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n fmrp ab  (Novus Biologicals)
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N Fmrp Ab, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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anti‐fmrp (nbp02‐01770)  (Novus Biologicals)
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Novus Biologicals anti‐fmrp (nbp02‐01770)
STING analysis of <t>published</t> <t>IRE1</t> interactome proteins in relation to <t>FMRP</t> (Acosta‐Alvear et al , ). HEK293T cells were co‐transfected with IRE1 and FMRP plasmids and stimulated with TG (600 nM) or TM (1 mg/ml) for 2 h. Protein lysates were immunoprecipitated (IP) with anti‐IRE1 or IgG (control) antibodies and analyzed by Western blotting using specific antibodies for FMRP and IRE1 ( n = 3 biological replicates). RAW 264.7 mouse macrophages were treated with either oxLDL (50 µg/ml) or TG (300 nM) for 6 h. Protein lysates were treated with λ Phosphatase (PPase) for 30 min and analyzed by Western blotting using specific antibodies for pFMRP, FMRP, pIRE1, IRE1, and β‐Actin. pFMRP/FMRP fold induction is depicted above the blots ( n = 6 biological replicates). Apoe −/− mice were fed with chow diet (CD) or western diet (WD) for 16 weeks followed by peritoneal macrophage (PM) isolation. Protein lysates were analyzed by Western blotting using specific antibodies for pFMRP, FMRP, pIRE1, IRE1, and β‐Actin. pFMRP/FMRP‐fold induction is depicted above the blots ( n = 5 mice per group). Control‐ or IRE1‐siRNA transfected HEK293T cells were stimulated by either PA (500 µM) or TG (600 nM) for 4 h. Protein lysates were analyzed by Western blotting using specific antibodies for pFMRP, FMRP, pIRE1, IRE1, and β‐Actin. pFMRP/FMRP fold induction is depicted above the blots ( n = 4 biological replicates). Protein lysates of thioglycolate‐elicited PM from IRE1α +/+ and IRE1α −/− mice (after 16 weeks on WD) were analyzed by Western blotting using specific antibodies for pFMRP, FMRP, pIRE1, IRE1, and β‐Actin. pFMRP/FMRP fold induction is depicted above the blots ( n = 4 mice per group). MEF cells were transfected with either empty vector, EGFP‐FMRP or 3xFLAG‐IRE1 plasmids then pre‐treated either with vehicle (dimethyl sulfoxide, DMSO) or AMG‐18 (25 µM; 1 h) followed by TG (600 nM) stimulation for 4 h. Protein lysates were analyzed by Western blotting using specific antibodies for pFMRP, FMRP, pIRE1, IRE1, and β‐Actin. pFMRP/FMRP fold induction is depicted above the blots ( n = 4 biological replicates). C57BL/6 were injected either with DMSO or AMG‐18 (30 mg/kg; 8 h), followed by TM injection (1 mg/kg; 8 h). Protein lysates of thioglycolate‐elicited PM were analyzed by Western blotting using antibodies for pFMRP, FMRP, pIRE1, IRE1, and β‐Actin. pFMRP/FMRP fold induction is depicted above the blots ( n = 4 mice per group). HEK293T cells were transfected with either empty vector (EV), IRE1‐WT, or IRE1–KD plasmids and stimulated by TG (600 nM; 1 h). Protein lysates from each transfection were separately immunoprecipitated (IP) with anti‐IRE1 antibody and subjected to a kinase reaction with purified hFMRP protein and ATP‐γ‐S (100 µM) in kinase buffer. The IP protein were analyzed by Western blotting using specific antibodies for thiophosphate esters (ThioP), IRE1, and FMRP ( n = 3 biological replicates). Purified FMRP and IRE1 kinase (activated) proteins were subjected to kinase assay and analyzed by Western blotting using specific antibodies for ThioP, IRE1, and FMRP ( n = 3 biological replicates) and with LC‐MS/MS. Identified IRE1 kinase‐mediated FMRP phosphorylation sites (bottom). Fmr1 −/− mouse embryonic fibroblasts (MEF) were transfected either with EV, WT‐FMRP, SA‐FMRP, or STSA‐FMRP plasmids followed by PA treatment (500 µM; 6 h). Protein lysates were analyzed by Western blotting using specific antibodies for FMRP, pFMRP, pIRE1, and β‐Actin ( n = 3 biological replicates). Data information: A representative blot is shown. In D, E, G, and H data are cumulative results of two independent experiments. Data are mean ± SEM. Unpaired t‐ test with Welch’s correction or paired t‐ test. Source data are available online for this figure.
Anti‐Fmrp (Nbp02‐01770), supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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antisense oligonucleotides lyophilised human plcc-1 01770–03.0200  (Biognostic GmbH)
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Biognostic GmbH antisense oligonucleotides lyophilised human plcc-1 01770–03.0200
STING analysis of <t>published</t> <t>IRE1</t> interactome proteins in relation to <t>FMRP</t> (Acosta‐Alvear et al , ). HEK293T cells were co‐transfected with IRE1 and FMRP plasmids and stimulated with TG (600 nM) or TM (1 mg/ml) for 2 h. Protein lysates were immunoprecipitated (IP) with anti‐IRE1 or IgG (control) antibodies and analyzed by Western blotting using specific antibodies for FMRP and IRE1 ( n = 3 biological replicates). RAW 264.7 mouse macrophages were treated with either oxLDL (50 µg/ml) or TG (300 nM) for 6 h. Protein lysates were treated with λ Phosphatase (PPase) for 30 min and analyzed by Western blotting using specific antibodies for pFMRP, FMRP, pIRE1, IRE1, and β‐Actin. pFMRP/FMRP fold induction is depicted above the blots ( n = 6 biological replicates). Apoe −/− mice were fed with chow diet (CD) or western diet (WD) for 16 weeks followed by peritoneal macrophage (PM) isolation. Protein lysates were analyzed by Western blotting using specific antibodies for pFMRP, FMRP, pIRE1, IRE1, and β‐Actin. pFMRP/FMRP‐fold induction is depicted above the blots ( n = 5 mice per group). Control‐ or IRE1‐siRNA transfected HEK293T cells were stimulated by either PA (500 µM) or TG (600 nM) for 4 h. Protein lysates were analyzed by Western blotting using specific antibodies for pFMRP, FMRP, pIRE1, IRE1, and β‐Actin. pFMRP/FMRP fold induction is depicted above the blots ( n = 4 biological replicates). Protein lysates of thioglycolate‐elicited PM from IRE1α +/+ and IRE1α −/− mice (after 16 weeks on WD) were analyzed by Western blotting using specific antibodies for pFMRP, FMRP, pIRE1, IRE1, and β‐Actin. pFMRP/FMRP fold induction is depicted above the blots ( n = 4 mice per group). MEF cells were transfected with either empty vector, EGFP‐FMRP or 3xFLAG‐IRE1 plasmids then pre‐treated either with vehicle (dimethyl sulfoxide, DMSO) or AMG‐18 (25 µM; 1 h) followed by TG (600 nM) stimulation for 4 h. Protein lysates were analyzed by Western blotting using specific antibodies for pFMRP, FMRP, pIRE1, IRE1, and β‐Actin. pFMRP/FMRP fold induction is depicted above the blots ( n = 4 biological replicates). C57BL/6 were injected either with DMSO or AMG‐18 (30 mg/kg; 8 h), followed by TM injection (1 mg/kg; 8 h). Protein lysates of thioglycolate‐elicited PM were analyzed by Western blotting using antibodies for pFMRP, FMRP, pIRE1, IRE1, and β‐Actin. pFMRP/FMRP fold induction is depicted above the blots ( n = 4 mice per group). HEK293T cells were transfected with either empty vector (EV), IRE1‐WT, or IRE1–KD plasmids and stimulated by TG (600 nM; 1 h). Protein lysates from each transfection were separately immunoprecipitated (IP) with anti‐IRE1 antibody and subjected to a kinase reaction with purified hFMRP protein and ATP‐γ‐S (100 µM) in kinase buffer. The IP protein were analyzed by Western blotting using specific antibodies for thiophosphate esters (ThioP), IRE1, and FMRP ( n = 3 biological replicates). Purified FMRP and IRE1 kinase (activated) proteins were subjected to kinase assay and analyzed by Western blotting using specific antibodies for ThioP, IRE1, and FMRP ( n = 3 biological replicates) and with LC‐MS/MS. Identified IRE1 kinase‐mediated FMRP phosphorylation sites (bottom). Fmr1 −/− mouse embryonic fibroblasts (MEF) were transfected either with EV, WT‐FMRP, SA‐FMRP, or STSA‐FMRP plasmids followed by PA treatment (500 µM; 6 h). Protein lysates were analyzed by Western blotting using specific antibodies for FMRP, pFMRP, pIRE1, and β‐Actin ( n = 3 biological replicates). Data information: A representative blot is shown. In D, E, G, and H data are cumulative results of two independent experiments. Data are mean ± SEM. Unpaired t‐ test with Welch’s correction or paired t‐ test. Source data are available online for this figure.
Antisense Oligonucleotides Lyophilised Human Plcc 1 01770–03.0200, supplied by Biognostic GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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STING analysis of published IRE1 interactome proteins in relation to FMRP (Acosta‐Alvear et al , ). HEK293T cells were co‐transfected with IRE1 and FMRP plasmids and stimulated with TG (600 nM) or TM (1 mg/ml) for 2 h. Protein lysates were immunoprecipitated (IP) with anti‐IRE1 or IgG (control) antibodies and analyzed by Western blotting using specific antibodies for FMRP and IRE1 ( n = 3 biological replicates). RAW 264.7 mouse macrophages were treated with either oxLDL (50 µg/ml) or TG (300 nM) for 6 h. Protein lysates were treated with λ Phosphatase (PPase) for 30 min and analyzed by Western blotting using specific antibodies for pFMRP, FMRP, pIRE1, IRE1, and β‐Actin. pFMRP/FMRP fold induction is depicted above the blots ( n = 6 biological replicates). Apoe −/− mice were fed with chow diet (CD) or western diet (WD) for 16 weeks followed by peritoneal macrophage (PM) isolation. Protein lysates were analyzed by Western blotting using specific antibodies for pFMRP, FMRP, pIRE1, IRE1, and β‐Actin. pFMRP/FMRP‐fold induction is depicted above the blots ( n = 5 mice per group). Control‐ or IRE1‐siRNA transfected HEK293T cells were stimulated by either PA (500 µM) or TG (600 nM) for 4 h. Protein lysates were analyzed by Western blotting using specific antibodies for pFMRP, FMRP, pIRE1, IRE1, and β‐Actin. pFMRP/FMRP fold induction is depicted above the blots ( n = 4 biological replicates). Protein lysates of thioglycolate‐elicited PM from IRE1α +/+ and IRE1α −/− mice (after 16 weeks on WD) were analyzed by Western blotting using specific antibodies for pFMRP, FMRP, pIRE1, IRE1, and β‐Actin. pFMRP/FMRP fold induction is depicted above the blots ( n = 4 mice per group). MEF cells were transfected with either empty vector, EGFP‐FMRP or 3xFLAG‐IRE1 plasmids then pre‐treated either with vehicle (dimethyl sulfoxide, DMSO) or AMG‐18 (25 µM; 1 h) followed by TG (600 nM) stimulation for 4 h. Protein lysates were analyzed by Western blotting using specific antibodies for pFMRP, FMRP, pIRE1, IRE1, and β‐Actin. pFMRP/FMRP fold induction is depicted above the blots ( n = 4 biological replicates). C57BL/6 were injected either with DMSO or AMG‐18 (30 mg/kg; 8 h), followed by TM injection (1 mg/kg; 8 h). Protein lysates of thioglycolate‐elicited PM were analyzed by Western blotting using antibodies for pFMRP, FMRP, pIRE1, IRE1, and β‐Actin. pFMRP/FMRP fold induction is depicted above the blots ( n = 4 mice per group). HEK293T cells were transfected with either empty vector (EV), IRE1‐WT, or IRE1–KD plasmids and stimulated by TG (600 nM; 1 h). Protein lysates from each transfection were separately immunoprecipitated (IP) with anti‐IRE1 antibody and subjected to a kinase reaction with purified hFMRP protein and ATP‐γ‐S (100 µM) in kinase buffer. The IP protein were analyzed by Western blotting using specific antibodies for thiophosphate esters (ThioP), IRE1, and FMRP ( n = 3 biological replicates). Purified FMRP and IRE1 kinase (activated) proteins were subjected to kinase assay and analyzed by Western blotting using specific antibodies for ThioP, IRE1, and FMRP ( n = 3 biological replicates) and with LC‐MS/MS. Identified IRE1 kinase‐mediated FMRP phosphorylation sites (bottom). Fmr1 −/− mouse embryonic fibroblasts (MEF) were transfected either with EV, WT‐FMRP, SA‐FMRP, or STSA‐FMRP plasmids followed by PA treatment (500 µM; 6 h). Protein lysates were analyzed by Western blotting using specific antibodies for FMRP, pFMRP, pIRE1, and β‐Actin ( n = 3 biological replicates). Data information: A representative blot is shown. In D, E, G, and H data are cumulative results of two independent experiments. Data are mean ± SEM. Unpaired t‐ test with Welch’s correction or paired t‐ test. Source data are available online for this figure.

Journal: EMBO Molecular Medicine

Article Title: Intercepting IRE1 kinase‐FMRP signaling prevents atherosclerosis progression

doi: 10.15252/emmm.202115344

Figure Lengend Snippet: STING analysis of published IRE1 interactome proteins in relation to FMRP (Acosta‐Alvear et al , ). HEK293T cells were co‐transfected with IRE1 and FMRP plasmids and stimulated with TG (600 nM) or TM (1 mg/ml) for 2 h. Protein lysates were immunoprecipitated (IP) with anti‐IRE1 or IgG (control) antibodies and analyzed by Western blotting using specific antibodies for FMRP and IRE1 ( n = 3 biological replicates). RAW 264.7 mouse macrophages were treated with either oxLDL (50 µg/ml) or TG (300 nM) for 6 h. Protein lysates were treated with λ Phosphatase (PPase) for 30 min and analyzed by Western blotting using specific antibodies for pFMRP, FMRP, pIRE1, IRE1, and β‐Actin. pFMRP/FMRP fold induction is depicted above the blots ( n = 6 biological replicates). Apoe −/− mice were fed with chow diet (CD) or western diet (WD) for 16 weeks followed by peritoneal macrophage (PM) isolation. Protein lysates were analyzed by Western blotting using specific antibodies for pFMRP, FMRP, pIRE1, IRE1, and β‐Actin. pFMRP/FMRP‐fold induction is depicted above the blots ( n = 5 mice per group). Control‐ or IRE1‐siRNA transfected HEK293T cells were stimulated by either PA (500 µM) or TG (600 nM) for 4 h. Protein lysates were analyzed by Western blotting using specific antibodies for pFMRP, FMRP, pIRE1, IRE1, and β‐Actin. pFMRP/FMRP fold induction is depicted above the blots ( n = 4 biological replicates). Protein lysates of thioglycolate‐elicited PM from IRE1α +/+ and IRE1α −/− mice (after 16 weeks on WD) were analyzed by Western blotting using specific antibodies for pFMRP, FMRP, pIRE1, IRE1, and β‐Actin. pFMRP/FMRP fold induction is depicted above the blots ( n = 4 mice per group). MEF cells were transfected with either empty vector, EGFP‐FMRP or 3xFLAG‐IRE1 plasmids then pre‐treated either with vehicle (dimethyl sulfoxide, DMSO) or AMG‐18 (25 µM; 1 h) followed by TG (600 nM) stimulation for 4 h. Protein lysates were analyzed by Western blotting using specific antibodies for pFMRP, FMRP, pIRE1, IRE1, and β‐Actin. pFMRP/FMRP fold induction is depicted above the blots ( n = 4 biological replicates). C57BL/6 were injected either with DMSO or AMG‐18 (30 mg/kg; 8 h), followed by TM injection (1 mg/kg; 8 h). Protein lysates of thioglycolate‐elicited PM were analyzed by Western blotting using antibodies for pFMRP, FMRP, pIRE1, IRE1, and β‐Actin. pFMRP/FMRP fold induction is depicted above the blots ( n = 4 mice per group). HEK293T cells were transfected with either empty vector (EV), IRE1‐WT, or IRE1–KD plasmids and stimulated by TG (600 nM; 1 h). Protein lysates from each transfection were separately immunoprecipitated (IP) with anti‐IRE1 antibody and subjected to a kinase reaction with purified hFMRP protein and ATP‐γ‐S (100 µM) in kinase buffer. The IP protein were analyzed by Western blotting using specific antibodies for thiophosphate esters (ThioP), IRE1, and FMRP ( n = 3 biological replicates). Purified FMRP and IRE1 kinase (activated) proteins were subjected to kinase assay and analyzed by Western blotting using specific antibodies for ThioP, IRE1, and FMRP ( n = 3 biological replicates) and with LC‐MS/MS. Identified IRE1 kinase‐mediated FMRP phosphorylation sites (bottom). Fmr1 −/− mouse embryonic fibroblasts (MEF) were transfected either with EV, WT‐FMRP, SA‐FMRP, or STSA‐FMRP plasmids followed by PA treatment (500 µM; 6 h). Protein lysates were analyzed by Western blotting using specific antibodies for FMRP, pFMRP, pIRE1, and β‐Actin ( n = 3 biological replicates). Data information: A representative blot is shown. In D, E, G, and H data are cumulative results of two independent experiments. Data are mean ± SEM. Unpaired t‐ test with Welch’s correction or paired t‐ test. Source data are available online for this figure.

Article Snippet: Primary antibodies used for immunoblotting were from the following companies: anti‐pIRE1 (phsopho‐S724; 124945), anti‐FMRP (ab17722), anti‐LRP1 (ab92544), anti‐α‐SMA (ab5694), Anti‐IL‐1 beta antibody (ab9722), Anti‐pro Caspase1 + p10 + p12 antibody [EPR16883] (ab179515), and anti‐Thiophosphate ester antibody (ab133473) were purchased from Abcam; anti‐pFMRP (phosphor‐S499; p1125‐499) from PhosphoSolutions; anti‐IRE1 (3294), anti‐LRP1 (64099) and anti‐FMRP (4317) from Cell‐Signaling; anti‐FMRP (NBP02‐01770), anti‐ABCA1 (NB400‐105), and anti‐ABCG1 (NB400‐132) from Novus Biologicals; anti‐β‐Actin‐horse radish peroxidase (47778) and Secondary IgG‐Goat (sc‐2354) from Santa Cruz Biotechnology; anti‐MOMA‐2 from Bio‐Rad; anti‐PE‐F4/80 (123110), anti‐FMRP (834601), Propidium Iodide Solution, PI (421301), Cell Staining Buffer (420201), and TruStain FcX (anti‐CD16/32, 101319) from Biolegend.

Techniques: Transfection, Immunoprecipitation, Western Blot, Isolation, Plasmid Preparation, Injection, Purification, Kinase Assay, Liquid Chromatography with Mass Spectroscopy

A, B RNA lysates from Fmr1 +/+ and Fmr1 −/− BMDM that were treated with PA (500 µM; 6 h) were fractionated using a 10–50% sucrose gradient and separated to polysome, monosome/NTR fractions. The absorbance (260 nm) of RNA was measured and plotted as a function of time ( n = 3 biological replicates). (A) Representative profile for RNA distribution from genotypes based on UV absorbance readings after sucrose gradient fractionation. (B) The ratio of the Abca1, Abcg1, Mertk, Lrp1, Cd36, Cd47, and Rac1 mRNA in polysome to NTR fraction ( n = 3 biological replicates). C BMDM were isolated from Fmr1 +/+ and Fmr1 −/− , and protein lysates were analyzed by Western blotting using specific antibodies for ABCA1, ABCG1, MerTK, LRP1, FMRP, and β‐Actin antibodies and fold inductions relative to β‐Actin are depicted above the blots ( n = 6 biological replicates). D Fmr1 −/− MEF cells were transfected with EV, WT‐FMRP, or STSA‐FMRP plasmids followed by PA treatment (500 µM; 6 h). Protein lysates were analyzed by Western blotting using specific antibodies for ABCA1, MerTK, LRP1, pFMRP, FMRP, and β‐Actin and fold inductions relative to β‐Actin are depicted above the blots ( n = 5 biological replicates). Data information: A representative blot is shown. In C and D, data are cumulative results of 2 and 3 independent experiments, respectively. In Western blots, the protein expression fold change was calculated relative to β‐Actin and depicted above the blots and a representative blot was shown. Data are mean ± SEM. Unpaired t‐ test with Welch’s correction. Source data are available online for this figure.

Journal: EMBO Molecular Medicine

Article Title: Intercepting IRE1 kinase‐FMRP signaling prevents atherosclerosis progression

doi: 10.15252/emmm.202115344

Figure Lengend Snippet: A, B RNA lysates from Fmr1 +/+ and Fmr1 −/− BMDM that were treated with PA (500 µM; 6 h) were fractionated using a 10–50% sucrose gradient and separated to polysome, monosome/NTR fractions. The absorbance (260 nm) of RNA was measured and plotted as a function of time ( n = 3 biological replicates). (A) Representative profile for RNA distribution from genotypes based on UV absorbance readings after sucrose gradient fractionation. (B) The ratio of the Abca1, Abcg1, Mertk, Lrp1, Cd36, Cd47, and Rac1 mRNA in polysome to NTR fraction ( n = 3 biological replicates). C BMDM were isolated from Fmr1 +/+ and Fmr1 −/− , and protein lysates were analyzed by Western blotting using specific antibodies for ABCA1, ABCG1, MerTK, LRP1, FMRP, and β‐Actin antibodies and fold inductions relative to β‐Actin are depicted above the blots ( n = 6 biological replicates). D Fmr1 −/− MEF cells were transfected with EV, WT‐FMRP, or STSA‐FMRP plasmids followed by PA treatment (500 µM; 6 h). Protein lysates were analyzed by Western blotting using specific antibodies for ABCA1, MerTK, LRP1, pFMRP, FMRP, and β‐Actin and fold inductions relative to β‐Actin are depicted above the blots ( n = 5 biological replicates). Data information: A representative blot is shown. In C and D, data are cumulative results of 2 and 3 independent experiments, respectively. In Western blots, the protein expression fold change was calculated relative to β‐Actin and depicted above the blots and a representative blot was shown. Data are mean ± SEM. Unpaired t‐ test with Welch’s correction. Source data are available online for this figure.

Article Snippet: Primary antibodies used for immunoblotting were from the following companies: anti‐pIRE1 (phsopho‐S724; 124945), anti‐FMRP (ab17722), anti‐LRP1 (ab92544), anti‐α‐SMA (ab5694), Anti‐IL‐1 beta antibody (ab9722), Anti‐pro Caspase1 + p10 + p12 antibody [EPR16883] (ab179515), and anti‐Thiophosphate ester antibody (ab133473) were purchased from Abcam; anti‐pFMRP (phosphor‐S499; p1125‐499) from PhosphoSolutions; anti‐IRE1 (3294), anti‐LRP1 (64099) and anti‐FMRP (4317) from Cell‐Signaling; anti‐FMRP (NBP02‐01770), anti‐ABCA1 (NB400‐105), and anti‐ABCG1 (NB400‐132) from Novus Biologicals; anti‐β‐Actin‐horse radish peroxidase (47778) and Secondary IgG‐Goat (sc‐2354) from Santa Cruz Biotechnology; anti‐MOMA‐2 from Bio‐Rad; anti‐PE‐F4/80 (123110), anti‐FMRP (834601), Propidium Iodide Solution, PI (421301), Cell Staining Buffer (420201), and TruStain FcX (anti‐CD16/32, 101319) from Biolegend.

Techniques: Fractionation, Isolation, Western Blot, Transfection, Expressing

IRE1‐mediated FMRP phosphorylation suppresses translation of mRNA for key cholesterol transporters and efferocytosis receptors in macrophages and promotes atherosclerosis.

Journal: EMBO Molecular Medicine

Article Title: Intercepting IRE1 kinase‐FMRP signaling prevents atherosclerosis progression

doi: 10.15252/emmm.202115344

Figure Lengend Snippet: IRE1‐mediated FMRP phosphorylation suppresses translation of mRNA for key cholesterol transporters and efferocytosis receptors in macrophages and promotes atherosclerosis.

Article Snippet: Primary antibodies used for immunoblotting were from the following companies: anti‐pIRE1 (phsopho‐S724; 124945), anti‐FMRP (ab17722), anti‐LRP1 (ab92544), anti‐α‐SMA (ab5694), Anti‐IL‐1 beta antibody (ab9722), Anti‐pro Caspase1 + p10 + p12 antibody [EPR16883] (ab179515), and anti‐Thiophosphate ester antibody (ab133473) were purchased from Abcam; anti‐pFMRP (phosphor‐S499; p1125‐499) from PhosphoSolutions; anti‐IRE1 (3294), anti‐LRP1 (64099) and anti‐FMRP (4317) from Cell‐Signaling; anti‐FMRP (NBP02‐01770), anti‐ABCA1 (NB400‐105), and anti‐ABCG1 (NB400‐132) from Novus Biologicals; anti‐β‐Actin‐horse radish peroxidase (47778) and Secondary IgG‐Goat (sc‐2354) from Santa Cruz Biotechnology; anti‐MOMA‐2 from Bio‐Rad; anti‐PE‐F4/80 (123110), anti‐FMRP (834601), Propidium Iodide Solution, PI (421301), Cell Staining Buffer (420201), and TruStain FcX (anti‐CD16/32, 101319) from Biolegend.

Techniques: