Proteintech recombinant human ifnβ

A. A schematic illustration of experiments using siRNAs and conditioned media (CM) performed in this figure. B, C. Knockdown of Irf3 or Sting abolished the reduction of the monomeric TDP-43 by TBK1-CM. Efficient reduction of Irf3 and Sting mRNA expression, without affecting hTBK1 , in CM-donor cells was confirmed by qPCR (B). Cells treated with the indicated CM conditions were analyzed by immunoblotting (C). D. TBK1 overexpression in Neuro2a cells markedly induced <t>IFNβ</t> ( Ifnb1 ). Expression levels of the indicated genes were analyzed by qPCR. E. qPCR revealed that knockdown of either Sting or Irf3 markedly suppressed Ifnb1 induction by TBK1 in Neuro2a cells. F, G. Knockdown of Ifnb1 abolished the reduction of the monomeric TDP-43 by TBK1-CM. Significant reduction of Ifnb1 expression in CM-donor cells was confirmed by qPCR (F). Cells treated with the indicated CM conditions were analyzed by immunoblotting (G). (H) Pan-JAK inhibition abolished the reduction of the monomeric TDP-43 by TBK1-CM. Neuro2a cells transiently transfected with TDP-43 6M -3xFLAG were treated with either Mock-or TBK1-CM in the presence of either DMSO or 5 μM Tofacitinib. Data are expressed as means ± SEM. ns, not significant. *p < 0.05, **p < 0.01, and ****p < 0.0001.

Recombinant Human Ifnβ, 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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Journal: bioRxiv

Article Title: TBK1 eliminates aggregation-prone monomeric TDP-43 through the IFNβ-immunoproteasome pathway

doi: 10.1101/2025.04.29.650889

Figure Lengend Snippet: A. A schematic illustration of experiments using siRNAs and conditioned media (CM) performed in this figure. B, C. Knockdown of Irf3 or Sting abolished the reduction of the monomeric TDP-43 by TBK1-CM. Efficient reduction of Irf3 and Sting mRNA expression, without affecting hTBK1 , in CM-donor cells was confirmed by qPCR (B). Cells treated with the indicated CM conditions were analyzed by immunoblotting (C). D. TBK1 overexpression in Neuro2a cells markedly induced IFNβ ( Ifnb1 ). Expression levels of the indicated genes were analyzed by qPCR. E. qPCR revealed that knockdown of either Sting or Irf3 markedly suppressed Ifnb1 induction by TBK1 in Neuro2a cells. F, G. Knockdown of Ifnb1 abolished the reduction of the monomeric TDP-43 by TBK1-CM. Significant reduction of Ifnb1 expression in CM-donor cells was confirmed by qPCR (F). Cells treated with the indicated CM conditions were analyzed by immunoblotting (G). (H) Pan-JAK inhibition abolished the reduction of the monomeric TDP-43 by TBK1-CM. Neuro2a cells transiently transfected with TDP-43 6M -3xFLAG were treated with either Mock-or TBK1-CM in the presence of either DMSO or 5 μM Tofacitinib. Data are expressed as means ± SEM. ns, not significant. *p < 0.05, **p < 0.01, and ****p < 0.0001.

Article Snippet: Reagents were obtained from the following suppliers: Bafilomycin A1 (#B1793, Sigma-Aldrich), Tofacitinib (#S2789, Selleck Chemicals, Houston, TX, USA), recombinant mouse IFNβ (#581302, BioLegend, San Diego, CA, USA), recombinant human IFNβ(#HZ-1298, Proteintech), MG132 (#3175-v, Peptide Institute, Osaka, Japan), Lactacystin (#4368-v, Peptide Institute), Ac-ANW-AMC(#26640, Cayman Chemical, Ann Arbor, MI, USA), ONX-0914 (#16271, Cayman Chemical), BX795 (#SML0694, Sigma-Aldrich), and Doxycycline (#D9891, Sigma-Aldrich).

Techniques: Knockdown, Expressing, Western Blot, Over Expression, Inhibition, Transfection

$A, B. Recombinant IFNβ treatment reduced monomeric TDP-43 mutants and suppressed pTDP accumulation. Neuro2a cells transiently transfected with expression vectors of the indicated TDP-43 mutants were treated with either PBS or 10 ng/ml mouse IFNβ for 42h, fractionated into 1% TritonX-100-soluble and -insoluble fractions, and analyzed by immunoblotting (A). Reduction of pTDP-positive cells by recombinant IFNβ was confirmed by immunocytochemistry (B). Only images of the TDP-43 6M case are shown. The number of pTDP-positive cells in the counted area is presented in the graph. Scale bar, 50 μm. C. Recombinant IFNβ selectively reduced the monomeric TDP-43 mutant in stable lines. Neuro2a cells stably expressing Dox-inducible TDP-43 WT or TDP-43 6M -3xFLAG were treated with 1.5 μg/ml Dox and either PBS or 10 ng/ml mouse IFNβ for 48h and analyzed by immunoblotting. D, E. Recombinant IFNβ treatment reduced TDP-43 in SH-SY5Y but not in HEK293. SH-SY5Y cells (D) and HEK293 cells (E) were transiently transfected with the indicated expression vectors, treated with either PBS or 10ng/mL human IFNβ for 48h, and analyzed by immunoblotting. Data are expressed as means ± SEM. ns, not significant. *p < 0.05, **p < 0.01***, p < 0.001, and ****p < 0.0001.$

Journal: bioRxiv

Article Title: TBK1 eliminates aggregation-prone monomeric TDP-43 through the IFNβ-immunoproteasome pathway

doi: 10.1101/2025.04.29.650889

Figure Lengend Snippet: A, B. Recombinant IFNβ treatment reduced monomeric TDP-43 mutants and suppressed pTDP accumulation. Neuro2a cells transiently transfected with expression vectors of the indicated TDP-43 mutants were treated with either PBS or 10 ng/ml mouse IFNβ for 42h, fractionated into 1% TritonX-100-soluble and -insoluble fractions, and analyzed by immunoblotting (A). Reduction of pTDP-positive cells by recombinant IFNβ was confirmed by immunocytochemistry (B). Only images of the TDP-43 6M case are shown. The number of pTDP-positive cells in the counted area is presented in the graph. Scale bar, 50 μm. C. Recombinant IFNβ selectively reduced the monomeric TDP-43 mutant in stable lines. Neuro2a cells stably expressing Dox-inducible TDP-43 WT or TDP-43 6M -3xFLAG were treated with 1.5 μg/ml Dox and either PBS or 10 ng/ml mouse IFNβ for 48h and analyzed by immunoblotting. D, E. Recombinant IFNβ treatment reduced TDP-43 in SH-SY5Y but not in HEK293. SH-SY5Y cells (D) and HEK293 cells (E) were transiently transfected with the indicated expression vectors, treated with either PBS or 10ng/mL human IFNβ for 48h, and analyzed by immunoblotting. Data are expressed as means ± SEM. ns, not significant. *p < 0.05, **p < 0.01***, p < 0.001, and ****p < 0.0001.

Techniques: Recombinant, Transfection, Expressing, Western Blot, Immunocytochemistry, Mutagenesis, Stable Transfection

A, B. Proteasome inhibitors abolished the reduction of TDP-43 6M by IFNβ treatment. NSC34 cells stably expressing Dox-inducible TDP-43 6M -3xFLAG were treated with 1.5 μg/ml Dox and either PBS or 10 ng/ml mouse IFNβ for 24h under either DMSO or 10 μM MG132 (A), or 2.5 μM lactacystin (B) treatment. C. A schematic illustration of immunoproteasome. D - F. IFNβ induced expression of immunoproteasome subunits in neuronal cells. In D, the indicated cell lines were treated with either PBS or 10 ng/ml human/mouse IFNβ for 30h and analyzed by immunoblotting to assess protein levels of immunoproteasome subunits, PSMB8 and PSMB9 (D). ISG15 was assessed to confirm a general response to IFNβ. N2a, Neuro2a. In E and F, Neuro2a cells were treated with either PBS or 10 ng/ml mouse IFNβ, or either Mock- or TBK1-CM for 24h and expression levels of proteasome catalytic β subunits (E) and regulatory subunits (F) were quantified by qPCR. G, H. IFNβ induced functional immunoproteasome. Neuro2a cells treated with either PBS or 10 ng/ml mouse IFNβ, or either Mock- or TBK1-CM for 24h were analyzed by immunoproteasome activity assay. Representative kinetic assay results (G) and relative fluorescent unit (RFU) at end points of the assay (H) were shown. ONX-0914-treated samples were prepared as negative controls. I. Immunoproteasome-specific inhibition by ONX-0914 abolished the reduction of TDP-43 6M by IFNβ. NSC34 cells stably expressing Dox-inducible TDP43 6M -3xFLAG were treated with Dox and either PBS or 10 ng/m mouse IFNβ for 24h under DMSO or 0.5 µM ONX-0914 treatment. Data are expressed as means ± SEM. ns, not significant. *p < 0.05, **p < 0.01, ***p < 0.001, and ****p < 0.0001.

Journal: bioRxiv

Article Title: TBK1 eliminates aggregation-prone monomeric TDP-43 through the IFNβ-immunoproteasome pathway

doi: 10.1101/2025.04.29.650889

Figure Lengend Snippet: A, B. Proteasome inhibitors abolished the reduction of TDP-43 6M by IFNβ treatment. NSC34 cells stably expressing Dox-inducible TDP-43 6M -3xFLAG were treated with 1.5 μg/ml Dox and either PBS or 10 ng/ml mouse IFNβ for 24h under either DMSO or 10 μM MG132 (A), or 2.5 μM lactacystin (B) treatment. C. A schematic illustration of immunoproteasome. D - F. IFNβ induced expression of immunoproteasome subunits in neuronal cells. In D, the indicated cell lines were treated with either PBS or 10 ng/ml human/mouse IFNβ for 30h and analyzed by immunoblotting to assess protein levels of immunoproteasome subunits, PSMB8 and PSMB9 (D). ISG15 was assessed to confirm a general response to IFNβ. N2a, Neuro2a. In E and F, Neuro2a cells were treated with either PBS or 10 ng/ml mouse IFNβ, or either Mock- or TBK1-CM for 24h and expression levels of proteasome catalytic β subunits (E) and regulatory subunits (F) were quantified by qPCR. G, H. IFNβ induced functional immunoproteasome. Neuro2a cells treated with either PBS or 10 ng/ml mouse IFNβ, or either Mock- or TBK1-CM for 24h were analyzed by immunoproteasome activity assay. Representative kinetic assay results (G) and relative fluorescent unit (RFU) at end points of the assay (H) were shown. ONX-0914-treated samples were prepared as negative controls. I. Immunoproteasome-specific inhibition by ONX-0914 abolished the reduction of TDP-43 6M by IFNβ. NSC34 cells stably expressing Dox-inducible TDP43 6M -3xFLAG were treated with Dox and either PBS or 10 ng/m mouse IFNβ for 24h under DMSO or 0.5 µM ONX-0914 treatment. Data are expressed as means ± SEM. ns, not significant. *p < 0.05, **p < 0.01, ***p < 0.001, and ****p < 0.0001.

Techniques: Stable Transfection, Expressing, Western Blot, Functional Assay, Activity Assay, Kinetic Assay, Inhibition

A, B. Increased IFN response with aging in lumbar spinal cords and cerebral cortices of wild-type (WT) mice. Total RNAs were extracted from lumbar spinal cords (A) or cerebral cortices (B) of WT mice at the indicated ages. Expression levels of the downstream genes of IFN signaling were analyzed by qPCR. M, month-old. C, D . Increased immunoproteasome subunits with aging in lumbar spinal cords and cerebral cortices of mice. Expression levels of immunoproteasome subunits, Psmb8 and Psmb9 , were analyzed as with A and B. G, H. Increased expression of PSMB8 in ChAT-positive spinal motor neurons and CTIP2-positive layer V cortical neurons in 12-month-old WT mice. NeuN was co-stained as a pan-neuron marker. Scale bar, 100 μm. M, month-old. Data are expressed as means ± SEM. ns, not significant. *p < 0.05, **p < 0.01, and ***p < 0.001.

Journal: bioRxiv

Article Title: TBK1 eliminates aggregation-prone monomeric TDP-43 through the IFNβ-immunoproteasome pathway

doi: 10.1101/2025.04.29.650889

Figure Lengend Snippet: A, B. Increased IFN response with aging in lumbar spinal cords and cerebral cortices of wild-type (WT) mice. Total RNAs were extracted from lumbar spinal cords (A) or cerebral cortices (B) of WT mice at the indicated ages. Expression levels of the downstream genes of IFN signaling were analyzed by qPCR. M, month-old. C, D . Increased immunoproteasome subunits with aging in lumbar spinal cords and cerebral cortices of mice. Expression levels of immunoproteasome subunits, Psmb8 and Psmb9 , were analyzed as with A and B. G, H. Increased expression of PSMB8 in ChAT-positive spinal motor neurons and CTIP2-positive layer V cortical neurons in 12-month-old WT mice. NeuN was co-stained as a pan-neuron marker. Scale bar, 100 μm. M, month-old. Data are expressed as means ± SEM. ns, not significant. *p < 0.05, **p < 0.01, and ***p < 0.001.

Techniques: Expressing, Staining, Marker

$A. Canonical proteasome catalytic β subunits, Psmb6 and Psmb7 , were downregulated in lumbar spinal cords of SOD1 G93A mice at onset stage. Total RNAs were extracted from lumbar spinal cords of 2-month-old (pre-onset stage) or 3.5-month-old (onset stage) SOD1 G93A mice and age-matched wild-type (WT) mice. Relative mRNA expression levels of the indicated genes were analyzed by qPCR. B. Immunoproteasome β subunits, Psmb8 and Psmb9 , were upregulated in lumbar spinal cords of SOD1 G93A mice at onset stage. Relative mRNA expression levels of the indicated genes were analyzed as with A. C-E. Heterozygous knockout of Tbk1 in SOD1 G93A mice impaired the induction of IFN response and immunoproteasome in lumbar spinal cords at onset stage. Total RNAs were extracted from lumbar spinal cords of 3.5-month-old mice with the indicated genotypes and relative mRNA expression levels of the indicated genes were analyzed by qPCR. F. Heterozygous knockout of Tbk1 in SOD1 G93A mice increased 1% TritonX-100-insoluble poly-ubiquitinated proteins in lumbar spinal cords. Total proteins were extracted from lumbar spinal cords of 3.5-month-old mice with the indicated genotypes, fractionated into 1% TritonX-100-soluble and -insoluble fractions, and analyzed by immunoblotting. Data are expressed as means ± SEM. ns, not significant. *p < 0.05, **p < 0.01, ***p < 0.001, and ****p < 0.0001.$

Journal: bioRxiv

Article Title: TBK1 eliminates aggregation-prone monomeric TDP-43 through the IFNβ-immunoproteasome pathway

doi: 10.1101/2025.04.29.650889

Figure Lengend Snippet: A. Canonical proteasome catalytic β subunits, Psmb6 and Psmb7 , were downregulated in lumbar spinal cords of SOD1 G93A mice at onset stage. Total RNAs were extracted from lumbar spinal cords of 2-month-old (pre-onset stage) or 3.5-month-old (onset stage) SOD1 G93A mice and age-matched wild-type (WT) mice. Relative mRNA expression levels of the indicated genes were analyzed by qPCR. B. Immunoproteasome β subunits, Psmb8 and Psmb9 , were upregulated in lumbar spinal cords of SOD1 G93A mice at onset stage. Relative mRNA expression levels of the indicated genes were analyzed as with A. C-E. Heterozygous knockout of Tbk1 in SOD1 G93A mice impaired the induction of IFN response and immunoproteasome in lumbar spinal cords at onset stage. Total RNAs were extracted from lumbar spinal cords of 3.5-month-old mice with the indicated genotypes and relative mRNA expression levels of the indicated genes were analyzed by qPCR. F. Heterozygous knockout of Tbk1 in SOD1 G93A mice increased 1% TritonX-100-insoluble poly-ubiquitinated proteins in lumbar spinal cords. Total proteins were extracted from lumbar spinal cords of 3.5-month-old mice with the indicated genotypes, fractionated into 1% TritonX-100-soluble and -insoluble fractions, and analyzed by immunoblotting. Data are expressed as means ± SEM. ns, not significant. *p < 0.05, **p < 0.01, ***p < 0.001, and ****p < 0.0001.

Techniques: Expressing, Knock-Out, Western Blot

TBK1 is activated by various cellular stresses such as proteostatic stress ( Watanabe et al , 2023 ) and mitochondrial DNA (mtDNA) release ( Yu et al , 2020 ). Activated phospho-TBK1 phosphorylates STING and IRF3, leading to the induction of IFNβ. IFNβ subsequently upregulates the immunoproteasome in neurons, thereby promoting the degradation of aggregation-prone monomeric TDP-43. In ALS/FTD patients, phospho-TBK1 ( Shao et al , 2022 ; Watanabe et al , 2023 ) and IFNAR1 are dysregulated (this paper).

Journal: bioRxiv

Article Title: TBK1 eliminates aggregation-prone monomeric TDP-43 through the IFNβ-immunoproteasome pathway

doi: 10.1101/2025.04.29.650889

Figure Lengend Snippet: TBK1 is activated by various cellular stresses such as proteostatic stress ( Watanabe et al , 2023 ) and mitochondrial DNA (mtDNA) release ( Yu et al , 2020 ). Activated phospho-TBK1 phosphorylates STING and IRF3, leading to the induction of IFNβ. IFNβ subsequently upregulates the immunoproteasome in neurons, thereby promoting the degradation of aggregation-prone monomeric TDP-43. In ALS/FTD patients, phospho-TBK1 ( Shao et al , 2022 ; Watanabe et al , 2023 ) and IFNAR1 are dysregulated (this paper).

Techniques:

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