fascin Search Results


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  • 94
    Millipore fascin
    Schematic representation of the β-catenin–mediated mechanisms that regulate TGF-β–induced EMT in LECs. TGF-β–induced downregulation of <t>E-cadherin</t> leads to disruption of E-cadherin/β-catenin complex that results in interaction of β-catenin with CBP. Free β-catenin may interact with either Smad 67 in a CBP-dependent manner or TCF, and regulate TGF-β–induced α-SMA, <t>fascin,</t> and MMP9 expression. Inhibition of interaction between β-catenin and TCF fails to inhibit TGF-β–induced EMT-like changes in LECs. However, inhibition of interaction between β-catenin and CBP prevents TGF-β–induced EMT in lens explants.
    Fascin, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 43 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 94 stars, based on 43 article reviews
    Price from $9.99 to $1999.99
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    94/100 stars
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    90
    Abcam fascin
    <t>Rab35</t> is required for IL-17A–induced phosphorylation of PKCα and <t>fascin</t> in ASMCs. ( A ) Mouse WT, Act1 KO ASMC, and AMSC infected with lentivirus containing control (ctrl) or Rab35 shRNA were treated with IL-17A for 0, 15, and 30 min. Cell lysates were subjected to Western blot (WB) with indicated Abs. ( B ) Mouse ASMCs were treated with IL-17A for 0, 15, 30, and 60 min. Lysates were subjected to immunoprecipitation (IP) with anti-Rab35 GTP Ab, after which they were analyzed by WB with indicated Abs. ( C ) WT mouse ASMCs were infected with lentivirus containing ctrl or Rab35 shRNA and treated with IL-17A for 0, 15, and 30 min. Lysates were subjected to IP with anti-fascin Ab, after which they were analyzed by WB with indicated Abs. ( D ) Model: upon IL-17A stimulation (orange dots), Rab35/GDP is recruited to IL-17R/Act1 complex, which, in turn, recruits DennD1C, switching Rab35/GDP (purple) to Rab35/GTP (red). While the complex Act1/Rab35/GTP mediates PKCα activation (p-S657; phosphorylation is depicted as red asterisk), DennD1C brings actin/fascin bundles close to the complex. The activated PKCα then interacts with and phosphorylates fascin on Ser39, resulting in the dissociation of fascin from actin bundles. The release of actin bundles from fascin allows them to interact with myosin assembling into stress fibers, generating contraction force.
    Fascin, supplied by Abcam, used in various techniques. Bioz Stars score: 90/100, based on 83 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 90 stars, based on 83 article reviews
    Price from $9.99 to $1999.99
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    90/100 stars
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    90
    Thermo Fisher fascin
    Model for the role of miR-143 and -145 in VSMC migration and podosome formation. Vascular stress triggers the PDGF response, which activates Src, which in turn inhibits p53 and thus represses miR-143 and -145 expression. This relieves miR-143 repression of the expression of <t>PKC-ε</t> and PDGF-Rα and miR-145 repression of <t>fascin,</t> allowing the formation of podosomes and an increased migratory capacity. Thus, loss of both miRs increases the activity of pathways involved in cell migration.
    Fascin, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 90 stars, based on 6 article reviews
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    86
    Agilent technologies epitope fascin
    Model for the role of miR-143 and -145 in VSMC migration and podosome formation. Vascular stress triggers the PDGF response, which activates Src, which in turn inhibits p53 and thus represses miR-143 and -145 expression. This relieves miR-143 repression of the expression of <t>PKC-ε</t> and PDGF-Rα and miR-145 repression of <t>fascin,</t> allowing the formation of podosomes and an increased migratory capacity. Thus, loss of both miRs increases the activity of pathways involved in cell migration.
    Epitope Fascin, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 86/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/epitope fascin/product/Agilent technologies
    Average 86 stars, based on 9 article reviews
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    88
    Agilent technologies fascin 1
    <t>Fascin-1</t> overexpression in 143B cells promotes intratibial primary tumor growth and lung metastasis in SCID mice. (a) Representative X-ray images of tumor-bearing hind limbs of mice injected with 143B/EV cells (upper panel) or with 143B/Fascin-1 (lower panel). The images show primary tumor appearance on indicated days after tumor cell injection. (b) Representative X-ray images of tumor-bearing hind limbs of mice injected with 143B/Ctrl ShRNA cells (upper panel) or with 143B/ShFascin-1 cells (lower panel). (c) Mean primary tumor growth over time in mice intratibially injected with 143B/EV cells (black), with 143B/Fascin-1 cells (red), with 143B/Ctrl ShRNA (grey) or with 143B/ShFascin-1 blue). (d) Quantification of the number of metastatic lesions in lungs
    Fascin 1, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 88/100, based on 26 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Abcam anti fascin
    NF-κB binds to the <t>fascin</t> promoter in response to IL-6 in a STAT3-dependent manner. (A) MKN45 cells were treated with IL-6 for 30 min and ChIP assays were performed with an NF-κB antibody and primers flanking the potential NF-κB binding site. (B) Results from (A) were quantitated by densitometry and expressed as ChIP/input with the untreated sample. (C) MKN45 cells were transfected with STAT3 siRNA or AG490 and cultured for 3 days. Cells were treated with IL-6 for 30 min and ChIP assays were performed with STAT3 or NF-κB antibodies and primers flanking the potential STAT3/NF-κB binding sites. (D) MKN45 cells were transfected with NF-κB <t>p50</t> siRNA and cultured for 4 days. Whole cell extracts were prepared and western blotting was performed with antibodies against NF-κB p50 and GAPDH. (E) MKN45 cells transfected with control or NF-κB p50 siRNA were treated with IL-6 for 30 min. RNA was subjected to quantitative polymerase chain reaction for fascin and GAPDH. Results were standardized to GAPDH and expressed as fold induction with control siRNA. Values represent the mean ± standard deviation. ** P
    Anti Fascin, supplied by Abcam, used in various techniques. Bioz Stars score: 93/100, based on 20 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Santa Cruz Biotechnology fascin
    Analysis of Cdc42 and <t>fascin</t> in <t>MYC-nick–expressing</t> cells. ( A ) MYC-nick–overexpressing HFF cells show increased filopodia formation that is further enhanced when Cdc42 is activated. (Magnification: 63×.) ( B ) HCT116 cells overexpressing
    Fascin, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 90/100, based on 60 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 90 stars, based on 60 article reviews
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    99
    Cell Signaling Technology Inc fascin
    MST1 depletion causes morphological changes. a – d MST0-211H and H2452 cells were transfected with siNeg, siMST1, or siMST1+pcDNAMST1, analysed 48 h after transfection. Expression of MST1 was analysed by reverse transcription-quantitative real-time PCR (RT-qPCR) ( a ) and western blot ( b ), using glyceraldehyde-3-phosphate dehydrogenase (GAPDH) as an internal control. Quantification of number of cytoplasmic extensions and their size (µm) after <t>α-Tubulin</t> staining ( c ) and quantification of <t>Fascin</t> expression ( d ) by immunofluorescence and confocal microscopy in almost 200 cells using ImageJ software. Representative confocal pictures ( c , d ) are presented for cells stained for α-Tubulin (red), Fascin (green), and nuclei stained with 4′,6-diamidino-2-phenylindole (DAPI). For all histograms, error bars indicate the SEM of at least three independent experiments; * p
    Fascin, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 27 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/fascin/product/Cell Signaling Technology Inc
    Average 99 stars, based on 27 article reviews
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    86
    Abcam fascin ab74487 abcam
    MST1 depletion causes morphological changes. a – d MST0-211H and H2452 cells were transfected with siNeg, siMST1, or siMST1+pcDNAMST1, analysed 48 h after transfection. Expression of MST1 was analysed by reverse transcription-quantitative real-time PCR (RT-qPCR) ( a ) and western blot ( b ), using glyceraldehyde-3-phosphate dehydrogenase (GAPDH) as an internal control. Quantification of number of cytoplasmic extensions and their size (µm) after <t>α-Tubulin</t> staining ( c ) and quantification of <t>Fascin</t> expression ( d ) by immunofluorescence and confocal microscopy in almost 200 cells using ImageJ software. Representative confocal pictures ( c , d ) are presented for cells stained for α-Tubulin (red), Fascin (green), and nuclei stained with 4′,6-diamidino-2-phenylindole (DAPI). For all histograms, error bars indicate the SEM of at least three independent experiments; * p
    Fascin Ab74487 Abcam, supplied by Abcam, used in various techniques. Bioz Stars score: 86/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/fascin ab74487 abcam/product/Abcam
    Average 86 stars, based on 4 article reviews
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    90
    Ventana Medical fascin
    MST1 depletion causes morphological changes. a – d MST0-211H and H2452 cells were transfected with siNeg, siMST1, or siMST1+pcDNAMST1, analysed 48 h after transfection. Expression of MST1 was analysed by reverse transcription-quantitative real-time PCR (RT-qPCR) ( a ) and western blot ( b ), using glyceraldehyde-3-phosphate dehydrogenase (GAPDH) as an internal control. Quantification of number of cytoplasmic extensions and their size (µm) after <t>α-Tubulin</t> staining ( c ) and quantification of <t>Fascin</t> expression ( d ) by immunofluorescence and confocal microscopy in almost 200 cells using ImageJ software. Representative confocal pictures ( c , d ) are presented for cells stained for α-Tubulin (red), Fascin (green), and nuclei stained with 4′,6-diamidino-2-phenylindole (DAPI). For all histograms, error bars indicate the SEM of at least three independent experiments; * p
    Fascin, supplied by Ventana Medical, used in various techniques. Bioz Stars score: 90/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/fascin/product/Ventana Medical
    Average 90 stars, based on 6 article reviews
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    90
    3-D Matrix fascin
    <t>Fascin</t> is important for <t>invadopodia</t> assembly and matrix degradation
    Fascin, supplied by 3-D Matrix, used in various techniques. Bioz Stars score: 90/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/fascin/product/3-D Matrix
    Average 90 stars, based on 4 article reviews
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    92
    Syntaxin fascin
    <t>Fascin</t> is important for <t>invadopodia</t> assembly and matrix degradation
    Fascin, supplied by Syntaxin, used in various techniques. Bioz Stars score: 92/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/fascin/product/Syntaxin
    Average 92 stars, based on 8 article reviews
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    91
    Epitomics fascin
    <t>Fascin</t> is important for <t>invadopodia</t> assembly and matrix degradation
    Fascin, supplied by Epitomics, used in various techniques. Bioz Stars score: 91/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/fascin/product/Epitomics
    Average 91 stars, based on 5 article reviews
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    90
    Novocastra fascin
    <t>Fascin</t> is important for <t>invadopodia</t> assembly and matrix degradation
    Fascin, supplied by Novocastra, used in various techniques. Bioz Stars score: 90/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/fascin/product/Novocastra
    Average 90 stars, based on 12 article reviews
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    93
    Prospec fascin
    <t>Fascin</t> is important for <t>invadopodia</t> assembly and matrix degradation
    Fascin, supplied by Prospec, used in various techniques. Bioz Stars score: 93/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/fascin/product/Prospec
    Average 93 stars, based on 8 article reviews
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    92
    Abcam anti phospho s39 fascin
    <t>Fascin</t> is important for <t>invadopodia</t> assembly and matrix degradation
    Anti Phospho S39 Fascin, supplied by Abcam, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Schematic representation of the β-catenin–mediated mechanisms that regulate TGF-β–induced EMT in LECs. TGF-β–induced downregulation of E-cadherin leads to disruption of E-cadherin/β-catenin complex that results in interaction of β-catenin with CBP. Free β-catenin may interact with either Smad 67 in a CBP-dependent manner or TCF, and regulate TGF-β–induced α-SMA, fascin, and MMP9 expression. Inhibition of interaction between β-catenin and TCF fails to inhibit TGF-β–induced EMT-like changes in LECs. However, inhibition of interaction between β-catenin and CBP prevents TGF-β–induced EMT in lens explants.

    Journal: Investigative Ophthalmology & Visual Science

    Article Title: β-Catenin/CBP–Dependent Signaling Regulates TGF-β–Induced Epithelial to Mesenchymal Transition of Lens Epithelial Cells

    doi: 10.1167/iovs.16-20162

    Figure Lengend Snippet: Schematic representation of the β-catenin–mediated mechanisms that regulate TGF-β–induced EMT in LECs. TGF-β–induced downregulation of E-cadherin leads to disruption of E-cadherin/β-catenin complex that results in interaction of β-catenin with CBP. Free β-catenin may interact with either Smad 67 in a CBP-dependent manner or TCF, and regulate TGF-β–induced α-SMA, fascin, and MMP9 expression. Inhibition of interaction between β-catenin and TCF fails to inhibit TGF-β–induced EMT-like changes in LECs. However, inhibition of interaction between β-catenin and CBP prevents TGF-β–induced EMT in lens explants.

    Article Snippet: As to primary antibodies, fascin was from Millipore (Temecula, CA, USA), E-cadherin from BD Transduction Laboratories (Lexington, KY, USA), active β-catenin (clone 8E7) from Upstate (Lake Placid, NY, USA), MMP9 and GAPDH from Abcam (Cambridge, MA, USA), α-SMA fluorescein isothiocyanate (FITC) conjugated and unconjugated from Sigma-Aldrich Corp., Pan actin from Abcam.

    Techniques: Expressing, Inhibition

    Rab35 is required for IL-17A–induced phosphorylation of PKCα and fascin in ASMCs. ( A ) Mouse WT, Act1 KO ASMC, and AMSC infected with lentivirus containing control (ctrl) or Rab35 shRNA were treated with IL-17A for 0, 15, and 30 min. Cell lysates were subjected to Western blot (WB) with indicated Abs. ( B ) Mouse ASMCs were treated with IL-17A for 0, 15, 30, and 60 min. Lysates were subjected to immunoprecipitation (IP) with anti-Rab35 GTP Ab, after which they were analyzed by WB with indicated Abs. ( C ) WT mouse ASMCs were infected with lentivirus containing ctrl or Rab35 shRNA and treated with IL-17A for 0, 15, and 30 min. Lysates were subjected to IP with anti-fascin Ab, after which they were analyzed by WB with indicated Abs. ( D ) Model: upon IL-17A stimulation (orange dots), Rab35/GDP is recruited to IL-17R/Act1 complex, which, in turn, recruits DennD1C, switching Rab35/GDP (purple) to Rab35/GTP (red). While the complex Act1/Rab35/GTP mediates PKCα activation (p-S657; phosphorylation is depicted as red asterisk), DennD1C brings actin/fascin bundles close to the complex. The activated PKCα then interacts with and phosphorylates fascin on Ser39, resulting in the dissociation of fascin from actin bundles. The release of actin bundles from fascin allows them to interact with myosin assembling into stress fibers, generating contraction force.

    Journal: The Journal of Immunology Author Choice

    Article Title: IL-17A Recruits Rab35 to IL-17R to Mediate PKCα-Dependent Stress Fiber Formation and Airway Smooth Muscle Contractility

    doi: 10.4049/jimmunol.1801025

    Figure Lengend Snippet: Rab35 is required for IL-17A–induced phosphorylation of PKCα and fascin in ASMCs. ( A ) Mouse WT, Act1 KO ASMC, and AMSC infected with lentivirus containing control (ctrl) or Rab35 shRNA were treated with IL-17A for 0, 15, and 30 min. Cell lysates were subjected to Western blot (WB) with indicated Abs. ( B ) Mouse ASMCs were treated with IL-17A for 0, 15, 30, and 60 min. Lysates were subjected to immunoprecipitation (IP) with anti-Rab35 GTP Ab, after which they were analyzed by WB with indicated Abs. ( C ) WT mouse ASMCs were infected with lentivirus containing ctrl or Rab35 shRNA and treated with IL-17A for 0, 15, and 30 min. Lysates were subjected to IP with anti-fascin Ab, after which they were analyzed by WB with indicated Abs. ( D ) Model: upon IL-17A stimulation (orange dots), Rab35/GDP is recruited to IL-17R/Act1 complex, which, in turn, recruits DennD1C, switching Rab35/GDP (purple) to Rab35/GTP (red). While the complex Act1/Rab35/GTP mediates PKCα activation (p-S657; phosphorylation is depicted as red asterisk), DennD1C brings actin/fascin bundles close to the complex. The activated PKCα then interacts with and phosphorylates fascin on Ser39, resulting in the dissociation of fascin from actin bundles. The release of actin bundles from fascin allows them to interact with myosin assembling into stress fibers, generating contraction force.

    Article Snippet: We purchased Abs from following companies: FLAG M2 tag and hemagglutinin tag (Sigma-Aldrich and Cell Signaling); V5 tag (Invitrogen); myc tag (Cell Signaling); smooth muscle–myosin H chain (SM-MHC) and fascin (Abcam); SMA (Sigma-Aldrich); Rab35 (Cell Signaling); activated Rab35-GTP (NewEast Biosciences); p-IκB, IκB, p-p65, PKCα, p-PKCα, and p-myosin (Cell Signaling); p-fascin (ECM Biosciences); Act1 (custom generated); GAPDH (Ambion); and β actin (Cytoskeleton).

    Techniques: Infection, shRNA, Western Blot, Immunoprecipitation, Activation Assay

    Model for the role of miR-143 and -145 in VSMC migration and podosome formation. Vascular stress triggers the PDGF response, which activates Src, which in turn inhibits p53 and thus represses miR-143 and -145 expression. This relieves miR-143 repression of the expression of PKC-ε and PDGF-Rα and miR-145 repression of fascin, allowing the formation of podosomes and an increased migratory capacity. Thus, loss of both miRs increases the activity of pathways involved in cell migration.

    Journal: The Journal of Cell Biology

    Article Title: MicroRNA control of podosome formation in vascular smooth muscle cells in vivo and in vitro

    doi: 10.1083/jcb.200912096

    Figure Lengend Snippet: Model for the role of miR-143 and -145 in VSMC migration and podosome formation. Vascular stress triggers the PDGF response, which activates Src, which in turn inhibits p53 and thus represses miR-143 and -145 expression. This relieves miR-143 repression of the expression of PKC-ε and PDGF-Rα and miR-145 repression of fascin, allowing the formation of podosomes and an increased migratory capacity. Thus, loss of both miRs increases the activity of pathways involved in cell migration.

    Article Snippet: RNA interference Smart pool siRNAs for scrambled, PKC-ε, and fascin were purchased from Thermo Fisher Scientific and transfected into Src-3T3 using Lipofectamine 2000.

    Techniques: Migration, Expressing, Activity Assay

    miR-143 and -145 targets. (A) Representative immunoblot of primary VSMCs isolated from miR-143(145) KO mice transduced with adenovirus (Ad-miR) with an empty expression cassette (−) or expressing miR-143, -145, or -208. (B) Luciferase reporter assay on 3T3 cells performed by cotransfection of 20 nM miR-143, miR-145, or scrambled oligonucleotide (+) with a renilla reporter gene linked to 10 ng WT (wt) or mutated (mt) 3′ UTR of PKC-ε, PDGF-Rα, or fascin. All measurements were calculated as the percentage of control (WT 3′ UTR), and error bars were calculated as propagated standard errors of the mean of triplicate measurements from each experiment. *, P

    Journal: The Journal of Cell Biology

    Article Title: MicroRNA control of podosome formation in vascular smooth muscle cells in vivo and in vitro

    doi: 10.1083/jcb.200912096

    Figure Lengend Snippet: miR-143 and -145 targets. (A) Representative immunoblot of primary VSMCs isolated from miR-143(145) KO mice transduced with adenovirus (Ad-miR) with an empty expression cassette (−) or expressing miR-143, -145, or -208. (B) Luciferase reporter assay on 3T3 cells performed by cotransfection of 20 nM miR-143, miR-145, or scrambled oligonucleotide (+) with a renilla reporter gene linked to 10 ng WT (wt) or mutated (mt) 3′ UTR of PKC-ε, PDGF-Rα, or fascin. All measurements were calculated as the percentage of control (WT 3′ UTR), and error bars were calculated as propagated standard errors of the mean of triplicate measurements from each experiment. *, P

    Article Snippet: RNA interference Smart pool siRNAs for scrambled, PKC-ε, and fascin were purchased from Thermo Fisher Scientific and transfected into Src-3T3 using Lipofectamine 2000.

    Techniques: Isolation, Mouse Assay, Transduction, Expressing, Luciferase, Reporter Assay, Cotransfection

    Fascin-1 overexpression in 143B cells promotes intratibial primary tumor growth and lung metastasis in SCID mice. (a) Representative X-ray images of tumor-bearing hind limbs of mice injected with 143B/EV cells (upper panel) or with 143B/Fascin-1 (lower panel). The images show primary tumor appearance on indicated days after tumor cell injection. (b) Representative X-ray images of tumor-bearing hind limbs of mice injected with 143B/Ctrl ShRNA cells (upper panel) or with 143B/ShFascin-1 cells (lower panel). (c) Mean primary tumor growth over time in mice intratibially injected with 143B/EV cells (black), with 143B/Fascin-1 cells (red), with 143B/Ctrl ShRNA (grey) or with 143B/ShFascin-1 blue). (d) Quantification of the number of metastatic lesions in lungs

    Journal: BMC Cancer

    Article Title: Fascin-1 enhances experimental osteosarcoma tumor formation and metastasis and is related to poor patient outcome

    doi: 10.1186/s12885-019-5303-3

    Figure Lengend Snippet: Fascin-1 overexpression in 143B cells promotes intratibial primary tumor growth and lung metastasis in SCID mice. (a) Representative X-ray images of tumor-bearing hind limbs of mice injected with 143B/EV cells (upper panel) or with 143B/Fascin-1 (lower panel). The images show primary tumor appearance on indicated days after tumor cell injection. (b) Representative X-ray images of tumor-bearing hind limbs of mice injected with 143B/Ctrl ShRNA cells (upper panel) or with 143B/ShFascin-1 cells (lower panel). (c) Mean primary tumor growth over time in mice intratibially injected with 143B/EV cells (black), with 143B/Fascin-1 cells (red), with 143B/Ctrl ShRNA (grey) or with 143B/ShFascin-1 blue). (d) Quantification of the number of metastatic lesions in lungs

    Article Snippet: Primary antibodies used were directed against Fascin-1 (1:400; DAKO) and V5 antibody (1:5000; Invitrogen).

    Techniques: Over Expression, Mouse Assay, Injection, shRNA

    Kaplan-Meier analysis correlating immunohistochemical staining of Fascin-1 in human OS tissues with overall survival of the patients. ( A ) Representative images of TMA sections showing entire spots (upper panel) and higher magnification (lower panel) with non-detectable ( a ), weak ( b ), moderate ( c ), and intense ( d ) Fascin-1 immunostaining. ( B ) Overall survival of OS patients with non-detectable (Fascin-1 neg) or detectable (Fascin-1 pos) immunostaining of tumor tissues. ( C ) Overall survival of patients without (Mets neg) or with (Mets pos) metastases and Fascin-1 neg or Fascin-1 pos tumors

    Journal: BMC Cancer

    Article Title: Fascin-1 enhances experimental osteosarcoma tumor formation and metastasis and is related to poor patient outcome

    doi: 10.1186/s12885-019-5303-3

    Figure Lengend Snippet: Kaplan-Meier analysis correlating immunohistochemical staining of Fascin-1 in human OS tissues with overall survival of the patients. ( A ) Representative images of TMA sections showing entire spots (upper panel) and higher magnification (lower panel) with non-detectable ( a ), weak ( b ), moderate ( c ), and intense ( d ) Fascin-1 immunostaining. ( B ) Overall survival of OS patients with non-detectable (Fascin-1 neg) or detectable (Fascin-1 pos) immunostaining of tumor tissues. ( C ) Overall survival of patients without (Mets neg) or with (Mets pos) metastases and Fascin-1 neg or Fascin-1 pos tumors

    Article Snippet: Primary antibodies used were directed against Fascin-1 (1:400; DAKO) and V5 antibody (1:5000; Invitrogen).

    Techniques: Immunohistochemistry, Staining, Immunostaining

    Validation and characterization of OS cell lines with altered Fascin-1 expression. ( a ) Western blot analysis with antibodies to Fascin-1 (top panel), to V5 (middle panel), and to GAPDH as a loading control (lower panel) of protein extracts from SaOS-2 (left panel) and 143B (right panel) cells stably transduced with a scrambled control ShRNA (Ctrl ShRNA), a Fascin-1-specific ShRNA (ShFascin-1), a pLenti6/V5-DEST empty vector (EV), or pLenti6/V5-DEST-Fascin-1 (Fascin-1). ( b ) SaOS-2/WT (upper row), SaOS-2/Fascin-1 (middle row), and SaOS-2/ShFascin-1 (bottom row) cells stained with anti-Fascin-1 (green), with Alexa-633-phalloidin (filamentous actin, red), and with NucBlue (nuclei in blue). ( c ) While silencing Fascin-1 reduces the perimeter of the cells in both cases, overexpression has little impact ( n = 34–57)

    Journal: BMC Cancer

    Article Title: Fascin-1 enhances experimental osteosarcoma tumor formation and metastasis and is related to poor patient outcome

    doi: 10.1186/s12885-019-5303-3

    Figure Lengend Snippet: Validation and characterization of OS cell lines with altered Fascin-1 expression. ( a ) Western blot analysis with antibodies to Fascin-1 (top panel), to V5 (middle panel), and to GAPDH as a loading control (lower panel) of protein extracts from SaOS-2 (left panel) and 143B (right panel) cells stably transduced with a scrambled control ShRNA (Ctrl ShRNA), a Fascin-1-specific ShRNA (ShFascin-1), a pLenti6/V5-DEST empty vector (EV), or pLenti6/V5-DEST-Fascin-1 (Fascin-1). ( b ) SaOS-2/WT (upper row), SaOS-2/Fascin-1 (middle row), and SaOS-2/ShFascin-1 (bottom row) cells stained with anti-Fascin-1 (green), with Alexa-633-phalloidin (filamentous actin, red), and with NucBlue (nuclei in blue). ( c ) While silencing Fascin-1 reduces the perimeter of the cells in both cases, overexpression has little impact ( n = 34–57)

    Article Snippet: Primary antibodies used were directed against Fascin-1 (1:400; DAKO) and V5 antibody (1:5000; Invitrogen).

    Techniques: Expressing, Western Blot, Stable Transfection, Transduction, shRNA, Plasmid Preparation, Staining, Over Expression

    Fascin-1 overexpression in SaOS-2 cells promotes intratibial primary tumor growth and lung metastasis in SCID mice. ( a ) Representative X-ray images of tumor-bearing hind limbs of mice injected with SaOS-2/EV cells (upper panel) or with SaOS-2/Fascin-1 (lower panel). The images show primary tumor appearance on indicated days after tumor cell injection. ( b ) Representative X-ray images of tumor-bearing hind limbs of mice injected with SaOS-2/Ctrl ShRNA cells (upper panel) or with SaOS-2/ShFascin-1 cells (lower panel). ( c ) Mean primary tumor growth over time in mice intratibially injected with SaOS-2/EV cells (black), with SaOS-2/Fascin-1 cells (red), with SaOS-2/Ctrl ShRNA (grey) or with SaOS-2/ShFascin-1 blue). ( d ) Mean number ± SEM of metastatic lesions in the lungs

    Journal: BMC Cancer

    Article Title: Fascin-1 enhances experimental osteosarcoma tumor formation and metastasis and is related to poor patient outcome

    doi: 10.1186/s12885-019-5303-3

    Figure Lengend Snippet: Fascin-1 overexpression in SaOS-2 cells promotes intratibial primary tumor growth and lung metastasis in SCID mice. ( a ) Representative X-ray images of tumor-bearing hind limbs of mice injected with SaOS-2/EV cells (upper panel) or with SaOS-2/Fascin-1 (lower panel). The images show primary tumor appearance on indicated days after tumor cell injection. ( b ) Representative X-ray images of tumor-bearing hind limbs of mice injected with SaOS-2/Ctrl ShRNA cells (upper panel) or with SaOS-2/ShFascin-1 cells (lower panel). ( c ) Mean primary tumor growth over time in mice intratibially injected with SaOS-2/EV cells (black), with SaOS-2/Fascin-1 cells (red), with SaOS-2/Ctrl ShRNA (grey) or with SaOS-2/ShFascin-1 blue). ( d ) Mean number ± SEM of metastatic lesions in the lungs

    Article Snippet: Primary antibodies used were directed against Fascin-1 (1:400; DAKO) and V5 antibody (1:5000; Invitrogen).

    Techniques: Over Expression, Mouse Assay, Injection, shRNA

    Migration assessed by wound healing . Overexpression of Fascin-1 in SaOS-2 ( a ) or in 143B (b) OS cells increases significantly the migration ability. Similarly, silencing of Fascin-1 slightly decreased the migratory rate of SaOS-2 ( a ) and 143B ( b ) cells. Results are the mean ± SEM of at least three independent experiments. ( c ) Zymography analysis showing increased MMP-9 activity in SaOS-2/Fascin-1 (left panel) and in 143B/Fascin-1 (right panel) in comparison to control SaOS-1/EV and 143B/EV cells respectively. Results are the mean ± SEM of three independent experiments

    Journal: BMC Cancer

    Article Title: Fascin-1 enhances experimental osteosarcoma tumor formation and metastasis and is related to poor patient outcome

    doi: 10.1186/s12885-019-5303-3

    Figure Lengend Snippet: Migration assessed by wound healing . Overexpression of Fascin-1 in SaOS-2 ( a ) or in 143B (b) OS cells increases significantly the migration ability. Similarly, silencing of Fascin-1 slightly decreased the migratory rate of SaOS-2 ( a ) and 143B ( b ) cells. Results are the mean ± SEM of at least three independent experiments. ( c ) Zymography analysis showing increased MMP-9 activity in SaOS-2/Fascin-1 (left panel) and in 143B/Fascin-1 (right panel) in comparison to control SaOS-1/EV and 143B/EV cells respectively. Results are the mean ± SEM of three independent experiments

    Article Snippet: Primary antibodies used were directed against Fascin-1 (1:400; DAKO) and V5 antibody (1:5000; Invitrogen).

    Techniques: Migration, Over Expression, Zymography, Activity Assay

    Distribution of the actin-binding protein fascin during spreading of U251 transfectants. U251NG2.51 (a, b, e, f, i, and j) and U251NG2/t3.4 (c, d, g, h, k, and l) cells were allowed to spread for 40 min on PLL–, mAb β1–, and mAb D120–coated surfaces. Cells were then fixed with methanol and stained with mAbs against either β-actin (act; a, e, i, c, g, and k) or fascin (fas; b, f, j, d, h, and l). On PLL, both cell types contain radial actin spikes decorated with fascin (a–d), whereas on mAb β1, these radial spikes are absent (e–h; note some evidence of stress fiber formation in panel e, although the β-actin antibody is substantially inferior to phalloidin in labeling these structures). On mAb D120 (i–l), radial actin spikes decorated with fascin are seen only in the case of the NG2/t3.4 transfectants. Bar in d, 10 μm.

    Journal: Molecular Biology of the Cell

    Article Title: Cytoskeletal Reorganization Induced by Engagement of the NG2 Proteoglycan Leads to Cell Spreading and Migration

    doi:

    Figure Lengend Snippet: Distribution of the actin-binding protein fascin during spreading of U251 transfectants. U251NG2.51 (a, b, e, f, i, and j) and U251NG2/t3.4 (c, d, g, h, k, and l) cells were allowed to spread for 40 min on PLL–, mAb β1–, and mAb D120–coated surfaces. Cells were then fixed with methanol and stained with mAbs against either β-actin (act; a, e, i, c, g, and k) or fascin (fas; b, f, j, d, h, and l). On PLL, both cell types contain radial actin spikes decorated with fascin (a–d), whereas on mAb β1, these radial spikes are absent (e–h; note some evidence of stress fiber formation in panel e, although the β-actin antibody is substantially inferior to phalloidin in labeling these structures). On mAb D120 (i–l), radial actin spikes decorated with fascin are seen only in the case of the NG2/t3.4 transfectants. Bar in d, 10 μm.

    Article Snippet: Rabbit antibodies and mouse mAbs against rat NG2 have been described previously ( , ; ), as has a rabbit antibody against the L1 cytoplasmic domain ( ). mAbs against the human β1 integrin subunit (GIBCO-BRL, Gaithersburg, MD), rat CD44 (PharMingen, La Jolla, CA), fascin (DAKO, Carpenteria, CA), β-actin (Sigma, St. Louis, MO), and vinculin (Sigma) were obtained commercially.

    Techniques: Binding Assay, Staining, Activated Clotting Time Assay, Labeling

    Cell contacts between DC and T cells. Double immunohistochemical stainings (Envision TM Doublestain system, Dako) of CD209 + -DC (brown, 1:50) vs. CD3 + -T cells (red, 1:80) and fascin + -DC (brown, 1:100) vs. CD3 + -T cells (red, 1:80) were performed to show cell contacts between DC and T cells. (A) Negative (isotype) controls and (B) control myocardium (left) compared to infarcted myocardium (right). Direct cell contacts are indicated by circles.

    Journal: International Journal of Biomedical Science : IJBS

    Article Title: Emergence of Dendritic Cells in the Myocardium after Acute Myocardial Infarction - Implications for Inflammatory Myocardial Damage

    doi:

    Figure Lengend Snippet: Cell contacts between DC and T cells. Double immunohistochemical stainings (Envision TM Doublestain system, Dako) of CD209 + -DC (brown, 1:50) vs. CD3 + -T cells (red, 1:80) and fascin + -DC (brown, 1:100) vs. CD3 + -T cells (red, 1:80) were performed to show cell contacts between DC and T cells. (A) Negative (isotype) controls and (B) control myocardium (left) compared to infarcted myocardium (right). Direct cell contacts are indicated by circles.

    Article Snippet: Immunohistochemical Analysis For immunohistochemical staining, the following monoclonal antibodies were used: anti-CD209 (1:50; Becton Dickinson, Heidelberg, Germany) for immature and anti-fascin (1:100; Dako, Hamburg, Germany) for mature myeloid DC, anti-CD3 (1:80; Dako, Hamburg, Germany) for T cells, anti-CD68 (prediluted, Dako) for macrophages, and anti-HLA-DR (1:25; Dako).

    Techniques: Immunohistochemistry

    Emergence of myeloid DC in infarcted myocardium. (A) Negative (isotype) controls for CD 209, HLA-DR, CD 3, and CD 68 (CSA immunostaining) as well as for fascin (Envision G/2 immunostaining) in control (left) and infarcted myocardium (right). (B, C) Identification of DC by the specific markers CD 209 (CSA, Becton Dickinson 1:50) and fascin (Envision G/2, Dako, 1:100), and corresponding expression of HLA-DR (CSA, Dako, 1:25) in control (left) and infarcted myocardium (right). Histographical presentation: box plot of the number of CD 209 + - and fascin + -DC (cells/0.25 µm 2 ) in control (CTL) and infarcted (AMI) myocardium. Statistical analysis by Mann-Whitney Rank Sum Test.

    Journal: International Journal of Biomedical Science : IJBS

    Article Title: Emergence of Dendritic Cells in the Myocardium after Acute Myocardial Infarction - Implications for Inflammatory Myocardial Damage

    doi:

    Figure Lengend Snippet: Emergence of myeloid DC in infarcted myocardium. (A) Negative (isotype) controls for CD 209, HLA-DR, CD 3, and CD 68 (CSA immunostaining) as well as for fascin (Envision G/2 immunostaining) in control (left) and infarcted myocardium (right). (B, C) Identification of DC by the specific markers CD 209 (CSA, Becton Dickinson 1:50) and fascin (Envision G/2, Dako, 1:100), and corresponding expression of HLA-DR (CSA, Dako, 1:25) in control (left) and infarcted myocardium (right). Histographical presentation: box plot of the number of CD 209 + - and fascin + -DC (cells/0.25 µm 2 ) in control (CTL) and infarcted (AMI) myocardium. Statistical analysis by Mann-Whitney Rank Sum Test.

    Article Snippet: Immunohistochemical Analysis For immunohistochemical staining, the following monoclonal antibodies were used: anti-CD209 (1:50; Becton Dickinson, Heidelberg, Germany) for immature and anti-fascin (1:100; Dako, Hamburg, Germany) for mature myeloid DC, anti-CD3 (1:80; Dako, Hamburg, Germany) for T cells, anti-CD68 (prediluted, Dako) for macrophages, and anti-HLA-DR (1:25; Dako).

    Techniques: Immunostaining, Expressing, CTL Assay, MANN-WHITNEY

    Emergence of different immune cells and HLA-DR in occluded coronaries. Immunohistochemical stainings (conditions see Figure 2 ) of CD209 + -DC, fascin + -DC, CD3 + -T cells, CD69 + -macrophages, and high HLA-DR expression in a thrombotically occluded intramyocardial coronary artery.

    Journal: International Journal of Biomedical Science : IJBS

    Article Title: Emergence of Dendritic Cells in the Myocardium after Acute Myocardial Infarction - Implications for Inflammatory Myocardial Damage

    doi:

    Figure Lengend Snippet: Emergence of different immune cells and HLA-DR in occluded coronaries. Immunohistochemical stainings (conditions see Figure 2 ) of CD209 + -DC, fascin + -DC, CD3 + -T cells, CD69 + -macrophages, and high HLA-DR expression in a thrombotically occluded intramyocardial coronary artery.

    Article Snippet: Immunohistochemical Analysis For immunohistochemical staining, the following monoclonal antibodies were used: anti-CD209 (1:50; Becton Dickinson, Heidelberg, Germany) for immature and anti-fascin (1:100; Dako, Hamburg, Germany) for mature myeloid DC, anti-CD3 (1:80; Dako, Hamburg, Germany) for T cells, anti-CD68 (prediluted, Dako) for macrophages, and anti-HLA-DR (1:25; Dako).

    Techniques: Immunohistochemistry, Expressing

    Representative IHC case revealing LMP1 and Fascin co-expression in a high grade invasive CRC cancer tissue sample. Magnification value is 40X. This analysis was performed using TMA methodology; and the presence of EBV was confirmed by PCR using specific primers for LMP1 and EBNA1 genes in all our samples with all the necessary controls, as described in the Materials and Methods section.

    Journal: Human Vaccines & Immunotherapeutics

    Article Title: Epstein–Barr virus and its association with Fascin expression in colorectal cancers in the Syrian population: A tissue microarray study

    doi: 10.1080/21645515.2017.1302046

    Figure Lengend Snippet: Representative IHC case revealing LMP1 and Fascin co-expression in a high grade invasive CRC cancer tissue sample. Magnification value is 40X. This analysis was performed using TMA methodology; and the presence of EBV was confirmed by PCR using specific primers for LMP1 and EBNA1 genes in all our samples with all the necessary controls, as described in the Materials and Methods section.

    Article Snippet: IHC analysis investigating the expression of LMP1 and Fascin were performed using standard procedures as described previously by our group., Primary LMP1 and Fascin antibodies were obtained from Dako (clone 1–4 and 55K-2; Dako, Canada).

    Techniques: Immunohistochemistry, Expressing, Polymerase Chain Reaction

    Illustrative case of LMP1 and Fascin expression in an intermediate grade invasive CRC sample. Magnification value is 40X. We note that the left zone of the sample is normal tissue which is negative for both LMP1 and Fascin; however, the lower-right zone shows cancer cells that are positive for LMP1 and Fascin.

    Journal: Human Vaccines & Immunotherapeutics

    Article Title: Epstein–Barr virus and its association with Fascin expression in colorectal cancers in the Syrian population: A tissue microarray study

    doi: 10.1080/21645515.2017.1302046

    Figure Lengend Snippet: Illustrative case of LMP1 and Fascin expression in an intermediate grade invasive CRC sample. Magnification value is 40X. We note that the left zone of the sample is normal tissue which is negative for both LMP1 and Fascin; however, the lower-right zone shows cancer cells that are positive for LMP1 and Fascin.

    Article Snippet: IHC analysis investigating the expression of LMP1 and Fascin were performed using standard procedures as described previously by our group., Primary LMP1 and Fascin antibodies were obtained from Dako (clone 1–4 and 55K-2; Dako, Canada).

    Techniques: Expressing

    LMP1 and Fascin co-expression in a high grade invasive CRC cancer sample (Magnification 100X).

    Journal: Human Vaccines & Immunotherapeutics

    Article Title: Epstein–Barr virus and its association with Fascin expression in colorectal cancers in the Syrian population: A tissue microarray study

    doi: 10.1080/21645515.2017.1302046

    Figure Lengend Snippet: LMP1 and Fascin co-expression in a high grade invasive CRC cancer sample (Magnification 100X).

    Article Snippet: IHC analysis investigating the expression of LMP1 and Fascin were performed using standard procedures as described previously by our group., Primary LMP1 and Fascin antibodies were obtained from Dako (clone 1–4 and 55K-2; Dako, Canada).

    Techniques: Expressing

    NF-κB binds to the fascin promoter in response to IL-6 in a STAT3-dependent manner. (A) MKN45 cells were treated with IL-6 for 30 min and ChIP assays were performed with an NF-κB antibody and primers flanking the potential NF-κB binding site. (B) Results from (A) were quantitated by densitometry and expressed as ChIP/input with the untreated sample. (C) MKN45 cells were transfected with STAT3 siRNA or AG490 and cultured for 3 days. Cells were treated with IL-6 for 30 min and ChIP assays were performed with STAT3 or NF-κB antibodies and primers flanking the potential STAT3/NF-κB binding sites. (D) MKN45 cells were transfected with NF-κB p50 siRNA and cultured for 4 days. Whole cell extracts were prepared and western blotting was performed with antibodies against NF-κB p50 and GAPDH. (E) MKN45 cells transfected with control or NF-κB p50 siRNA were treated with IL-6 for 30 min. RNA was subjected to quantitative polymerase chain reaction for fascin and GAPDH. Results were standardized to GAPDH and expressed as fold induction with control siRNA. Values represent the mean ± standard deviation. ** P

    Journal: Oncology Letters

    Article Title: Signal transducer and activator of transcription 3 signaling upregulates fascin via nuclear factor-?B in gastric cancer: Implications in cell invasion and migration

    doi: 10.3892/ol.2014.1804

    Figure Lengend Snippet: NF-κB binds to the fascin promoter in response to IL-6 in a STAT3-dependent manner. (A) MKN45 cells were treated with IL-6 for 30 min and ChIP assays were performed with an NF-κB antibody and primers flanking the potential NF-κB binding site. (B) Results from (A) were quantitated by densitometry and expressed as ChIP/input with the untreated sample. (C) MKN45 cells were transfected with STAT3 siRNA or AG490 and cultured for 3 days. Cells were treated with IL-6 for 30 min and ChIP assays were performed with STAT3 or NF-κB antibodies and primers flanking the potential STAT3/NF-κB binding sites. (D) MKN45 cells were transfected with NF-κB p50 siRNA and cultured for 4 days. Whole cell extracts were prepared and western blotting was performed with antibodies against NF-κB p50 and GAPDH. (E) MKN45 cells transfected with control or NF-κB p50 siRNA were treated with IL-6 for 30 min. RNA was subjected to quantitative polymerase chain reaction for fascin and GAPDH. Results were standardized to GAPDH and expressed as fold induction with control siRNA. Values represent the mean ± standard deviation. ** P

    Article Snippet: Antibodies used for western blotting and chromatin immunoprecipitation (ChIP) assays were anti-phosphotyrosine (p)STAT3 (Cell Signaling Technology, Inc., Beverly, MA, USA), anti-STAT3 (Cell Signaling Technology, Inc.), anti-nuclear factor (NF)-κB p50 (Santa Cruz Biotechnology, Inc., Santa Cruz, CA, USA), anti-fascin (Abcam, Cambridge, UK), anti-hairy and enhancer of split-1 (Hes-1; Abcam), anti-activated-Notch1 (Abcam), anti-activated-Notch2 (Abcam), anti-matrix metalloproteinase (MMP)-2 and anti-MMP-9 (Cell Signaling Technology, Inc.), anti-GAPDH (Abcam), anti-rabbit immunoglobulin (Ig)G and horseradish peroxidase-linked antibody (Cell Signaling Technology, Inc.).

    Techniques: Chromatin Immunoprecipitation, Binding Assay, Transfection, Cell Culture, Western Blot, Real-time Polymerase Chain Reaction, Standard Deviation

    Analysis of Cdc42 and fascin in MYC-nick–expressing cells. ( A ) MYC-nick–overexpressing HFF cells show increased filopodia formation that is further enhanced when Cdc42 is activated. (Magnification: 63×.) ( B ) HCT116 cells overexpressing

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: MYC-nick promotes cell migration by inducing fascin expression and Cdc42 activation

    doi: 10.1073/pnas.1610994113

    Figure Lengend Snippet: Analysis of Cdc42 and fascin in MYC-nick–expressing cells. ( A ) MYC-nick–overexpressing HFF cells show increased filopodia formation that is further enhanced when Cdc42 is activated. (Magnification: 63×.) ( B ) HCT116 cells overexpressing

    Article Snippet: Antibodies against c-MYC (9E10), Sin3, and fascin were from Santa Cruz Biotechnology.

    Techniques: Expressing

    Immunohistochemistry (IHC) of fascin and Cdc42 in human colon cancer biopsies. Representative IHC in normal mucosa, central area of the tumor, and the invasive front of the same tumor is shown. ( A – C ) Cdc42 IHC ( A ), fascin IHC ( B ), and MYC IHC

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: MYC-nick promotes cell migration by inducing fascin expression and Cdc42 activation

    doi: 10.1073/pnas.1610994113

    Figure Lengend Snippet: Immunohistochemistry (IHC) of fascin and Cdc42 in human colon cancer biopsies. Representative IHC in normal mucosa, central area of the tumor, and the invasive front of the same tumor is shown. ( A – C ) Cdc42 IHC ( A ), fascin IHC ( B ), and MYC IHC

    Article Snippet: Antibodies against c-MYC (9E10), Sin3, and fascin were from Santa Cruz Biotechnology.

    Techniques: Immunohistochemistry

    Analysis of fascin expression in MYC-nick induced cell migration. ( A ) Effect of MYC-nick on abundance of endogenous fascin and exogenous GFP-fascin. ( B ) Fascin expression in murine intestinal and colonic lesions derived from different genetic backgrounds

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: MYC-nick promotes cell migration by inducing fascin expression and Cdc42 activation

    doi: 10.1073/pnas.1610994113

    Figure Lengend Snippet: Analysis of fascin expression in MYC-nick induced cell migration. ( A ) Effect of MYC-nick on abundance of endogenous fascin and exogenous GFP-fascin. ( B ) Fascin expression in murine intestinal and colonic lesions derived from different genetic backgrounds

    Article Snippet: Antibodies against c-MYC (9E10), Sin3, and fascin were from Santa Cruz Biotechnology.

    Techniques: Expressing, Migration, Derivative Assay

    Fascin is a direct target gene of Smad4 in basal-like breast cancer cells. A , Western blot showing that TGFβ treatment (5 ng/ml, 72-h treatment in growth medium) and ectopically expressed FLAG-Smad4 and FLAG-Smad3 increased fascin protein levels

    Journal: The Journal of Biological Chemistry

    Article Title: GATA3 Transcription Factor Abrogates Smad4 Transcription Factor-mediated Fascin Overexpression, Invadopodium Formation, and Breast Cancer Cell Invasion *

    doi: 10.1074/jbc.M113.506535

    Figure Lengend Snippet: Fascin is a direct target gene of Smad4 in basal-like breast cancer cells. A , Western blot showing that TGFβ treatment (5 ng/ml, 72-h treatment in growth medium) and ectopically expressed FLAG-Smad4 and FLAG-Smad3 increased fascin protein levels

    Article Snippet: The following antibodies were used in this study: anti-fascin (#sc-21743), anti-Smad4 (#sc-7154), and anti-GATA3 (#sc-22206) were from Santa Cruz Biotechnology; anti-Smad3 (#9523) was from Cell Signaling; anti-HA (#SAB4300603) and anti-GAPDH (#G8795) were from Sigma.

    Techniques: Western Blot

    GATA3 expression levels negatively correlated with fascin in breast cancer patients. A , correlation between fascin (FSCN1) and GATA3 probe sets in two cohorts of breast cancer patients (the MSKCC cohort and the Stockholm cohort). Pearson correlation coefficients

    Journal: The Journal of Biological Chemistry

    Article Title: GATA3 Transcription Factor Abrogates Smad4 Transcription Factor-mediated Fascin Overexpression, Invadopodium Formation, and Breast Cancer Cell Invasion *

    doi: 10.1074/jbc.M113.506535

    Figure Lengend Snippet: GATA3 expression levels negatively correlated with fascin in breast cancer patients. A , correlation between fascin (FSCN1) and GATA3 probe sets in two cohorts of breast cancer patients (the MSKCC cohort and the Stockholm cohort). Pearson correlation coefficients

    Article Snippet: The following antibodies were used in this study: anti-fascin (#sc-21743), anti-Smad4 (#sc-7154), and anti-GATA3 (#sc-22206) were from Santa Cruz Biotechnology; anti-Smad3 (#9523) was from Cell Signaling; anti-HA (#SAB4300603) and anti-GAPDH (#G8795) were from Sigma.

    Techniques: Expressing

    GATA3 abrogated the interaction between Smad4 and its binding sites on fascin and p21 promoters. A , the upper panel shows potential GATA3 binding sites on fascin promoter, and the lower panel shows luciferase assay results, showing that ectopic GATA3

    Journal: The Journal of Biological Chemistry

    Article Title: GATA3 Transcription Factor Abrogates Smad4 Transcription Factor-mediated Fascin Overexpression, Invadopodium Formation, and Breast Cancer Cell Invasion *

    doi: 10.1074/jbc.M113.506535

    Figure Lengend Snippet: GATA3 abrogated the interaction between Smad4 and its binding sites on fascin and p21 promoters. A , the upper panel shows potential GATA3 binding sites on fascin promoter, and the lower panel shows luciferase assay results, showing that ectopic GATA3

    Article Snippet: The following antibodies were used in this study: anti-fascin (#sc-21743), anti-Smad4 (#sc-7154), and anti-GATA3 (#sc-22206) were from Santa Cruz Biotechnology; anti-Smad3 (#9523) was from Cell Signaling; anti-HA (#SAB4300603) and anti-GAPDH (#G8795) were from Sigma.

    Techniques: Binding Assay, Luciferase

    Ectopic GATA3 abrogated TGFβ- and Smad4-mediated transcription of fascin in basal-like breast cancer cells. A and B , ectopic GATA3 abrogated TGFβ ( A ) and Smad4-induced ( B ) overexpression of fascin protein in MDA-MB-231 and MDA-MB-468 cells.

    Journal: The Journal of Biological Chemistry

    Article Title: GATA3 Transcription Factor Abrogates Smad4 Transcription Factor-mediated Fascin Overexpression, Invadopodium Formation, and Breast Cancer Cell Invasion *

    doi: 10.1074/jbc.M113.506535

    Figure Lengend Snippet: Ectopic GATA3 abrogated TGFβ- and Smad4-mediated transcription of fascin in basal-like breast cancer cells. A and B , ectopic GATA3 abrogated TGFβ ( A ) and Smad4-induced ( B ) overexpression of fascin protein in MDA-MB-231 and MDA-MB-468 cells.

    Article Snippet: The following antibodies were used in this study: anti-fascin (#sc-21743), anti-Smad4 (#sc-7154), and anti-GATA3 (#sc-22206) were from Santa Cruz Biotechnology; anti-Smad3 (#9523) was from Cell Signaling; anti-HA (#SAB4300603) and anti-GAPDH (#G8795) were from Sigma.

    Techniques: Over Expression, Multiple Displacement Amplification

    Fascin colocalizes and physically interacts with Pol2 inside the nucleus. ( A ) BT-20 cells were grown on coverlips, fixed and stained for confocal microscopy. Primary antibodies against pFascin (red) and Pol2 (green) were used followed by visualization using Alexa-conjugated secondary antibodies. The arrows point to colocalizing clusters. Top right hand panel: Scatter plot of Fascin and Pol2 intensities. Top right corner: Calculated pearson correlation coefficient. Scale bar, 10 μm. -Ab: primary antibodies omitted. ( B ) BT-20 nuclear protein extracts were fractionated using size exclusion chromatography followed by western blot analysis using the indicated Pol2 and pFascin antibodies. Arrows point to fractions where Pol2 and pFascin co-elute.

    Journal: Scientific Reports

    Article Title: Insights into a novel nuclear function for Fascin in the regulation of the amino-acid transporter SLC3A2

    doi: 10.1038/srep36699

    Figure Lengend Snippet: Fascin colocalizes and physically interacts with Pol2 inside the nucleus. ( A ) BT-20 cells were grown on coverlips, fixed and stained for confocal microscopy. Primary antibodies against pFascin (red) and Pol2 (green) were used followed by visualization using Alexa-conjugated secondary antibodies. The arrows point to colocalizing clusters. Top right hand panel: Scatter plot of Fascin and Pol2 intensities. Top right corner: Calculated pearson correlation coefficient. Scale bar, 10 μm. -Ab: primary antibodies omitted. ( B ) BT-20 nuclear protein extracts were fractionated using size exclusion chromatography followed by western blot analysis using the indicated Pol2 and pFascin antibodies. Arrows point to fractions where Pol2 and pFascin co-elute.

    Article Snippet: Antibodies targeting Fascin (Santa cruz, sc-21743, 1:200), pFascin (ECM biosciences, FP-2661, 1:1000), Pol2 (Covance, 8WG16, 1:200), mTOR (Cell signalling technologies, 2983, 1:500) were then added directly to the blocking buffer for 1 hour.

    Techniques: Staining, Confocal Microscopy, Size-exclusion Chromatography, Western Blot

    ChIP-seq analysis reveals remarkable colocalization of pFascin with H3K4me3. ( A ) Histogram representing pFascin binding sites distribution and density relative to H3K4me3 peaks. ( B ) Histogram representing pFascin and H3K4me3 binding sites distribution and density relative to the transcription start site (TSS). ( C ) The interaction of Fascin protein with H3K4 methylatransferase complex was analyzed following immunoprecipitation of BT-20 extracts with antibodies directed against pFascin followed by western blot analysis and immunochemical detection of RbBP5 and pFascin. ( D ) Screenshot from Scaffold 4 program showing the results of mass spectrometry data of H3K4me3 core subunits interactors. Fascin is clearly and specifically interacting with RbBP5. For each subunit, the immunoprecipitation was done in triplicate. The percentages represent the peptide identification probability.

    Journal: Scientific Reports

    Article Title: Insights into a novel nuclear function for Fascin in the regulation of the amino-acid transporter SLC3A2

    doi: 10.1038/srep36699

    Figure Lengend Snippet: ChIP-seq analysis reveals remarkable colocalization of pFascin with H3K4me3. ( A ) Histogram representing pFascin binding sites distribution and density relative to H3K4me3 peaks. ( B ) Histogram representing pFascin and H3K4me3 binding sites distribution and density relative to the transcription start site (TSS). ( C ) The interaction of Fascin protein with H3K4 methylatransferase complex was analyzed following immunoprecipitation of BT-20 extracts with antibodies directed against pFascin followed by western blot analysis and immunochemical detection of RbBP5 and pFascin. ( D ) Screenshot from Scaffold 4 program showing the results of mass spectrometry data of H3K4me3 core subunits interactors. Fascin is clearly and specifically interacting with RbBP5. For each subunit, the immunoprecipitation was done in triplicate. The percentages represent the peptide identification probability.

    Article Snippet: Antibodies targeting Fascin (Santa cruz, sc-21743, 1:200), pFascin (ECM biosciences, FP-2661, 1:1000), Pol2 (Covance, 8WG16, 1:200), mTOR (Cell signalling technologies, 2983, 1:500) were then added directly to the blocking buffer for 1 hour.

    Techniques: Chromatin Immunoprecipitation, Binding Assay, Immunoprecipitation, Western Blot, Mass Spectrometry

    Fascin localizes to the nucleus in both breast cancer cell lines and tissue. Fascin and pFascin show similar localization in vitro and in vivo . ( A ) BT-20 and MDA-MB-231 cells were grown on coverlips, fixed and stained for confocal microscopy. Primary antibodies against Fascin (green) and pFascin (red) were used followed by visualization using Alexa-conjugated secondary antibodies. Punctate staining corresponding to both Fascin isoforms is visible inside the nucleus. Scale bar, 10 μm. -Ab: primary antibodies omitted. ( B ) Cytoplasmic and nuclear extracts were prepared from WT and Fascin knockdown BT-20 cells and immunoblotted for Fascin and pFascin with corresponding antibodies. GAPDH and Lamin were used as fractionation controls. ( C ) Representative images of immunohistochemical staining of Fascin and pFascin in a multi-tissueTMA. Magnification: 40x. ( D , E ) Distribution of Fascin and pFascin in nuclear and cytoplasmic fractions analyzed by immunoblotting. ( D–F ) Fascin and P-Fascin expression across different stages of breast cancer progression. ( D ) Representative images of Fascin and P-Fascin expression in benign tissue (BN) and breast cancer (CA). ( E ) Fascin and P-Fascin protein expression at different stages of breast cancer progression and ( F ) lymph nodes status. Confidence intervals (95%) show normalized mean intensity value units of Fascin and P-Fascin as determined by quantitative evaluation of immunohistochemistry. The y-axis represents numerical values corresponding to the intensity of Fascin and P-Fascin expression (0, negative; 1, weak; 2, moderate and 3, high intensity). pN0: lymph nodes pathologically negative and pN+: lymph nodes pathologically positive.

    Journal: Scientific Reports

    Article Title: Insights into a novel nuclear function for Fascin in the regulation of the amino-acid transporter SLC3A2

    doi: 10.1038/srep36699

    Figure Lengend Snippet: Fascin localizes to the nucleus in both breast cancer cell lines and tissue. Fascin and pFascin show similar localization in vitro and in vivo . ( A ) BT-20 and MDA-MB-231 cells were grown on coverlips, fixed and stained for confocal microscopy. Primary antibodies against Fascin (green) and pFascin (red) were used followed by visualization using Alexa-conjugated secondary antibodies. Punctate staining corresponding to both Fascin isoforms is visible inside the nucleus. Scale bar, 10 μm. -Ab: primary antibodies omitted. ( B ) Cytoplasmic and nuclear extracts were prepared from WT and Fascin knockdown BT-20 cells and immunoblotted for Fascin and pFascin with corresponding antibodies. GAPDH and Lamin were used as fractionation controls. ( C ) Representative images of immunohistochemical staining of Fascin and pFascin in a multi-tissueTMA. Magnification: 40x. ( D , E ) Distribution of Fascin and pFascin in nuclear and cytoplasmic fractions analyzed by immunoblotting. ( D–F ) Fascin and P-Fascin expression across different stages of breast cancer progression. ( D ) Representative images of Fascin and P-Fascin expression in benign tissue (BN) and breast cancer (CA). ( E ) Fascin and P-Fascin protein expression at different stages of breast cancer progression and ( F ) lymph nodes status. Confidence intervals (95%) show normalized mean intensity value units of Fascin and P-Fascin as determined by quantitative evaluation of immunohistochemistry. The y-axis represents numerical values corresponding to the intensity of Fascin and P-Fascin expression (0, negative; 1, weak; 2, moderate and 3, high intensity). pN0: lymph nodes pathologically negative and pN+: lymph nodes pathologically positive.

    Article Snippet: Antibodies targeting Fascin (Santa cruz, sc-21743, 1:200), pFascin (ECM biosciences, FP-2661, 1:1000), Pol2 (Covance, 8WG16, 1:200), mTOR (Cell signalling technologies, 2983, 1:500) were then added directly to the blocking buffer for 1 hour.

    Techniques: In Vitro, In Vivo, Multiple Displacement Amplification, Staining, Confocal Microscopy, Fractionation, Immunohistochemistry, Expressing

    MST1 depletion causes morphological changes. a – d MST0-211H and H2452 cells were transfected with siNeg, siMST1, or siMST1+pcDNAMST1, analysed 48 h after transfection. Expression of MST1 was analysed by reverse transcription-quantitative real-time PCR (RT-qPCR) ( a ) and western blot ( b ), using glyceraldehyde-3-phosphate dehydrogenase (GAPDH) as an internal control. Quantification of number of cytoplasmic extensions and their size (µm) after α-Tubulin staining ( c ) and quantification of Fascin expression ( d ) by immunofluorescence and confocal microscopy in almost 200 cells using ImageJ software. Representative confocal pictures ( c , d ) are presented for cells stained for α-Tubulin (red), Fascin (green), and nuclei stained with 4′,6-diamidino-2-phenylindole (DAPI). For all histograms, error bars indicate the SEM of at least three independent experiments; * p

    Journal: British Journal of Cancer

    Article Title: MST1/Hippo promoter gene methylation predicts poor survival in patients with malignant pleural mesothelioma in the IFCT-GFPC-0701 MAPS Phase 3 trial

    doi: 10.1038/s41416-019-0379-8

    Figure Lengend Snippet: MST1 depletion causes morphological changes. a – d MST0-211H and H2452 cells were transfected with siNeg, siMST1, or siMST1+pcDNAMST1, analysed 48 h after transfection. Expression of MST1 was analysed by reverse transcription-quantitative real-time PCR (RT-qPCR) ( a ) and western blot ( b ), using glyceraldehyde-3-phosphate dehydrogenase (GAPDH) as an internal control. Quantification of number of cytoplasmic extensions and their size (µm) after α-Tubulin staining ( c ) and quantification of Fascin expression ( d ) by immunofluorescence and confocal microscopy in almost 200 cells using ImageJ software. Representative confocal pictures ( c , d ) are presented for cells stained for α-Tubulin (red), Fascin (green), and nuclei stained with 4′,6-diamidino-2-phenylindole (DAPI). For all histograms, error bars indicate the SEM of at least three independent experiments; * p

    Article Snippet: The primary antibodies were YAP (Cell Signaling, 1/150), TAZ (Cell Signaling, 1/150), alpha-tubulin (Sigma Aldrich, 1/300), actin (Cell Signaling, 1/300), Fascin (Cell Signaling, 1/300) or cytochrome C (BD Biosciences, 1/50).

    Techniques: Transfection, Expressing, Real-time Polymerase Chain Reaction, Quantitative RT-PCR, Western Blot, Staining, Immunofluorescence, Confocal Microscopy, Software

    Fascin is important for invadopodia assembly and matrix degradation

    Journal: Current biology : CB

    Article Title: The actin bundling protein fascin stabilizes actin in invadopodia and potentiates protrusive invasion

    doi: 10.1016/j.cub.2009.12.035

    Figure Lengend Snippet: Fascin is important for invadopodia assembly and matrix degradation

    Article Snippet: Since fascin stabilizes actin at invadopodia, we investigated a role for fascin in invasion into 3D matrix.

    Techniques:

    Fascin is stably associated with invadopodia and promotes long lifetime

    Journal: Current biology : CB

    Article Title: The actin bundling protein fascin stabilizes actin in invadopodia and potentiates protrusive invasion

    doi: 10.1016/j.cub.2009.12.035

    Figure Lengend Snippet: Fascin is stably associated with invadopodia and promotes long lifetime

    Article Snippet: Since fascin stabilizes actin at invadopodia, we investigated a role for fascin in invasion into 3D matrix.

    Techniques: Stable Transfection