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OriGene wild type birc3

Stereospecificity of NPD1 bioactivity selectively upregulates <t>BIRC3</t> expression. ( a ) BIRC1 to 8 in response to 600 μ M H 2 O 2 /10 ng/ml TNF- α in the presence or absence of 100 nM NPD1 at 2, 4 and 6 h of treatment. ( b ) BIRC3 mRNA expression in response to 100 nM maresin 1, lipoxin-A4 and RvE1 along with NPD1 and its stereoisomers SS-NPD1 and RR-NPD1 and ( c ) in an siRNA dose-dependent curve. ARPE-19 cells were transfected with 0, 5, 10, 20, 50 and 100 pmol of siRNA per ml of culture media and treated with 400 μ M H 2 O 2 /10 ng/ml TNF- α in the presence or absence of 100 nM NPD1. ( i – vi ) Structure of the lipid mediators used in ( b ). The bars represent the mean of three triplicates ± standard error. * P <0.05, NS=non-significant P- value. NPD1-treated samples=blue bars; OS+NPD1=light blue bars

Wild Type Birc3, supplied by OriGene, used in various techniques. Bioz Stars score: 90/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/api+2/pmc04495360-152-0-9?v=OriGene
Average 90 stars, based on 7 article reviews

wild type birc3 - by Bioz Stars, 2026-07

90/100 stars

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1) Product Images from "NPD1-mediated stereoselective regulation of BIRC3 expression through cREL is decisive for neural cell survival"

Article Title: NPD1-mediated stereoselective regulation of BIRC3 expression through cREL is decisive for neural cell survival

Journal: Cell Death and Differentiation

doi: 10.1038/cdd.2014.233

Stereospecificity of NPD1 bioactivity selectively upregulates BIRC3 expression. ( a ) BIRC1 to 8 in response to 600 μ M H 2 O 2 /10 ng/ml TNF- α in the presence or absence of 100 nM NPD1 at 2, 4 and 6 h of treatment. ( b ) BIRC3 mRNA expression in response to 100 nM maresin 1, lipoxin-A4 and RvE1 along with NPD1 and its stereoisomers SS-NPD1 and RR-NPD1 and ( c ) in an siRNA dose-dependent curve. ARPE-19 cells were transfected with 0, 5, 10, 20, 50 and 100 pmol of siRNA per ml of culture media and treated with 400 μ M H 2 O 2 /10 ng/ml TNF- α in the presence or absence of 100 nM NPD1. ( i – vi ) Structure of the lipid mediators used in ( b ). The bars represent the mean of three triplicates ± standard error. * P <0.05, NS=non-significant P- value. NPD1-treated samples=blue bars; OS+NPD1=light blue bars

Figure Legend Snippet: Stereospecificity of NPD1 bioactivity selectively upregulates BIRC3 expression. ( a ) BIRC1 to 8 in response to 600 μ M H 2 O 2 /10 ng/ml TNF- α in the presence or absence of 100 nM NPD1 at 2, 4 and 6 h of treatment. ( b ) BIRC3 mRNA expression in response to 100 nM maresin 1, lipoxin-A4 and RvE1 along with NPD1 and its stereoisomers SS-NPD1 and RR-NPD1 and ( c ) in an siRNA dose-dependent curve. ARPE-19 cells were transfected with 0, 5, 10, 20, 50 and 100 pmol of siRNA per ml of culture media and treated with 400 μ M H 2 O 2 /10 ng/ml TNF- α in the presence or absence of 100 nM NPD1. ( i – vi ) Structure of the lipid mediators used in ( b ). The bars represent the mean of three triplicates ± standard error. * P <0.05, NS=non-significant P- value. NPD1-treated samples=blue bars; OS+NPD1=light blue bars

Techniques Used: Expressing, Transfection

TNFR1 stably-silenced cells display enhanced BIRC3 expression and cell survival upon oxidative stress (OS). ( a and b ) TNFR1 and NC shRNA-expressing ARPE-19 cells were subjected to OS in the presence or absence of NPD1. ( a ) Representative pictures and ( b ) quantification of apoptotic TNFR1 and NC shRNA-expressing cells in the presence or absence of 50 nM NPD1. ( c ) BIRC3 expression induced by NPD1 upon OS by the means of real-time PCR in TNFR1-deficient cells. ( d and e ) Western blot showing the time-dependent phosphorylation of ( d ) I k B α and ( e ) I k B β after 0, 15, 30 and 60 min of OS treatment in the presence or absence of 100 nM NPD1. ( f ) NPD1 effects on canonical NF- κ B activation measured by the means of luciferase reporter assay in OS conditions. OS: 600 μ M H 2 O 2 /10 ng/ml TNF- α . NPD1: 100 nM. Bars represent the mean of triplicates ± standard error of the mean. * P <0.05, NS=non-significant P -value. NPD1 treated samples=blue bars; OS+NPD1=light blue bars

Figure Legend Snippet: TNFR1 stably-silenced cells display enhanced BIRC3 expression and cell survival upon oxidative stress (OS). ( a and b ) TNFR1 and NC shRNA-expressing ARPE-19 cells were subjected to OS in the presence or absence of NPD1. ( a ) Representative pictures and ( b ) quantification of apoptotic TNFR1 and NC shRNA-expressing cells in the presence or absence of 50 nM NPD1. ( c ) BIRC3 expression induced by NPD1 upon OS by the means of real-time PCR in TNFR1-deficient cells. ( d and e ) Western blot showing the time-dependent phosphorylation of ( d ) I k B α and ( e ) I k B β after 0, 15, 30 and 60 min of OS treatment in the presence or absence of 100 nM NPD1. ( f ) NPD1 effects on canonical NF- κ B activation measured by the means of luciferase reporter assay in OS conditions. OS: 600 μ M H 2 O 2 /10 ng/ml TNF- α . NPD1: 100 nM. Bars represent the mean of triplicates ± standard error of the mean. * P <0.05, NS=non-significant P -value. NPD1 treated samples=blue bars; OS+NPD1=light blue bars

Techniques Used: Stable Transfection, Expressing, shRNA, Real-time Polymerase Chain Reaction, Western Blot, Activation Assay, Luciferase, Reporter Assay

NPD1-mediated BIRC3 promoter activation. BIRC3 promoter was analyzed using a luciferase reporter assay. ( a ) Schematic representation of the constructs used for deletion and mutation. ( b ) BIRC3 promoter deletion analysis using constructs containing 527, 247, 200, 174 and 93 bp (depicted in a ) upstream of the transcription start site. Transfected cells were treated with 130 μ M H 2 O 2 /10 ng/ml TNF- α in the presence or absence of 200 nM NPD1. ( c ) Site directed mutation analysis on the NF- κ B sites. Cells were treated with 400 μ M H 2 O 2 /10 ng/ml TNF- α in the presence or absence of 200 nM NPD1. ( d ) Luciferase activity was standardized by GFP fluorescence. Bars represent the mean of triplicates ± standard error of the mean. * P <0.05, NS=non-significant P- value. NPD1-treated samples=blue bars; OS+NPD1=light blue bars

Figure Legend Snippet: NPD1-mediated BIRC3 promoter activation. BIRC3 promoter was analyzed using a luciferase reporter assay. ( a ) Schematic representation of the constructs used for deletion and mutation. ( b ) BIRC3 promoter deletion analysis using constructs containing 527, 247, 200, 174 and 93 bp (depicted in a ) upstream of the transcription start site. Transfected cells were treated with 130 μ M H 2 O 2 /10 ng/ml TNF- α in the presence or absence of 200 nM NPD1. ( c ) Site directed mutation analysis on the NF- κ B sites. Cells were treated with 400 μ M H 2 O 2 /10 ng/ml TNF- α in the presence or absence of 200 nM NPD1. ( d ) Luciferase activity was standardized by GFP fluorescence. Bars represent the mean of triplicates ± standard error of the mean. * P <0.05, NS=non-significant P- value. NPD1-treated samples=blue bars; OS+NPD1=light blue bars

Techniques Used: Activation Assay, Luciferase, Reporter Assay, Construct, Mutagenesis, Transfection, Activity Assay, Fluorescence

$cREL nuclear translocation and binding to BIRC3 promoter to induce the activation of its expression. Changes of distribution, activity and expression of cRel were assessed at three time points (2, 4 and 6 h) in ARPE-19 cells treated with 400 μ M H 2 O 2 /10 ng/ml TNF- α in the presence or absence of 100 nM NPD1. ( a – c ) Immunocytochemistry of cREL in cells: ( a ) representative pictures showing the distribution of the cREL signal (red). Nuclei were stained with DAPI (blue). ( b and c ) Portion of cells depicting cREL nuclear or cytoplasmic signal. ( d and e ) cREL protein content evaluated by western blot ( d ) in the nuclear fraction standardized using TBP at 2 h and ( e ) in whole cells standardized by GAPDH after 4 h of OS or OS+NPD1. ( f ) ChiP assay at 4 h showing the binding of cREL to BIRC3 promoter. The co-immunoprecipitated genomic DNA was amplified and standardized by the input. ( g ) Co-immunoprecipitation of cREL and p65/RelA at 4 h of treatment standardized by GAPDH. ( h ) p65/RelA, RelB and cRel expression determined by real-time PCR. ( i – k ) Silencing of cRel induced changes in the expression of: ( i ) cREL, ( j ) RelB and ( k ) BIRC3 in human RPE (hRPE) cells established by the means of real-time PCR. Concentrations of 2.5, 10 and 50 pmol siRNA per ml of cell culture medium were used to show a concentration-dependent effect on the expression at 4 h. ( l and m ) Schematization of the temporal pattern of ( l ) cREL, RelB and BIRC3 expression and ( m ) cREL translocation. The values are represented as the mean of triplicates ± the standard error. * P <0.05, NS=non-significant P- value. NPD1-treated samples=blue bars; OS+NPD1=light blue bars$
Figure Legend Snippet: cREL nuclear translocation and binding to BIRC3 promoter to induce the activation of its expression. Changes of distribution, activity and expression of cRel were assessed at three time points (2, 4 and 6 h) in ARPE-19 cells treated with 400 μ M H 2 O 2 /10 ng/ml TNF- α in the presence or absence of 100 nM NPD1. ( a – c ) Immunocytochemistry of cREL in cells: ( a ) representative pictures showing the distribution of the cREL signal (red). Nuclei were stained with DAPI (blue). ( b and c ) Portion of cells depicting cREL nuclear or cytoplasmic signal. ( d and e ) cREL protein content evaluated by western blot ( d ) in the nuclear fraction standardized using TBP at 2 h and ( e ) in whole cells standardized by GAPDH after 4 h of OS or OS+NPD1. ( f ) ChiP assay at 4 h showing the binding of cREL to BIRC3 promoter. The co-immunoprecipitated genomic DNA was amplified and standardized by the input. ( g ) Co-immunoprecipitation of cREL and p65/RelA at 4 h of treatment standardized by GAPDH. ( h ) p65/RelA, RelB and cRel expression determined by real-time PCR. ( i – k ) Silencing of cRel induced changes in the expression of: ( i ) cREL, ( j ) RelB and ( k ) BIRC3 in human RPE (hRPE) cells established by the means of real-time PCR. Concentrations of 2.5, 10 and 50 pmol siRNA per ml of cell culture medium were used to show a concentration-dependent effect on the expression at 4 h. ( l and m ) Schematization of the temporal pattern of ( l ) cREL, RelB and BIRC3 expression and ( m ) cREL translocation. The values are represented as the mean of triplicates ± the standard error. * P <0.05, NS=non-significant P- value. NPD1-treated samples=blue bars; OS+NPD1=light blue bars

Techniques Used: Translocation Assay, Binding Assay, Activation Assay, Expressing, Activity Assay, Immunocytochemistry, Staining, Western Blot, Immunoprecipitation, Amplification, Real-time Polymerase Chain Reaction, Cell Culture, Concentration Assay

NPD1 fails to rescue BIRC3 silenced cells. ( a – e ) Apoptosis noted as percentage of Hoechst- or TUNEL-positive cells was assessed on ARPE-19 ( a – c ) or primary human RPE (hRPE) cells ( d and e ). ( a ) Representative images of TUNEL staining performed on ARPE-19 cells, ( b and c ) Quantification of TUNEL and Hoechst-positive cells when transfected with BIRC3 or control siRNA and treated with 0, 400 and 600 μ M H 2 O 2 /10 ng/ml TNF- α with or without 200 nM NPD1. BIRC3 ( d ), cREL ( e ) or control siRNA-transfected hRPE cells treated with 600 μ M H 2 O 2 /10 ng/ml TNF- α in the presence or absence of NPD1 100 nM. cREL and BIRC3 ( f ) and BIRC3 ( g ) protein content when cREL and BIRC3, respectively, were overexpressed. ( h ) Percentage of apoptosis in ARPE-19 cells overexpressing cREL or BIRC3 when confronted with OS in the presence or absence of NPD1. ( i and j ) Overexpression of ( i ) cREL or ( j ) BIRC3 using a wild-type open reading frame (ORF) or one carrying silent mutations at the siRNAs binding sites (ORFmut) to prevent its silencing and rescue from the knocked down phenotype. Upper panels show representative western blots for the corresponding protein content in each sample. Lower panels depict percentage of apoptosis for each treatment. ( k and l ) Activation of effector caspases 3 and 7 as a result of OS treatment in BIRC3-silenced cells. ( k ) Representative nuclei and staining of cells: upper panel, control; lower panel, OS. ( m and n ) Apoptosis and necrosis measured by the means of AnnexinV and 7-Amino actinomycinD when cells were treated with OS and NPD1 in the presence of z-VAD, a pan caspase inhibitor or Necrostatin 1 (Nec1). ( o ) cREL translocation (upper panel) and percentage of apoptosis of control and cREL-silenced (lower panel) ARPE-19 cells subjected to OS with the addition NPD1 or DHA plus 10 ng/ml of PEDF, FGF, CNTF or BDNF to endogenously induce NPD1 synthesis. ( p ) Schematization of the model obtained by the integration of the data obtained in this report and the context. Bars represent the mean of triplicates + standard error of the mean. * P <0.05 NS=non-significant P -value. NPD1-treated samples=blue bars; OS+NPD1=light blue bars; DHA+growth factors=teal bars; OS+DHA+growth factors=light teal bars

Figure Legend Snippet: NPD1 fails to rescue BIRC3 silenced cells. ( a – e ) Apoptosis noted as percentage of Hoechst- or TUNEL-positive cells was assessed on ARPE-19 ( a – c ) or primary human RPE (hRPE) cells ( d and e ). ( a ) Representative images of TUNEL staining performed on ARPE-19 cells, ( b and c ) Quantification of TUNEL and Hoechst-positive cells when transfected with BIRC3 or control siRNA and treated with 0, 400 and 600 μ M H 2 O 2 /10 ng/ml TNF- α with or without 200 nM NPD1. BIRC3 ( d ), cREL ( e ) or control siRNA-transfected hRPE cells treated with 600 μ M H 2 O 2 /10 ng/ml TNF- α in the presence or absence of NPD1 100 nM. cREL and BIRC3 ( f ) and BIRC3 ( g ) protein content when cREL and BIRC3, respectively, were overexpressed. ( h ) Percentage of apoptosis in ARPE-19 cells overexpressing cREL or BIRC3 when confronted with OS in the presence or absence of NPD1. ( i and j ) Overexpression of ( i ) cREL or ( j ) BIRC3 using a wild-type open reading frame (ORF) or one carrying silent mutations at the siRNAs binding sites (ORFmut) to prevent its silencing and rescue from the knocked down phenotype. Upper panels show representative western blots for the corresponding protein content in each sample. Lower panels depict percentage of apoptosis for each treatment. ( k and l ) Activation of effector caspases 3 and 7 as a result of OS treatment in BIRC3-silenced cells. ( k ) Representative nuclei and staining of cells: upper panel, control; lower panel, OS. ( m and n ) Apoptosis and necrosis measured by the means of AnnexinV and 7-Amino actinomycinD when cells were treated with OS and NPD1 in the presence of z-VAD, a pan caspase inhibitor or Necrostatin 1 (Nec1). ( o ) cREL translocation (upper panel) and percentage of apoptosis of control and cREL-silenced (lower panel) ARPE-19 cells subjected to OS with the addition NPD1 or DHA plus 10 ng/ml of PEDF, FGF, CNTF or BDNF to endogenously induce NPD1 synthesis. ( p ) Schematization of the model obtained by the integration of the data obtained in this report and the context. Bars represent the mean of triplicates + standard error of the mean. * P <0.05 NS=non-significant P -value. NPD1-treated samples=blue bars; OS+NPD1=light blue bars; DHA+growth factors=teal bars; OS+DHA+growth factors=light teal bars

Techniques Used: TUNEL Assay, Staining, Transfection, Over Expression, Binding Assay, Western Blot, Activation Assay, Translocation Assay

BIRC3 mediates the pro-survival response induced by the DHA/NPD1 pathway in an ischemia-reperfusion stroke model. ( a – c ) Model for inducing ischemia-reperfusion by middle cerebral artery occlusion (MCAo) in rats. ( a ) Timeline showing surgery, treatment and tests performed. ( b ) Coronal brain diagram (bregma level –0.3 mm) showing locations of regions for western blot and immunohistochemistry for , and lipidomic analysis (A: anterior; P: posterior). ( c ) Diagram of MCAo model obtained by introducing intraluminal filament (red). ( d ) Total neurological score (normal score =0, maximal deficit=12), tactile placing (proprioceptive, lateral, dorsal reactions; normal score=0, maximal deficit=2) in rats after MCAo. DHA treatment improved the total and placing deficits on days 1, 3 and 7 compared with the saline-treated group. ( e ) Content of NPD1 and a second product of the stabilized precursor, 17HDHA, in penumbra regions of rats subjected to MCAo and treated with DHA or vehicle as a control. Data are means±standard error of the mean; n =6 per group. * P <0.05 in repeated-measures, ANOVA followed by Bonferroni test. DHA treatment=teal bars

Figure Legend Snippet: BIRC3 mediates the pro-survival response induced by the DHA/NPD1 pathway in an ischemia-reperfusion stroke model. ( a – c ) Model for inducing ischemia-reperfusion by middle cerebral artery occlusion (MCAo) in rats. ( a ) Timeline showing surgery, treatment and tests performed. ( b ) Coronal brain diagram (bregma level –0.3 mm) showing locations of regions for western blot and immunohistochemistry for , and lipidomic analysis (A: anterior; P: posterior). ( c ) Diagram of MCAo model obtained by introducing intraluminal filament (red). ( d ) Total neurological score (normal score =0, maximal deficit=12), tactile placing (proprioceptive, lateral, dorsal reactions; normal score=0, maximal deficit=2) in rats after MCAo. DHA treatment improved the total and placing deficits on days 1, 3 and 7 compared with the saline-treated group. ( e ) Content of NPD1 and a second product of the stabilized precursor, 17HDHA, in penumbra regions of rats subjected to MCAo and treated with DHA or vehicle as a control. Data are means±standard error of the mean; n =6 per group. * P <0.05 in repeated-measures, ANOVA followed by Bonferroni test. DHA treatment=teal bars

Techniques Used: Western Blot, Immunohistochemistry

DHA/NPD1 induce translocation of cREL and increased BIRC3 in vivo . ( a ) Western blot on days 1, 3 and 7 after DHA treatment performed on the posterior section. ( b – e ) Translocation of cREL in neurons of the penumbra, areas A1-3 and P1-3 (see ). ( b ) Representative images of nuclear translocation of cREL in saline- and DHA-treated animals in the P2 region 1 day after treatment. (NeuN red; c-REL green). ( c ) High magnification. cREL ( d ) total (upper panels) and ( e ) nuclear (lower panels) quantification from areas A1 to 3 (upper panels) and P1-3 (lower panels). ( f ) BIRC3 (red) and NeuN (green), and ( g ) BIRC3 (red) and GFAP (green) double staining on day 1 after stroke. ( h ) Quantification of the co-localization studies in ( f and g) . Data are means±S.E.M.; n =6 per group. * P <0.05 in repeated-measures, ANOVA followed by Bonferroni test. DHA treatment=teal bars

Figure Legend Snippet: DHA/NPD1 induce translocation of cREL and increased BIRC3 in vivo . ( a ) Western blot on days 1, 3 and 7 after DHA treatment performed on the posterior section. ( b – e ) Translocation of cREL in neurons of the penumbra, areas A1-3 and P1-3 (see ). ( b ) Representative images of nuclear translocation of cREL in saline- and DHA-treated animals in the P2 region 1 day after treatment. (NeuN red; c-REL green). ( c ) High magnification. cREL ( d ) total (upper panels) and ( e ) nuclear (lower panels) quantification from areas A1 to 3 (upper panels) and P1-3 (lower panels). ( f ) BIRC3 (red) and NeuN (green), and ( g ) BIRC3 (red) and GFAP (green) double staining on day 1 after stroke. ( h ) Quantification of the co-localization studies in ( f and g) . Data are means±S.E.M.; n =6 per group. * P <0.05 in repeated-measures, ANOVA followed by Bonferroni test. DHA treatment=teal bars

Techniques Used: Translocation Assay, In Vivo, Western Blot, Double Staining

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$Red light inhibits type I collagen degradation via AKT/NRF2/HO-1 signaling pathway activation A, B: qPCR analysis of NRF2 (A) and HO-1 (B) mRNA expression in mouse skin tissue following red light treatment. n =4. C: Representative western blot assays of p-AKT, HO-1, NRF2, and type I collagen expression in aged mice treated with red light, API-2, or both. D: Western blot analysis of nuclear-cytoplasmic separation in skin tissue. Cytosolic and nuclear extracts were immunoblotted for NRF2, while GAPDH and histone H3 proteins were probed to confirm thorough separation of the cytosolic and nuclear fractions. E: Representative western blot analysis of type I collagen expression in skin tissue after red light treatment with or without HO-1i. F: Representative immunofluorescence images of type I collagen in skin sections from aged mice after 28 days of red light treatment with or without HO-1i. Scale bar: 50 μm. G: Heatmaps showing relative expression levels of DEGs involved in various MMPs. n =3. H: qPCR analysis of MMP3, MMP9, MMP12, and MMP13 mRNA expression in mouse skin tissue following red light treatment, with and without HO-1i. *** : P <0.001; **** : P <0.0001 compared to control group, and #### : P <0.0001 compared to indicated groups, one-way ANOVA for multiple groups. Data are mean±SEM.$

Journal: Zoological Research

Article Title: Red light promotes dermis-epidermis remodeling via TGFβ and AKT-mediated collagen dynamics in naturally aging mice

doi: 10.24272/j.issn.2095-8137.2024.405

Figure Lengend Snippet: Red light inhibits type I collagen degradation via AKT/NRF2/HO-1 signaling pathway activation A, B: qPCR analysis of NRF2 (A) and HO-1 (B) mRNA expression in mouse skin tissue following red light treatment. n =4. C: Representative western blot assays of p-AKT, HO-1, NRF2, and type I collagen expression in aged mice treated with red light, API-2, or both. D: Western blot analysis of nuclear-cytoplasmic separation in skin tissue. Cytosolic and nuclear extracts were immunoblotted for NRF2, while GAPDH and histone H3 proteins were probed to confirm thorough separation of the cytosolic and nuclear fractions. E: Representative western blot analysis of type I collagen expression in skin tissue after red light treatment with or without HO-1i. F: Representative immunofluorescence images of type I collagen in skin sections from aged mice after 28 days of red light treatment with or without HO-1i. Scale bar: 50 μm. G: Heatmaps showing relative expression levels of DEGs involved in various MMPs. n =3. H: qPCR analysis of MMP3, MMP9, MMP12, and MMP13 mRNA expression in mouse skin tissue following red light treatment, with and without HO-1i. *** : P <0.001; **** : P <0.0001 compared to control group, and #### : P <0.0001 compared to indicated groups, one-way ANOVA for multiple groups. Data are mean±SEM.

Article Snippet: To inhibit AKT, mice received intraperitoneal (i.p.) injections of API-2 (HY-15457, MCE, USA) at a dose of 2 mg/kg every 48 h. To inhibit TGFβ, mice received i.p. injections of SB431542 (HY-10431, MCE, USA), a TGFβR1 inhibitor, at a dose of 10 mg/kg every 48 h. To inhibit cAMP, mice received i.p. injections of SQ22536 (HY-100396, MCE, USA), an adenylate cyclase (AC) inhibitor, at a dose of 10 mg/kg every 48 h. To inhibit HO-1, mice received i.p. injections of HO-1i (HY-111798A, MCE, USA) at a dose of 1.357 mg/kg every 48 h. To inhibit intracellular free Ca 2+ , mice received i.p. injections of diltiazem (HY-B0632, MCE, USA) at a dose of 20 mg/kg every 48 h. To inhibit reactive oxygen species (ROS), mice received daily topical application of 100 mg/mL ascorbic acid (HY-B0166, MCE, USA), applied to the skin 30 min after red light exposure.

Techniques: Activation Assay, Expressing, Western Blot, Immunofluorescence, Control

Cur decreases A/R injury in H9c2 cells via Sirt1. Expression of (A) apoptosis-associated proteins in A/R-injured H9c2 cells following Cur pretreatment, Sirt1 silencing and targeted inhibition of AKT activity. (B) Relative protein expression of Bcl2. (C) represents the relative protein expression of Bax. Expression of Sirt1 (D) in A/R-injured H9c2 cells following Cur pretreatment, Sirt1 silencing and targeted inhibition of AKT activity. (E) Relative protein expression of Sirt1. Apoptosis rate of H9c2 cells was measured by flow cytometry (F and G) illustrates the proportion of apoptotic cells as determined by flow cytometry. (H) caspase 3, (I) LDH activity and (J) viability of A/R injured H9c2 cells after Cur pretreatment, silencing of Sirt1 expression and targeted inhibition of AKT activity. * P<0.05, ** P<0.01, *** P<0.001. Cur, curcumin; A/R, anoxia/reoxygenation; Sirt, silent information regulator 1; LDH, Lactate dehydrogenase; si, small interfering; NC, non-targeting control; API-2, triciribine; CON, control.

Journal: International Journal of Molecular Medicine

Article Title: Curcumin attenuates myocardial ischemia-reperfusion-induced autophagy-dependent ferroptosis via Sirt1/AKT/FoxO3a signaling

doi: 10.3892/ijmm.2025.5492

Figure Lengend Snippet: Cur decreases A/R injury in H9c2 cells via Sirt1. Expression of (A) apoptosis-associated proteins in A/R-injured H9c2 cells following Cur pretreatment, Sirt1 silencing and targeted inhibition of AKT activity. (B) Relative protein expression of Bcl2. (C) represents the relative protein expression of Bax. Expression of Sirt1 (D) in A/R-injured H9c2 cells following Cur pretreatment, Sirt1 silencing and targeted inhibition of AKT activity. (E) Relative protein expression of Sirt1. Apoptosis rate of H9c2 cells was measured by flow cytometry (F and G) illustrates the proportion of apoptotic cells as determined by flow cytometry. (H) caspase 3, (I) LDH activity and (J) viability of A/R injured H9c2 cells after Cur pretreatment, silencing of Sirt1 expression and targeted inhibition of AKT activity. * P<0.05, ** P<0.01, *** P<0.001. Cur, curcumin; A/R, anoxia/reoxygenation; Sirt, silent information regulator 1; LDH, Lactate dehydrogenase; si, small interfering; NC, non-targeting control; API-2, triciribine; CON, control.

Article Snippet: Cur (purity ≥98%, batch no. DC0279-0005) was purchased from Dester Technology Co., Ltd. and Akt inhibitor triciribine (API-2; cat. no. GC15392) was purchased from GLPBIO Technology LLC.

Techniques: Expressing, Inhibition, Activity Assay, Flow Cytometry, Control

Cur reduces autophagy-dependent ferroptosis in H9c2 cells associated with A/R injury via Sirt1. Expression of autophagy-(A) and ferroptosis-related proteins (B) in A/R-injured H9c2 cells following Cur pretreatment, Sirt1 silencing and targeted inhibition of AKT activity. (C) Relative protein expression of P62 and the ratio of LC3II/I. (D) Relative protein expression of NCOA4 and FTH1. Detection of (E) total iron ions, (F) MDA, (G) GSSG, (H) GSH, (I) GSH/GSSG and (J) SOD in A/R injured H9c2 cells following Cur pretreatment, Sirt1 silencing and targeted inhibition of AKT activity. Fluorescence intensity of (K) lysosomes, (L) ROS and (M) Fe 2+ in A/R-injured H9c2 cells following Cur pretreatment, Sirt1 silencing and targeted inhibition of AKT activity (magnification, ×200; scale bar, 400 μ m). ** P<0.05, *** P<0.01. Cur, curcumin; A/R, anoxia/reoxygenation; Sirt, silent information regulator 1; MDA, malondialdehyde; GSSG, glutathione disulfide; GSH, glutathione; SOD, superoxide dismutase; ROS, reactive oxygen species; NCOA4, nuclear receptor coactivator 4; FTH1, ferritin heavy chain 1; CON, control; si, small interfering; prot, protein; API, triciribine; LC3II, microtubule-associated protein 1 light chain 3 β; NC, non-targeting control.

Journal: International Journal of Molecular Medicine

Article Title: Curcumin attenuates myocardial ischemia-reperfusion-induced autophagy-dependent ferroptosis via Sirt1/AKT/FoxO3a signaling

doi: 10.3892/ijmm.2025.5492

Figure Lengend Snippet: Cur reduces autophagy-dependent ferroptosis in H9c2 cells associated with A/R injury via Sirt1. Expression of autophagy-(A) and ferroptosis-related proteins (B) in A/R-injured H9c2 cells following Cur pretreatment, Sirt1 silencing and targeted inhibition of AKT activity. (C) Relative protein expression of P62 and the ratio of LC3II/I. (D) Relative protein expression of NCOA4 and FTH1. Detection of (E) total iron ions, (F) MDA, (G) GSSG, (H) GSH, (I) GSH/GSSG and (J) SOD in A/R injured H9c2 cells following Cur pretreatment, Sirt1 silencing and targeted inhibition of AKT activity. Fluorescence intensity of (K) lysosomes, (L) ROS and (M) Fe 2+ in A/R-injured H9c2 cells following Cur pretreatment, Sirt1 silencing and targeted inhibition of AKT activity (magnification, ×200; scale bar, 400 μ m). ** P<0.05, *** P<0.01. Cur, curcumin; A/R, anoxia/reoxygenation; Sirt, silent information regulator 1; MDA, malondialdehyde; GSSG, glutathione disulfide; GSH, glutathione; SOD, superoxide dismutase; ROS, reactive oxygen species; NCOA4, nuclear receptor coactivator 4; FTH1, ferritin heavy chain 1; CON, control; si, small interfering; prot, protein; API, triciribine; LC3II, microtubule-associated protein 1 light chain 3 β; NC, non-targeting control.

Techniques: Expressing, Inhibition, Activity Assay, Fluorescence, Control

Cur mediates nuclear localization of FoxO3a via Sirt1/AKT. (A) Western blot analysis of (B) phosphorylation of AKT and FoxO3a in A/R-injured H9c2 cells after Cur pretreatment, Sirt1 silencing and targeted inhibition of AKT activity. (C) Western blot analysis of (D) distribution of FoxO3a in the cytoplasm and nucleus of A/R-injured H9c2 cells following Cur pretreatment, Sirt1 silencing and targeted inhibition of AKT activity. *** P<0.01. Cur, curcumin; PCNA, proliferating cell nuclear antigen; Sirt, silent information regulator 1; A/R, anoxia/reoxygenation; p-, phosphorylated; si, small interfering; NC, non-targeting control; API, Triciribine; CON, control.

Journal: International Journal of Molecular Medicine

Article Title: Curcumin attenuates myocardial ischemia-reperfusion-induced autophagy-dependent ferroptosis via Sirt1/AKT/FoxO3a signaling

doi: 10.3892/ijmm.2025.5492

Figure Lengend Snippet: Cur mediates nuclear localization of FoxO3a via Sirt1/AKT. (A) Western blot analysis of (B) phosphorylation of AKT and FoxO3a in A/R-injured H9c2 cells after Cur pretreatment, Sirt1 silencing and targeted inhibition of AKT activity. (C) Western blot analysis of (D) distribution of FoxO3a in the cytoplasm and nucleus of A/R-injured H9c2 cells following Cur pretreatment, Sirt1 silencing and targeted inhibition of AKT activity. *** P<0.01. Cur, curcumin; PCNA, proliferating cell nuclear antigen; Sirt, silent information regulator 1; A/R, anoxia/reoxygenation; p-, phosphorylated; si, small interfering; NC, non-targeting control; API, Triciribine; CON, control.

Techniques: Western Blot, Inhibition, Activity Assay, Control