell line HeLa (American Type Culture Collection), Human Epstein-Barr virus (EBV)-transformed B lymphoblastoid cell line RPMI8866 (ECACC General Cell Collection), freshly EBV-transformed B lymphoblastoid cell line from healthy donor AS (BLAS, established by EBV (B95-8) immortalization of mature B cells and characterized by Genethon (Evry, France)), human immortalized T cell line Jurkat (American Type Culture Collection) and their derivatives were used in the study.

    Techniques: Immunoprecipitation, Expressing, Recombinant, Western Blot, Staining, Negative Control, Control, Transfection, Magnetic Beads, In Vitro, Binding Assay, Incubation, SDS Page, Concentration Assay, Positive Control, Flow Cytometry