protein kinase rock inhibitor y 27632  (ATCC)


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    ATCC protein kinase rock inhibitor y 27632
    ( A ) Representative phase-contrast images show the morphology of cells (Scale bars: 200 μm). Quantitative data on cell number ( B ) and cell viability ( C ) are shown. ( D ) Morphological index, the ratio of longitudinal to the transverse axis. LA: Longitudinal axis; TA: Transverse axis. All data are presented as mean ± SD from three independent experiments. AP: atmospheric pressure; PP: positive pressure; PP+Y27: positive pressure plus ROCK inhibitor Y-27632. PP+SB43: positive pressure plus ALK5 inhibitor SB-431542. * p < 0.0001 vs . AP group; # p < 0.0001 vs . PP group; & p < 0.0001 vs . PP+SB43 group in all time points, 6 and 48 hours.
    Protein Kinase Rock Inhibitor Y 27632, supplied by ATCC, 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 "Hydrostatic pressure mediates epithelial-mesenchymal transition of cholangiocytes through RhoA/ROCK and TGF-β/smad pathways"

    Article Title: Hydrostatic pressure mediates epithelial-mesenchymal transition of cholangiocytes through RhoA/ROCK and TGF-β/smad pathways

    Journal: PLOS ONE

    doi: 10.1371/journal.pone.0300548

    ( A ) Representative phase-contrast images show the morphology of cells (Scale bars: 200 μm). Quantitative data on cell number ( B ) and cell viability ( C ) are shown. ( D ) Morphological index, the ratio of longitudinal to the transverse axis. LA: Longitudinal axis; TA: Transverse axis. All data are presented as mean ± SD from three independent experiments. AP: atmospheric pressure; PP: positive pressure; PP+Y27: positive pressure plus ROCK inhibitor Y-27632. PP+SB43: positive pressure plus ALK5 inhibitor SB-431542. * p < 0.0001 vs . AP group; # p < 0.0001 vs . PP group; & p < 0.0001 vs . PP+SB43 group in all time points, 6 and 48 hours.
    Figure Legend Snippet: ( A ) Representative phase-contrast images show the morphology of cells (Scale bars: 200 μm). Quantitative data on cell number ( B ) and cell viability ( C ) are shown. ( D ) Morphological index, the ratio of longitudinal to the transverse axis. LA: Longitudinal axis; TA: Transverse axis. All data are presented as mean ± SD from three independent experiments. AP: atmospheric pressure; PP: positive pressure; PP+Y27: positive pressure plus ROCK inhibitor Y-27632. PP+SB43: positive pressure plus ALK5 inhibitor SB-431542. * p < 0.0001 vs . AP group; # p < 0.0001 vs . PP group; & p < 0.0001 vs . PP+SB43 group in all time points, 6 and 48 hours.

    Techniques Used:

    Immunofluorescent images of vimentin (left panel) and quantitative data (right side) at 6 hours ( A ) and 48 hours ( B ) after treatments (Scale bars in images: 20 μm). Immunofluorescent images of ZEB1 expression (left panel) and quantitative data (right side) at 6 hr ( C ) and 48 hr ( D ) after treatment (Scale bars in images: 50 μm). All data are presented as mean ± SD from three independent experiments. AP: atmospheric pressure; PP: positive pressure; PP+Y27: positive pressure plus ROCK inhibitor Y-27632. PP+SB43: positive pressure plus ALK5 inhibitor SB-431542. * p < 0.0001 vs . AP group; # p < 0.0001 vs . PP group; $ p < 0.0001 vs . PP+SB43 group.
    Figure Legend Snippet: Immunofluorescent images of vimentin (left panel) and quantitative data (right side) at 6 hours ( A ) and 48 hours ( B ) after treatments (Scale bars in images: 20 μm). Immunofluorescent images of ZEB1 expression (left panel) and quantitative data (right side) at 6 hr ( C ) and 48 hr ( D ) after treatment (Scale bars in images: 50 μm). All data are presented as mean ± SD from three independent experiments. AP: atmospheric pressure; PP: positive pressure; PP+Y27: positive pressure plus ROCK inhibitor Y-27632. PP+SB43: positive pressure plus ALK5 inhibitor SB-431542. * p < 0.0001 vs . AP group; # p < 0.0001 vs . PP group; $ p < 0.0001 vs . PP+SB43 group.

    Techniques Used: Expressing

    Representative images (left) and quantitative data (right bar graph) show the immunostaining of the pSmad2/3 at 48 hr after treatments (Scale bars: 50 μm). All data are presented as mean ± SD from three independent experiments. AP: atmospheric pressure; PP: positive pressure; PP+Y27: positive pressure plus ROCK inhibitor Y-27632. PP+SB43: positive pressure plus ALK5 inhibitor SB-431542. * p < 0.0001 vs . AP group; # p < 0.0001 vs . PP group; $ p < 0.0001 vs . PP+SB43 group.
    Figure Legend Snippet: Representative images (left) and quantitative data (right bar graph) show the immunostaining of the pSmad2/3 at 48 hr after treatments (Scale bars: 50 μm). All data are presented as mean ± SD from three independent experiments. AP: atmospheric pressure; PP: positive pressure; PP+Y27: positive pressure plus ROCK inhibitor Y-27632. PP+SB43: positive pressure plus ALK5 inhibitor SB-431542. * p < 0.0001 vs . AP group; # p < 0.0001 vs . PP group; $ p < 0.0001 vs . PP+SB43 group.

    Techniques Used: Immunostaining

    Double immunostaining analysis on the expression of collagen 1α (Green) and fibronectin (Red) in cholangiocytes at 48 hr after treatments (Scale bars: 20 μm). All data are presented as mean ± SD from four independent experiments. AP: atmospheric pressure; PP: positive pressure; PP+Y27: positive pressure plus ROCK inhibitor Y-27632. PP+SB43: positive pressure plus ALK5 inhibitor SB-431542. * p < 0.0001 vs . AP group; # p < 0.0001 vs . PP group; $ p < 0.0001 vs . PP+SB43 group.
    Figure Legend Snippet: Double immunostaining analysis on the expression of collagen 1α (Green) and fibronectin (Red) in cholangiocytes at 48 hr after treatments (Scale bars: 20 μm). All data are presented as mean ± SD from four independent experiments. AP: atmospheric pressure; PP: positive pressure; PP+Y27: positive pressure plus ROCK inhibitor Y-27632. PP+SB43: positive pressure plus ALK5 inhibitor SB-431542. * p < 0.0001 vs . AP group; # p < 0.0001 vs . PP group; $ p < 0.0001 vs . PP+SB43 group.

    Techniques Used: Double Immunostaining, Expressing

    rho kinase inhibitor  (ATCC)


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    ATCC rho kinase inhibitor
    Rho Kinase Inhibitor, supplied by ATCC, 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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    rho kinase inhibitor  (ATCC)


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    ATCC rho kinase inhibitor
    Rho Kinase Inhibitor, supplied by ATCC, 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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    dclk1 kinase inhibitor  (ATCC)


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    ATCC dclk1 kinase inhibitor
    Dclk1 Kinase Inhibitor, supplied by ATCC, 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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    tyrosine kinase inhibitor  (ATCC)


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    ATCC tyrosine kinase inhibitor
    Tyrosine Kinase Inhibitor, supplied by ATCC, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/tyrosine kinase inhibitor/product/ATCC
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    dclk1 kinase inhibitor  (ATCC)


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    ATCC dclk1 kinase inhibitor
    CRISPR/Cas9-mediated knockdown of <t>DCLK1</t> blocks SARS-CoV-2 replication-transcription processes. (A) LentiCRISPR-v2 vectors expressing anti-DCLK1 synthetic guide RNAs (sgRNAs #1, #2, and #3; lanes 3–5) were used to target DCLK1, while control synthetic guide RNA was used as a control (sgRNA-C, lane 2). Additional controls included untreated cells (Calu-3-wt, lane 1). Puromycin-resistant cells were pooled to determine the relative expression of DCLK1. sgRNA #2-treated cells showed 70% inhibition of DCLK1 (Calu-3-DKO cells) and were selected for further study. (B) Calu-3 cells were infected with SARS-CoV-2 for 48 h and imaged by confocal microscope after immunofluorescence staining for microtubules (green), Spike protein (red), and nuclei (blue). (C) Western blots of total lysates of infected cell lines for Spike protein, N protein, and actin. (D) Reverse transcription-quantitative PCR for average copy number of viral gRNA (left) and N protein mRNA (right) in infected cell lines. *P ≤ 0.05, **P ≤ 0.01, ****P ≤ 0.0001, ns (not significant) P > 0.05.
    Dclk1 Kinase Inhibitor, supplied by ATCC, 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 "Blocking of doublecortin-like kinase 1-regulated SARS-CoV-2 replication cycle restores cell signaling network"

    Article Title: Blocking of doublecortin-like kinase 1-regulated SARS-CoV-2 replication cycle restores cell signaling network

    Journal: Journal of Virology

    doi: 10.1128/jvi.01194-23

    CRISPR/Cas9-mediated knockdown of DCLK1 blocks SARS-CoV-2 replication-transcription processes. (A) LentiCRISPR-v2 vectors expressing anti-DCLK1 synthetic guide RNAs (sgRNAs #1, #2, and #3; lanes 3–5) were used to target DCLK1, while control synthetic guide RNA was used as a control (sgRNA-C, lane 2). Additional controls included untreated cells (Calu-3-wt, lane 1). Puromycin-resistant cells were pooled to determine the relative expression of DCLK1. sgRNA #2-treated cells showed 70% inhibition of DCLK1 (Calu-3-DKO cells) and were selected for further study. (B) Calu-3 cells were infected with SARS-CoV-2 for 48 h and imaged by confocal microscope after immunofluorescence staining for microtubules (green), Spike protein (red), and nuclei (blue). (C) Western blots of total lysates of infected cell lines for Spike protein, N protein, and actin. (D) Reverse transcription-quantitative PCR for average copy number of viral gRNA (left) and N protein mRNA (right) in infected cell lines. *P ≤ 0.05, **P ≤ 0.01, ****P ≤ 0.0001, ns (not significant) P > 0.05.
    Figure Legend Snippet: CRISPR/Cas9-mediated knockdown of DCLK1 blocks SARS-CoV-2 replication-transcription processes. (A) LentiCRISPR-v2 vectors expressing anti-DCLK1 synthetic guide RNAs (sgRNAs #1, #2, and #3; lanes 3–5) were used to target DCLK1, while control synthetic guide RNA was used as a control (sgRNA-C, lane 2). Additional controls included untreated cells (Calu-3-wt, lane 1). Puromycin-resistant cells were pooled to determine the relative expression of DCLK1. sgRNA #2-treated cells showed 70% inhibition of DCLK1 (Calu-3-DKO cells) and were selected for further study. (B) Calu-3 cells were infected with SARS-CoV-2 for 48 h and imaged by confocal microscope after immunofluorescence staining for microtubules (green), Spike protein (red), and nuclei (blue). (C) Western blots of total lysates of infected cell lines for Spike protein, N protein, and actin. (D) Reverse transcription-quantitative PCR for average copy number of viral gRNA (left) and N protein mRNA (right) in infected cell lines. *P ≤ 0.05, **P ≤ 0.01, ****P ≤ 0.0001, ns (not significant) P > 0.05.

    Techniques Used: CRISPR, Expressing, Inhibition, Infection, Microscopy, Immunofluorescence, Staining, Western Blot, Real-time Polymerase Chain Reaction

    SARS-CoV-2-mediated alteration in proteomic profile of lung epithelial cells are restored following DCLK1 inhibition. Calu-3 cell lysates from uninfected (A1), SARS-CoV-2-infected (A2), infected cells treated with vehicle (DMSO) (A3), or DCLK1-IN-1 (A4) underwent proteomic analysis (experiments performed in triplicate). (A) Principal component analysis of total protein abundance for each sample shows close clustering of total normalized protein abundance (peak area) for A1 and A4 compared to A2 and A3. (B) Heat map clustering for differential protein abundance for each experimental condition. (C) Heat maps show multiple proteins induced by SARS-CoV-2 (A2 and A3, red) and normalization toward levels in uninfected cells (A1, green) following treatment with DCLK1-IN-1 (A4, green). (D) Volcano plots show significantly increased (red circles) and decreased (green circles) protein levels in infected (A2) compared to uninfected (A1) cells. (E) Eight proteins are identified that were induced by infection and normalized by DCLK1-IN-1. (F) Western blots validate proteomic data for a subset of proteins normalized by DCLK1-IN-1 as indicated. (G) Twenty-one genes were downregulated in SARS-CoV-2-infected cells, and expression was restored by DCLK1-IN-1 (see box; the six most downregulated genes are shown in red). (H) Heat map showing six proteins most downregulated by infection (A2) compared to uninfected control (A1). Downregulated protein expression is restored by DCLK1-IN-1 (A4) and not DMSO (A3). (I) Examples of protein levels in infected cells that were restored by DCLK1-IN-1. *P ≤ 0.05, **P ≤ 0.01, ***P ≤ 0.001, ****P ≤ 0.0001, ns (not significant) P > 0.05.
    Figure Legend Snippet: SARS-CoV-2-mediated alteration in proteomic profile of lung epithelial cells are restored following DCLK1 inhibition. Calu-3 cell lysates from uninfected (A1), SARS-CoV-2-infected (A2), infected cells treated with vehicle (DMSO) (A3), or DCLK1-IN-1 (A4) underwent proteomic analysis (experiments performed in triplicate). (A) Principal component analysis of total protein abundance for each sample shows close clustering of total normalized protein abundance (peak area) for A1 and A4 compared to A2 and A3. (B) Heat map clustering for differential protein abundance for each experimental condition. (C) Heat maps show multiple proteins induced by SARS-CoV-2 (A2 and A3, red) and normalization toward levels in uninfected cells (A1, green) following treatment with DCLK1-IN-1 (A4, green). (D) Volcano plots show significantly increased (red circles) and decreased (green circles) protein levels in infected (A2) compared to uninfected (A1) cells. (E) Eight proteins are identified that were induced by infection and normalized by DCLK1-IN-1. (F) Western blots validate proteomic data for a subset of proteins normalized by DCLK1-IN-1 as indicated. (G) Twenty-one genes were downregulated in SARS-CoV-2-infected cells, and expression was restored by DCLK1-IN-1 (see box; the six most downregulated genes are shown in red). (H) Heat map showing six proteins most downregulated by infection (A2) compared to uninfected control (A1). Downregulated protein expression is restored by DCLK1-IN-1 (A4) and not DMSO (A3). (I) Examples of protein levels in infected cells that were restored by DCLK1-IN-1. *P ≤ 0.05, **P ≤ 0.01, ***P ≤ 0.001, ****P ≤ 0.0001, ns (not significant) P > 0.05.

    Techniques Used: Inhibition, Infection, Western Blot, Expressing

    SARS-CoV-2 encoded structural and non-structural protein expression is blocked by DCLK1 inhibition. Viral structural (A–C) and regulatory proteins (D–F) of SARS-CoV-2 are significantly downregulated by DCLK1-IN-1 treatment of infected Calu3 cells when compared to untreated infected controls. Analyses were carried out using quantitative proteomics. A1, uninfected; A2, infected; A3, infected and treated with DMSO as vehicle; and A4, infected and treated with DCLK1-IN-1. **P ≤ 0.01, ***P ≤ 0.001, ***P ≤ 0.0001, ns (not significant) P > 0.05.
    Figure Legend Snippet: SARS-CoV-2 encoded structural and non-structural protein expression is blocked by DCLK1 inhibition. Viral structural (A–C) and regulatory proteins (D–F) of SARS-CoV-2 are significantly downregulated by DCLK1-IN-1 treatment of infected Calu3 cells when compared to untreated infected controls. Analyses were carried out using quantitative proteomics. A1, uninfected; A2, infected; A3, infected and treated with DMSO as vehicle; and A4, infected and treated with DCLK1-IN-1. **P ≤ 0.01, ***P ≤ 0.001, ***P ≤ 0.0001, ns (not significant) P > 0.05.

    Techniques Used: Expressing, Inhibition, Infection

    DCLK1 regulates phosphorylation of nucleocapsid (N) protein. (A) Quantitative phosphoproteomic analysis of SARS-CoV-2-infected Calu-3 cells after treatment with DCLK1-IN-1 (blue bars, A4P) or DMSO (orange bars, A3P). These data are compared with the abundance of phosphopeptides in infected cells (red bars, A2P). Lysates from uninfected/untreated Calu-3 cells are also shown (negative controls, A1P). (B) Amino acid sequence in the SR-rich region of N protein. Phosphorylated serines are shown in red with stars indicating sites that had a reduction in phosphorylation after treatment with DCLK1-IN-1. Reduction in serine phosphorylation by DMSO is indicated by hashtags. (C) DCLK1-IN-1-mediated inhibition of phosphorylation is directed primarily toward conserved serines (red) in the highly conserved SR-rich region of N protein that is found in all omicron variants (BA.1 through BA.5) and the original Wuhan strain (top). (D) DCLK1-IN-1 inhibits Omicron strain viral production in infected Calu-3 cells; TCID50 for DMSO (vehicle) set at 100% and compared with DCLK1-IN-1. (E) Enhanced phosphorylation of eight host proteins due to SARS-CoV-2 infection is repressed by DCLK1-IN-1 (sample designation as in panel A). (F) Examples of host proteins (MAD1L1 and SYMPK) where phosphorylation is restored by DCLK1-IN-1 (blue bars) compared with uninfected Calu-3 cells (green bars). Reduction of protein phosphorylation due to infection (A2P) is not restored by DMSO (A3P). CTD, C-terminal domain; NTD, N-terminal domain.*P ≤ 0.05, **P ≤ 0.01, ***P ≤ 0.001, ****P ≤ 0.0001, ns (not significant) P > 0.05.
    Figure Legend Snippet: DCLK1 regulates phosphorylation of nucleocapsid (N) protein. (A) Quantitative phosphoproteomic analysis of SARS-CoV-2-infected Calu-3 cells after treatment with DCLK1-IN-1 (blue bars, A4P) or DMSO (orange bars, A3P). These data are compared with the abundance of phosphopeptides in infected cells (red bars, A2P). Lysates from uninfected/untreated Calu-3 cells are also shown (negative controls, A1P). (B) Amino acid sequence in the SR-rich region of N protein. Phosphorylated serines are shown in red with stars indicating sites that had a reduction in phosphorylation after treatment with DCLK1-IN-1. Reduction in serine phosphorylation by DMSO is indicated by hashtags. (C) DCLK1-IN-1-mediated inhibition of phosphorylation is directed primarily toward conserved serines (red) in the highly conserved SR-rich region of N protein that is found in all omicron variants (BA.1 through BA.5) and the original Wuhan strain (top). (D) DCLK1-IN-1 inhibits Omicron strain viral production in infected Calu-3 cells; TCID50 for DMSO (vehicle) set at 100% and compared with DCLK1-IN-1. (E) Enhanced phosphorylation of eight host proteins due to SARS-CoV-2 infection is repressed by DCLK1-IN-1 (sample designation as in panel A). (F) Examples of host proteins (MAD1L1 and SYMPK) where phosphorylation is restored by DCLK1-IN-1 (blue bars) compared with uninfected Calu-3 cells (green bars). Reduction of protein phosphorylation due to infection (A2P) is not restored by DMSO (A3P). CTD, C-terminal domain; NTD, N-terminal domain.*P ≤ 0.05, **P ≤ 0.01, ***P ≤ 0.001, ****P ≤ 0.0001, ns (not significant) P > 0.05.

    Techniques Used: Infection, Sequencing, Inhibition

    SARS-CoV-2-induced alterations in EGFR family members’ kinase activity are restored following DCLK1 inhibition. Proteomic and phospho-proteomic analyses of total cell lysates from uninfected cells (A1), SARS-CoV-2-infected Calu-3 cells (A2), and infected cells treated with DMSO (A3) or DCLK1-IN-1 (A4) identify significant changes in the abundance of cellular kinases. (A) Heat map shows an altered abundance of 21 kinases in infected cells; these changes are partly restored by DCLK1-IN-1. Red and green stars are the known interactors of the M and N proteins, respectively. (B) Phosphorylation signatures for eight kinases are altered by SARS-CoV-2 infection (A2P). The degree of phosphorylation at these sites (A1P) is significantly restored by DCLK1-IN-1 (A4P). Red and green stars represent known interactors based on BiGRID database for SARS-CoV-2 M and N proteins. (C) KEGG pathway analysis of differentially abundant kinases (see Materials and Methods for details). (D) A protein-protein interaction network for 28 proteins shows significant changes in abundance in response to SARS-CoV-2 infection (1.5‐fold, P < 0.05). Non-interacting nodes are not shown. Line colors indicate the strength of data based on experimental results (pink), co‐expression (black), gene‐fusion (red), or co‐occurrence (blue) (http://string-db.org/).
    Figure Legend Snippet: SARS-CoV-2-induced alterations in EGFR family members’ kinase activity are restored following DCLK1 inhibition. Proteomic and phospho-proteomic analyses of total cell lysates from uninfected cells (A1), SARS-CoV-2-infected Calu-3 cells (A2), and infected cells treated with DMSO (A3) or DCLK1-IN-1 (A4) identify significant changes in the abundance of cellular kinases. (A) Heat map shows an altered abundance of 21 kinases in infected cells; these changes are partly restored by DCLK1-IN-1. Red and green stars are the known interactors of the M and N proteins, respectively. (B) Phosphorylation signatures for eight kinases are altered by SARS-CoV-2 infection (A2P). The degree of phosphorylation at these sites (A1P) is significantly restored by DCLK1-IN-1 (A4P). Red and green stars represent known interactors based on BiGRID database for SARS-CoV-2 M and N proteins. (C) KEGG pathway analysis of differentially abundant kinases (see Materials and Methods for details). (D) A protein-protein interaction network for 28 proteins shows significant changes in abundance in response to SARS-CoV-2 infection (1.5‐fold, P < 0.05). Non-interacting nodes are not shown. Line colors indicate the strength of data based on experimental results (pink), co‐expression (black), gene‐fusion (red), or co‐occurrence (blue) (http://string-db.org/).

    Techniques Used: Activity Assay, Inhibition, Infection, Expressing

    Expression of viral proteins and RNAs are blocked by DCLK1-IN-1 in the K18-hACE2 model of SARS-CoV-2 infection. K18-hACE2 transgenic mice are a model for SARS-CoV-2 infection. (A) Western blots of total cell lysates from necropsied lungs of uninfected mice (U1–U6) or mice infected with SARS-CoV-2 (M1–M6); lysates were prepared 5 days post-infection, and each group consisted of three male and three female mice. (B and C) Quantitative evaluation of band intensities for host proteins shown in panel A; band intensities for Spike and N proteins were not quantified since these proteins were undetectable in uninfected mice. (D) Representative H&E stained lung for each treatment group (n = 6). Histopathological outcomes for DMSO-treated or DCLK1-IN-1-treated mice were compared with infected (group 1) and uninfected (group 4) mice; the experiment was replicated once with similar results (data not shown). (E) Total RNAs from mouse lung by qRT-PCR with copy numbers of viral genomic RNA (left panel) and N protein mRNA (right panel) calculated from C t values. As controls, group 4 mice were negative for both RNAs; for group 2 mice, RNA levels were similar to those of group 1 (data not shown). (F) Western blots for Spike and N proteins from total lung cell lysates for two representative mice in each group. (G) Quantified band intensities of Spike and N proteins (repeated twice, n = 6) were quantitated using Image J software. (H) Quantitative qRT-PCR for IL-6, TNF-α, and IL-1β mRNAs in DCLK1-IN-1-treated and control mice using total RNAs isolated from mouse lung (n = 3 per group). *P ≤ 0.05, **P ≤ 0.01, ***P ≤ 0.001, ****P ≤ 0.0001, ns (not significant) P > 0.05.
    Figure Legend Snippet: Expression of viral proteins and RNAs are blocked by DCLK1-IN-1 in the K18-hACE2 model of SARS-CoV-2 infection. K18-hACE2 transgenic mice are a model for SARS-CoV-2 infection. (A) Western blots of total cell lysates from necropsied lungs of uninfected mice (U1–U6) or mice infected with SARS-CoV-2 (M1–M6); lysates were prepared 5 days post-infection, and each group consisted of three male and three female mice. (B and C) Quantitative evaluation of band intensities for host proteins shown in panel A; band intensities for Spike and N proteins were not quantified since these proteins were undetectable in uninfected mice. (D) Representative H&E stained lung for each treatment group (n = 6). Histopathological outcomes for DMSO-treated or DCLK1-IN-1-treated mice were compared with infected (group 1) and uninfected (group 4) mice; the experiment was replicated once with similar results (data not shown). (E) Total RNAs from mouse lung by qRT-PCR with copy numbers of viral genomic RNA (left panel) and N protein mRNA (right panel) calculated from C t values. As controls, group 4 mice were negative for both RNAs; for group 2 mice, RNA levels were similar to those of group 1 (data not shown). (F) Western blots for Spike and N proteins from total lung cell lysates for two representative mice in each group. (G) Quantified band intensities of Spike and N proteins (repeated twice, n = 6) were quantitated using Image J software. (H) Quantitative qRT-PCR for IL-6, TNF-α, and IL-1β mRNAs in DCLK1-IN-1-treated and control mice using total RNAs isolated from mouse lung (n = 3 per group). *P ≤ 0.05, **P ≤ 0.01, ***P ≤ 0.001, ****P ≤ 0.0001, ns (not significant) P > 0.05.

    Techniques Used: Expressing, Infection, Transgenic Assay, Western Blot, Staining, Quantitative RT-PCR, Software, Isolation

    DCLK1-IN-1 shows efficacy in the treatment of SARS-CoV-2-infected K18-hACE2 mice. Lungs from K18-hACE2 transgenic mice were obtained at necropsy 5 days post-infection with SARS-CoV-2. (A) Confocal microscopy shows immunofluorescence staining for SP-C (cyan), Spike (red), Dclk1 (magenta), and CD206 (green) from infected mice and infected mice treated with DCLK1-IN-1 (blue, nucleus; ×20 magnification). (B) Spike-negative and CD206+ M2-like macrophages stain for SP-C and DCLK1 and are highlighted in close contact with infected cells (×40 magnification). (C) Quantitation of staining intensities for Spike and Dclk1 for all groups as indicated. (D) Lungs stained for Spike (red), CD206 (green), Dclk1 (magenta), SP-C (cyan), and nuclei (blue) were scanned by AxioScan (magnification ×10) and images shown for DMSO treated (control, upper panel) and DCLK1-IN-1 treated (lower panel). (E) Representative images of lungs from groups of mice stained for hACE2 (green), Spike (red), Dclk1 (cyan), S100A9 (magenta), and nuclei (blue). (F) Infected lung cells co-expressing Dclk1 and S100A9 are highlighted (magnification ×40). *P ≤ 0.05, **P ≤ 0.01, ns (not significant) P > 0.05.
    Figure Legend Snippet: DCLK1-IN-1 shows efficacy in the treatment of SARS-CoV-2-infected K18-hACE2 mice. Lungs from K18-hACE2 transgenic mice were obtained at necropsy 5 days post-infection with SARS-CoV-2. (A) Confocal microscopy shows immunofluorescence staining for SP-C (cyan), Spike (red), Dclk1 (magenta), and CD206 (green) from infected mice and infected mice treated with DCLK1-IN-1 (blue, nucleus; ×20 magnification). (B) Spike-negative and CD206+ M2-like macrophages stain for SP-C and DCLK1 and are highlighted in close contact with infected cells (×40 magnification). (C) Quantitation of staining intensities for Spike and Dclk1 for all groups as indicated. (D) Lungs stained for Spike (red), CD206 (green), Dclk1 (magenta), SP-C (cyan), and nuclei (blue) were scanned by AxioScan (magnification ×10) and images shown for DMSO treated (control, upper panel) and DCLK1-IN-1 treated (lower panel). (E) Representative images of lungs from groups of mice stained for hACE2 (green), Spike (red), Dclk1 (cyan), S100A9 (magenta), and nuclei (blue). (F) Infected lung cells co-expressing Dclk1 and S100A9 are highlighted (magnification ×40). *P ≤ 0.05, **P ≤ 0.01, ns (not significant) P > 0.05.

    Techniques Used: Infection, Transgenic Assay, Confocal Microscopy, Immunofluorescence, Staining, Quantitation Assay, Expressing

    Proposed mechanism of action for efficacy of DCLK1 kinase inhibitor in SARS-CoV-2 infection. SARS-CoV-2 enters target cells through interactions of Spike protein with cellular surface protein ACE2. Subsequently, Spike protein is cleaved by transmembrane serine protease 2. After entry into the cytosol, gRNA containing 5′ cap (red circles) and a poly(A) tail is released from nucleocapsid (N) protein core particles and translated to produce polyproteins (pp1a and pp1b). These polyproteins are cleaved into 16 non-structural proteins that assemble into RTCs. RTCs synthesize new gRNAs via negative-strand RNA intermediates and also produce subgenomic mRNAs that encode structural and accessory proteins. The exact composition and involvement of cellular proteins in the regulation of RTCs are poorly defined. Viral particles are assembled by coating gRNAs with heavily phosphorylated N proteins to produce structures that bud into the endoplasmic reticulum-golgi intermediate compartment. During this process, viral particles acquire a lipid bilayer containing Spike, membrane (M), and envelope (E) proteins. Doublecortin motifs of DCLK1 can help with the movement of RTCs and transport viral particles by regulating microtubule dynamics. Thus, DCLK1-IN-1 acts on multiple steps of the viral replication cycle. gRNA, genomic RNA; RTC, replication-transcription complex.
    Figure Legend Snippet: Proposed mechanism of action for efficacy of DCLK1 kinase inhibitor in SARS-CoV-2 infection. SARS-CoV-2 enters target cells through interactions of Spike protein with cellular surface protein ACE2. Subsequently, Spike protein is cleaved by transmembrane serine protease 2. After entry into the cytosol, gRNA containing 5′ cap (red circles) and a poly(A) tail is released from nucleocapsid (N) protein core particles and translated to produce polyproteins (pp1a and pp1b). These polyproteins are cleaved into 16 non-structural proteins that assemble into RTCs. RTCs synthesize new gRNAs via negative-strand RNA intermediates and also produce subgenomic mRNAs that encode structural and accessory proteins. The exact composition and involvement of cellular proteins in the regulation of RTCs are poorly defined. Viral particles are assembled by coating gRNAs with heavily phosphorylated N proteins to produce structures that bud into the endoplasmic reticulum-golgi intermediate compartment. During this process, viral particles acquire a lipid bilayer containing Spike, membrane (M), and envelope (E) proteins. Doublecortin motifs of DCLK1 can help with the movement of RTCs and transport viral particles by regulating microtubule dynamics. Thus, DCLK1-IN-1 acts on multiple steps of the viral replication cycle. gRNA, genomic RNA; RTC, replication-transcription complex.

    Techniques Used: Infection, Membrane

    egfr tyrosine kinase inhibitors  (ATCC)


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    ATCC protein kinase rock inhibitor y 27632
    ( A ) Representative phase-contrast images show the morphology of cells (Scale bars: 200 μm). Quantitative data on cell number ( B ) and cell viability ( C ) are shown. ( D ) Morphological index, the ratio of longitudinal to the transverse axis. LA: Longitudinal axis; TA: Transverse axis. All data are presented as mean ± SD from three independent experiments. AP: atmospheric pressure; PP: positive pressure; PP+Y27: positive pressure plus ROCK inhibitor Y-27632. PP+SB43: positive pressure plus ALK5 inhibitor SB-431542. * p < 0.0001 vs . AP group; # p < 0.0001 vs . PP group; & p < 0.0001 vs . PP+SB43 group in all time points, 6 and 48 hours.
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    ( A ) Representative phase-contrast images show the morphology of cells (Scale bars: 200 μm). Quantitative data on cell number ( B ) and cell viability ( C ) are shown. ( D ) Morphological index, the ratio of longitudinal to the transverse axis. LA: Longitudinal axis; TA: Transverse axis. All data are presented as mean ± SD from three independent experiments. AP: atmospheric pressure; PP: positive pressure; PP+Y27: positive pressure plus ROCK inhibitor Y-27632. PP+SB43: positive pressure plus ALK5 inhibitor SB-431542. * p < 0.0001 vs . AP group; # p < 0.0001 vs . PP group; & p < 0.0001 vs . PP+SB43 group in all time points, 6 and 48 hours.
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    ( A ) Representative phase-contrast images show the morphology of cells (Scale bars: 200 μm). Quantitative data on cell number ( B ) and cell viability ( C ) are shown. ( D ) Morphological index, the ratio of longitudinal to the transverse axis. LA: Longitudinal axis; TA: Transverse axis. All data are presented as mean ± SD from three independent experiments. AP: atmospheric pressure; PP: positive pressure; PP+Y27: positive pressure plus ROCK inhibitor Y-27632. PP+SB43: positive pressure plus ALK5 inhibitor SB-431542. * p < 0.0001 vs . AP group; # p < 0.0001 vs . PP group; & p < 0.0001 vs . PP+SB43 group in all time points, 6 and 48 hours.
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    ( A ) Representative phase-contrast images show the morphology of cells (Scale bars: 200 μm). Quantitative data on cell number ( B ) and cell viability ( C ) are shown. ( D ) Morphological index, the ratio of longitudinal to the transverse axis. LA: Longitudinal axis; TA: Transverse axis. All data are presented as mean ± SD from three independent experiments. AP: atmospheric pressure; PP: positive pressure; PP+Y27: positive pressure plus ROCK inhibitor Y-27632. PP+SB43: positive pressure plus ALK5 inhibitor SB-431542. * p < 0.0001 vs . AP group; # p < 0.0001 vs . PP group; & p < 0.0001 vs . PP+SB43 group in all time points, 6 and 48 hours.
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    ( A ) Representative phase-contrast images show the morphology of cells (Scale bars: 200 μm). Quantitative data on cell number ( B ) and cell viability ( C ) are shown. ( D ) Morphological index, the ratio of longitudinal to the transverse axis. LA: Longitudinal axis; TA: Transverse axis. All data are presented as mean ± SD from three independent experiments. AP: atmospheric pressure; PP: positive pressure; PP+Y27: positive pressure plus ROCK inhibitor Y-27632. PP+SB43: positive pressure plus ALK5 inhibitor SB-431542. * p < 0.0001 vs . AP group; # p < 0.0001 vs . PP group; & p < 0.0001 vs . PP+SB43 group in all time points, 6 and 48 hours.
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    ( A ) Representative phase-contrast images show the morphology of cells (Scale bars: 200 μm). Quantitative data on cell number ( B ) and cell viability ( C ) are shown. ( D ) Morphological index, the ratio of longitudinal to the transverse axis. LA: Longitudinal axis; TA: Transverse axis. All data are presented as mean ± SD from three independent experiments. AP: atmospheric pressure; PP: positive pressure; PP+Y27: positive pressure plus ROCK inhibitor Y-27632. PP+SB43: positive pressure plus ALK5 inhibitor SB-431542. * p < 0.0001 vs . AP group; # p < 0.0001 vs . PP group; & p < 0.0001 vs . PP+SB43 group in all time points, 6 and 48 hours.

    Journal: PLOS ONE

    Article Title: Hydrostatic pressure mediates epithelial-mesenchymal transition of cholangiocytes through RhoA/ROCK and TGF-β/smad pathways

    doi: 10.1371/journal.pone.0300548

    Figure Lengend Snippet: ( A ) Representative phase-contrast images show the morphology of cells (Scale bars: 200 μm). Quantitative data on cell number ( B ) and cell viability ( C ) are shown. ( D ) Morphological index, the ratio of longitudinal to the transverse axis. LA: Longitudinal axis; TA: Transverse axis. All data are presented as mean ± SD from three independent experiments. AP: atmospheric pressure; PP: positive pressure; PP+Y27: positive pressure plus ROCK inhibitor Y-27632. PP+SB43: positive pressure plus ALK5 inhibitor SB-431542. * p < 0.0001 vs . AP group; # p < 0.0001 vs . PP group; & p < 0.0001 vs . PP+SB43 group in all time points, 6 and 48 hours.

    Article Snippet: When the cells were grown to 50–70% confluence, we randomly kept the cells at following conditions: 1) under normal atmospheric condition in ordinary incubator (AP group); 2) under 50 mmHg hydrostatic pressure induced by a commercial device as described previously [ ] (PP group); 3) under 50 mmHg hydrostatic pressure with the addition of Rho-associated protein kinase (ROCK) inhibitor Y-27632 (10 μM; ATCC, ACS-3030 ™ , USA) in medium (PP+Y27 group); and 4) under 50 mmHg hydrostatic pressure with the addition of SB-431542 (10 μM; MCE, HY-10431, Japan), an inhibitor to activin receptor-like kinase 5 (ALK5, also known as TGF-β type I receptor) (PP+SB43 group).

    Techniques:

    Immunofluorescent images of vimentin (left panel) and quantitative data (right side) at 6 hours ( A ) and 48 hours ( B ) after treatments (Scale bars in images: 20 μm). Immunofluorescent images of ZEB1 expression (left panel) and quantitative data (right side) at 6 hr ( C ) and 48 hr ( D ) after treatment (Scale bars in images: 50 μm). All data are presented as mean ± SD from three independent experiments. AP: atmospheric pressure; PP: positive pressure; PP+Y27: positive pressure plus ROCK inhibitor Y-27632. PP+SB43: positive pressure plus ALK5 inhibitor SB-431542. * p < 0.0001 vs . AP group; # p < 0.0001 vs . PP group; $ p < 0.0001 vs . PP+SB43 group.

    Journal: PLOS ONE

    Article Title: Hydrostatic pressure mediates epithelial-mesenchymal transition of cholangiocytes through RhoA/ROCK and TGF-β/smad pathways

    doi: 10.1371/journal.pone.0300548

    Figure Lengend Snippet: Immunofluorescent images of vimentin (left panel) and quantitative data (right side) at 6 hours ( A ) and 48 hours ( B ) after treatments (Scale bars in images: 20 μm). Immunofluorescent images of ZEB1 expression (left panel) and quantitative data (right side) at 6 hr ( C ) and 48 hr ( D ) after treatment (Scale bars in images: 50 μm). All data are presented as mean ± SD from three independent experiments. AP: atmospheric pressure; PP: positive pressure; PP+Y27: positive pressure plus ROCK inhibitor Y-27632. PP+SB43: positive pressure plus ALK5 inhibitor SB-431542. * p < 0.0001 vs . AP group; # p < 0.0001 vs . PP group; $ p < 0.0001 vs . PP+SB43 group.

    Article Snippet: When the cells were grown to 50–70% confluence, we randomly kept the cells at following conditions: 1) under normal atmospheric condition in ordinary incubator (AP group); 2) under 50 mmHg hydrostatic pressure induced by a commercial device as described previously [ ] (PP group); 3) under 50 mmHg hydrostatic pressure with the addition of Rho-associated protein kinase (ROCK) inhibitor Y-27632 (10 μM; ATCC, ACS-3030 ™ , USA) in medium (PP+Y27 group); and 4) under 50 mmHg hydrostatic pressure with the addition of SB-431542 (10 μM; MCE, HY-10431, Japan), an inhibitor to activin receptor-like kinase 5 (ALK5, also known as TGF-β type I receptor) (PP+SB43 group).

    Techniques: Expressing

    Representative images (left) and quantitative data (right bar graph) show the immunostaining of the pSmad2/3 at 48 hr after treatments (Scale bars: 50 μm). All data are presented as mean ± SD from three independent experiments. AP: atmospheric pressure; PP: positive pressure; PP+Y27: positive pressure plus ROCK inhibitor Y-27632. PP+SB43: positive pressure plus ALK5 inhibitor SB-431542. * p < 0.0001 vs . AP group; # p < 0.0001 vs . PP group; $ p < 0.0001 vs . PP+SB43 group.

    Journal: PLOS ONE

    Article Title: Hydrostatic pressure mediates epithelial-mesenchymal transition of cholangiocytes through RhoA/ROCK and TGF-β/smad pathways

    doi: 10.1371/journal.pone.0300548

    Figure Lengend Snippet: Representative images (left) and quantitative data (right bar graph) show the immunostaining of the pSmad2/3 at 48 hr after treatments (Scale bars: 50 μm). All data are presented as mean ± SD from three independent experiments. AP: atmospheric pressure; PP: positive pressure; PP+Y27: positive pressure plus ROCK inhibitor Y-27632. PP+SB43: positive pressure plus ALK5 inhibitor SB-431542. * p < 0.0001 vs . AP group; # p < 0.0001 vs . PP group; $ p < 0.0001 vs . PP+SB43 group.

    Article Snippet: When the cells were grown to 50–70% confluence, we randomly kept the cells at following conditions: 1) under normal atmospheric condition in ordinary incubator (AP group); 2) under 50 mmHg hydrostatic pressure induced by a commercial device as described previously [ ] (PP group); 3) under 50 mmHg hydrostatic pressure with the addition of Rho-associated protein kinase (ROCK) inhibitor Y-27632 (10 μM; ATCC, ACS-3030 ™ , USA) in medium (PP+Y27 group); and 4) under 50 mmHg hydrostatic pressure with the addition of SB-431542 (10 μM; MCE, HY-10431, Japan), an inhibitor to activin receptor-like kinase 5 (ALK5, also known as TGF-β type I receptor) (PP+SB43 group).

    Techniques: Immunostaining

    Double immunostaining analysis on the expression of collagen 1α (Green) and fibronectin (Red) in cholangiocytes at 48 hr after treatments (Scale bars: 20 μm). All data are presented as mean ± SD from four independent experiments. AP: atmospheric pressure; PP: positive pressure; PP+Y27: positive pressure plus ROCK inhibitor Y-27632. PP+SB43: positive pressure plus ALK5 inhibitor SB-431542. * p < 0.0001 vs . AP group; # p < 0.0001 vs . PP group; $ p < 0.0001 vs . PP+SB43 group.

    Journal: PLOS ONE

    Article Title: Hydrostatic pressure mediates epithelial-mesenchymal transition of cholangiocytes through RhoA/ROCK and TGF-β/smad pathways

    doi: 10.1371/journal.pone.0300548

    Figure Lengend Snippet: Double immunostaining analysis on the expression of collagen 1α (Green) and fibronectin (Red) in cholangiocytes at 48 hr after treatments (Scale bars: 20 μm). All data are presented as mean ± SD from four independent experiments. AP: atmospheric pressure; PP: positive pressure; PP+Y27: positive pressure plus ROCK inhibitor Y-27632. PP+SB43: positive pressure plus ALK5 inhibitor SB-431542. * p < 0.0001 vs . AP group; # p < 0.0001 vs . PP group; $ p < 0.0001 vs . PP+SB43 group.

    Article Snippet: When the cells were grown to 50–70% confluence, we randomly kept the cells at following conditions: 1) under normal atmospheric condition in ordinary incubator (AP group); 2) under 50 mmHg hydrostatic pressure induced by a commercial device as described previously [ ] (PP group); 3) under 50 mmHg hydrostatic pressure with the addition of Rho-associated protein kinase (ROCK) inhibitor Y-27632 (10 μM; ATCC, ACS-3030 ™ , USA) in medium (PP+Y27 group); and 4) under 50 mmHg hydrostatic pressure with the addition of SB-431542 (10 μM; MCE, HY-10431, Japan), an inhibitor to activin receptor-like kinase 5 (ALK5, also known as TGF-β type I receptor) (PP+SB43 group).

    Techniques: Double Immunostaining, Expressing