anti rnf126  (Proteintech)

 
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    Proteintech anti rnf126
    Anti Rnf126, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    rnf126  (Proteintech)

     
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    Proteintech rnf126
    (A) The percentage of invasive BC tumors with <t>RNF126</t> positive staining was elevated, compared to that of adjacent regions (χ2 test, P<0.001). (B) Representative RNF126 staining detected by immunohistochemistry in adjacent normal and invasive BC tissues. Anti-RNF126 antibody (ab183102) was used. Adjacent normal tissues were collected 5 cm away from the edge of tumors. Specimens were surgically removed before patients were exposed to any neoadjuvant treatment. (C) Logistic regression analysis of RNF126 expression and clinicopathological parameters. RNF126 expression had no obvious relationship with the indicated clinicopathological variables. (D) Kaplan–Meier survival analysis in patients with invasive BC. Increased RNF126 expression correlates with a lower probability of cumulative survival. Recurrence, metastasis, or death were the final events (n=110). (E) Kaplan–Meier survival analysis in patients with invasive BC who received adjuvant chemotherapy. RNF126 positive staining was also associated with a poor prognosis in patients with a subtype of invasive breast tumor who received chemotherapy (n=90). (F) Expression of RNF126 was an independent predictor of a poor prognosis. Multivariate analyses of RNF126 expression and clinicopathological parameters in a cox proportional hazards model are indicated. RNF126 positive staining was an independent factor related to patients’ poor outcomes (HR: Hazard Ratio, 95% CI: 95% Confidence Interval).
    Rnf126, supplied by Proteintech, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "RNF126 as a biomarker of a poor prognosis in invasive breast cancer and CHK1 inhibitor efficacy in breast cancer cells"

    Article Title: RNF126 as a biomarker of a poor prognosis in invasive breast cancer and CHK1 inhibitor efficacy in breast cancer cells

    Journal: Clinical cancer research : an official journal of the American Association for Cancer Research

    doi: 10.1158/1078-0432.CCR-17-2242

    (A) The percentage of invasive BC tumors with RNF126 positive staining was elevated, compared to that of adjacent regions (χ2 test, P<0.001). (B) Representative RNF126 staining detected by immunohistochemistry in adjacent normal and invasive BC tissues. Anti-RNF126 antibody (ab183102) was used. Adjacent normal tissues were collected 5 cm away from the edge of tumors. Specimens were surgically removed before patients were exposed to any neoadjuvant treatment. (C) Logistic regression analysis of RNF126 expression and clinicopathological parameters. RNF126 expression had no obvious relationship with the indicated clinicopathological variables. (D) Kaplan–Meier survival analysis in patients with invasive BC. Increased RNF126 expression correlates with a lower probability of cumulative survival. Recurrence, metastasis, or death were the final events (n=110). (E) Kaplan–Meier survival analysis in patients with invasive BC who received adjuvant chemotherapy. RNF126 positive staining was also associated with a poor prognosis in patients with a subtype of invasive breast tumor who received chemotherapy (n=90). (F) Expression of RNF126 was an independent predictor of a poor prognosis. Multivariate analyses of RNF126 expression and clinicopathological parameters in a cox proportional hazards model are indicated. RNF126 positive staining was an independent factor related to patients’ poor outcomes (HR: Hazard Ratio, 95% CI: 95% Confidence Interval).
    Figure Legend Snippet: (A) The percentage of invasive BC tumors with RNF126 positive staining was elevated, compared to that of adjacent regions (χ2 test, P<0.001). (B) Representative RNF126 staining detected by immunohistochemistry in adjacent normal and invasive BC tissues. Anti-RNF126 antibody (ab183102) was used. Adjacent normal tissues were collected 5 cm away from the edge of tumors. Specimens were surgically removed before patients were exposed to any neoadjuvant treatment. (C) Logistic regression analysis of RNF126 expression and clinicopathological parameters. RNF126 expression had no obvious relationship with the indicated clinicopathological variables. (D) Kaplan–Meier survival analysis in patients with invasive BC. Increased RNF126 expression correlates with a lower probability of cumulative survival. Recurrence, metastasis, or death were the final events (n=110). (E) Kaplan–Meier survival analysis in patients with invasive BC who received adjuvant chemotherapy. RNF126 positive staining was also associated with a poor prognosis in patients with a subtype of invasive breast tumor who received chemotherapy (n=90). (F) Expression of RNF126 was an independent predictor of a poor prognosis. Multivariate analyses of RNF126 expression and clinicopathological parameters in a cox proportional hazards model are indicated. RNF126 positive staining was an independent factor related to patients’ poor outcomes (HR: Hazard Ratio, 95% CI: 95% Confidence Interval).

    Techniques Used: Staining, Immunohistochemistry, Expressing

    (A, B) RNF126 knockdown by shRNAs led to decreased expression of CHK1 protein in MCF7 (A) and MDA-MB-231 cells (B) (upper panels). Band intensities of RNF126 and CHK1 protein expression in cells, with or without RNF126 depletion, were quantified using ImageJ software, and normalized to β-actin. n=3. (lower panels) (MCF7: P1=0.040, P2=0.014, P3=0.016, P4=0.013; MDA-MB-231: P1=0.012, P2=0.002, P3=0.021, P4=0.024). (C) RNF126 and CHK1 mRNA levels in MCF7 or MDA-MB-231 cells, with or without RNF126 knockdown by shRNAs. n=3. (One-way ANOVA, P1=0.002, P2=0.002, P3=0.012, P4=0.007, P5=0.007, P6=0.005, P7=0.014, P8=0.005). (D, E) Flag-RNF126 overexpression resulted in increased CHK1 protein expression in MCF7 and MDA-MB-231 cells. CHK1 protein band intensities were quantified using ImageJ software, and normalized to β-actin. n=3. (D). One of three independent experiments is presented (E). (F) The level of CHK1 mRNA expression in MCF7 or MDA-MB-231 cells, with or without Flag-RNF126WT overexpression. n=3. (Paired t test). (G, H) The expression of an E3 ligase mutant of RNF126 did not affect CHK1 protein expression. MCF7 or MDA-MB-231 cells were transfected with control vector, Flag-RNF126-WT, or E3 ligase-deficient RNF126 (Flag-RNF126-C229A/C232A) plasmids and levels of CHK1 protein were then detected by western blotting. RNF126 and CHK1 protein band intensities were quantified using ImageJ software, and normalized to β-actin. n=3. (One-way ANOVA, P1=0.037, P2=0.008, P3=0.001, P4=0.001, P5=0.023, P6=0.004, P7=0.008, P8=0.013) (G). One of three independent experiments is presented (H).
    Figure Legend Snippet: (A, B) RNF126 knockdown by shRNAs led to decreased expression of CHK1 protein in MCF7 (A) and MDA-MB-231 cells (B) (upper panels). Band intensities of RNF126 and CHK1 protein expression in cells, with or without RNF126 depletion, were quantified using ImageJ software, and normalized to β-actin. n=3. (lower panels) (MCF7: P1=0.040, P2=0.014, P3=0.016, P4=0.013; MDA-MB-231: P1=0.012, P2=0.002, P3=0.021, P4=0.024). (C) RNF126 and CHK1 mRNA levels in MCF7 or MDA-MB-231 cells, with or without RNF126 knockdown by shRNAs. n=3. (One-way ANOVA, P1=0.002, P2=0.002, P3=0.012, P4=0.007, P5=0.007, P6=0.005, P7=0.014, P8=0.005). (D, E) Flag-RNF126 overexpression resulted in increased CHK1 protein expression in MCF7 and MDA-MB-231 cells. CHK1 protein band intensities were quantified using ImageJ software, and normalized to β-actin. n=3. (D). One of three independent experiments is presented (E). (F) The level of CHK1 mRNA expression in MCF7 or MDA-MB-231 cells, with or without Flag-RNF126WT overexpression. n=3. (Paired t test). (G, H) The expression of an E3 ligase mutant of RNF126 did not affect CHK1 protein expression. MCF7 or MDA-MB-231 cells were transfected with control vector, Flag-RNF126-WT, or E3 ligase-deficient RNF126 (Flag-RNF126-C229A/C232A) plasmids and levels of CHK1 protein were then detected by western blotting. RNF126 and CHK1 protein band intensities were quantified using ImageJ software, and normalized to β-actin. n=3. (One-way ANOVA, P1=0.037, P2=0.008, P3=0.001, P4=0.001, P5=0.023, P6=0.004, P7=0.008, P8=0.013) (G). One of three independent experiments is presented (H).

    Techniques Used: Expressing, Software, Over Expression, Mutagenesis, Transfection, Plasmid Preparation, Western Blot

    (A) Co-expression of RNF126 and CHK1 proteins was analyzed by tissue microarrays (TMAs; n=67). (B) Typical immuno-staining patterns for serial sections of the same tumor for RNF126 and CHK1. TMA immunostaining was visualized with 3,3’-diaminobenzidine substrate following probing with antibodies against RNF126 (ab183102, 1:100, Abcam) and CHK1 (25887-1-AP, 1:150, Proteintech). (C) The expression of RNF126, CHK1 and Cyclin E proteins in a panel of 16 human breast cancer (BC)-derived cell lines by western blotting. Normal primary cultured MCF10A cells were used as a control. Four cell lines chosen for the toxicity assay are labeled either in blue (lower expression) or yellow (higher expression). (D) Band intensities of RNF126 and CHK1 protein expression in BC cell lines were quantified using ImageJ software, and normalized to β-actin. n=3. (E) Positive correlation between RNF126 and CHK1 proteins in BC cell lines (Spearman rank correlation, r=0.682, P=0.004). (F) The mRNA expression of RNF126 and CHK1 in a panel of BC cell lines was detected by quantitative real time PCR. n=3. (G) RNF126 protein levels paralleled CHK1 mRNA levels (Spearman rank correlation, r=0.532, P=0.034). (H) RNF126 protein and mRNA transcripts did not correlate in tested BC cell lines (Spearman rank correlation, r=0.300, P=0.259)
    Figure Legend Snippet: (A) Co-expression of RNF126 and CHK1 proteins was analyzed by tissue microarrays (TMAs; n=67). (B) Typical immuno-staining patterns for serial sections of the same tumor for RNF126 and CHK1. TMA immunostaining was visualized with 3,3’-diaminobenzidine substrate following probing with antibodies against RNF126 (ab183102, 1:100, Abcam) and CHK1 (25887-1-AP, 1:150, Proteintech). (C) The expression of RNF126, CHK1 and Cyclin E proteins in a panel of 16 human breast cancer (BC)-derived cell lines by western blotting. Normal primary cultured MCF10A cells were used as a control. Four cell lines chosen for the toxicity assay are labeled either in blue (lower expression) or yellow (higher expression). (D) Band intensities of RNF126 and CHK1 protein expression in BC cell lines were quantified using ImageJ software, and normalized to β-actin. n=3. (E) Positive correlation between RNF126 and CHK1 proteins in BC cell lines (Spearman rank correlation, r=0.682, P=0.004). (F) The mRNA expression of RNF126 and CHK1 in a panel of BC cell lines was detected by quantitative real time PCR. n=3. (G) RNF126 protein levels paralleled CHK1 mRNA levels (Spearman rank correlation, r=0.532, P=0.034). (H) RNF126 protein and mRNA transcripts did not correlate in tested BC cell lines (Spearman rank correlation, r=0.300, P=0.259)

    Techniques Used: Expressing, Immunostaining, Derivative Assay, Western Blot, Cell Culture, Labeling, Software, Real-time Polymerase Chain Reaction

    (A) A (3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assay following CHK1 inhibition by LY2603618 in BC cells with higher RNF126 expression vs. BC cells with lower RNF126 expression. Cells were treated with various concentrations of LY2603618 for 72 h. n=3. (Two-way ANOVA, PBT474 VS. MDA-MB-231<0.001; P BT474 VS. MDA-MB-468<0.001; PZR751 VS. MDA-MB-231 P<0.001; PZR751 VS. MDA-MB-468<0.001). (B) MTT assay for observing the effect of the CHK1 inhibitor, LY2603618, on MCF7 and MDA-MB-231 cell proliferation. Cells were treated with various concentrations of LY2603618 for 72 h. n=3. (Two-way ANOVA). (C) Clonogenic survival following CHK1 inhibition by LY2603618 in MCF7 and MDA-MB-231 cells. n=3. (Two-way ANOVA). (D) CHK1 inhibition was monitored by measuring levels of CHK1 p-S345 and CDC25A by western blots. Cells were treated with various concentrations of LY2603618 for 8 h. The representative result from three independent experiments is presented.
    Figure Legend Snippet: (A) A (3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assay following CHK1 inhibition by LY2603618 in BC cells with higher RNF126 expression vs. BC cells with lower RNF126 expression. Cells were treated with various concentrations of LY2603618 for 72 h. n=3. (Two-way ANOVA, PBT474 VS. MDA-MB-231<0.001; P BT474 VS. MDA-MB-468<0.001; PZR751 VS. MDA-MB-231 P<0.001; PZR751 VS. MDA-MB-468<0.001). (B) MTT assay for observing the effect of the CHK1 inhibitor, LY2603618, on MCF7 and MDA-MB-231 cell proliferation. Cells were treated with various concentrations of LY2603618 for 72 h. n=3. (Two-way ANOVA). (C) Clonogenic survival following CHK1 inhibition by LY2603618 in MCF7 and MDA-MB-231 cells. n=3. (Two-way ANOVA). (D) CHK1 inhibition was monitored by measuring levels of CHK1 p-S345 and CDC25A by western blots. Cells were treated with various concentrations of LY2603618 for 8 h. The representative result from three independent experiments is presented.

    Techniques Used: MTT Assay, Inhibition, Expressing, Western Blot

    (A, C) The proportion of cells with foci of phosphorylated RPA2 (p-RPA2, green) (A) or γ-H2AX (red) (C) in MCF7 cells, with or without RNF126 knockdown (left panels). Cells were treated with LY2603618 (5 µM) for the indicated times and then subjected to immunofluorescence staining. Representative foci of p-RPA2 or γ-H2AX are indicated (right panels). n=3. (Two-way ANOVA). (B, D) CHK1 inhibition by LY2603618 (5 µM) led to a greater increase in levels of p-RPA2 and γ-H2AX in parental MCF7 cells compared to MCF7 cells with RNF126 knockdown as determined by western blot. (E) CHK1 inhibition by LY2603618 (5 µM) led to a greater increase in the levels of p-RPA2 and γ-H2AX proteins in parental MDA-MB-231 cells, compared to MDA-MB-231 cells with RNF126 knockdown, as determined by western blotting. (F) The proportion of cells with foci of p-RPA2 (left panel) or γ-H2AX (right panel) in MDA-MB-231 cells, with or without RNF126 knockdown, as determined by immunofluorescence. n=3. (Two-way ANOVA).
    Figure Legend Snippet: (A, C) The proportion of cells with foci of phosphorylated RPA2 (p-RPA2, green) (A) or γ-H2AX (red) (C) in MCF7 cells, with or without RNF126 knockdown (left panels). Cells were treated with LY2603618 (5 µM) for the indicated times and then subjected to immunofluorescence staining. Representative foci of p-RPA2 or γ-H2AX are indicated (right panels). n=3. (Two-way ANOVA). (B, D) CHK1 inhibition by LY2603618 (5 µM) led to a greater increase in levels of p-RPA2 and γ-H2AX in parental MCF7 cells compared to MCF7 cells with RNF126 knockdown as determined by western blot. (E) CHK1 inhibition by LY2603618 (5 µM) led to a greater increase in the levels of p-RPA2 and γ-H2AX proteins in parental MDA-MB-231 cells, compared to MDA-MB-231 cells with RNF126 knockdown, as determined by western blotting. (F) The proportion of cells with foci of p-RPA2 (left panel) or γ-H2AX (right panel) in MDA-MB-231 cells, with or without RNF126 knockdown, as determined by immunofluorescence. n=3. (Two-way ANOVA).

    Techniques Used: Immunofluorescence, Staining, Inhibition, Western Blot

    (A) Schematic of DNA fiber analysis (left panel) in MCF7 cells. Red tracks, IdU; Green tracks, CldU. (B, C) CHK1 inhibition by LY2603618 (5 µM) increased the rate of replication initiation, particularly in cells with intact RNF126, compared to cells depleted of RNF126. The frequency of new origins was calculated as the number of green signals (b) divided by the total of green (b) plus green/red signals (a+b; right panel). (B: MCF7; C: MDA-MB-231, n=3, One-way ANOVA). (D) CHK1 inhibition led to an increase in non-extractable CDC45 protein, particularly in parental cells with RNF126 compared to cells with RNF126 knockdown, as determined by western blotting. ORC2 was used as a loading control. (E) Measurement of CDC45 chromatin loading by immunostaining after pre-extraction of cells with detergent. Cells presenting with CDC45 staining were considered positive. n=3. (Two-way ANOVA). (F, G) CHK1 inhibition induced a greater decrease in replication fork speeds in MCF7 (F) and MDA-MB-231 cells (G) compared to corresponding cells with RNF126 knockdown. The CIdu/Idu ratio was used to determine elongation. (n=3, One-way ANOVA). (H) Model for targeting BC cells expressing RNF126 by CHK1 inhibitors.
    Figure Legend Snippet: (A) Schematic of DNA fiber analysis (left panel) in MCF7 cells. Red tracks, IdU; Green tracks, CldU. (B, C) CHK1 inhibition by LY2603618 (5 µM) increased the rate of replication initiation, particularly in cells with intact RNF126, compared to cells depleted of RNF126. The frequency of new origins was calculated as the number of green signals (b) divided by the total of green (b) plus green/red signals (a+b; right panel). (B: MCF7; C: MDA-MB-231, n=3, One-way ANOVA). (D) CHK1 inhibition led to an increase in non-extractable CDC45 protein, particularly in parental cells with RNF126 compared to cells with RNF126 knockdown, as determined by western blotting. ORC2 was used as a loading control. (E) Measurement of CDC45 chromatin loading by immunostaining after pre-extraction of cells with detergent. Cells presenting with CDC45 staining were considered positive. n=3. (Two-way ANOVA). (F, G) CHK1 inhibition induced a greater decrease in replication fork speeds in MCF7 (F) and MDA-MB-231 cells (G) compared to corresponding cells with RNF126 knockdown. The CIdu/Idu ratio was used to determine elongation. (n=3, One-way ANOVA). (H) Model for targeting BC cells expressing RNF126 by CHK1 inhibitors.

    Techniques Used: Inhibition, Western Blot, Immunostaining, Staining, Expressing

    f algeriense nrrl 66647  (Illumina Inc)

     
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    Proteintech rnf126
    (A) The percentage of invasive BC tumors with <t>RNF126</t> positive staining was elevated, compared to that of adjacent regions (χ2 test, P<0.001). (B) Representative RNF126 staining detected by immunohistochemistry in adjacent normal and invasive BC tissues. Anti-RNF126 antibody (ab183102) was used. Adjacent normal tissues were collected 5 cm away from the edge of tumors. Specimens were surgically removed before patients were exposed to any neoadjuvant treatment. (C) Logistic regression analysis of RNF126 expression and clinicopathological parameters. RNF126 expression had no obvious relationship with the indicated clinicopathological variables. (D) Kaplan–Meier survival analysis in patients with invasive BC. Increased RNF126 expression correlates with a lower probability of cumulative survival. Recurrence, metastasis, or death were the final events (n=110). (E) Kaplan–Meier survival analysis in patients with invasive BC who received adjuvant chemotherapy. RNF126 positive staining was also associated with a poor prognosis in patients with a subtype of invasive breast tumor who received chemotherapy (n=90). (F) Expression of RNF126 was an independent predictor of a poor prognosis. Multivariate analyses of RNF126 expression and clinicopathological parameters in a cox proportional hazards model are indicated. RNF126 positive staining was an independent factor related to patients’ poor outcomes (HR: Hazard Ratio, 95% CI: 95% Confidence Interval).
    Rnf126, supplied by Proteintech, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    (A) The percentage of invasive BC tumors with <t>RNF126</t> positive staining was elevated, compared to that of adjacent regions (χ2 test, P<0.001). (B) Representative RNF126 staining detected by immunohistochemistry in adjacent normal and invasive BC tissues. Anti-RNF126 antibody (ab183102) was used. Adjacent normal tissues were collected 5 cm away from the edge of tumors. Specimens were surgically removed before patients were exposed to any neoadjuvant treatment. (C) Logistic regression analysis of RNF126 expression and clinicopathological parameters. RNF126 expression had no obvious relationship with the indicated clinicopathological variables. (D) Kaplan–Meier survival analysis in patients with invasive BC. Increased RNF126 expression correlates with a lower probability of cumulative survival. Recurrence, metastasis, or death were the final events (n=110). (E) Kaplan–Meier survival analysis in patients with invasive BC who received adjuvant chemotherapy. RNF126 positive staining was also associated with a poor prognosis in patients with a subtype of invasive breast tumor who received chemotherapy (n=90). (F) Expression of RNF126 was an independent predictor of a poor prognosis. Multivariate analyses of RNF126 expression and clinicopathological parameters in a cox proportional hazards model are indicated. RNF126 positive staining was an independent factor related to patients’ poor outcomes (HR: Hazard Ratio, 95% CI: 95% Confidence Interval).
    F Algeriense Nrrl 66647, supplied by Illumina Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    (A) The percentage of invasive BC tumors with <t>RNF126</t> positive staining was elevated, compared to that of adjacent regions (χ2 test, P<0.001). (B) Representative RNF126 staining detected by immunohistochemistry in adjacent normal and invasive BC tissues. Anti-RNF126 antibody (ab183102) was used. Adjacent normal tissues were collected 5 cm away from the edge of tumors. Specimens were surgically removed before patients were exposed to any neoadjuvant treatment. (C) Logistic regression analysis of RNF126 expression and clinicopathological parameters. RNF126 expression had no obvious relationship with the indicated clinicopathological variables. (D) Kaplan–Meier survival analysis in patients with invasive BC. Increased RNF126 expression correlates with a lower probability of cumulative survival. Recurrence, metastasis, or death were the final events (n=110). (E) Kaplan–Meier survival analysis in patients with invasive BC who received adjuvant chemotherapy. RNF126 positive staining was also associated with a poor prognosis in patients with a subtype of invasive breast tumor who received chemotherapy (n=90). (F) Expression of RNF126 was an independent predictor of a poor prognosis. Multivariate analyses of RNF126 expression and clinicopathological parameters in a cox proportional hazards model are indicated. RNF126 positive staining was an independent factor related to patients’ poor outcomes (HR: Hazard Ratio, 95% CI: 95% Confidence Interval).
    66647 01 H S, supplied by Projekte GmbH, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    (A) The percentage of invasive BC tumors with RNF126 positive staining was elevated, compared to that of adjacent regions (χ2 test, P<0.001). (B) Representative RNF126 staining detected by immunohistochemistry in adjacent normal and invasive BC tissues. Anti-RNF126 antibody (ab183102) was used. Adjacent normal tissues were collected 5 cm away from the edge of tumors. Specimens were surgically removed before patients were exposed to any neoadjuvant treatment. (C) Logistic regression analysis of RNF126 expression and clinicopathological parameters. RNF126 expression had no obvious relationship with the indicated clinicopathological variables. (D) Kaplan–Meier survival analysis in patients with invasive BC. Increased RNF126 expression correlates with a lower probability of cumulative survival. Recurrence, metastasis, or death were the final events (n=110). (E) Kaplan–Meier survival analysis in patients with invasive BC who received adjuvant chemotherapy. RNF126 positive staining was also associated with a poor prognosis in patients with a subtype of invasive breast tumor who received chemotherapy (n=90). (F) Expression of RNF126 was an independent predictor of a poor prognosis. Multivariate analyses of RNF126 expression and clinicopathological parameters in a cox proportional hazards model are indicated. RNF126 positive staining was an independent factor related to patients’ poor outcomes (HR: Hazard Ratio, 95% CI: 95% Confidence Interval).

    Journal: Clinical cancer research : an official journal of the American Association for Cancer Research

    Article Title: RNF126 as a biomarker of a poor prognosis in invasive breast cancer and CHK1 inhibitor efficacy in breast cancer cells

    doi: 10.1158/1078-0432.CCR-17-2242

    Figure Lengend Snippet: (A) The percentage of invasive BC tumors with RNF126 positive staining was elevated, compared to that of adjacent regions (χ2 test, P<0.001). (B) Representative RNF126 staining detected by immunohistochemistry in adjacent normal and invasive BC tissues. Anti-RNF126 antibody (ab183102) was used. Adjacent normal tissues were collected 5 cm away from the edge of tumors. Specimens were surgically removed before patients were exposed to any neoadjuvant treatment. (C) Logistic regression analysis of RNF126 expression and clinicopathological parameters. RNF126 expression had no obvious relationship with the indicated clinicopathological variables. (D) Kaplan–Meier survival analysis in patients with invasive BC. Increased RNF126 expression correlates with a lower probability of cumulative survival. Recurrence, metastasis, or death were the final events (n=110). (E) Kaplan–Meier survival analysis in patients with invasive BC who received adjuvant chemotherapy. RNF126 positive staining was also associated with a poor prognosis in patients with a subtype of invasive breast tumor who received chemotherapy (n=90). (F) Expression of RNF126 was an independent predictor of a poor prognosis. Multivariate analyses of RNF126 expression and clinicopathological parameters in a cox proportional hazards model are indicated. RNF126 positive staining was an independent factor related to patients’ poor outcomes (HR: Hazard Ratio, 95% CI: 95% Confidence Interval).

    Article Snippet: TMA immunostaining was visualized with 3,3’-diaminobenzidine substrate following probing with antibodies against RNF126 (ab183102, 1:100, Abcam) and CHK1 (25887-1-AP, 1:150, Proteintech). ( C ) The expression of RNF126, CHK1 and Cyclin E proteins in a panel of 16 human breast cancer (BC)-derived cell lines by western blotting.

    Techniques: Staining, Immunohistochemistry, Expressing

    (A, B) RNF126 knockdown by shRNAs led to decreased expression of CHK1 protein in MCF7 (A) and MDA-MB-231 cells (B) (upper panels). Band intensities of RNF126 and CHK1 protein expression in cells, with or without RNF126 depletion, were quantified using ImageJ software, and normalized to β-actin. n=3. (lower panels) (MCF7: P1=0.040, P2=0.014, P3=0.016, P4=0.013; MDA-MB-231: P1=0.012, P2=0.002, P3=0.021, P4=0.024). (C) RNF126 and CHK1 mRNA levels in MCF7 or MDA-MB-231 cells, with or without RNF126 knockdown by shRNAs. n=3. (One-way ANOVA, P1=0.002, P2=0.002, P3=0.012, P4=0.007, P5=0.007, P6=0.005, P7=0.014, P8=0.005). (D, E) Flag-RNF126 overexpression resulted in increased CHK1 protein expression in MCF7 and MDA-MB-231 cells. CHK1 protein band intensities were quantified using ImageJ software, and normalized to β-actin. n=3. (D). One of three independent experiments is presented (E). (F) The level of CHK1 mRNA expression in MCF7 or MDA-MB-231 cells, with or without Flag-RNF126WT overexpression. n=3. (Paired t test). (G, H) The expression of an E3 ligase mutant of RNF126 did not affect CHK1 protein expression. MCF7 or MDA-MB-231 cells were transfected with control vector, Flag-RNF126-WT, or E3 ligase-deficient RNF126 (Flag-RNF126-C229A/C232A) plasmids and levels of CHK1 protein were then detected by western blotting. RNF126 and CHK1 protein band intensities were quantified using ImageJ software, and normalized to β-actin. n=3. (One-way ANOVA, P1=0.037, P2=0.008, P3=0.001, P4=0.001, P5=0.023, P6=0.004, P7=0.008, P8=0.013) (G). One of three independent experiments is presented (H).

    Journal: Clinical cancer research : an official journal of the American Association for Cancer Research

    Article Title: RNF126 as a biomarker of a poor prognosis in invasive breast cancer and CHK1 inhibitor efficacy in breast cancer cells

    doi: 10.1158/1078-0432.CCR-17-2242

    Figure Lengend Snippet: (A, B) RNF126 knockdown by shRNAs led to decreased expression of CHK1 protein in MCF7 (A) and MDA-MB-231 cells (B) (upper panels). Band intensities of RNF126 and CHK1 protein expression in cells, with or without RNF126 depletion, were quantified using ImageJ software, and normalized to β-actin. n=3. (lower panels) (MCF7: P1=0.040, P2=0.014, P3=0.016, P4=0.013; MDA-MB-231: P1=0.012, P2=0.002, P3=0.021, P4=0.024). (C) RNF126 and CHK1 mRNA levels in MCF7 or MDA-MB-231 cells, with or without RNF126 knockdown by shRNAs. n=3. (One-way ANOVA, P1=0.002, P2=0.002, P3=0.012, P4=0.007, P5=0.007, P6=0.005, P7=0.014, P8=0.005). (D, E) Flag-RNF126 overexpression resulted in increased CHK1 protein expression in MCF7 and MDA-MB-231 cells. CHK1 protein band intensities were quantified using ImageJ software, and normalized to β-actin. n=3. (D). One of three independent experiments is presented (E). (F) The level of CHK1 mRNA expression in MCF7 or MDA-MB-231 cells, with or without Flag-RNF126WT overexpression. n=3. (Paired t test). (G, H) The expression of an E3 ligase mutant of RNF126 did not affect CHK1 protein expression. MCF7 or MDA-MB-231 cells were transfected with control vector, Flag-RNF126-WT, or E3 ligase-deficient RNF126 (Flag-RNF126-C229A/C232A) plasmids and levels of CHK1 protein were then detected by western blotting. RNF126 and CHK1 protein band intensities were quantified using ImageJ software, and normalized to β-actin. n=3. (One-way ANOVA, P1=0.037, P2=0.008, P3=0.001, P4=0.001, P5=0.023, P6=0.004, P7=0.008, P8=0.013) (G). One of three independent experiments is presented (H).

    Article Snippet: TMA immunostaining was visualized with 3,3’-diaminobenzidine substrate following probing with antibodies against RNF126 (ab183102, 1:100, Abcam) and CHK1 (25887-1-AP, 1:150, Proteintech). ( C ) The expression of RNF126, CHK1 and Cyclin E proteins in a panel of 16 human breast cancer (BC)-derived cell lines by western blotting.

    Techniques: Expressing, Software, Over Expression, Mutagenesis, Transfection, Plasmid Preparation, Western Blot

    (A) Co-expression of RNF126 and CHK1 proteins was analyzed by tissue microarrays (TMAs; n=67). (B) Typical immuno-staining patterns for serial sections of the same tumor for RNF126 and CHK1. TMA immunostaining was visualized with 3,3’-diaminobenzidine substrate following probing with antibodies against RNF126 (ab183102, 1:100, Abcam) and CHK1 (25887-1-AP, 1:150, Proteintech). (C) The expression of RNF126, CHK1 and Cyclin E proteins in a panel of 16 human breast cancer (BC)-derived cell lines by western blotting. Normal primary cultured MCF10A cells were used as a control. Four cell lines chosen for the toxicity assay are labeled either in blue (lower expression) or yellow (higher expression). (D) Band intensities of RNF126 and CHK1 protein expression in BC cell lines were quantified using ImageJ software, and normalized to β-actin. n=3. (E) Positive correlation between RNF126 and CHK1 proteins in BC cell lines (Spearman rank correlation, r=0.682, P=0.004). (F) The mRNA expression of RNF126 and CHK1 in a panel of BC cell lines was detected by quantitative real time PCR. n=3. (G) RNF126 protein levels paralleled CHK1 mRNA levels (Spearman rank correlation, r=0.532, P=0.034). (H) RNF126 protein and mRNA transcripts did not correlate in tested BC cell lines (Spearman rank correlation, r=0.300, P=0.259)

    Journal: Clinical cancer research : an official journal of the American Association for Cancer Research

    Article Title: RNF126 as a biomarker of a poor prognosis in invasive breast cancer and CHK1 inhibitor efficacy in breast cancer cells

    doi: 10.1158/1078-0432.CCR-17-2242

    Figure Lengend Snippet: (A) Co-expression of RNF126 and CHK1 proteins was analyzed by tissue microarrays (TMAs; n=67). (B) Typical immuno-staining patterns for serial sections of the same tumor for RNF126 and CHK1. TMA immunostaining was visualized with 3,3’-diaminobenzidine substrate following probing with antibodies against RNF126 (ab183102, 1:100, Abcam) and CHK1 (25887-1-AP, 1:150, Proteintech). (C) The expression of RNF126, CHK1 and Cyclin E proteins in a panel of 16 human breast cancer (BC)-derived cell lines by western blotting. Normal primary cultured MCF10A cells were used as a control. Four cell lines chosen for the toxicity assay are labeled either in blue (lower expression) or yellow (higher expression). (D) Band intensities of RNF126 and CHK1 protein expression in BC cell lines were quantified using ImageJ software, and normalized to β-actin. n=3. (E) Positive correlation between RNF126 and CHK1 proteins in BC cell lines (Spearman rank correlation, r=0.682, P=0.004). (F) The mRNA expression of RNF126 and CHK1 in a panel of BC cell lines was detected by quantitative real time PCR. n=3. (G) RNF126 protein levels paralleled CHK1 mRNA levels (Spearman rank correlation, r=0.532, P=0.034). (H) RNF126 protein and mRNA transcripts did not correlate in tested BC cell lines (Spearman rank correlation, r=0.300, P=0.259)

    Article Snippet: TMA immunostaining was visualized with 3,3’-diaminobenzidine substrate following probing with antibodies against RNF126 (ab183102, 1:100, Abcam) and CHK1 (25887-1-AP, 1:150, Proteintech). ( C ) The expression of RNF126, CHK1 and Cyclin E proteins in a panel of 16 human breast cancer (BC)-derived cell lines by western blotting.

    Techniques: Expressing, Immunostaining, Derivative Assay, Western Blot, Cell Culture, Labeling, Software, Real-time Polymerase Chain Reaction

    (A) A (3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assay following CHK1 inhibition by LY2603618 in BC cells with higher RNF126 expression vs. BC cells with lower RNF126 expression. Cells were treated with various concentrations of LY2603618 for 72 h. n=3. (Two-way ANOVA, PBT474 VS. MDA-MB-231<0.001; P BT474 VS. MDA-MB-468<0.001; PZR751 VS. MDA-MB-231 P<0.001; PZR751 VS. MDA-MB-468<0.001). (B) MTT assay for observing the effect of the CHK1 inhibitor, LY2603618, on MCF7 and MDA-MB-231 cell proliferation. Cells were treated with various concentrations of LY2603618 for 72 h. n=3. (Two-way ANOVA). (C) Clonogenic survival following CHK1 inhibition by LY2603618 in MCF7 and MDA-MB-231 cells. n=3. (Two-way ANOVA). (D) CHK1 inhibition was monitored by measuring levels of CHK1 p-S345 and CDC25A by western blots. Cells were treated with various concentrations of LY2603618 for 8 h. The representative result from three independent experiments is presented.

    Journal: Clinical cancer research : an official journal of the American Association for Cancer Research

    Article Title: RNF126 as a biomarker of a poor prognosis in invasive breast cancer and CHK1 inhibitor efficacy in breast cancer cells

    doi: 10.1158/1078-0432.CCR-17-2242

    Figure Lengend Snippet: (A) A (3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assay following CHK1 inhibition by LY2603618 in BC cells with higher RNF126 expression vs. BC cells with lower RNF126 expression. Cells were treated with various concentrations of LY2603618 for 72 h. n=3. (Two-way ANOVA, PBT474 VS. MDA-MB-231<0.001; P BT474 VS. MDA-MB-468<0.001; PZR751 VS. MDA-MB-231 P<0.001; PZR751 VS. MDA-MB-468<0.001). (B) MTT assay for observing the effect of the CHK1 inhibitor, LY2603618, on MCF7 and MDA-MB-231 cell proliferation. Cells were treated with various concentrations of LY2603618 for 72 h. n=3. (Two-way ANOVA). (C) Clonogenic survival following CHK1 inhibition by LY2603618 in MCF7 and MDA-MB-231 cells. n=3. (Two-way ANOVA). (D) CHK1 inhibition was monitored by measuring levels of CHK1 p-S345 and CDC25A by western blots. Cells were treated with various concentrations of LY2603618 for 8 h. The representative result from three independent experiments is presented.

    Article Snippet: TMA immunostaining was visualized with 3,3’-diaminobenzidine substrate following probing with antibodies against RNF126 (ab183102, 1:100, Abcam) and CHK1 (25887-1-AP, 1:150, Proteintech). ( C ) The expression of RNF126, CHK1 and Cyclin E proteins in a panel of 16 human breast cancer (BC)-derived cell lines by western blotting.

    Techniques: MTT Assay, Inhibition, Expressing, Western Blot

    (A, C) The proportion of cells with foci of phosphorylated RPA2 (p-RPA2, green) (A) or γ-H2AX (red) (C) in MCF7 cells, with or without RNF126 knockdown (left panels). Cells were treated with LY2603618 (5 µM) for the indicated times and then subjected to immunofluorescence staining. Representative foci of p-RPA2 or γ-H2AX are indicated (right panels). n=3. (Two-way ANOVA). (B, D) CHK1 inhibition by LY2603618 (5 µM) led to a greater increase in levels of p-RPA2 and γ-H2AX in parental MCF7 cells compared to MCF7 cells with RNF126 knockdown as determined by western blot. (E) CHK1 inhibition by LY2603618 (5 µM) led to a greater increase in the levels of p-RPA2 and γ-H2AX proteins in parental MDA-MB-231 cells, compared to MDA-MB-231 cells with RNF126 knockdown, as determined by western blotting. (F) The proportion of cells with foci of p-RPA2 (left panel) or γ-H2AX (right panel) in MDA-MB-231 cells, with or without RNF126 knockdown, as determined by immunofluorescence. n=3. (Two-way ANOVA).

    Journal: Clinical cancer research : an official journal of the American Association for Cancer Research

    Article Title: RNF126 as a biomarker of a poor prognosis in invasive breast cancer and CHK1 inhibitor efficacy in breast cancer cells

    doi: 10.1158/1078-0432.CCR-17-2242

    Figure Lengend Snippet: (A, C) The proportion of cells with foci of phosphorylated RPA2 (p-RPA2, green) (A) or γ-H2AX (red) (C) in MCF7 cells, with or without RNF126 knockdown (left panels). Cells were treated with LY2603618 (5 µM) for the indicated times and then subjected to immunofluorescence staining. Representative foci of p-RPA2 or γ-H2AX are indicated (right panels). n=3. (Two-way ANOVA). (B, D) CHK1 inhibition by LY2603618 (5 µM) led to a greater increase in levels of p-RPA2 and γ-H2AX in parental MCF7 cells compared to MCF7 cells with RNF126 knockdown as determined by western blot. (E) CHK1 inhibition by LY2603618 (5 µM) led to a greater increase in the levels of p-RPA2 and γ-H2AX proteins in parental MDA-MB-231 cells, compared to MDA-MB-231 cells with RNF126 knockdown, as determined by western blotting. (F) The proportion of cells with foci of p-RPA2 (left panel) or γ-H2AX (right panel) in MDA-MB-231 cells, with or without RNF126 knockdown, as determined by immunofluorescence. n=3. (Two-way ANOVA).

    Article Snippet: TMA immunostaining was visualized with 3,3’-diaminobenzidine substrate following probing with antibodies against RNF126 (ab183102, 1:100, Abcam) and CHK1 (25887-1-AP, 1:150, Proteintech). ( C ) The expression of RNF126, CHK1 and Cyclin E proteins in a panel of 16 human breast cancer (BC)-derived cell lines by western blotting.

    Techniques: Immunofluorescence, Staining, Inhibition, Western Blot

    (A) Schematic of DNA fiber analysis (left panel) in MCF7 cells. Red tracks, IdU; Green tracks, CldU. (B, C) CHK1 inhibition by LY2603618 (5 µM) increased the rate of replication initiation, particularly in cells with intact RNF126, compared to cells depleted of RNF126. The frequency of new origins was calculated as the number of green signals (b) divided by the total of green (b) plus green/red signals (a+b; right panel). (B: MCF7; C: MDA-MB-231, n=3, One-way ANOVA). (D) CHK1 inhibition led to an increase in non-extractable CDC45 protein, particularly in parental cells with RNF126 compared to cells with RNF126 knockdown, as determined by western blotting. ORC2 was used as a loading control. (E) Measurement of CDC45 chromatin loading by immunostaining after pre-extraction of cells with detergent. Cells presenting with CDC45 staining were considered positive. n=3. (Two-way ANOVA). (F, G) CHK1 inhibition induced a greater decrease in replication fork speeds in MCF7 (F) and MDA-MB-231 cells (G) compared to corresponding cells with RNF126 knockdown. The CIdu/Idu ratio was used to determine elongation. (n=3, One-way ANOVA). (H) Model for targeting BC cells expressing RNF126 by CHK1 inhibitors.

    Journal: Clinical cancer research : an official journal of the American Association for Cancer Research

    Article Title: RNF126 as a biomarker of a poor prognosis in invasive breast cancer and CHK1 inhibitor efficacy in breast cancer cells

    doi: 10.1158/1078-0432.CCR-17-2242

    Figure Lengend Snippet: (A) Schematic of DNA fiber analysis (left panel) in MCF7 cells. Red tracks, IdU; Green tracks, CldU. (B, C) CHK1 inhibition by LY2603618 (5 µM) increased the rate of replication initiation, particularly in cells with intact RNF126, compared to cells depleted of RNF126. The frequency of new origins was calculated as the number of green signals (b) divided by the total of green (b) plus green/red signals (a+b; right panel). (B: MCF7; C: MDA-MB-231, n=3, One-way ANOVA). (D) CHK1 inhibition led to an increase in non-extractable CDC45 protein, particularly in parental cells with RNF126 compared to cells with RNF126 knockdown, as determined by western blotting. ORC2 was used as a loading control. (E) Measurement of CDC45 chromatin loading by immunostaining after pre-extraction of cells with detergent. Cells presenting with CDC45 staining were considered positive. n=3. (Two-way ANOVA). (F, G) CHK1 inhibition induced a greater decrease in replication fork speeds in MCF7 (F) and MDA-MB-231 cells (G) compared to corresponding cells with RNF126 knockdown. The CIdu/Idu ratio was used to determine elongation. (n=3, One-way ANOVA). (H) Model for targeting BC cells expressing RNF126 by CHK1 inhibitors.

    Article Snippet: TMA immunostaining was visualized with 3,3’-diaminobenzidine substrate following probing with antibodies against RNF126 (ab183102, 1:100, Abcam) and CHK1 (25887-1-AP, 1:150, Proteintech). ( C ) The expression of RNF126, CHK1 and Cyclin E proteins in a panel of 16 human breast cancer (BC)-derived cell lines by western blotting.

    Techniques: Inhibition, Western Blot, Immunostaining, Staining, Expressing