anti ps tq  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti ps tq
    Anti Ps Tq, supplied by Cell Signaling Technology 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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    anti ps iκbα  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti ps iκbα
    Graphical summary of this study. 70COLGA suppresses pro-inflammatory molecules. NO: nitric oxide, LPS: lipopolysaccharide, TLR4: Toll-like receptor 4, NF-κB: nuclear factor kappa-light-chain-enhancer of activated B cells, <t>IκBα:</t> inhibitory protein kappa B alpha, MAPK: mitogen-activated protein kinase, ERK: extracellular signal-regulated <t>kinase,</t> <t>JNK:</t> jun N-terminal kinase, JAK: janus kinase, STAT: signal transducers and activators of transcription, iNOS: inducible nitric oxide synthase, COX-2: cyclooxygenase 2, 70COLGA: Chamaecyparis obtusa (Siebold & Zucc.) Endl. leaf 70% EtOH extract fermented by Ganoderma applanatum. This summary figure was created using BioRender.com.
    Anti Ps Iκbα, supplied by Cell Signaling Technology 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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    1) Product Images from "Anti-Inflammatory Effects of Chamaecyparis obtusa (Siebold & Zucc.) Endl. Leaf Extract Fermented by Ganoderma applanatum Mycelia"

    Article Title: Anti-Inflammatory Effects of Chamaecyparis obtusa (Siebold & Zucc.) Endl. Leaf Extract Fermented by Ganoderma applanatum Mycelia

    Journal: Pharmaceutics

    doi: 10.3390/pharmaceutics16030365

    Graphical summary of this study. 70COLGA suppresses pro-inflammatory molecules. NO: nitric oxide, LPS: lipopolysaccharide, TLR4: Toll-like receptor 4, NF-κB: nuclear factor kappa-light-chain-enhancer of activated B cells, IκBα: inhibitory protein kappa B alpha, MAPK: mitogen-activated protein kinase, ERK: extracellular signal-regulated kinase, JNK: jun N-terminal kinase, JAK: janus kinase, STAT: signal transducers and activators of transcription, iNOS: inducible nitric oxide synthase, COX-2: cyclooxygenase 2, 70COLGA: Chamaecyparis obtusa (Siebold & Zucc.) Endl. leaf 70% EtOH extract fermented by Ganoderma applanatum. This summary figure was created using BioRender.com.
    Figure Legend Snippet: Graphical summary of this study. 70COLGA suppresses pro-inflammatory molecules. NO: nitric oxide, LPS: lipopolysaccharide, TLR4: Toll-like receptor 4, NF-κB: nuclear factor kappa-light-chain-enhancer of activated B cells, IκBα: inhibitory protein kappa B alpha, MAPK: mitogen-activated protein kinase, ERK: extracellular signal-regulated kinase, JNK: jun N-terminal kinase, JAK: janus kinase, STAT: signal transducers and activators of transcription, iNOS: inducible nitric oxide synthase, COX-2: cyclooxygenase 2, 70COLGA: Chamaecyparis obtusa (Siebold & Zucc.) Endl. leaf 70% EtOH extract fermented by Ganoderma applanatum. This summary figure was created using BioRender.com.

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    anti ps nfκb  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti ps nfκb
    Anti Ps Nfκb, supplied by Cell Signaling Technology 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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    anti ps pt q  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti ps pt q
    Anti Ps Pt Q, supplied by Cell Signaling Technology 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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    anti ps pt p antibody  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti ps pt p antibody
    Anti Ps Pt P Antibody, supplied by Cell Signaling Technology 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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    anti ps 616 drp1  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti ps 616 drp1
    Mitochondrial dynamics via proteins clustered at TM4SF5‐enriched MLCSs. (A) SNU449 cells transfected with mCherry‐TM4SF5 and mito‐GFP were subjected to confocal live imaging. Representative images are shown as snapshots. (B‐C) SNU449 cells stably expressing HA‐EV or HA‐TM4SF5 were glucose starved and then replete before electron microscopy imaging. Multiple images of cells ( n = 13, 12, 12, or 14) were processed for mitochondrial length measurement under each experimental condition (C). *** P < 0.001, ordinary one‐way ANOVA. (D‐E) SNU449 (D) or Huh7 (E) cells transfected with TM4SF5‐v5‐TurboID were glucose depleted for 16 h and then replete (10 mmol/L or 25 mmol/L glucose for various times or 30 min, respectively). Whole‐cell lysates were subjected to streptavidin PD and immunoblot. (F) SNU449 cells with stable HA‐EV or HA‐TM4SF5 expression were transfected with mito‐GFP plasmids and treated with 1 μmol/L TSAHC for 16 h. Confocal images for anti‐HA, <t>anti‐DRP1,</t> or anti‐p‐DRP1 were captured, and DRP1‐mitochondria ( n = 93, 72, or 40) or p‐DRP1‐mitochondria ( n = 83, 73, or 38) colocalization was assessed by Pearson's correlation. * P < 0.05, ** P < 0.01, and *** P < 0.001, ordinary one‐way ANOVA. Data were represented as mean ± SD. (G) Animal study scheme for In vivo mitophagy using mtKeima TG mice. (H) Representative images of red In vivo mitophagy signal in liver tissues from mice ( n = 3/group) intravenously injected with AAV8‐ Tbg ‐HA‐Tm4sf5, but not control virus (left). Ten random areas of liver from a mouse were imaged and the red signal was quantitated for a graph (right). **** P < 0.0001, two‐tailed unpaired t test. (I) Liver tissues from WT or KO mice (age‐matched control, AMC, or DEN‐treated for 45 weeks as an HCC model, n ≥ 5/group) were immuno‐stained as indicated. Representative images were shown. Data represent three isolated experiments. See also Supplementary Figure and Supplementary Figure . AMC, age‐matched control; DEN, diethylnitrosamine; DRP1, dynamin‐related protein 1; EV, empty vector; KO, knockout; MLCS, mitochondria‐lysosome contact site; PD, pulldown; SD, standard deviation; Tbg, thyroxine binding globulin; TM4SF5, transmembrane 4 L six family member 5; WT, wild‐type.
    Anti Ps 616 Drp1, supplied by Cell Signaling Technology 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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    1) Product Images from "Glucose‐mediated mitochondrial reprogramming by cholesterol export at TM4SF5‐enriched mitochondria‐lysosome contact sites"

    Article Title: Glucose‐mediated mitochondrial reprogramming by cholesterol export at TM4SF5‐enriched mitochondria‐lysosome contact sites

    Journal: Cancer Communications

    doi: 10.1002/cac2.12510

    Mitochondrial dynamics via proteins clustered at TM4SF5‐enriched MLCSs. (A) SNU449 cells transfected with mCherry‐TM4SF5 and mito‐GFP were subjected to confocal live imaging. Representative images are shown as snapshots. (B‐C) SNU449 cells stably expressing HA‐EV or HA‐TM4SF5 were glucose starved and then replete before electron microscopy imaging. Multiple images of cells ( n = 13, 12, 12, or 14) were processed for mitochondrial length measurement under each experimental condition (C). *** P < 0.001, ordinary one‐way ANOVA. (D‐E) SNU449 (D) or Huh7 (E) cells transfected with TM4SF5‐v5‐TurboID were glucose depleted for 16 h and then replete (10 mmol/L or 25 mmol/L glucose for various times or 30 min, respectively). Whole‐cell lysates were subjected to streptavidin PD and immunoblot. (F) SNU449 cells with stable HA‐EV or HA‐TM4SF5 expression were transfected with mito‐GFP plasmids and treated with 1 μmol/L TSAHC for 16 h. Confocal images for anti‐HA, anti‐DRP1, or anti‐p‐DRP1 were captured, and DRP1‐mitochondria ( n = 93, 72, or 40) or p‐DRP1‐mitochondria ( n = 83, 73, or 38) colocalization was assessed by Pearson's correlation. * P < 0.05, ** P < 0.01, and *** P < 0.001, ordinary one‐way ANOVA. Data were represented as mean ± SD. (G) Animal study scheme for In vivo mitophagy using mtKeima TG mice. (H) Representative images of red In vivo mitophagy signal in liver tissues from mice ( n = 3/group) intravenously injected with AAV8‐ Tbg ‐HA‐Tm4sf5, but not control virus (left). Ten random areas of liver from a mouse were imaged and the red signal was quantitated for a graph (right). **** P < 0.0001, two‐tailed unpaired t test. (I) Liver tissues from WT or KO mice (age‐matched control, AMC, or DEN‐treated for 45 weeks as an HCC model, n ≥ 5/group) were immuno‐stained as indicated. Representative images were shown. Data represent three isolated experiments. See also Supplementary Figure and Supplementary Figure . AMC, age‐matched control; DEN, diethylnitrosamine; DRP1, dynamin‐related protein 1; EV, empty vector; KO, knockout; MLCS, mitochondria‐lysosome contact site; PD, pulldown; SD, standard deviation; Tbg, thyroxine binding globulin; TM4SF5, transmembrane 4 L six family member 5; WT, wild‐type.
    Figure Legend Snippet: Mitochondrial dynamics via proteins clustered at TM4SF5‐enriched MLCSs. (A) SNU449 cells transfected with mCherry‐TM4SF5 and mito‐GFP were subjected to confocal live imaging. Representative images are shown as snapshots. (B‐C) SNU449 cells stably expressing HA‐EV or HA‐TM4SF5 were glucose starved and then replete before electron microscopy imaging. Multiple images of cells ( n = 13, 12, 12, or 14) were processed for mitochondrial length measurement under each experimental condition (C). *** P < 0.001, ordinary one‐way ANOVA. (D‐E) SNU449 (D) or Huh7 (E) cells transfected with TM4SF5‐v5‐TurboID were glucose depleted for 16 h and then replete (10 mmol/L or 25 mmol/L glucose for various times or 30 min, respectively). Whole‐cell lysates were subjected to streptavidin PD and immunoblot. (F) SNU449 cells with stable HA‐EV or HA‐TM4SF5 expression were transfected with mito‐GFP plasmids and treated with 1 μmol/L TSAHC for 16 h. Confocal images for anti‐HA, anti‐DRP1, or anti‐p‐DRP1 were captured, and DRP1‐mitochondria ( n = 93, 72, or 40) or p‐DRP1‐mitochondria ( n = 83, 73, or 38) colocalization was assessed by Pearson's correlation. * P < 0.05, ** P < 0.01, and *** P < 0.001, ordinary one‐way ANOVA. Data were represented as mean ± SD. (G) Animal study scheme for In vivo mitophagy using mtKeima TG mice. (H) Representative images of red In vivo mitophagy signal in liver tissues from mice ( n = 3/group) intravenously injected with AAV8‐ Tbg ‐HA‐Tm4sf5, but not control virus (left). Ten random areas of liver from a mouse were imaged and the red signal was quantitated for a graph (right). **** P < 0.0001, two‐tailed unpaired t test. (I) Liver tissues from WT or KO mice (age‐matched control, AMC, or DEN‐treated for 45 weeks as an HCC model, n ≥ 5/group) were immuno‐stained as indicated. Representative images were shown. Data represent three isolated experiments. See also Supplementary Figure and Supplementary Figure . AMC, age‐matched control; DEN, diethylnitrosamine; DRP1, dynamin‐related protein 1; EV, empty vector; KO, knockout; MLCS, mitochondria‐lysosome contact site; PD, pulldown; SD, standard deviation; Tbg, thyroxine binding globulin; TM4SF5, transmembrane 4 L six family member 5; WT, wild‐type.

    Techniques Used: Transfection, Imaging, Stable Transfection, Expressing, Electron Microscopy, Western Blot, In Vivo, Injection, Virus, Two Tailed Test, Staining, Isolation, Plasmid Preparation, Knock-Out, Standard Deviation, Binding Assay

    A working model of mitochondrial reprograming by TM4SF5‐enriched MLCSs. Upon repletion of extracellular glucose, TM4SF5 localizes to lysosomes, and the TM4SF5‐enriched lysosomal membrane becomes closely in apposition to mitochondria to create MLCSs, depending on Rab7, CCZ1, and STBD1 expression. TM4SF5 on lysosome becomes tethered to FKBP8 on the outer mitochondria membrane via a direct interaction. TM4SF5 can be associated with or in proximity to TOM20, DRP1, NPC1, STARD3, and lysosome‐free cholesterol. Mitochondria at TM4SF5‐enriched MLCSs can also dynamically recruit (phospho‐) DRP1 for mitochondrial fission. TM4SF5‐bound cholesterol can be exported to mitochondria efficiently via TM4SF5‐bound NPC1 at the TM4SF5‐enriched MLCSs. Thereby, cholesterol enrichment into sterol‐poor mitochondria causes ETC impairment for inefficient mitochondrial respiration but increased glycolytic respiration. Concomitantly, the TCA cycle remains intact to supply a pool of metabolic intermediates as building blocks for cell proliferation. CCZ1, CCZ1 homolog, vacuolar protein trafficking and biogenesis associated; DRP1, dynamin‐related protein 1; NPC1, niemann‐pick disease type C1; STARD3, star‐related lipid transfer domain‐3; STBD1, starch binding domain 1; TCA cycle, tricarboxylic acid cycle; TOM20, translocase of outer mitochondrial membrane 20.
    Figure Legend Snippet: A working model of mitochondrial reprograming by TM4SF5‐enriched MLCSs. Upon repletion of extracellular glucose, TM4SF5 localizes to lysosomes, and the TM4SF5‐enriched lysosomal membrane becomes closely in apposition to mitochondria to create MLCSs, depending on Rab7, CCZ1, and STBD1 expression. TM4SF5 on lysosome becomes tethered to FKBP8 on the outer mitochondria membrane via a direct interaction. TM4SF5 can be associated with or in proximity to TOM20, DRP1, NPC1, STARD3, and lysosome‐free cholesterol. Mitochondria at TM4SF5‐enriched MLCSs can also dynamically recruit (phospho‐) DRP1 for mitochondrial fission. TM4SF5‐bound cholesterol can be exported to mitochondria efficiently via TM4SF5‐bound NPC1 at the TM4SF5‐enriched MLCSs. Thereby, cholesterol enrichment into sterol‐poor mitochondria causes ETC impairment for inefficient mitochondrial respiration but increased glycolytic respiration. Concomitantly, the TCA cycle remains intact to supply a pool of metabolic intermediates as building blocks for cell proliferation. CCZ1, CCZ1 homolog, vacuolar protein trafficking and biogenesis associated; DRP1, dynamin‐related protein 1; NPC1, niemann‐pick disease type C1; STARD3, star‐related lipid transfer domain‐3; STBD1, starch binding domain 1; TCA cycle, tricarboxylic acid cycle; TOM20, translocase of outer mitochondrial membrane 20.

    Techniques Used: Membrane, Expressing, Starch, Binding Assay

    phospho ck2 substrate ps pt  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phospho ck2 substrate ps pt
    Phospho Ck2 Substrate Ps Pt, supplied by Cell Signaling Technology 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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    ps atf2  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc ps atf2
    Ps Atf2, supplied by Cell Signaling Technology 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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    anti ps  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti ps
    Anti Ps, supplied by Cell Signaling Technology 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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    anti h 2 ax ps 139  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti h 2 ax ps 139
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    Cell Signaling Technology Inc anti ps tq
    Anti Ps Tq, supplied by Cell Signaling Technology 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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    Graphical summary of this study. 70COLGA suppresses pro-inflammatory molecules. NO: nitric oxide, LPS: lipopolysaccharide, TLR4: Toll-like receptor 4, NF-κB: nuclear factor kappa-light-chain-enhancer of activated B cells, <t>IκBα:</t> inhibitory protein kappa B alpha, MAPK: mitogen-activated protein kinase, ERK: extracellular signal-regulated <t>kinase,</t> <t>JNK:</t> jun N-terminal kinase, JAK: janus kinase, STAT: signal transducers and activators of transcription, iNOS: inducible nitric oxide synthase, COX-2: cyclooxygenase 2, 70COLGA: Chamaecyparis obtusa (Siebold & Zucc.) Endl. leaf 70% EtOH extract fermented by Ganoderma applanatum. This summary figure was created using BioRender.com.
    Anti Ps Iκbα, supplied by Cell Signaling Technology 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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    Graphical summary of this study. 70COLGA suppresses pro-inflammatory molecules. NO: nitric oxide, LPS: lipopolysaccharide, TLR4: Toll-like receptor 4, NF-κB: nuclear factor kappa-light-chain-enhancer of activated B cells, <t>IκBα:</t> inhibitory protein kappa B alpha, MAPK: mitogen-activated protein kinase, ERK: extracellular signal-regulated <t>kinase,</t> <t>JNK:</t> jun N-terminal kinase, JAK: janus kinase, STAT: signal transducers and activators of transcription, iNOS: inducible nitric oxide synthase, COX-2: cyclooxygenase 2, 70COLGA: Chamaecyparis obtusa (Siebold & Zucc.) Endl. leaf 70% EtOH extract fermented by Ganoderma applanatum. This summary figure was created using BioRender.com.
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    Graphical summary of this study. 70COLGA suppresses pro-inflammatory molecules. NO: nitric oxide, LPS: lipopolysaccharide, TLR4: Toll-like receptor 4, NF-κB: nuclear factor kappa-light-chain-enhancer of activated B cells, <t>IκBα:</t> inhibitory protein kappa B alpha, MAPK: mitogen-activated protein kinase, ERK: extracellular signal-regulated <t>kinase,</t> <t>JNK:</t> jun N-terminal kinase, JAK: janus kinase, STAT: signal transducers and activators of transcription, iNOS: inducible nitric oxide synthase, COX-2: cyclooxygenase 2, 70COLGA: Chamaecyparis obtusa (Siebold & Zucc.) Endl. leaf 70% EtOH extract fermented by Ganoderma applanatum. This summary figure was created using BioRender.com.
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    Graphical summary of this study. 70COLGA suppresses pro-inflammatory molecules. NO: nitric oxide, LPS: lipopolysaccharide, TLR4: Toll-like receptor 4, NF-κB: nuclear factor kappa-light-chain-enhancer of activated B cells, <t>IκBα:</t> inhibitory protein kappa B alpha, MAPK: mitogen-activated protein kinase, ERK: extracellular signal-regulated <t>kinase,</t> <t>JNK:</t> jun N-terminal kinase, JAK: janus kinase, STAT: signal transducers and activators of transcription, iNOS: inducible nitric oxide synthase, COX-2: cyclooxygenase 2, 70COLGA: Chamaecyparis obtusa (Siebold & Zucc.) Endl. leaf 70% EtOH extract fermented by Ganoderma applanatum. This summary figure was created using BioRender.com.
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    Mitochondrial dynamics via proteins clustered at TM4SF5‐enriched MLCSs. (A) SNU449 cells transfected with mCherry‐TM4SF5 and mito‐GFP were subjected to confocal live imaging. Representative images are shown as snapshots. (B‐C) SNU449 cells stably expressing HA‐EV or HA‐TM4SF5 were glucose starved and then replete before electron microscopy imaging. Multiple images of cells ( n = 13, 12, 12, or 14) were processed for mitochondrial length measurement under each experimental condition (C). *** P < 0.001, ordinary one‐way ANOVA. (D‐E) SNU449 (D) or Huh7 (E) cells transfected with TM4SF5‐v5‐TurboID were glucose depleted for 16 h and then replete (10 mmol/L or 25 mmol/L glucose for various times or 30 min, respectively). Whole‐cell lysates were subjected to streptavidin PD and immunoblot. (F) SNU449 cells with stable HA‐EV or HA‐TM4SF5 expression were transfected with mito‐GFP plasmids and treated with 1 μmol/L TSAHC for 16 h. Confocal images for anti‐HA, <t>anti‐DRP1,</t> or anti‐p‐DRP1 were captured, and DRP1‐mitochondria ( n = 93, 72, or 40) or p‐DRP1‐mitochondria ( n = 83, 73, or 38) colocalization was assessed by Pearson's correlation. * P < 0.05, ** P < 0.01, and *** P < 0.001, ordinary one‐way ANOVA. Data were represented as mean ± SD. (G) Animal study scheme for In vivo mitophagy using mtKeima TG mice. (H) Representative images of red In vivo mitophagy signal in liver tissues from mice ( n = 3/group) intravenously injected with AAV8‐ Tbg ‐HA‐Tm4sf5, but not control virus (left). Ten random areas of liver from a mouse were imaged and the red signal was quantitated for a graph (right). **** P < 0.0001, two‐tailed unpaired t test. (I) Liver tissues from WT or KO mice (age‐matched control, AMC, or DEN‐treated for 45 weeks as an HCC model, n ≥ 5/group) were immuno‐stained as indicated. Representative images were shown. Data represent three isolated experiments. See also Supplementary Figure and Supplementary Figure . AMC, age‐matched control; DEN, diethylnitrosamine; DRP1, dynamin‐related protein 1; EV, empty vector; KO, knockout; MLCS, mitochondria‐lysosome contact site; PD, pulldown; SD, standard deviation; Tbg, thyroxine binding globulin; TM4SF5, transmembrane 4 L six family member 5; WT, wild‐type.
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    Mitochondrial dynamics via proteins clustered at TM4SF5‐enriched MLCSs. (A) SNU449 cells transfected with mCherry‐TM4SF5 and mito‐GFP were subjected to confocal live imaging. Representative images are shown as snapshots. (B‐C) SNU449 cells stably expressing HA‐EV or HA‐TM4SF5 were glucose starved and then replete before electron microscopy imaging. Multiple images of cells ( n = 13, 12, 12, or 14) were processed for mitochondrial length measurement under each experimental condition (C). *** P < 0.001, ordinary one‐way ANOVA. (D‐E) SNU449 (D) or Huh7 (E) cells transfected with TM4SF5‐v5‐TurboID were glucose depleted for 16 h and then replete (10 mmol/L or 25 mmol/L glucose for various times or 30 min, respectively). Whole‐cell lysates were subjected to streptavidin PD and immunoblot. (F) SNU449 cells with stable HA‐EV or HA‐TM4SF5 expression were transfected with mito‐GFP plasmids and treated with 1 μmol/L TSAHC for 16 h. Confocal images for anti‐HA, <t>anti‐DRP1,</t> or anti‐p‐DRP1 were captured, and DRP1‐mitochondria ( n = 93, 72, or 40) or p‐DRP1‐mitochondria ( n = 83, 73, or 38) colocalization was assessed by Pearson's correlation. * P < 0.05, ** P < 0.01, and *** P < 0.001, ordinary one‐way ANOVA. Data were represented as mean ± SD. (G) Animal study scheme for In vivo mitophagy using mtKeima TG mice. (H) Representative images of red In vivo mitophagy signal in liver tissues from mice ( n = 3/group) intravenously injected with AAV8‐ Tbg ‐HA‐Tm4sf5, but not control virus (left). Ten random areas of liver from a mouse were imaged and the red signal was quantitated for a graph (right). **** P < 0.0001, two‐tailed unpaired t test. (I) Liver tissues from WT or KO mice (age‐matched control, AMC, or DEN‐treated for 45 weeks as an HCC model, n ≥ 5/group) were immuno‐stained as indicated. Representative images were shown. Data represent three isolated experiments. See also Supplementary Figure and Supplementary Figure . AMC, age‐matched control; DEN, diethylnitrosamine; DRP1, dynamin‐related protein 1; EV, empty vector; KO, knockout; MLCS, mitochondria‐lysosome contact site; PD, pulldown; SD, standard deviation; Tbg, thyroxine binding globulin; TM4SF5, transmembrane 4 L six family member 5; WT, wild‐type.
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    Mitochondrial dynamics via proteins clustered at TM4SF5‐enriched MLCSs. (A) SNU449 cells transfected with mCherry‐TM4SF5 and mito‐GFP were subjected to confocal live imaging. Representative images are shown as snapshots. (B‐C) SNU449 cells stably expressing HA‐EV or HA‐TM4SF5 were glucose starved and then replete before electron microscopy imaging. Multiple images of cells ( n = 13, 12, 12, or 14) were processed for mitochondrial length measurement under each experimental condition (C). *** P < 0.001, ordinary one‐way ANOVA. (D‐E) SNU449 (D) or Huh7 (E) cells transfected with TM4SF5‐v5‐TurboID were glucose depleted for 16 h and then replete (10 mmol/L or 25 mmol/L glucose for various times or 30 min, respectively). Whole‐cell lysates were subjected to streptavidin PD and immunoblot. (F) SNU449 cells with stable HA‐EV or HA‐TM4SF5 expression were transfected with mito‐GFP plasmids and treated with 1 μmol/L TSAHC for 16 h. Confocal images for anti‐HA, <t>anti‐DRP1,</t> or anti‐p‐DRP1 were captured, and DRP1‐mitochondria ( n = 93, 72, or 40) or p‐DRP1‐mitochondria ( n = 83, 73, or 38) colocalization was assessed by Pearson's correlation. * P < 0.05, ** P < 0.01, and *** P < 0.001, ordinary one‐way ANOVA. Data were represented as mean ± SD. (G) Animal study scheme for In vivo mitophagy using mtKeima TG mice. (H) Representative images of red In vivo mitophagy signal in liver tissues from mice ( n = 3/group) intravenously injected with AAV8‐ Tbg ‐HA‐Tm4sf5, but not control virus (left). Ten random areas of liver from a mouse were imaged and the red signal was quantitated for a graph (right). **** P < 0.0001, two‐tailed unpaired t test. (I) Liver tissues from WT or KO mice (age‐matched control, AMC, or DEN‐treated for 45 weeks as an HCC model, n ≥ 5/group) were immuno‐stained as indicated. Representative images were shown. Data represent three isolated experiments. See also Supplementary Figure and Supplementary Figure . AMC, age‐matched control; DEN, diethylnitrosamine; DRP1, dynamin‐related protein 1; EV, empty vector; KO, knockout; MLCS, mitochondria‐lysosome contact site; PD, pulldown; SD, standard deviation; Tbg, thyroxine binding globulin; TM4SF5, transmembrane 4 L six family member 5; WT, wild‐type.
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    Mitochondrial dynamics via proteins clustered at TM4SF5‐enriched MLCSs. (A) SNU449 cells transfected with mCherry‐TM4SF5 and mito‐GFP were subjected to confocal live imaging. Representative images are shown as snapshots. (B‐C) SNU449 cells stably expressing HA‐EV or HA‐TM4SF5 were glucose starved and then replete before electron microscopy imaging. Multiple images of cells ( n = 13, 12, 12, or 14) were processed for mitochondrial length measurement under each experimental condition (C). *** P < 0.001, ordinary one‐way ANOVA. (D‐E) SNU449 (D) or Huh7 (E) cells transfected with TM4SF5‐v5‐TurboID were glucose depleted for 16 h and then replete (10 mmol/L or 25 mmol/L glucose for various times or 30 min, respectively). Whole‐cell lysates were subjected to streptavidin PD and immunoblot. (F) SNU449 cells with stable HA‐EV or HA‐TM4SF5 expression were transfected with mito‐GFP plasmids and treated with 1 μmol/L TSAHC for 16 h. Confocal images for anti‐HA, <t>anti‐DRP1,</t> or anti‐p‐DRP1 were captured, and DRP1‐mitochondria ( n = 93, 72, or 40) or p‐DRP1‐mitochondria ( n = 83, 73, or 38) colocalization was assessed by Pearson's correlation. * P < 0.05, ** P < 0.01, and *** P < 0.001, ordinary one‐way ANOVA. Data were represented as mean ± SD. (G) Animal study scheme for In vivo mitophagy using mtKeima TG mice. (H) Representative images of red In vivo mitophagy signal in liver tissues from mice ( n = 3/group) intravenously injected with AAV8‐ Tbg ‐HA‐Tm4sf5, but not control virus (left). Ten random areas of liver from a mouse were imaged and the red signal was quantitated for a graph (right). **** P < 0.0001, two‐tailed unpaired t test. (I) Liver tissues from WT or KO mice (age‐matched control, AMC, or DEN‐treated for 45 weeks as an HCC model, n ≥ 5/group) were immuno‐stained as indicated. Representative images were shown. Data represent three isolated experiments. See also Supplementary Figure and Supplementary Figure . AMC, age‐matched control; DEN, diethylnitrosamine; DRP1, dynamin‐related protein 1; EV, empty vector; KO, knockout; MLCS, mitochondria‐lysosome contact site; PD, pulldown; SD, standard deviation; Tbg, thyroxine binding globulin; TM4SF5, transmembrane 4 L six family member 5; WT, wild‐type.
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    Mitochondrial dynamics via proteins clustered at TM4SF5‐enriched MLCSs. (A) SNU449 cells transfected with mCherry‐TM4SF5 and mito‐GFP were subjected to confocal live imaging. Representative images are shown as snapshots. (B‐C) SNU449 cells stably expressing HA‐EV or HA‐TM4SF5 were glucose starved and then replete before electron microscopy imaging. Multiple images of cells ( n = 13, 12, 12, or 14) were processed for mitochondrial length measurement under each experimental condition (C). *** P < 0.001, ordinary one‐way ANOVA. (D‐E) SNU449 (D) or Huh7 (E) cells transfected with TM4SF5‐v5‐TurboID were glucose depleted for 16 h and then replete (10 mmol/L or 25 mmol/L glucose for various times or 30 min, respectively). Whole‐cell lysates were subjected to streptavidin PD and immunoblot. (F) SNU449 cells with stable HA‐EV or HA‐TM4SF5 expression were transfected with mito‐GFP plasmids and treated with 1 μmol/L TSAHC for 16 h. Confocal images for anti‐HA, <t>anti‐DRP1,</t> or anti‐p‐DRP1 were captured, and DRP1‐mitochondria ( n = 93, 72, or 40) or p‐DRP1‐mitochondria ( n = 83, 73, or 38) colocalization was assessed by Pearson's correlation. * P < 0.05, ** P < 0.01, and *** P < 0.001, ordinary one‐way ANOVA. Data were represented as mean ± SD. (G) Animal study scheme for In vivo mitophagy using mtKeima TG mice. (H) Representative images of red In vivo mitophagy signal in liver tissues from mice ( n = 3/group) intravenously injected with AAV8‐ Tbg ‐HA‐Tm4sf5, but not control virus (left). Ten random areas of liver from a mouse were imaged and the red signal was quantitated for a graph (right). **** P < 0.0001, two‐tailed unpaired t test. (I) Liver tissues from WT or KO mice (age‐matched control, AMC, or DEN‐treated for 45 weeks as an HCC model, n ≥ 5/group) were immuno‐stained as indicated. Representative images were shown. Data represent three isolated experiments. See also Supplementary Figure and Supplementary Figure . AMC, age‐matched control; DEN, diethylnitrosamine; DRP1, dynamin‐related protein 1; EV, empty vector; KO, knockout; MLCS, mitochondria‐lysosome contact site; PD, pulldown; SD, standard deviation; Tbg, thyroxine binding globulin; TM4SF5, transmembrane 4 L six family member 5; WT, wild‐type.
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    Image Search Results


    Graphical summary of this study. 70COLGA suppresses pro-inflammatory molecules. NO: nitric oxide, LPS: lipopolysaccharide, TLR4: Toll-like receptor 4, NF-κB: nuclear factor kappa-light-chain-enhancer of activated B cells, IκBα: inhibitory protein kappa B alpha, MAPK: mitogen-activated protein kinase, ERK: extracellular signal-regulated kinase, JNK: jun N-terminal kinase, JAK: janus kinase, STAT: signal transducers and activators of transcription, iNOS: inducible nitric oxide synthase, COX-2: cyclooxygenase 2, 70COLGA: Chamaecyparis obtusa (Siebold & Zucc.) Endl. leaf 70% EtOH extract fermented by Ganoderma applanatum. This summary figure was created using BioRender.com.

    Journal: Pharmaceutics

    Article Title: Anti-Inflammatory Effects of Chamaecyparis obtusa (Siebold & Zucc.) Endl. Leaf Extract Fermented by Ganoderma applanatum Mycelia

    doi: 10.3390/pharmaceutics16030365

    Figure Lengend Snippet: Graphical summary of this study. 70COLGA suppresses pro-inflammatory molecules. NO: nitric oxide, LPS: lipopolysaccharide, TLR4: Toll-like receptor 4, NF-κB: nuclear factor kappa-light-chain-enhancer of activated B cells, IκBα: inhibitory protein kappa B alpha, MAPK: mitogen-activated protein kinase, ERK: extracellular signal-regulated kinase, JNK: jun N-terminal kinase, JAK: janus kinase, STAT: signal transducers and activators of transcription, iNOS: inducible nitric oxide synthase, COX-2: cyclooxygenase 2, 70COLGA: Chamaecyparis obtusa (Siebold & Zucc.) Endl. leaf 70% EtOH extract fermented by Ganoderma applanatum. This summary figure was created using BioRender.com.

    Article Snippet: Anti-COX-2 (#12282), anti-pY-STAT1 (#8826), anti-STAT1 (#9172), anti-pY-STAT3 (#9145), anti-STAT3 (#30835), anti-pT/Y-p44/42 MAPK (Erk1/2) (#9101), anti-p44/42 MAPK (Erk1/2) (#4695), anti-pT/Y-SAPK/JNK (#9251), anti-SAPK/JNK (#9252), anti-pT/Y-p38 MAPK (#9211), anti-p38 MAPK (#9212), anti-pS-IκBα (#2859) and anti-pS-NFκB (#3033) were purchased from Cell Signaling Technology (Danvers, MA, USA).

    Techniques:

    Mitochondrial dynamics via proteins clustered at TM4SF5‐enriched MLCSs. (A) SNU449 cells transfected with mCherry‐TM4SF5 and mito‐GFP were subjected to confocal live imaging. Representative images are shown as snapshots. (B‐C) SNU449 cells stably expressing HA‐EV or HA‐TM4SF5 were glucose starved and then replete before electron microscopy imaging. Multiple images of cells ( n = 13, 12, 12, or 14) were processed for mitochondrial length measurement under each experimental condition (C). *** P < 0.001, ordinary one‐way ANOVA. (D‐E) SNU449 (D) or Huh7 (E) cells transfected with TM4SF5‐v5‐TurboID were glucose depleted for 16 h and then replete (10 mmol/L or 25 mmol/L glucose for various times or 30 min, respectively). Whole‐cell lysates were subjected to streptavidin PD and immunoblot. (F) SNU449 cells with stable HA‐EV or HA‐TM4SF5 expression were transfected with mito‐GFP plasmids and treated with 1 μmol/L TSAHC for 16 h. Confocal images for anti‐HA, anti‐DRP1, or anti‐p‐DRP1 were captured, and DRP1‐mitochondria ( n = 93, 72, or 40) or p‐DRP1‐mitochondria ( n = 83, 73, or 38) colocalization was assessed by Pearson's correlation. * P < 0.05, ** P < 0.01, and *** P < 0.001, ordinary one‐way ANOVA. Data were represented as mean ± SD. (G) Animal study scheme for In vivo mitophagy using mtKeima TG mice. (H) Representative images of red In vivo mitophagy signal in liver tissues from mice ( n = 3/group) intravenously injected with AAV8‐ Tbg ‐HA‐Tm4sf5, but not control virus (left). Ten random areas of liver from a mouse were imaged and the red signal was quantitated for a graph (right). **** P < 0.0001, two‐tailed unpaired t test. (I) Liver tissues from WT or KO mice (age‐matched control, AMC, or DEN‐treated for 45 weeks as an HCC model, n ≥ 5/group) were immuno‐stained as indicated. Representative images were shown. Data represent three isolated experiments. See also Supplementary Figure and Supplementary Figure . AMC, age‐matched control; DEN, diethylnitrosamine; DRP1, dynamin‐related protein 1; EV, empty vector; KO, knockout; MLCS, mitochondria‐lysosome contact site; PD, pulldown; SD, standard deviation; Tbg, thyroxine binding globulin; TM4SF5, transmembrane 4 L six family member 5; WT, wild‐type.

    Journal: Cancer Communications

    Article Title: Glucose‐mediated mitochondrial reprogramming by cholesterol export at TM4SF5‐enriched mitochondria‐lysosome contact sites

    doi: 10.1002/cac2.12510

    Figure Lengend Snippet: Mitochondrial dynamics via proteins clustered at TM4SF5‐enriched MLCSs. (A) SNU449 cells transfected with mCherry‐TM4SF5 and mito‐GFP were subjected to confocal live imaging. Representative images are shown as snapshots. (B‐C) SNU449 cells stably expressing HA‐EV or HA‐TM4SF5 were glucose starved and then replete before electron microscopy imaging. Multiple images of cells ( n = 13, 12, 12, or 14) were processed for mitochondrial length measurement under each experimental condition (C). *** P < 0.001, ordinary one‐way ANOVA. (D‐E) SNU449 (D) or Huh7 (E) cells transfected with TM4SF5‐v5‐TurboID were glucose depleted for 16 h and then replete (10 mmol/L or 25 mmol/L glucose for various times or 30 min, respectively). Whole‐cell lysates were subjected to streptavidin PD and immunoblot. (F) SNU449 cells with stable HA‐EV or HA‐TM4SF5 expression were transfected with mito‐GFP plasmids and treated with 1 μmol/L TSAHC for 16 h. Confocal images for anti‐HA, anti‐DRP1, or anti‐p‐DRP1 were captured, and DRP1‐mitochondria ( n = 93, 72, or 40) or p‐DRP1‐mitochondria ( n = 83, 73, or 38) colocalization was assessed by Pearson's correlation. * P < 0.05, ** P < 0.01, and *** P < 0.001, ordinary one‐way ANOVA. Data were represented as mean ± SD. (G) Animal study scheme for In vivo mitophagy using mtKeima TG mice. (H) Representative images of red In vivo mitophagy signal in liver tissues from mice ( n = 3/group) intravenously injected with AAV8‐ Tbg ‐HA‐Tm4sf5, but not control virus (left). Ten random areas of liver from a mouse were imaged and the red signal was quantitated for a graph (right). **** P < 0.0001, two‐tailed unpaired t test. (I) Liver tissues from WT or KO mice (age‐matched control, AMC, or DEN‐treated for 45 weeks as an HCC model, n ≥ 5/group) were immuno‐stained as indicated. Representative images were shown. Data represent three isolated experiments. See also Supplementary Figure and Supplementary Figure . AMC, age‐matched control; DEN, diethylnitrosamine; DRP1, dynamin‐related protein 1; EV, empty vector; KO, knockout; MLCS, mitochondria‐lysosome contact site; PD, pulldown; SD, standard deviation; Tbg, thyroxine binding globulin; TM4SF5, transmembrane 4 L six family member 5; WT, wild‐type.

    Article Snippet: The primary antibodies were anti‐LAMP1 (#9091), anti‐DRP1 (#8570), anti‐pS 616 DRP1 (#3455), and anti‐LC3B (#2775) from Cell Signaling Technology; anti‐ZO1 (402200) from Invitrogen; and anti‐EGFR (sc‐03) from Santa Cruz.

    Techniques: Transfection, Imaging, Stable Transfection, Expressing, Electron Microscopy, Western Blot, In Vivo, Injection, Virus, Two Tailed Test, Staining, Isolation, Plasmid Preparation, Knock-Out, Standard Deviation, Binding Assay

    A working model of mitochondrial reprograming by TM4SF5‐enriched MLCSs. Upon repletion of extracellular glucose, TM4SF5 localizes to lysosomes, and the TM4SF5‐enriched lysosomal membrane becomes closely in apposition to mitochondria to create MLCSs, depending on Rab7, CCZ1, and STBD1 expression. TM4SF5 on lysosome becomes tethered to FKBP8 on the outer mitochondria membrane via a direct interaction. TM4SF5 can be associated with or in proximity to TOM20, DRP1, NPC1, STARD3, and lysosome‐free cholesterol. Mitochondria at TM4SF5‐enriched MLCSs can also dynamically recruit (phospho‐) DRP1 for mitochondrial fission. TM4SF5‐bound cholesterol can be exported to mitochondria efficiently via TM4SF5‐bound NPC1 at the TM4SF5‐enriched MLCSs. Thereby, cholesterol enrichment into sterol‐poor mitochondria causes ETC impairment for inefficient mitochondrial respiration but increased glycolytic respiration. Concomitantly, the TCA cycle remains intact to supply a pool of metabolic intermediates as building blocks for cell proliferation. CCZ1, CCZ1 homolog, vacuolar protein trafficking and biogenesis associated; DRP1, dynamin‐related protein 1; NPC1, niemann‐pick disease type C1; STARD3, star‐related lipid transfer domain‐3; STBD1, starch binding domain 1; TCA cycle, tricarboxylic acid cycle; TOM20, translocase of outer mitochondrial membrane 20.

    Journal: Cancer Communications

    Article Title: Glucose‐mediated mitochondrial reprogramming by cholesterol export at TM4SF5‐enriched mitochondria‐lysosome contact sites

    doi: 10.1002/cac2.12510

    Figure Lengend Snippet: A working model of mitochondrial reprograming by TM4SF5‐enriched MLCSs. Upon repletion of extracellular glucose, TM4SF5 localizes to lysosomes, and the TM4SF5‐enriched lysosomal membrane becomes closely in apposition to mitochondria to create MLCSs, depending on Rab7, CCZ1, and STBD1 expression. TM4SF5 on lysosome becomes tethered to FKBP8 on the outer mitochondria membrane via a direct interaction. TM4SF5 can be associated with or in proximity to TOM20, DRP1, NPC1, STARD3, and lysosome‐free cholesterol. Mitochondria at TM4SF5‐enriched MLCSs can also dynamically recruit (phospho‐) DRP1 for mitochondrial fission. TM4SF5‐bound cholesterol can be exported to mitochondria efficiently via TM4SF5‐bound NPC1 at the TM4SF5‐enriched MLCSs. Thereby, cholesterol enrichment into sterol‐poor mitochondria causes ETC impairment for inefficient mitochondrial respiration but increased glycolytic respiration. Concomitantly, the TCA cycle remains intact to supply a pool of metabolic intermediates as building blocks for cell proliferation. CCZ1, CCZ1 homolog, vacuolar protein trafficking and biogenesis associated; DRP1, dynamin‐related protein 1; NPC1, niemann‐pick disease type C1; STARD3, star‐related lipid transfer domain‐3; STBD1, starch binding domain 1; TCA cycle, tricarboxylic acid cycle; TOM20, translocase of outer mitochondrial membrane 20.

    Article Snippet: The primary antibodies were anti‐LAMP1 (#9091), anti‐DRP1 (#8570), anti‐pS 616 DRP1 (#3455), and anti‐LC3B (#2775) from Cell Signaling Technology; anti‐ZO1 (402200) from Invitrogen; and anti‐EGFR (sc‐03) from Santa Cruz.

    Techniques: Membrane, Expressing, Starch, Binding Assay