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rabbit polyclonal antibodies against securin  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc rabbit polyclonal antibodies against securin
    HMGB1 inhibitor glycyrrhizic acid prevents rotenone-induced G2/M arrest. A , representative confocal images of cells stained with pH3S10 ( red ), HMGB1 ( green ) and DAPI ( blue ) following rotenone treatment in the presence or absence of the HMGB1 inhibitor glycyrrhizic acid (GA) (1.5 mM). (scale bar = 10 μm). B , quantification of SH-SY5Y cells with cytoplasmic enriched HMGB1 ( left panel ) and pH3S10 positive cells indicating cells arrested at G2/M ( right panel ) for each treatment condition. (n = 100 cells for each quantification). C , immunoblot analysis of HMGB1 protein levels in the nuclear and cytosolic fraction of SH-SY5Y cells treated with rotenone for 24 h in the presence or absence of GA. GAPDH was used as cytosolic loading control and lamin A/C was used as a nuclear loading control ( upper panel ). The nuclear to cytoplasmic ratio was quantified using the lower band obtained in the cytoplasmic fraction of the gels ( lower panel ). D , representative flow cytometry histograms depicting DNA content in SH-SY5Y cells stained with propidium iodide (PI). Distinct peaks correspond to cells in the G0/G1 phase (first peak), S phase (intermediate region), and G2/M phase (second peak). SH-SY5Y cells were treated with Rot, GA or pre-incubated with GA before Rot treatment for 24 h and the data is compared with DMSO control. The quantification of cells in each phase of the cell cycle are shown in the right panel. E and F , immunoblot analysis of Cyclin B1, <t>Securin</t> ( E ) and BubR1 ( F ) protein levels in the whole-cell extracts of SH-SY5Y cells 24 h post-rotenone treatment in the presence or absence of GA. β-Actin was used as a loading control. G , schematic representation showing association of rotenone-induced G2/M arrest with HMGB1 nuclear exit and the effect of GA on the process. Data are presented as mean ± SD. Statistical significance was determined by one-way ANOVA with Tukey’s multiple comparison test (∗∗∗ p < 0.01; n = 3 biological replicates).
    Rabbit Polyclonal Antibodies Against Securin, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 27 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rabbit+anti+securin/Securin+Rabbit+mAb/pmc12538445-325-0-19
    Average 93 stars, based on 27 article reviews
    rabbit polyclonal antibodies against securin - by Bioz Stars, 2026-10
    93/100 stars

    Images

    1) Product Images from "Tubulin hyperacetylation drives HMGB1 nuclear exit via the ROS-PARP1 axis, leading to rotenone-induced G2/M arrest"

    Article Title: Tubulin hyperacetylation drives HMGB1 nuclear exit via the ROS-PARP1 axis, leading to rotenone-induced G2/M arrest

    Journal: The Journal of Biological Chemistry

    doi: 10.1016/j.jbc.2025.110695

    HMGB1 inhibitor glycyrrhizic acid prevents rotenone-induced G2/M arrest. A , representative confocal images of cells stained with pH3S10 ( red ), HMGB1 ( green ) and DAPI ( blue ) following rotenone treatment in the presence or absence of the HMGB1 inhibitor glycyrrhizic acid (GA) (1.5 mM). (scale bar = 10 μm). B , quantification of SH-SY5Y cells with cytoplasmic enriched HMGB1 ( left panel ) and pH3S10 positive cells indicating cells arrested at G2/M ( right panel ) for each treatment condition. (n = 100 cells for each quantification). C , immunoblot analysis of HMGB1 protein levels in the nuclear and cytosolic fraction of SH-SY5Y cells treated with rotenone for 24 h in the presence or absence of GA. GAPDH was used as cytosolic loading control and lamin A/C was used as a nuclear loading control ( upper panel ). The nuclear to cytoplasmic ratio was quantified using the lower band obtained in the cytoplasmic fraction of the gels ( lower panel ). D , representative flow cytometry histograms depicting DNA content in SH-SY5Y cells stained with propidium iodide (PI). Distinct peaks correspond to cells in the G0/G1 phase (first peak), S phase (intermediate region), and G2/M phase (second peak). SH-SY5Y cells were treated with Rot, GA or pre-incubated with GA before Rot treatment for 24 h and the data is compared with DMSO control. The quantification of cells in each phase of the cell cycle are shown in the right panel. E and F , immunoblot analysis of Cyclin B1, Securin ( E ) and BubR1 ( F ) protein levels in the whole-cell extracts of SH-SY5Y cells 24 h post-rotenone treatment in the presence or absence of GA. β-Actin was used as a loading control. G , schematic representation showing association of rotenone-induced G2/M arrest with HMGB1 nuclear exit and the effect of GA on the process. Data are presented as mean ± SD. Statistical significance was determined by one-way ANOVA with Tukey’s multiple comparison test (∗∗∗ p < 0.01; n = 3 biological replicates).
    Figure Legend Snippet: HMGB1 inhibitor glycyrrhizic acid prevents rotenone-induced G2/M arrest. A , representative confocal images of cells stained with pH3S10 ( red ), HMGB1 ( green ) and DAPI ( blue ) following rotenone treatment in the presence or absence of the HMGB1 inhibitor glycyrrhizic acid (GA) (1.5 mM). (scale bar = 10 μm). B , quantification of SH-SY5Y cells with cytoplasmic enriched HMGB1 ( left panel ) and pH3S10 positive cells indicating cells arrested at G2/M ( right panel ) for each treatment condition. (n = 100 cells for each quantification). C , immunoblot analysis of HMGB1 protein levels in the nuclear and cytosolic fraction of SH-SY5Y cells treated with rotenone for 24 h in the presence or absence of GA. GAPDH was used as cytosolic loading control and lamin A/C was used as a nuclear loading control ( upper panel ). The nuclear to cytoplasmic ratio was quantified using the lower band obtained in the cytoplasmic fraction of the gels ( lower panel ). D , representative flow cytometry histograms depicting DNA content in SH-SY5Y cells stained with propidium iodide (PI). Distinct peaks correspond to cells in the G0/G1 phase (first peak), S phase (intermediate region), and G2/M phase (second peak). SH-SY5Y cells were treated with Rot, GA or pre-incubated with GA before Rot treatment for 24 h and the data is compared with DMSO control. The quantification of cells in each phase of the cell cycle are shown in the right panel. E and F , immunoblot analysis of Cyclin B1, Securin ( E ) and BubR1 ( F ) protein levels in the whole-cell extracts of SH-SY5Y cells 24 h post-rotenone treatment in the presence or absence of GA. β-Actin was used as a loading control. G , schematic representation showing association of rotenone-induced G2/M arrest with HMGB1 nuclear exit and the effect of GA on the process. Data are presented as mean ± SD. Statistical significance was determined by one-way ANOVA with Tukey’s multiple comparison test (∗∗∗ p < 0.01; n = 3 biological replicates).

    Techniques Used: Staining, Western Blot, Control, Flow Cytometry, Incubation, Comparison

    Rotenone causes persistent DNA damage that cannot be reversed following its withdrawal. A , schematic outline of experimental strategy to study mitotic release in the presence of rotenone or nocodazole. B , representative confocal image of SH-SY5Y cells fixed at 12 h post-release following 24 h treatment with rotenone or nocodazole and stained with pH3S10 ( red ) and DAPI ( blue ). (n = 100 cells for each quantification; right panel ). (scale bar = 25 μm). C , representative confocal image of PC12 cells fixed at 12 h post-release following 24 h treatment with rotenone or nocodazole and stained with pH3S10 ( red ) and DAPI ( blue ). (n = 100 cells for each quantification; bottom panel ). (scale bar = 25 μm). D , representative confocal images of SH-SY5Y cells stained with phospho-γH2AX ( green ) and DAPI ( blue ) fixed at 12 h post-release following 24 h treatment with rotenone or nocodazole ( left panel ). Quantification of phospho-γH2AX foci/cell ( right panel ) (n = 100 cells for each quantification). (scale bar = 10 μm). E , immunoblot analysis of Cyclin B1 and Securin protein levels in the whole-cell extracts of SH-SY5Y cells at 12 h post-release following 24 h treatment with rotenone or nocodazole. β-Actin was used as a loading control. Data are presented as mean ± SD. Statistical significance was determined by two-way ANOVA with Tukey’s multiple comparison test (∗∗∗ p < 0.001; n = 3 biological replicates).
    Figure Legend Snippet: Rotenone causes persistent DNA damage that cannot be reversed following its withdrawal. A , schematic outline of experimental strategy to study mitotic release in the presence of rotenone or nocodazole. B , representative confocal image of SH-SY5Y cells fixed at 12 h post-release following 24 h treatment with rotenone or nocodazole and stained with pH3S10 ( red ) and DAPI ( blue ). (n = 100 cells for each quantification; right panel ). (scale bar = 25 μm). C , representative confocal image of PC12 cells fixed at 12 h post-release following 24 h treatment with rotenone or nocodazole and stained with pH3S10 ( red ) and DAPI ( blue ). (n = 100 cells for each quantification; bottom panel ). (scale bar = 25 μm). D , representative confocal images of SH-SY5Y cells stained with phospho-γH2AX ( green ) and DAPI ( blue ) fixed at 12 h post-release following 24 h treatment with rotenone or nocodazole ( left panel ). Quantification of phospho-γH2AX foci/cell ( right panel ) (n = 100 cells for each quantification). (scale bar = 10 μm). E , immunoblot analysis of Cyclin B1 and Securin protein levels in the whole-cell extracts of SH-SY5Y cells at 12 h post-release following 24 h treatment with rotenone or nocodazole. β-Actin was used as a loading control. Data are presented as mean ± SD. Statistical significance was determined by two-way ANOVA with Tukey’s multiple comparison test (∗∗∗ p < 0.001; n = 3 biological replicates).

    Techniques Used: Staining, Western Blot, Control, Comparison

    Related Articles

    other:

    Article Title: SUMO targets the APC/C to regulate transition from metaphase to anaphase
    Article Snippet: Peters, Vienna) , rabbit anti-KIF18B (Bethyl, A303-982A), and rabbit anti-Securin (Cell Signaling Technology, CST13445).

    Western Blot:

    Article Title: Glutamine synthetase licenses APC/C-mediated mitotic progression to drive cell growth.
    Article Snippet: 1Zhejiang Provincial Key Laboratory of Pancreatic Disease, First Affiliated Hospital, and Institute of Translational Medicine, Zhejiang University School of Medicine, Hangzhou, China.. 2Cancer Center, Zhejiang University, Hangzhou, China.. 3Shanghai Advanced Institute of Immunochemical Studies, ShanghaiTech University, Shanghai, China.

    Control:

    Article Title: CENP-F-dependent DRP1 function regulates APC/C activity during oocyte meiosis I
    Article Snippet: Samples were run on 4%-15% Mini-PROTEAN TGX Gels (BIO-RAD) and transferred onto a nitrocellulose membrane. .. Primary antibodies used were rabbit anti-CENPF (Abcam ab5; 1:500), mouse anti-DRP1 (Abcam ab56788; 1:200), rabbit anti-DRP1 (Ser616) Antibody (Cell Signaling Technology 3455; 1:400), rabbit anti-DRP1 (Ser637) Antibody (Cell Signaling Technology 4867; 1:400), rabbit anti-β-Tubulin (loading Control, Abcam ab6046; 1:500), mouse anti-cMyc (Thermo Fisher R950-25; 1:400), mouse anti-EGFP (Abcam ab184601; 1:400), rabbit anti-cyclinB1 (Cell Signaling 4138; 1:200), goat anti-cyclinB2 (R&D Systems AF6004; 1:400), rabbit anti-FLAG (Sigma-Aldrich F7425; 1:400), rabbit anti-Securin (Cell Signaling 13445; 1:200), rabbit anti-APC2 (Cell Signaling 12301S; 1:200), rabbit anti-APC11 (Abcam ab154546; 1:200), rabbit anti-UbcH5/Ubc4 (Proteintech 28328-AP; 1:200), and rabbit anti-ubiquitin (PTM BIO PTM-1106; 1:200). .. Secondary antibodies used were Peroxidase-conjugated secondary Goat Anti-Mouse (Jackson Immuno Research Laboratories 115-035-003; 1:2000), Donkey Anti-Rabbit (Jackson 711-035-152; 1:2000), and Donkey Anti-Goat (Jackson 705-035-003; 1:2000).



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    TNKS regulates BubR1/MPF activity, and <t>Securin</t> accumulation in mouse oocyte. (A) Representative images of BubR1 signals at the kinetochore in oocytes from the control and JW55 treatment groups. Green, BubR1. Red, ACA. Blue, DNA. Bar = 5 μm. (B) The percentage of positive BubR1 signals at the kinetochore in oocytes from the control (n = 53) and JW55 (n = 50) treatment groups. ***, P < 0.001. (C) Representative images of oocytes PB1 extrusion after 12 h culture in the Control, control + Milri, control + 10 μM ETOP, JW55 + 10 μM ETOP and JW55 groups. GV oocytes were exposed to etoposide (ETOP) at concentrations of 1 μM and 10 μM for 30 min in the presence 4 μM milrinone (Milri) to prevent GVBD during this treatment. Bar = 80 μm. (D) The percentage of PB1 or large PB1 extrusion in the control (n = 94), control + Milri (n = 89), control + 1 μM ETOP (n = 98), control + 10 μM ETOP (n = 97), JW55 + 1 μ M ETOP (n = 128), JW55 + 10 μM ETOP (n = 120), and JW55 treatment (n = 114) oocytes after ETOP pretreatment. ns, P > 0.05. **, P < 0.01. ***, P < 0.001. (E) Representative images of γ-H2AX in MI stage oocyte from the control + 10 μM ETOP and JW55 + 10 μM ETOP oocytes. Red, γ-H2AX. Blue, DNA. Bar = 5 μm. (F) Relative intensity of γ-H2AX in MI stage oocyte from the control + 10 μM ETOP (n = 47) and JW55 + 10 μM ETOP (n = 39) oocytes. ***, P < 0.001. (G) Western blot of Cyclin B1 and Securin in oocytes from the control and JW55 treatment groups after 6 h of culture. (H) Western blot of pT161-CDK1 and CDC20 in oocytes from the control and JW55 treatment groups after 6 h of culture, and band intensity analysis of their protein levels in oocytes from the control and JW55 treatment groups. *, P < 0.05. **, P < 0.01. (I) Band intensity analysis of pT161-CDK1, pY15-CDK1, and Securin in oocytes from the control and JW55 treatment groups after 3 h of culture. ns, P > 0.05. *, P < 0.05. (J) Band intensity analysis <t>of</t> <t>CDC25C,</t> Cyclin B1, and pT14-CDK1 in oocytes from the control and JW55 treatment groups after 3 h of culture. *, P < 0.05. **, P < 0.01. (K) Protein-protein interaction network analysis of cell cycle-related proteins identified by mass spectrometry and MPF/Securin/CDC20/CDC25C upon STRING database. Different node color indicated core and non-core nodes, while edge thickness edge represented interaction strength. (L) Co-IP analysis with an anti-TNKS antibody. The immunoblot was probed with anti-CDC20 and anti-CDC25C antibodies. (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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    TNKS regulates BubR1/MPF activity, and Securin accumulation in mouse oocyte. (A) Representative images of BubR1 signals at the kinetochore in oocytes from the control and JW55 treatment groups. Green, BubR1. Red, ACA. Blue, DNA. Bar = 5 μm. (B) The percentage of positive BubR1 signals at the kinetochore in oocytes from the control (n = 53) and JW55 (n = 50) treatment groups. ***, P < 0.001. (C) Representative images of oocytes PB1 extrusion after 12 h culture in the Control, control + Milri, control + 10 μM ETOP, JW55 + 10 μM ETOP and JW55 groups. GV oocytes were exposed to etoposide (ETOP) at concentrations of 1 μM and 10 μM for 30 min in the presence 4 μM milrinone (Milri) to prevent GVBD during this treatment. Bar = 80 μm. (D) The percentage of PB1 or large PB1 extrusion in the control (n = 94), control + Milri (n = 89), control + 1 μM ETOP (n = 98), control + 10 μM ETOP (n = 97), JW55 + 1 μ M ETOP (n = 128), JW55 + 10 μM ETOP (n = 120), and JW55 treatment (n = 114) oocytes after ETOP pretreatment. ns, P > 0.05. **, P < 0.01. ***, P < 0.001. (E) Representative images of γ-H2AX in MI stage oocyte from the control + 10 μM ETOP and JW55 + 10 μM ETOP oocytes. Red, γ-H2AX. Blue, DNA. Bar = 5 μm. (F) Relative intensity of γ-H2AX in MI stage oocyte from the control + 10 μM ETOP (n = 47) and JW55 + 10 μM ETOP (n = 39) oocytes. ***, P < 0.001. (G) Western blot of Cyclin B1 and Securin in oocytes from the control and JW55 treatment groups after 6 h of culture. (H) Western blot of pT161-CDK1 and CDC20 in oocytes from the control and JW55 treatment groups after 6 h of culture, and band intensity analysis of their protein levels in oocytes from the control and JW55 treatment groups. *, P < 0.05. **, P < 0.01. (I) Band intensity analysis of pT161-CDK1, pY15-CDK1, and Securin in oocytes from the control and JW55 treatment groups after 3 h of culture. ns, P > 0.05. *, P < 0.05. (J) Band intensity analysis of CDC25C, Cyclin B1, and pT14-CDK1 in oocytes from the control and JW55 treatment groups after 3 h of culture. *, P < 0.05. **, P < 0.01. (K) Protein-protein interaction network analysis of cell cycle-related proteins identified by mass spectrometry and MPF/Securin/CDC20/CDC25C upon STRING database. Different node color indicated core and non-core nodes, while edge thickness edge represented interaction strength. (L) Co-IP analysis with an anti-TNKS antibody. The immunoblot was probed with anti-CDC20 and anti-CDC25C antibodies. (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article.)

    Journal: Journal of Advanced Research

    Article Title: Tankyrase activity is essential for asymmetric division and chromosome segregation in oocyte meiosis

    doi: 10.1016/j.jare.2025.07.008

    Figure Lengend Snippet: TNKS regulates BubR1/MPF activity, and Securin accumulation in mouse oocyte. (A) Representative images of BubR1 signals at the kinetochore in oocytes from the control and JW55 treatment groups. Green, BubR1. Red, ACA. Blue, DNA. Bar = 5 μm. (B) The percentage of positive BubR1 signals at the kinetochore in oocytes from the control (n = 53) and JW55 (n = 50) treatment groups. ***, P < 0.001. (C) Representative images of oocytes PB1 extrusion after 12 h culture in the Control, control + Milri, control + 10 μM ETOP, JW55 + 10 μM ETOP and JW55 groups. GV oocytes were exposed to etoposide (ETOP) at concentrations of 1 μM and 10 μM for 30 min in the presence 4 μM milrinone (Milri) to prevent GVBD during this treatment. Bar = 80 μm. (D) The percentage of PB1 or large PB1 extrusion in the control (n = 94), control + Milri (n = 89), control + 1 μM ETOP (n = 98), control + 10 μM ETOP (n = 97), JW55 + 1 μ M ETOP (n = 128), JW55 + 10 μM ETOP (n = 120), and JW55 treatment (n = 114) oocytes after ETOP pretreatment. ns, P > 0.05. **, P < 0.01. ***, P < 0.001. (E) Representative images of γ-H2AX in MI stage oocyte from the control + 10 μM ETOP and JW55 + 10 μM ETOP oocytes. Red, γ-H2AX. Blue, DNA. Bar = 5 μm. (F) Relative intensity of γ-H2AX in MI stage oocyte from the control + 10 μM ETOP (n = 47) and JW55 + 10 μM ETOP (n = 39) oocytes. ***, P < 0.001. (G) Western blot of Cyclin B1 and Securin in oocytes from the control and JW55 treatment groups after 6 h of culture. (H) Western blot of pT161-CDK1 and CDC20 in oocytes from the control and JW55 treatment groups after 6 h of culture, and band intensity analysis of their protein levels in oocytes from the control and JW55 treatment groups. *, P < 0.05. **, P < 0.01. (I) Band intensity analysis of pT161-CDK1, pY15-CDK1, and Securin in oocytes from the control and JW55 treatment groups after 3 h of culture. ns, P > 0.05. *, P < 0.05. (J) Band intensity analysis of CDC25C, Cyclin B1, and pT14-CDK1 in oocytes from the control and JW55 treatment groups after 3 h of culture. *, P < 0.05. **, P < 0.01. (K) Protein-protein interaction network analysis of cell cycle-related proteins identified by mass spectrometry and MPF/Securin/CDC20/CDC25C upon STRING database. Different node color indicated core and non-core nodes, while edge thickness edge represented interaction strength. (L) Co-IP analysis with an anti-TNKS antibody. The immunoblot was probed with anti-CDC20 and anti-CDC25C antibodies. (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article.)

    Article Snippet: Rabbit anti-α-Tubulin antibody (11224-1-AP), rabbit polyclonal anti-GAPDH antibody (10494-1-AP), rabbit anti-GRP78 antibody (11587-1-AP), rabbit anti-TNKS1 antibody (18030-1-AP), rabbit anti-Ran antibody (10469-1-AP), and rabbit anti-Rab11a antibody (67902-1-Ig), rabbit anti-Securin antibody (18040-1-AP), rabbit anti-CDC25C antibody (66912-1-Ig), rabbit anti-Formin2 antibody (11259-1-AP), rabbit anti-BubR1 (11504-2-AP) were from Proteintech.

    Techniques: Activity Assay, Control, Western Blot, Mass Spectrometry, Co-Immunoprecipitation Assay

    HMGB1 inhibitor glycyrrhizic acid prevents rotenone-induced G2/M arrest. A , representative confocal images of cells stained with pH3S10 ( red ), HMGB1 ( green ) and DAPI ( blue ) following rotenone treatment in the presence or absence of the HMGB1 inhibitor glycyrrhizic acid (GA) (1.5 mM). (scale bar = 10 μm). B , quantification of SH-SY5Y cells with cytoplasmic enriched HMGB1 ( left panel ) and pH3S10 positive cells indicating cells arrested at G2/M ( right panel ) for each treatment condition. (n = 100 cells for each quantification). C , immunoblot analysis of HMGB1 protein levels in the nuclear and cytosolic fraction of SH-SY5Y cells treated with rotenone for 24 h in the presence or absence of GA. GAPDH was used as cytosolic loading control and lamin A/C was used as a nuclear loading control ( upper panel ). The nuclear to cytoplasmic ratio was quantified using the lower band obtained in the cytoplasmic fraction of the gels ( lower panel ). D , representative flow cytometry histograms depicting DNA content in SH-SY5Y cells stained with propidium iodide (PI). Distinct peaks correspond to cells in the G0/G1 phase (first peak), S phase (intermediate region), and G2/M phase (second peak). SH-SY5Y cells were treated with Rot, GA or pre-incubated with GA before Rot treatment for 24 h and the data is compared with DMSO control. The quantification of cells in each phase of the cell cycle are shown in the right panel. E and F , immunoblot analysis of Cyclin B1, Securin ( E ) and BubR1 ( F ) protein levels in the whole-cell extracts of SH-SY5Y cells 24 h post-rotenone treatment in the presence or absence of GA. β-Actin was used as a loading control. G , schematic representation showing association of rotenone-induced G2/M arrest with HMGB1 nuclear exit and the effect of GA on the process. Data are presented as mean ± SD. Statistical significance was determined by one-way ANOVA with Tukey’s multiple comparison test (∗∗∗ p < 0.01; n = 3 biological replicates).

    Journal: The Journal of Biological Chemistry

    Article Title: Tubulin hyperacetylation drives HMGB1 nuclear exit via the ROS-PARP1 axis, leading to rotenone-induced G2/M arrest

    doi: 10.1016/j.jbc.2025.110695

    Figure Lengend Snippet: HMGB1 inhibitor glycyrrhizic acid prevents rotenone-induced G2/M arrest. A , representative confocal images of cells stained with pH3S10 ( red ), HMGB1 ( green ) and DAPI ( blue ) following rotenone treatment in the presence or absence of the HMGB1 inhibitor glycyrrhizic acid (GA) (1.5 mM). (scale bar = 10 μm). B , quantification of SH-SY5Y cells with cytoplasmic enriched HMGB1 ( left panel ) and pH3S10 positive cells indicating cells arrested at G2/M ( right panel ) for each treatment condition. (n = 100 cells for each quantification). C , immunoblot analysis of HMGB1 protein levels in the nuclear and cytosolic fraction of SH-SY5Y cells treated with rotenone for 24 h in the presence or absence of GA. GAPDH was used as cytosolic loading control and lamin A/C was used as a nuclear loading control ( upper panel ). The nuclear to cytoplasmic ratio was quantified using the lower band obtained in the cytoplasmic fraction of the gels ( lower panel ). D , representative flow cytometry histograms depicting DNA content in SH-SY5Y cells stained with propidium iodide (PI). Distinct peaks correspond to cells in the G0/G1 phase (first peak), S phase (intermediate region), and G2/M phase (second peak). SH-SY5Y cells were treated with Rot, GA or pre-incubated with GA before Rot treatment for 24 h and the data is compared with DMSO control. The quantification of cells in each phase of the cell cycle are shown in the right panel. E and F , immunoblot analysis of Cyclin B1, Securin ( E ) and BubR1 ( F ) protein levels in the whole-cell extracts of SH-SY5Y cells 24 h post-rotenone treatment in the presence or absence of GA. β-Actin was used as a loading control. G , schematic representation showing association of rotenone-induced G2/M arrest with HMGB1 nuclear exit and the effect of GA on the process. Data are presented as mean ± SD. Statistical significance was determined by one-way ANOVA with Tukey’s multiple comparison test (∗∗∗ p < 0.01; n = 3 biological replicates).

    Article Snippet: Rabbit polyclonal antibodies against Securin (#13445), Cyclin B11 (#4138), BUBR1 (#4116) and Phospho-Histone 3 (Ser10) (#9701) were obtained from Cell Signaling Technology Inc. (CST).

    Techniques: Staining, Western Blot, Control, Flow Cytometry, Incubation, Comparison

    Rotenone causes persistent DNA damage that cannot be reversed following its withdrawal. A , schematic outline of experimental strategy to study mitotic release in the presence of rotenone or nocodazole. B , representative confocal image of SH-SY5Y cells fixed at 12 h post-release following 24 h treatment with rotenone or nocodazole and stained with pH3S10 ( red ) and DAPI ( blue ). (n = 100 cells for each quantification; right panel ). (scale bar = 25 μm). C , representative confocal image of PC12 cells fixed at 12 h post-release following 24 h treatment with rotenone or nocodazole and stained with pH3S10 ( red ) and DAPI ( blue ). (n = 100 cells for each quantification; bottom panel ). (scale bar = 25 μm). D , representative confocal images of SH-SY5Y cells stained with phospho-γH2AX ( green ) and DAPI ( blue ) fixed at 12 h post-release following 24 h treatment with rotenone or nocodazole ( left panel ). Quantification of phospho-γH2AX foci/cell ( right panel ) (n = 100 cells for each quantification). (scale bar = 10 μm). E , immunoblot analysis of Cyclin B1 and Securin protein levels in the whole-cell extracts of SH-SY5Y cells at 12 h post-release following 24 h treatment with rotenone or nocodazole. β-Actin was used as a loading control. Data are presented as mean ± SD. Statistical significance was determined by two-way ANOVA with Tukey’s multiple comparison test (∗∗∗ p < 0.001; n = 3 biological replicates).

    Journal: The Journal of Biological Chemistry

    Article Title: Tubulin hyperacetylation drives HMGB1 nuclear exit via the ROS-PARP1 axis, leading to rotenone-induced G2/M arrest

    doi: 10.1016/j.jbc.2025.110695

    Figure Lengend Snippet: Rotenone causes persistent DNA damage that cannot be reversed following its withdrawal. A , schematic outline of experimental strategy to study mitotic release in the presence of rotenone or nocodazole. B , representative confocal image of SH-SY5Y cells fixed at 12 h post-release following 24 h treatment with rotenone or nocodazole and stained with pH3S10 ( red ) and DAPI ( blue ). (n = 100 cells for each quantification; right panel ). (scale bar = 25 μm). C , representative confocal image of PC12 cells fixed at 12 h post-release following 24 h treatment with rotenone or nocodazole and stained with pH3S10 ( red ) and DAPI ( blue ). (n = 100 cells for each quantification; bottom panel ). (scale bar = 25 μm). D , representative confocal images of SH-SY5Y cells stained with phospho-γH2AX ( green ) and DAPI ( blue ) fixed at 12 h post-release following 24 h treatment with rotenone or nocodazole ( left panel ). Quantification of phospho-γH2AX foci/cell ( right panel ) (n = 100 cells for each quantification). (scale bar = 10 μm). E , immunoblot analysis of Cyclin B1 and Securin protein levels in the whole-cell extracts of SH-SY5Y cells at 12 h post-release following 24 h treatment with rotenone or nocodazole. β-Actin was used as a loading control. Data are presented as mean ± SD. Statistical significance was determined by two-way ANOVA with Tukey’s multiple comparison test (∗∗∗ p < 0.001; n = 3 biological replicates).

    Article Snippet: Rabbit polyclonal antibodies against Securin (#13445), Cyclin B11 (#4138), BUBR1 (#4116) and Phospho-Histone 3 (Ser10) (#9701) were obtained from Cell Signaling Technology Inc. (CST).

    Techniques: Staining, Western Blot, Control, Comparison