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BioResource International Inc mv1lu mink lung epithelial cells
Mv1lu Mink Lung Epithelial Cells, supplied by BioResource International Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/mv1lu+mink+lung+epithelial+cells/mv1lu+mink+lung+epithelial+cells/pm34502141-360-0-8
Average 90 stars, based on 1 article reviews

mv1lu mink lung epithelial cells - by Bioz Stars, 2026-10

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Proliferation Assay:

Article Title: Dimer Interface in Natural Variant NK1 Is Dispensable for HGF-Dependent Met Receptor Activation.
Article Snippet: .. Mv1Lu mink lung epithelial cells obtained from RIKEN BioResource Center (Tsukuba, Japan) were used for the cell proliferation assay [46,47]. ..

Article Title: Dimer Interface in Natural Variant NK1 Is Dispensable for HGF-Dependent Met Receptor Activation
Article Snippet: .. Mv1Lu mink lung epithelial cells obtained from RIKEN BioResource Center (Tsukuba, Japan) were used for the cell proliferation assay [ , ]. ..

Image Search Results

Optimizing hCoV-OC43 NG-ns12.9 ds-circDNA transfection and co-cultivation for infectious NG virus production. ( A ) The N protein promotes virus production from CPER-derived ds-circDNAs. HEK293T cells were co-transfected with an FL hCoV-OC43 NG-ns12.9 ds-circDNA along with an hCoV-OC43 N expression vector (pCOC42) or a control vector (pFLAG-CMV-5.1) and then co-cultivated with HCT-8 for 8 days. The numbers of NG + HCT-8 cells were counted and averaged from 10 random microscopic fields on days 6, 7, and 8 (D6–D8) post-transfection. ( B ) A representative microscopic field showing the NG + HCT-8 cells co-transfected by an FL hCoV-OC43 NG-ns12.9 ds-circDNA with an hCoV-OC43 N expression vector (pCOC42) or a control vector pFLAG-CMV-5.1 on D6 and D8. ( C, D ) Fetal bovine serum (FBS), but not new calf serum (NCS), is required for efficient virus production in HCT-8 cells. HEK293T cells were co-transfected with an FL hCoV-OC43 NG-ns12.9 ds-circDNA along with an N expression vector pCOC42 and maintained in DMEM supplemented with 2% FBS overnight. The transfected cells were then co-cultivated by the addition of HCT-8 cells with cell passage every 3 days for a total of 10 days in DMEM supplemented with 10% FBS or 10% NCS. The number of NG + HCT-8 cells was counted and averaged from 10 random microscopic fields on D8–D10 ( C ). Significantly more NG + HCT-8 cells were shown from the cells with an FL NG-ns12.9 ds-circDNA on D8–D10 when growing in the DMEM containing 10% FBS when compared with 10% NCS ( D ). ( E ) hCoV-OC43 induced visible and well-defined cytopathic effect (CPE) in both LLC-MK2 and Mv1Lu cells. The monolayer of LLC-MK2 or Mv1Lu cells in ~70% confluence was infected with WT hCoV-OC43 (100 µL supernatant of infected HCT-8 cells). One representative microscopic field is shown for each cell type. ( F ) Mv1Lu cells are more sensitive than LLC-MK2 cells for hCoV-OC43 infection and plaque formation. Plaque assays of LLC-MK2 and Mv1Lu cells were infected with 100 µL of each diluent after serial 10-fold dilutions of WT hCoV-OC43 virus and overlayed with semisolid media (1× DMEM, 0.5% methylcellulose and 10% FBS) for 8 days. The plaques were fixed for 30 min by 3.7% formaldehyde solution and stained with 1% crystal violet.

Journal: Journal of Virology

Article Title: Discontinuous template switching generates coronavirus subgenomic RNAs from the 3ʹ viral genome end by 5ʹ to 3ʹ transcription

doi: 10.1128/jvi.01438-25

Figure Lengend Snippet: Optimizing hCoV-OC43 NG-ns12.9 ds-circDNA transfection and co-cultivation for infectious NG virus production. ( A ) The N protein promotes virus production from CPER-derived ds-circDNAs. HEK293T cells were co-transfected with an FL hCoV-OC43 NG-ns12.9 ds-circDNA along with an hCoV-OC43 N expression vector (pCOC42) or a control vector (pFLAG-CMV-5.1) and then co-cultivated with HCT-8 for 8 days. The numbers of NG + HCT-8 cells were counted and averaged from 10 random microscopic fields on days 6, 7, and 8 (D6–D8) post-transfection. ( B ) A representative microscopic field showing the NG + HCT-8 cells co-transfected by an FL hCoV-OC43 NG-ns12.9 ds-circDNA with an hCoV-OC43 N expression vector (pCOC42) or a control vector pFLAG-CMV-5.1 on D6 and D8. ( C, D ) Fetal bovine serum (FBS), but not new calf serum (NCS), is required for efficient virus production in HCT-8 cells. HEK293T cells were co-transfected with an FL hCoV-OC43 NG-ns12.9 ds-circDNA along with an N expression vector pCOC42 and maintained in DMEM supplemented with 2% FBS overnight. The transfected cells were then co-cultivated by the addition of HCT-8 cells with cell passage every 3 days for a total of 10 days in DMEM supplemented with 10% FBS or 10% NCS. The number of NG + HCT-8 cells was counted and averaged from 10 random microscopic fields on D8–D10 ( C ). Significantly more NG + HCT-8 cells were shown from the cells with an FL NG-ns12.9 ds-circDNA on D8–D10 when growing in the DMEM containing 10% FBS when compared with 10% NCS ( D ). ( E ) hCoV-OC43 induced visible and well-defined cytopathic effect (CPE) in both LLC-MK2 and Mv1Lu cells. The monolayer of LLC-MK2 or Mv1Lu cells in ~70% confluence was infected with WT hCoV-OC43 (100 µL supernatant of infected HCT-8 cells). One representative microscopic field is shown for each cell type. ( F ) Mv1Lu cells are more sensitive than LLC-MK2 cells for hCoV-OC43 infection and plaque formation. Plaque assays of LLC-MK2 and Mv1Lu cells were infected with 100 µL of each diluent after serial 10-fold dilutions of WT hCoV-OC43 virus and overlayed with semisolid media (1× DMEM, 0.5% methylcellulose and 10% FBS) for 8 days. The plaques were fixed for 30 min by 3.7% formaldehyde solution and stained with 1% crystal violet.

Article Snippet: The human embryonic kidney HEK293T (CRL-3216), human colorectal adenocarcinoma HCT-8 (CCL-244), monkey kidney epithelial LLC-MK2 (CCL-7) and American mink lung epithelial Mv1Lu (CCL-64) cells were obtained from ATCC.

Techniques: Transfection, Virus, Derivative Assay, Expressing, Plasmid Preparation, Control, Infection, Staining

Positional NG insertion into the hCoV-OC43 genome to determine hCoV-OC43 replication and synthesis direction of viral sgRNAs. ( A ) Agarose gel electrophoresis of CPER-derived hCoV-OC43 ds-circDNAs (black arrow) of NG-Δns2 (lane 1) and NG-ns12.9 (lane 2). See for details. ( B and C ) Visualization and quantification of NG + HCT-8 cells after co-cultivation with HEK293T cells transfected with CPER-derived hCoV-OC43 NG-Δns2 or NG-ns12.9 ds-circDNAs. HEK293T cells were transfected with individual FL ds-circDNA products along with an hCoV-OC43 N protein expression vector pCOC42 and then co-cultivated by addition of HCT-8 cells for the indicated days. ( B ) Representative microscopic images on D6 showing NG + HCT-8 cells from the NG-Δns2 or NG-ns12.9 ds-circDNA. ( C ) Numbers of NG + cells quantified from 10 random microscopic fields on D5 and D6, showing more NG + cells (**, P < 0.01, Student’s t -test) for the NG-ns12.9 ds-circDNA than that of the NG-Δns2 ds-circDNA. ( D ) Northern blot analysis of hCoV-OC43 RNA from HCT-8 cells in co-cultivation with HEK293T cells transfected by CPER-derived NG-Δns2 ds-circDNA (lane 1) or NG-ns12.9 ds-circDNA (lane 2) or infected by wild-type (lane 3) viruses. Total RNA extracted from the D6 cells was analyzed by Northern blot using a 32 P-labeled probe antisense to the hCoV-OC43 N ORF. The sgRNAs containing inserted NG are labeled in green. ( E, F ) Virus titration of the HCT-8 cell culture supernatant collected on D8 co-cultivation by using methylcellulose-overlay fluorescent foci ( E ) and plaque ( F ) assays in Mv1Lu cells. ( E ) Representative images of fluorescent foci on D8 of infected Mv1Lu cells (left panel). The Mv1Lu cells were infected by 100 µL of each diluent after serial 10-fold dilutions of the collected HCT-8 culture supernatant collected on D6 described above ( C ). Virus titers are calculated as fluorescent-forming units (FFU/mL) (right bar graph), showing a higher titer of hCoV-OC43 NG-ns12.9 virus (1.2 × 10 6 FFU/mL) than hCoV-OC43 NG-Δns2 virus (4.0 × 10 4 FFU/mL). ( F ) Titration of hCoV-OC43 NG-Δns2 and NG-ns12.9 virus titers by plaque assays using Mv1Lu cells infected by 100 µL of each diluent after serial 10-fold dilutions of the HCT-8 culture supernatant collected on D6 of the cell co-cultivation. The visible virus plaques of hCoV-OC43 NG-Δns2 and hCoV-OC43 NG-ns12.9 on D8 in Mv1Lu cells were visualized by crystal violet staining.

Journal: Journal of Virology

Article Title: Discontinuous template switching generates coronavirus subgenomic RNAs from the 3ʹ viral genome end by 5ʹ to 3ʹ transcription

doi: 10.1128/jvi.01438-25

Figure Lengend Snippet: Positional NG insertion into the hCoV-OC43 genome to determine hCoV-OC43 replication and synthesis direction of viral sgRNAs. ( A ) Agarose gel electrophoresis of CPER-derived hCoV-OC43 ds-circDNAs (black arrow) of NG-Δns2 (lane 1) and NG-ns12.9 (lane 2). See for details. ( B and C ) Visualization and quantification of NG + HCT-8 cells after co-cultivation with HEK293T cells transfected with CPER-derived hCoV-OC43 NG-Δns2 or NG-ns12.9 ds-circDNAs. HEK293T cells were transfected with individual FL ds-circDNA products along with an hCoV-OC43 N protein expression vector pCOC42 and then co-cultivated by addition of HCT-8 cells for the indicated days. ( B ) Representative microscopic images on D6 showing NG + HCT-8 cells from the NG-Δns2 or NG-ns12.9 ds-circDNA. ( C ) Numbers of NG + cells quantified from 10 random microscopic fields on D5 and D6, showing more NG + cells (**, P < 0.01, Student’s t -test) for the NG-ns12.9 ds-circDNA than that of the NG-Δns2 ds-circDNA. ( D ) Northern blot analysis of hCoV-OC43 RNA from HCT-8 cells in co-cultivation with HEK293T cells transfected by CPER-derived NG-Δns2 ds-circDNA (lane 1) or NG-ns12.9 ds-circDNA (lane 2) or infected by wild-type (lane 3) viruses. Total RNA extracted from the D6 cells was analyzed by Northern blot using a 32 P-labeled probe antisense to the hCoV-OC43 N ORF. The sgRNAs containing inserted NG are labeled in green. ( E, F ) Virus titration of the HCT-8 cell culture supernatant collected on D8 co-cultivation by using methylcellulose-overlay fluorescent foci ( E ) and plaque ( F ) assays in Mv1Lu cells. ( E ) Representative images of fluorescent foci on D8 of infected Mv1Lu cells (left panel). The Mv1Lu cells were infected by 100 µL of each diluent after serial 10-fold dilutions of the collected HCT-8 culture supernatant collected on D6 described above ( C ). Virus titers are calculated as fluorescent-forming units (FFU/mL) (right bar graph), showing a higher titer of hCoV-OC43 NG-ns12.9 virus (1.2 × 10 6 FFU/mL) than hCoV-OC43 NG-Δns2 virus (4.0 × 10 4 FFU/mL). ( F ) Titration of hCoV-OC43 NG-Δns2 and NG-ns12.9 virus titers by plaque assays using Mv1Lu cells infected by 100 µL of each diluent after serial 10-fold dilutions of the HCT-8 culture supernatant collected on D6 of the cell co-cultivation. The visible virus plaques of hCoV-OC43 NG-Δns2 and hCoV-OC43 NG-ns12.9 on D8 in Mv1Lu cells were visualized by crystal violet staining.

Techniques: Agarose Gel Electrophoresis, Derivative Assay, Transfection, Expressing, Plasmid Preparation, Northern Blot, Infection, Labeling, Virus, Titration, Cell Culture, Staining

Determination of virus infectivity and replication capacity of hCoV-OC43 NG-Δns2 and NG-ns12.9 virions by de novo virus infection of HCT-8 and Mv1Lu cells. ( A and B ) hCoV-OC43 NG-Δns2 and NG-ns12.9 virions exhibit equal infectivity to HCT-8 cells. HCT-8 cells were infected in parallel with 0.01 MOI of hCoV-OC43 NG-Δns2 or NG-ns12.9 virions titrated, as described in . NG + HCT-8 cells were quantified from five random microscopic fields at days 1, 2, and 3 post infection (D1–D3) of the indicated virus. ( A ) No difference in NG + HCT-8 cells from infection with the NG-Δns2 to NG-ns12.9 virions. ( B ) Selectively shown are one representative fluorescent image each from the HCT-8 cells infected with the NG-Δns2 or NG-ns12.9 virions at D3 post-infection. ( C and D ) hCoV-OC43 NG-Δns2 and NG-ns12.9 virions from the infected HCT-8 cell culture supernatant exhibit equal replication capacity with similar virus titers in Mv1Lu cells. The supernatant from the HCT-8 cells infected by 0.01 MOI of NG-Δns2 or NG-ns12.9 virions was collected on D3 post infection and, after serial 10-fold dilutions, 100 µL of each diluent was used to infect Mv1Lu cells, and titration of viral infectivity was carried out by the methylcellulose-overlay fluorescent foci assay ( C ). Virus titers for NG-Δns2 and NG-ns12.9 virions were calculated as fluorescent-forming units (FFU/mL) shown in a bar graph with NG-Δns2, 1.5 × 10 4 FFU/mL and NG-ns12.9, 2.0 × 10 4 FFU/mL ( D ).

Journal: Journal of Virology

Article Title: Discontinuous template switching generates coronavirus subgenomic RNAs from the 3ʹ viral genome end by 5ʹ to 3ʹ transcription

doi: 10.1128/jvi.01438-25

Figure Lengend Snippet: Determination of virus infectivity and replication capacity of hCoV-OC43 NG-Δns2 and NG-ns12.9 virions by de novo virus infection of HCT-8 and Mv1Lu cells. ( A and B ) hCoV-OC43 NG-Δns2 and NG-ns12.9 virions exhibit equal infectivity to HCT-8 cells. HCT-8 cells were infected in parallel with 0.01 MOI of hCoV-OC43 NG-Δns2 or NG-ns12.9 virions titrated, as described in . NG + HCT-8 cells were quantified from five random microscopic fields at days 1, 2, and 3 post infection (D1–D3) of the indicated virus. ( A ) No difference in NG + HCT-8 cells from infection with the NG-Δns2 to NG-ns12.9 virions. ( B ) Selectively shown are one representative fluorescent image each from the HCT-8 cells infected with the NG-Δns2 or NG-ns12.9 virions at D3 post-infection. ( C and D ) hCoV-OC43 NG-Δns2 and NG-ns12.9 virions from the infected HCT-8 cell culture supernatant exhibit equal replication capacity with similar virus titers in Mv1Lu cells. The supernatant from the HCT-8 cells infected by 0.01 MOI of NG-Δns2 or NG-ns12.9 virions was collected on D3 post infection and, after serial 10-fold dilutions, 100 µL of each diluent was used to infect Mv1Lu cells, and titration of viral infectivity was carried out by the methylcellulose-overlay fluorescent foci assay ( C ). Virus titers for NG-Δns2 and NG-ns12.9 virions were calculated as fluorescent-forming units (FFU/mL) shown in a bar graph with NG-Δns2, 1.5 × 10 4 FFU/mL and NG-ns12.9, 2.0 × 10 4 FFU/mL ( D ).

Techniques: Virus, Infection, Cell Culture, Titration

C-Jun and EGFR OA activation, necessary for OA-cell migration, are decoupled in Mv1Lu cells. ( a ) The figure shows representative images of cell migration obtained under control conditions compared to those with 5 µM OA and OA plus 2,5 µM EGFRi after 24 h treatment. Scale bar 200 µm. ( b ) Plot represents cell migration as the difference obtained between the quantified areas at time 0 h and time 24 h in each condition. Asterisks indicate statistically significant differences between the selected conditions according to a one-way ANOVA statistical analysis: (*p < 0.05, **p < 0.005, ***p < 0.001 and ****p < 0.0001). ( c ) Total protein extracts from serum-starved sub-confluent Mv1Lu cells treated with 5 µM OA, EGF or DMSO equivalent volume as vehicle control. Different protein phosphorylation was assayed at the indicated times (h) targeting phospho-EGFR (Tyr 1068), phospho-ERK1/2 (Thr 202/Tyr 204), phospho-JNK1/2 (Thr 183/Tyr 185) and phospho-c-Jun (Ser 63). Additionally, total protein expression was assayed: ERK1/2, JNK1/2 and c-Jun. β-Actin was used as a loading control. A representative experiment is shown. ( d ) Plots with intensity values of each protein assayed by Western-blot, by gathering the data of three independent experiments. Asterisks indicate statistically significant differences between the selected conditions according to a one-way ANOVA statistical analysis: (*p < 0.05, **p < 0.005, ***p < 0.001 and ****p < 0.0001).

Journal: Scientific Reports

Article Title: Oleanolic acid stimulation of cell migration involves a biphasic signaling mechanism

doi: 10.1038/s41598-022-17553-w

Figure Lengend Snippet: C-Jun and EGFR OA activation, necessary for OA-cell migration, are decoupled in Mv1Lu cells. ( a ) The figure shows representative images of cell migration obtained under control conditions compared to those with 5 µM OA and OA plus 2,5 µM EGFRi after 24 h treatment. Scale bar 200 µm. ( b ) Plot represents cell migration as the difference obtained between the quantified areas at time 0 h and time 24 h in each condition. Asterisks indicate statistically significant differences between the selected conditions according to a one-way ANOVA statistical analysis: (*p < 0.05, **p < 0.005, ***p < 0.001 and ****p < 0.0001). ( c ) Total protein extracts from serum-starved sub-confluent Mv1Lu cells treated with 5 µM OA, EGF or DMSO equivalent volume as vehicle control. Different protein phosphorylation was assayed at the indicated times (h) targeting phospho-EGFR (Tyr 1068), phospho-ERK1/2 (Thr 202/Tyr 204), phospho-JNK1/2 (Thr 183/Tyr 185) and phospho-c-Jun (Ser 63). Additionally, total protein expression was assayed: ERK1/2, JNK1/2 and c-Jun. β-Actin was used as a loading control. A representative experiment is shown. ( d ) Plots with intensity values of each protein assayed by Western-blot, by gathering the data of three independent experiments. Asterisks indicate statistically significant differences between the selected conditions according to a one-way ANOVA statistical analysis: (*p < 0.05, **p < 0.005, ***p < 0.001 and ****p < 0.0001).

Article Snippet: Mink Lung Epithelial (Mv1Lu) , , cells were grown in Eagle's Minimum Essential Medium (EMEM) (Biowest, Nuaillé, France).

Techniques: Activation Assay, Migration, Control, Phospho-proteomics, Expressing, Western Blot

Specific inhibitors against EGFR, MEK and JNK, upon OA treatment, show the independent OA-activation on c-Jun at the edge of wound-scratched Mv1Lu cells at wound edge. ( a ) Confluent Mv1Lu cells were scratched and allowed to migrate for 6 h. Cells treated with 5 µM OA or DMSO equivalent volume were immunostained with specific antibodies against c-Jun transcription factor. Additionally, cells were treated 30 min before with the following inhibitors: 2.5 µM EGFRi, 50 µM MEKi and 15 µM JNKi. Co-staining with phalloidin and Hoechst-33258 was used to show actin cytoskeleton and nuclei, respectively. Images of p-c-Jun fluorescence were converted into pseudo-color with ImageJ software to show the intensity of c-Jun staining. Color rainbow scale represents fluorescence intensity for phospho-c-Jun. Actin fibers (F-actin): red. Nuclei: blue. Images were obtained with a confocal microscope. This experiment was repeated at least three times. Representative images are shown. Scale bar indicates 10 µm. ( b ) Plot represents the data obtained by p-c-Jun intensity at cell nuclei. In every condition, each point on the plot represents p-c-Jun intensity at the nucleus of one cell, quantified by ImageJ software. With the collected data of p-c-Jun intensity, a one-way ANOVA statistical analysis was performed (*p < 0.05, **p < 0.005, ***p < 0.001 and ****p < 0.0001).

Journal: Scientific Reports

Article Title: Oleanolic acid stimulation of cell migration involves a biphasic signaling mechanism

doi: 10.1038/s41598-022-17553-w

Figure Lengend Snippet: Specific inhibitors against EGFR, MEK and JNK, upon OA treatment, show the independent OA-activation on c-Jun at the edge of wound-scratched Mv1Lu cells at wound edge. ( a ) Confluent Mv1Lu cells were scratched and allowed to migrate for 6 h. Cells treated with 5 µM OA or DMSO equivalent volume were immunostained with specific antibodies against c-Jun transcription factor. Additionally, cells were treated 30 min before with the following inhibitors: 2.5 µM EGFRi, 50 µM MEKi and 15 µM JNKi. Co-staining with phalloidin and Hoechst-33258 was used to show actin cytoskeleton and nuclei, respectively. Images of p-c-Jun fluorescence were converted into pseudo-color with ImageJ software to show the intensity of c-Jun staining. Color rainbow scale represents fluorescence intensity for phospho-c-Jun. Actin fibers (F-actin): red. Nuclei: blue. Images were obtained with a confocal microscope. This experiment was repeated at least three times. Representative images are shown. Scale bar indicates 10 µm. ( b ) Plot represents the data obtained by p-c-Jun intensity at cell nuclei. In every condition, each point on the plot represents p-c-Jun intensity at the nucleus of one cell, quantified by ImageJ software. With the collected data of p-c-Jun intensity, a one-way ANOVA statistical analysis was performed (*p < 0.05, **p < 0.005, ***p < 0.001 and ****p < 0.0001).

Article Snippet: Mink Lung Epithelial (Mv1Lu) , , cells were grown in Eagle's Minimum Essential Medium (EMEM) (Biowest, Nuaillé, France).

Techniques: Activation Assay, Staining, Fluorescence, Software, Microscopy

OA promotes changes in FAs and actin cytoskeleton. Confluent Mv1Lu cells were scratched and allowed to migrate for 6 and 12 h. Cells treated with 5 µM OA or DMSO equivalent volume (vehicle control) were immunostained with specific antibodies against paxillin (green). Co-staining with phalloidin and Hoechst-33258 was used to show actin cytoskeleton (magenta) and nuclei (blue), respectively. This experiment was repeated at least three times. Representative images are shown. Scale bar indicates 10 µm. Quantification of the density of FA as FA number per filopodia area. Quantification of FA size (average size) at the filopodia area. One-way ANOVA statistical analysis was performed (*p < 0.05, **p < 0.005, ***p < 0.001 and ****p < 0.0001).

Journal: Scientific Reports

Article Title: Oleanolic acid stimulation of cell migration involves a biphasic signaling mechanism

doi: 10.1038/s41598-022-17553-w

Figure Lengend Snippet: OA promotes changes in FAs and actin cytoskeleton. Confluent Mv1Lu cells were scratched and allowed to migrate for 6 and 12 h. Cells treated with 5 µM OA or DMSO equivalent volume (vehicle control) were immunostained with specific antibodies against paxillin (green). Co-staining with phalloidin and Hoechst-33258 was used to show actin cytoskeleton (magenta) and nuclei (blue), respectively. This experiment was repeated at least three times. Representative images are shown. Scale bar indicates 10 µm. Quantification of the density of FA as FA number per filopodia area. Quantification of FA size (average size) at the filopodia area. One-way ANOVA statistical analysis was performed (*p < 0.05, **p < 0.005, ***p < 0.001 and ****p < 0.0001).

Article Snippet: Mink Lung Epithelial (Mv1Lu) , , cells were grown in Eagle's Minimum Essential Medium (EMEM) (Biowest, Nuaillé, France).

Techniques: Control, Staining

OA induces FAK phosphorylation and promotes its localization in focal adhesion with paxillin in Mv1Lu cells. ( a ) The activation of FAK was assessed by Western Blot at Tyr 925, at the indicated times in the presence of 5 µM OA, DMSO equivalent volume or EGF. Additionally, total protein expression was assayed: FAK. β-Actin was used as a loading control. Phospho-FAK intensity values in Western-blot were quantified by ImageJ to conduct a one-way ANOVA analysis showed on the plot (*p < 0.05, **p < 0.005, ***p < 0.001 and ****p < 0.0001). ( b ) Confluent Mv1Lu cells were scratched and allowed to migrate for 6 h. Pictures show the immunostaining with specific antibodies against phospho-FAK (Tyr 925) and paxillin. Co-staining with Hoechst-33258 was used to reveal nuclei. P-FAK: green. Paxillin: red. Nuclei: blue. ( c ) Pictures and graphs represent a colocalization analysis performed by Zeiss Efficient Navigation (ZEN) software. Colocalized pixels are highlighted in white at the immunostaining images. Graphs are dot plots representing both p-FAK and paxillin intensities in terms of number of pixels: p-FAK pixels on Y axis and paxillin pixels on X axis. The 3 quadrant (upper right) represents overlapped (common) pixels between both proteins. ( d ) Pictures of each condition (two) were divided in three horizontally distributed sectors. Pearson’s correlation coefficient in each sector of each condition was calculated by the average pixel intensity of p-FAK and paxillin overlapped pixels. The plot represents Pearson’s correlation values for each condition, each dot representing the value obtained in one sector. Asterisks indicate statistically significant differences between conditions according to one-way ANOVA statistical analysis: (*p < 0.05, **p < 0.005, ***p < 0.001 and ****p < 0.0001). This experiment was repeated at least three times. Representative images are shown. Scale bar indicates 10 µm.

Journal: Scientific Reports

Article Title: Oleanolic acid stimulation of cell migration involves a biphasic signaling mechanism

doi: 10.1038/s41598-022-17553-w

Figure Lengend Snippet: OA induces FAK phosphorylation and promotes its localization in focal adhesion with paxillin in Mv1Lu cells. ( a ) The activation of FAK was assessed by Western Blot at Tyr 925, at the indicated times in the presence of 5 µM OA, DMSO equivalent volume or EGF. Additionally, total protein expression was assayed: FAK. β-Actin was used as a loading control. Phospho-FAK intensity values in Western-blot were quantified by ImageJ to conduct a one-way ANOVA analysis showed on the plot (*p < 0.05, **p < 0.005, ***p < 0.001 and ****p < 0.0001). ( b ) Confluent Mv1Lu cells were scratched and allowed to migrate for 6 h. Pictures show the immunostaining with specific antibodies against phospho-FAK (Tyr 925) and paxillin. Co-staining with Hoechst-33258 was used to reveal nuclei. P-FAK: green. Paxillin: red. Nuclei: blue. ( c ) Pictures and graphs represent a colocalization analysis performed by Zeiss Efficient Navigation (ZEN) software. Colocalized pixels are highlighted in white at the immunostaining images. Graphs are dot plots representing both p-FAK and paxillin intensities in terms of number of pixels: p-FAK pixels on Y axis and paxillin pixels on X axis. The 3 quadrant (upper right) represents overlapped (common) pixels between both proteins. ( d ) Pictures of each condition (two) were divided in three horizontally distributed sectors. Pearson’s correlation coefficient in each sector of each condition was calculated by the average pixel intensity of p-FAK and paxillin overlapped pixels. The plot represents Pearson’s correlation values for each condition, each dot representing the value obtained in one sector. Asterisks indicate statistically significant differences between conditions according to one-way ANOVA statistical analysis: (*p < 0.05, **p < 0.005, ***p < 0.001 and ****p < 0.0001). This experiment was repeated at least three times. Representative images are shown. Scale bar indicates 10 µm.

Article Snippet: Mink Lung Epithelial (Mv1Lu) , , cells were grown in Eagle's Minimum Essential Medium (EMEM) (Biowest, Nuaillé, France).

Techniques: Phospho-proteomics, Activation Assay, Western Blot, Expressing, Control, Immunostaining, Staining, Software

EGFR and MEK inhibitors prevent OA-induced FAK localization at FA in Mv1Lu cells. ( a ) Confluent Mv1Lu cells were scratched and allowed to migrate for 6 h. Cells were treated 30 min before scratch and subsequent OA treatment with specific inhibitors 2,5 µM EGFRi, 50 µM MEKi and 15 µM JNKi. Pictures show the immunostaining with specific antibodies against phospho-FAK (Tyr 925) and paxillin. Co-staining with Hoechst-33258 was used to reveal nuclei. ( b ) The plot represents a colocalization analysis performed by Zeiss Efficient Navigation (ZEN) software. Pictures of each condition (two) were divided in three horizontally distributed sectors. Pearson’s correlation coefficient in each sector of each condition was calculated by the average pixel intensity of p-FAK and paxillin overlapped pixels. The plot represents Pearson’s correlation values for each condition, each dot representing the value obtained in one sector. Asterisks indicate statistically significant differences between conditions according to a one-way ANOVA statistical analysis: (*p < 0.05, **p < 0.005, ***p < 0.001 and ****p < 0.0001). This experiment was repeated at least three times. Representative images are shown. Scale bar indicates 10 µm.

Journal: Scientific Reports

Article Title: Oleanolic acid stimulation of cell migration involves a biphasic signaling mechanism

doi: 10.1038/s41598-022-17553-w

Figure Lengend Snippet: EGFR and MEK inhibitors prevent OA-induced FAK localization at FA in Mv1Lu cells. ( a ) Confluent Mv1Lu cells were scratched and allowed to migrate for 6 h. Cells were treated 30 min before scratch and subsequent OA treatment with specific inhibitors 2,5 µM EGFRi, 50 µM MEKi and 15 µM JNKi. Pictures show the immunostaining with specific antibodies against phospho-FAK (Tyr 925) and paxillin. Co-staining with Hoechst-33258 was used to reveal nuclei. ( b ) The plot represents a colocalization analysis performed by Zeiss Efficient Navigation (ZEN) software. Pictures of each condition (two) were divided in three horizontally distributed sectors. Pearson’s correlation coefficient in each sector of each condition was calculated by the average pixel intensity of p-FAK and paxillin overlapped pixels. The plot represents Pearson’s correlation values for each condition, each dot representing the value obtained in one sector. Asterisks indicate statistically significant differences between conditions according to a one-way ANOVA statistical analysis: (*p < 0.05, **p < 0.005, ***p < 0.001 and ****p < 0.0001). This experiment was repeated at least three times. Representative images are shown. Scale bar indicates 10 µm.

Article Snippet: Mink Lung Epithelial (Mv1Lu) , , cells were grown in Eagle's Minimum Essential Medium (EMEM) (Biowest, Nuaillé, France).

Techniques: Immunostaining, Staining, Software

Transiently overexpressed WWOX/TIAF1/p53 triad induces apoptosis, and determination of the kinetics of the triad formation. a L929 cells were electroporated with indicated plasmids. Overexpression of WWOX, TIAF1 and p53 induced apoptosis. Dominant-negative p53 (S46G) suppressed apoptosis mediated by p53 and TIAF1. EP: electroporation with medium only (Mean ± S.D., n = 3, * p < 0.05, student’s t test). b Ras rescue-based yeast two-hybrid analysis revealed the binding of TIAF1 to the N -terminal first WW domain of WWOX, as shown by the growth of yeast at 37 °C [ – ]. WWOX(Y33R) mutant abolished the binding. The SDR domain failed to bind TIAF1. In positive binding controls, MafB self-association and WWOX/p53 binding are shown, and empty pSos versus empty pMyr as negative controls. cDNAs constructed in the pSos are shown in the left, and pMyr in the right. c TNFα, at 100 ng/ml, rapidly upregulated the expression of TIAF1 in 30 min in L929 cells. Co-immunoprecipitation showed the binding of TIAF1 with WWOX. d By co-immunoprecipitation, TGF-β1 (5 ng/ml) had little or no effect on the binding of TIAF1 with pY-WWOX during treatment for 30 min in MCF7 cells. IgH: IgG heavy chain. e , f NCI-H1299 cells were transiently transfected with p53-DsRed, TIAF1-EGFP, and WWOX-ECFP. By 3-protein FRET analysis [ , ], Prima-1 induced p53 activation-dependent binding with WWOX and TIAF1 with time (see the number in red under FRETc columns, e Experiments were designed to let the FRET energy transfer from WWOX-ECFP to TIAF1-EGFP, and finally to p53-DsRed [ , ]. Prima-1 increased the triad complex formation in COS7 cells ( f ). g In Mv1Lu cells, TGF-β1 rapidly increased the triad complex formation in 1 h, followed by reduction ( n = 6; Student’s t test; experiments versus time 0 controls). h Prima-1 increased the binding of the first WW domain of WWOX with TIAF1 and p53 with time. Each bar represents an average of two experiments in ( f ) and ( h )

Journal: Cell Communication and Signaling : CCS

Article Title: A p53/TIAF1/WWOX triad exerts cancer suppression but may cause brain protein aggregation due to p53/WWOX functional antagonism

doi: 10.1186/s12964-019-0382-y

Figure Lengend Snippet: Transiently overexpressed WWOX/TIAF1/p53 triad induces apoptosis, and determination of the kinetics of the triad formation. a L929 cells were electroporated with indicated plasmids. Overexpression of WWOX, TIAF1 and p53 induced apoptosis. Dominant-negative p53 (S46G) suppressed apoptosis mediated by p53 and TIAF1. EP: electroporation with medium only (Mean ± S.D., n = 3, * p < 0.05, student’s t test). b Ras rescue-based yeast two-hybrid analysis revealed the binding of TIAF1 to the N -terminal first WW domain of WWOX, as shown by the growth of yeast at 37 °C [ – ]. WWOX(Y33R) mutant abolished the binding. The SDR domain failed to bind TIAF1. In positive binding controls, MafB self-association and WWOX/p53 binding are shown, and empty pSos versus empty pMyr as negative controls. cDNAs constructed in the pSos are shown in the left, and pMyr in the right. c TNFα, at 100 ng/ml, rapidly upregulated the expression of TIAF1 in 30 min in L929 cells. Co-immunoprecipitation showed the binding of TIAF1 with WWOX. d By co-immunoprecipitation, TGF-β1 (5 ng/ml) had little or no effect on the binding of TIAF1 with pY-WWOX during treatment for 30 min in MCF7 cells. IgH: IgG heavy chain. e , f NCI-H1299 cells were transiently transfected with p53-DsRed, TIAF1-EGFP, and WWOX-ECFP. By 3-protein FRET analysis [ , ], Prima-1 induced p53 activation-dependent binding with WWOX and TIAF1 with time (see the number in red under FRETc columns, e Experiments were designed to let the FRET energy transfer from WWOX-ECFP to TIAF1-EGFP, and finally to p53-DsRed [ , ]. Prima-1 increased the triad complex formation in COS7 cells ( f ). g In Mv1Lu cells, TGF-β1 rapidly increased the triad complex formation in 1 h, followed by reduction ( n = 6; Student’s t test; experiments versus time 0 controls). h Prima-1 increased the binding of the first WW domain of WWOX with TIAF1 and p53 with time. Each bar represents an average of two experiments in ( f ) and ( h )

Article Snippet: Cell lines used in this study included human breast MCF-7 and MDA-MB-231 cancer cells [ ], human prostate DU145 cells [ ], human monocytic U937 cells [ ], human lung p53-deficient NCI-H1299 [ ], murine L929 fibroblasts [ – ], monkey kidney SV40 virus-transformed COS7 fibroblasts [ , ], and primary mink lung epithelial Mv1Lu cells [ , ] (American Type Culture Collection).

Techniques: Over Expression, Dominant Negative Mutation, Electroporation, Binding Assay, Mutagenesis, Construct, Expressing, Immunoprecipitation, Transfection, Activation Assay

Amniotic membrane (AM) promotes cell protrusion generation and Paxillin expression in migrating Mv1Lu cells. ( a) Detailed pictures of the migrating edge of artificial wound assays treated with AM in combination with inhibitors. Scale Bar 50 µm. ( b) Western Blot of total protein extracts from sub-confluent Mv1Lu cells cultured in the presence of AM and/or inhibitors and collected after 24 hours. The dashed grey lines indicate that two distant parts of the very same blot were put together. ß-actin was used as loading control. (‡) Unspecific bands. ( c) Relative protein level plots generated from Western Blot quantification. C: serum starvation; JNKi: SP600125; MEKi: PD98059. Asterisks denote statistically significant differences between conditions according to ANOVA statistical analysis: (***) p < 0.001; (ns) not significant. All experiments were repeated at least three times. Representative pictures and results are shown.

Journal: Scientific Reports

Article Title: Amniotic membrane promotes focal adhesion remodeling to stimulate cell migration

doi: 10.1038/s41598-017-15509-z

Figure Lengend Snippet: Amniotic membrane (AM) promotes cell protrusion generation and Paxillin expression in migrating Mv1Lu cells. ( a) Detailed pictures of the migrating edge of artificial wound assays treated with AM in combination with inhibitors. Scale Bar 50 µm. ( b) Western Blot of total protein extracts from sub-confluent Mv1Lu cells cultured in the presence of AM and/or inhibitors and collected after 24 hours. The dashed grey lines indicate that two distant parts of the very same blot were put together. ß-actin was used as loading control. (‡) Unspecific bands. ( c) Relative protein level plots generated from Western Blot quantification. C: serum starvation; JNKi: SP600125; MEKi: PD98059. Asterisks denote statistically significant differences between conditions according to ANOVA statistical analysis: (***) p < 0.001; (ns) not significant. All experiments were repeated at least three times. Representative pictures and results are shown.

Article Snippet: Mink Lung Epithelial cells (Mv1Lu) , , , a kind gift from Dr. Inman, were grown in Eagle’s Minimum Essential Medium (EMEM) and spontaneously immortalized human keratinocyte (HaCaT) cells, obtained from ATCC, were cultured in Dulbecco’s Modified Eagle Medium (DMEM) high-glucose (Biowest, Nuaillé, France).

Techniques: Membrane, Expressing, Western Blot, Cell Culture, Control, Generated

Amniotic membrane (AM) treatment alters Paxillin distribution and focal structures arrangement in migrating Mv1Lu cells. ( a) Confocal microscopy images of Mv1Lu cells at the migrating edge of artificial wound assays. Scale Bar 50 µm. Juxtaposed field images were taken to show migration front from a wider perspective. ( b) 2.5x magnified detail from merged pictures in ( a ). Scale Bar 10 µm. ( c) Plots for average number and size of focal structures detected at the migrating leading edge. Asterisks denote statistically significant differences between conditions according to ANOVA statistical analysis: (*) p < 0.05, (**) p < 0.005 and (***) p < 0.001; (ns) not significant. Paxillin: green; Actin: red; Nuclei: blue; C: serum starvation; JNKi: SP600125; MEKi: PD98059; FS: focal structures. All the experiments were repeated at least three times. Representative pictures are shown.

Journal: Scientific Reports

Article Title: Amniotic membrane promotes focal adhesion remodeling to stimulate cell migration

doi: 10.1038/s41598-017-15509-z

Figure Lengend Snippet: Amniotic membrane (AM) treatment alters Paxillin distribution and focal structures arrangement in migrating Mv1Lu cells. ( a) Confocal microscopy images of Mv1Lu cells at the migrating edge of artificial wound assays. Scale Bar 50 µm. Juxtaposed field images were taken to show migration front from a wider perspective. ( b) 2.5x magnified detail from merged pictures in ( a ). Scale Bar 10 µm. ( c) Plots for average number and size of focal structures detected at the migrating leading edge. Asterisks denote statistically significant differences between conditions according to ANOVA statistical analysis: (*) p < 0.05, (**) p < 0.005 and (***) p < 0.001; (ns) not significant. Paxillin: green; Actin: red; Nuclei: blue; C: serum starvation; JNKi: SP600125; MEKi: PD98059; FS: focal structures. All the experiments were repeated at least three times. Representative pictures are shown.

Techniques: Membrane, Confocal Microscopy, Migration

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mv1lu mink lung epithelial cells (BioResource International Inc)

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