Journal: Cellular and Molecular Gastroenterology and Hepatology

Article Title: MFAP4 Deficiency Attenuates Liver Fibrosis by Regulating Hepatic Stellate Cell Fate Through Inhibition of the FAK/PI3K/NFκB Signaling Pathway

doi: 10.1016/j.jcmgh.2025.101548

Figure Lengend Snippet: The partial reversal of the MFAP4-induced phenotype by pathway inhibitors. The fibrotic and apoptotic phenotypes induced by rMFAP4 incubation in LX-2 cells and by MFAP4 overexpression in LX-2 cells can be partially reversed by the integrin αvβ3 inhibitors Cilengitide (1 μM) ( A-D ) and Cyclo(-RGDfK) (2 μM) ( G-H ). Quantitative analysis of Western blotting is shown on the right . ∗Indicates a statistical significance between the rMFAP4 or OE-MFAP4 group and the DMSO or OE-Vector group; #Indicates statistical significance between the rMFAP4 or OE-MFAP4 group and the rMFAP4 + inhibitor group or OE-MFAP4 + inhibitor group. ∗∗ P < .01, ∗∗∗ P < .001. # P < .05, ## P < .01, ### P < .001.

Article Snippet: Integrin inhibitors: cilengitide TFA (HY-16143, MCE) and Cyclo(-RGDfK) TFA (HY-P0023A, MCE).

Techniques: Incubation, Over Expression, Western Blot, Plasmid Preparation

Journal: Cellular and Molecular Gastroenterology and Hepatology

Article Title: MFAP4 Deficiency Attenuates Liver Fibrosis by Regulating Hepatic Stellate Cell Fate Through Inhibition of the FAK/PI3K/NFκB Signaling Pathway

doi: 10.1016/j.jcmgh.2025.101548

Figure Lengend Snippet: The relationship between MFAP4 and the activation of the FAK/PI3K/NFκB signaling pathway. ( A, B ) The integrin αvβ3 inhibitor Cilengitide (1 μM) partially reverses the activation of the FAK/PI3K/NFκB signaling pathway induced by rMFAP4 incubation or OE-MFAP4 in LX-2 cells. ( C, D ) Another integrin αvβ3 inhibitor, Cyclo(-RGDfK) (2 μM), partially reverses the activation of the FAK/PI3K/NFκB signaling pathway induced by rMFAP4 incubation or OE-MFAP4 in LX-2 cells. ( E, F ) The FAK-specific inhibitor Defactinib hydrochloride (10 μM) partially reverses the activation of the FAK/PI3K/NFκB signaling pathway induced by rMFAP4 incubation or OE-MFAP4 in LX-2 cells. Quantification of immunoblot results is shown on the right . ( G ) Immunofluorescence showing nuclear translocation of p-P65 in LX-2 cells after 24 hours of rMFAP4 incubation. Scale bars: 25 μm.

Article Snippet: Integrin inhibitors: cilengitide TFA (HY-16143, MCE) and Cyclo(-RGDfK) TFA (HY-P0023A, MCE).

Techniques: Activation Assay, Incubation, Western Blot, Immunofluorescence, Translocation Assay

Journal: Advanced Science

Article Title: Cyclic Arginine–Glycine–Aspartate‐Decorated Lipid Nanoparticle Targeting toward Inflammatory Lesions Involves Hitchhiking with Phagocytes

doi: 10.1002/advs.202100370

Figure Lengend Snippet: Figure 1. In vivo targeting kinetics studied with dynamic IVM. a–c) Snapshots and enlargements of Movie S1, Supporting Information, showing ring-like cRGD-NE agglomerates (a), as well as cRGD-NE agglomerates associated with circulating “black holes” (b,c). The rings and the “black holes” (indicated with arrowheads) were circular in shape with a diameter of 6–8 µm, which corresponds to the size of circulating neutrophils. d) Snapshots of a dynamic imaging series show binding events in angiogenic vasculature of 1–8 µm-sized cRGD-NE (red) agglomerates, appearing as “steps” in fluorescence versus time plots (each line represents the ROI signal intensity of a single binding event). e) cRAD-NE (red) extravasated gradually in the inflamed tissue. f) The averaged signal as a function of time for cRGD-NE (n = 4, 45 binding events) and cRAD-NE (n = 3). g) Targeting kinetics in angiogenic tumor tissue, observed with dynamic MRI in an earlier study (Δt = 21 s; n = 4 for each curve, Adapted with permission[21]). Scale bars: a–c = 10 µm; d,e = 50 µm. Error bars: f,g = SEM.

Article Snippet: [6] Half of the final NP formulation was conjugated with cRGD peptide (Peptides International, PCI-3699-PI) and the other half with control cRAD peptide (Peptides International, PCI-3959-PI) at 13.5 μg Adv.

Techniques: In Vivo, Imaging, Binding Assay

Journal: Advanced Science

Article Title: Cyclic Arginine–Glycine–Aspartate‐Decorated Lipid Nanoparticle Targeting toward Inflammatory Lesions Involves Hitchhiking with Phagocytes

doi: 10.1002/advs.202100370

Figure Lengend Snippet: Figure 2. Nanoemulsion association with immune cells and angiogenic tissue. a) High-speed imaging (Δt = 1.3 s) revealed both bound (white circles) and circulating cRGD-NE (red) positive cells (blood vessels delineated in yellow). b) cRGD-NE (Atto633-PE; red) accumulated extensively in cell-sized agglomerates in angiogenic vasculature adjacent to the wound (w) at 1 h post-injection. Several of these aggregates were also positive for co-injected cRAD-NE (Rhodamine-PE; green). c) cRGD-NE (red-hot look-up table to visualize colocalization with GFP) colocalizing with GFP positive endothelium (green) next to the wound (w). d) Z-stack with orthogonal projections showed non-endothelial cRGD-NE cell-sized agglomerates up to 24 h post- injection in the angiogenic vasculature (endothelial GFP; green). When cRGD-NE signal was enhanced (white box enlarged and enhanced), cRGD- NE colocalization with endothelium became evident. e) cRAD-NE (red) predominantly accumulated through passive diffusion from the vasculature (endothelial GFP; green), 1 h post-injection. Scale bars: b,c = 100 µm; a,e = 50 µm; d = 10 µm.

Article Snippet: [6] Half of the final NP formulation was conjugated with cRGD peptide (Peptides International, PCI-3699-PI) and the other half with control cRAD peptide (Peptides International, PCI-3959-PI) at 13.5 μg Adv.

Techniques: Imaging, Injection

Journal: Advanced Science

Article Title: Cyclic Arginine–Glycine–Aspartate‐Decorated Lipid Nanoparticle Targeting toward Inflammatory Lesions Involves Hitchhiking with Phagocytes

doi: 10.1002/advs.202100370

Figure Lengend Snippet: Figure 3. Ex vivo characterization of interactions between nanoemulsions and circulating immune cells. a–c) Ex vivo CLSM on immune cells isolated 5 min (a,b) and 10 min (c) post-injection of cRAD-NE (green) and cRGD-NE (red) showed that these cells associated with cRGD-NE to a much higher extent than with cRAD-NE. Cells in gray scale were imaged using transmission mode. (b) and (c) show orthogonal projections of z-stacks demonstrating the NE to be present on the cell membrane and intracellularly. d) Flow cytometry on circulating immune cells isolated 2 h after NE administration revealed myeloid-derived phagocytes to be the dominant population engaging the NE and confirmed that these cells associated with cRGD-NE to significantly higher extent than with cRAD-NE (n = 3; mean ± SEM). Flow cytometry histograms (Figure S5, Supporting Information) show data from representative animals revealing insignificant engagement of the NPs with lymphoid cells. Scale bars: a = 25 µm; b,c = 10 µm. p-values: * < 0.05.

Article Snippet: [6] Half of the final NP formulation was conjugated with cRGD peptide (Peptides International, PCI-3699-PI) and the other half with control cRAD peptide (Peptides International, PCI-3959-PI) at 13.5 μg Adv.

Techniques: Ex Vivo, Isolation, Injection, Transmission Assay, Membrane, Flow Cytometry, Derivative Assay

Journal: Advanced Science

Article Title: Cyclic Arginine–Glycine–Aspartate‐Decorated Lipid Nanoparticle Targeting toward Inflammatory Lesions Involves Hitchhiking with Phagocytes

doi: 10.1002/advs.202100370

Figure Lengend Snippet: Figure 4. Inflammation endothelium targeting by cRGD-LP. a) Snapshots of a dynamic imaging series show binding events in angiogenic vasculature of cRGD-LP (red) positive cells. b) These binding events appear as “steps” in fluorescence versus time plots for cRGD-LP (each line represents ROI signal intensity of a single binding event), while cRAD-LP gradually extravasate in the inflamed tissue. c) Snapshots from high-speed imaging (Δt = 1.3 s) 20 h post co-administration of cRGD-LP (red) and cRAD-LP (green). d) Orthogonal projections of z-stacks of white blood cells isolated 25 min post cRGD-LP (red) and cRAD-LP (green) co-administration. e) 6 h post-injection, colocalization between cRGD-LP (red) and GFP positive endothelium (green) as well as non-endothelial cell-sized cRGD-LP agglomerates bound in the vasculature were observed. f) Z-stack with orthogonal projections showing cRGD-LP (red) colocalization with GFP-positive endothelium (green) at 6 h post-injection. g) Flow cytometry on blood cells isolated 2 h after cRGD-LP (red) and cRAD-LP (blue) administration, revealed myeloid cells associating with cRGD-LP to significantly higher extent than with cRAD-LP (n = 6; mean ± SEM). Flow cytometry histograms (Figure S5, Supporting Information) show data from representative animals and confirm that LP also engaged insignificantly with lymphoid cells. Scale bars: a,c,e = 25 µm; d,f = 10 µm. p-values: * < 0.05, *** < 0.001, **** < 0.0001.

Article Snippet: [6] Half of the final NP formulation was conjugated with cRGD peptide (Peptides International, PCI-3699-PI) and the other half with control cRAD peptide (Peptides International, PCI-3959-PI) at 13.5 μg Adv.

Techniques: Imaging, Binding Assay, Isolation, Injection, Flow Cytometry

Journal: Carcinogenesis

Article Title: Leptin enhances cell migration in human chondrosarcoma cells through OBRl leptin receptor.

doi: 10.1093/carcin/bgp023

Figure Lengend Snippet: Fig. 1. Leptin-directed migration of human chondrosarcoma cells involves upregulation of avb3 integrins. JJ012 or SW1353 cells were incubated with various concentrations of leptin, and in vitro migration activities measured with the Transwell after 24 h (A and B). JJ012 cells were incubated with leptin for 24 h, and the cell surface avb3 integrin was determined using flow cytometry (C). Cells were incubated with leptin for 24 h, and the mRNA levels of av and b3 integrin was determined using qPCR (D and E). Cells were pretreated with avb3 monoclonal antibody (3 and 10 lg/ml), cyclic RGD (100 nM) or cyclic RAD (100 nM) for 30 min followed by stimulation with leptin. The in vitro migration activity was measured after 24 h (F). Total RNA were extracted from normal cartilage (lines 1–2), primary chondrocyte (lines 3–4), chondrosarcoma patients (lines 5–6) or from chondrosarcoma cell lines (SW1353 and JJ012) and subjected to qPCR analysis for av and b3 integrin (G). Results are expressed as the mean ± SEM. P ,0.05 compared with control; #P ,0.05 compared with leptin-treated group.

Article Snippet: A selective avb3 integrin antagonist cyclic RGD (cyclo-RGDfV) peptide and the cyclic RAD (cyclo-RADfV) peptide were purchased from Peptides International (Louisville, KY).

Techniques: Migration, Incubation, In Vitro, Cytometry, Activity Assay, Control

Journal: Carcinogenesis

Article Title: Leptin enhances cell migration in human chondrosarcoma cells through OBRl leptin receptor.

doi: 10.1093/carcin/bgp023

Figure Lengend Snippet: Fig. 2. OBRl receptor is involved in leptin-mediated migration of human chondrosarcoma cells. Total RNA were extracted from normal cartilage (lines 1–8), chondrosarcoma patients (lines 9–16) or from chondrosarcoma cell lines (SW1353 and JJ012) and subjected to qPCR analysis for OBRl and OBRs (A and B). Total RNA were extracted from primary chondrocyte (n 5 8), primary chondrosarcoma (n 5 8) or from chondrosarcoma cell lines (SW1353 and JJ012) and subjected to qPCR analysis for OBRl and OBRs (C and D). The migration activity of each cells measured in vitro with the Transwell chamber after 24 h showed a significantly higher invasion activity in primary chondrosarcoma and chondrosarcoma cell lines as compared with primary chondrocyte (E). Cells were transfected with OBRl antisense (AS)-ODN or missense (MM)-ODN for 24 h followed by stimulation with leptin, and in vitro migration (F) and cell surface avb3 integrin (G) were measured with the Transwell and flow cytometry after 24 h. Results are expressed as the mean ± SEM. P ,0.05 compared with control; #P ,0.05 compared with leptin-treated group.

Article Snippet: A selective avb3 integrin antagonist cyclic RGD (cyclo-RGDfV) peptide and the cyclic RAD (cyclo-RADfV) peptide were purchased from Peptides International (Louisville, KY).

Techniques: Migration, Activity Assay, In Vitro, Transfection, Cytometry, Control

Journal: Carcinogenesis

Article Title: Leptin enhances cell migration in human chondrosarcoma cells through OBRl leptin receptor.

doi: 10.1093/carcin/bgp023

Figure Lengend Snippet: Fig. 3. IRS-1 pathway is involved in leptin-mediated migration and integrin upregulation in human chondrosarcoma cells. (A) JJ012 cells were incubated with leptin for indicated time intervals. Cell lysates were immunoprecipitated (IP) with anti-IRS-1 antibody. IP proteins were separated by sodium dodecyl sulfate– polyacrylamide gel electrophoresis and immunoblotted (WB) with anti-phosphotyrosine (PY). Cells were transfected with IRS-1 or control siRNA for 24 h followed by stimulation with leptin, and in vitro migration (B and C) and cell surface avb3 integrin (D) were measured with the Transwell and flow cytometry after 24 h. Results are expressed as the mean ± SEM. P ,0.05 compared with control; #P ,0.05 compared with leptin-treated group.

Article Snippet: A selective avb3 integrin antagonist cyclic RGD (cyclo-RGDfV) peptide and the cyclic RAD (cyclo-RADfV) peptide were purchased from Peptides International (Louisville, KY).

Techniques: Migration, Incubation, Immunoprecipitation, Polyacrylamide Gel Electrophoresis, Transfection, Control, In Vitro, Cytometry

Journal: Carcinogenesis

Article Title: Leptin enhances cell migration in human chondrosarcoma cells through OBRl leptin receptor.

doi: 10.1093/carcin/bgp023

Figure Lengend Snippet: Fig. 4. PI3K/Akt pathway is involved in leptin-mediated migration and integrin upregulation in human chondrosarcoma cells. (A; upper panel) JJ012 cells were incubated with leptin for various time intervals and cell lysates were immunoprecipitated (IP) with anti-p85 antibody. IP proteins were separated by sodium dodecyl sulfate–polyacrylamide gel electrophoresis and immunoblotted (WB) with anti-phosphotyrosine (PY). (A; lower panel) JJ012 cells were incubated with leptin for various time intervals, and Akt phosphorylation was determined by immunoblotting using phospho-Akt-specific antibody. (B) Cells were pretreated for 30 min with Ly294002 and Akt inhibitor followed by stimulation with leptin, and cell surface a2b1 integrin were measured by flow cytometry. (C) Cells were pretreated for 30 min with Ly294002 (10 lM) and Akt inhibitor (10 lM) or transfected with dominant-negative (DN) mutant of p85 and Akt for 24 h followed by stimulation with leptin, and in vitro migrations were measured with the Transwell after 24 h. Results are expressed as the mean ± SE. P ,0.05 compared with control; #P ,0.05 compared with leptin-treated group.

Article Snippet: A selective avb3 integrin antagonist cyclic RGD (cyclo-RGDfV) peptide and the cyclic RAD (cyclo-RADfV) peptide were purchased from Peptides International (Louisville, KY).

Techniques: Migration, Incubation, Immunoprecipitation, Polyacrylamide Gel Electrophoresis, Phospho-proteomics, Western Blot, Cytometry, Transfection, Dominant Negative Mutation, Mutagenesis, In Vitro, Control

Journal: Carcinogenesis

Article Title: Leptin enhances cell migration in human chondrosarcoma cells through OBRl leptin receptor.

doi: 10.1093/carcin/bgp023

Figure Lengend Snippet: Fig. 5. Leptin induces cells migration and integrin upregulation through NF-jB. (A) Cells were pretreated for 30 min with PDTC (10 lM) or TPCK (3 lM) followed by stimulation with leptin, and in vitro migration was measured with the Transwell after 24 h. (B) Cells were pretreated for 30 min with PDTC (10 lM) or TPCK (3 lM) followed by stimulation with leptin for 24 h, and the cell surface avb3 integrin was measured by flow cytometry. (C) JJ012 cells were incubated with leptin for indicated time intervals, and p-IKKa/b, p-IjBa and p-p65 expression was determined by western blot analysis. (D) JJ012 cells were transfected with dominant-negative (DN) mutant of IKKa or IKKb for 24 h followed by stimulation with leptin, and in vitro migrations were measured with the Transwell after 24 h. JJ012 cells transiently transfected with jB-luciferase plasmid for 24 h and then pretreated with Ly294002, Akt inhibitor, PDTC and TPCK (E) for 30 min or cotransfection with p85, Akt, IKKa and IKKb mutant (F), before incubation with leptin for 24 h. Luciferase activity was measured, and the results were normalized to the b-galactosidase activity. Results are expressed as the mean ± SE. P ,0.05 compared with control; #P ,0.05 compared with leptin-treated group.

Article Snippet: A selective avb3 integrin antagonist cyclic RGD (cyclo-RGDfV) peptide and the cyclic RAD (cyclo-RADfV) peptide were purchased from Peptides International (Louisville, KY).

Techniques: Migration, In Vitro, Cytometry, Incubation, Expressing, Western Blot, Transfection, Dominant Negative Mutation, Mutagenesis, Luciferase, Plasmid Preparation, Cotransfection, Activity Assay, Control

Journal: ACS nano

Article Title: A Programmable DNA Origami Nanospring That Reports Dynamics of Single Integrin Motion, Force Magnitude and Force Orientation in Living Cells.

doi: 10.1021/acsnano.2c12545

Figure Lengend Snippet: Figure 1. Design of the 4HB DNA NS structure. (a) A cylinder model of the 4HB square lattice (see cross-section). Each cylindrical rod represents a single DNA double helix. Two insertion and deletion sites that produce a superhelical strain are shown in blue and red, respectively. (b) CanDo, a 3D DNA origami structure prediction server,24 predicted a coil structure. Single-stranded DNA (ssDNA) handles projecting out from both ends are shown as red and orange lines, respectively. The complementary ssDNA antihandles are modified with adhesive peptide (cRGDfK, blue hexagon) to the extracellular domain of integrins and biotin (black circle) to attach the NS to the bottom of the dish. (c) An AFM image of the 4HB-NS. The shape was flexible enough to measure single integrin traction force but also showed repetitive bending or expected loops. Scale bar, 200 nm.

Article Snippet: For positive control experiments (cell adhesion with biotinylated cRGDfK), after neutravidin was washed out, 200 μL of biotinylated cRGDfK (1−150 nM in DNA origami buffer, Peptides International, PCI-3697-PI) was added on the glass-bottomed dish, and the mixture was incubated for 10 min. Unbound biotinylated cRGDfK was washed out using a DNA origami buffer.

Techniques: Modification, Adhesive

Journal: ACS nano

Article Title: A Programmable DNA Origami Nanospring That Reports Dynamics of Single Integrin Motion, Force Magnitude and Force Orientation in Living Cells.

doi: 10.1021/acsnano.2c12545

Figure Lengend Snippet: Figure 2. Visualizing NS extensions by single integrins. (a) A typical fluorescence image of Cy3 NS (red) and GFP-paxillin (white) expressed in HFFs and observed by TIRFM. The boxed area is expanded in (b). Scale bar, 10 μm for (a) and 2 μm for (b). The right cartoon in (b) shows NSs attached with integrins via cRGDfK and the glass surface via the biotin−avidin system. (c) A histogram of flattening NS fluorescence spots located outside the cells. The flattening was calculated as 1 −σshort/σlong, where σshort and σlong, respectively, denote the standard deviation for the short and long axes when the fluorescence spot was fit to a 2D Gaussian function. (d, e) Histograms of flattening NS fluorescence spots within (d) and outside FAs underneath cells (e). (n = 370, 428, and 292 molecules from 6, 6, and 5 cells for (c, d, e), respectively.) (f, g) Time trajectories of the angle between the long axis of NS and the horizontal direction of the picture for the spots undergoing Brownian motion (f) and stretching within FAs (g). Each color represents an individual NS.

Article Snippet: For positive control experiments (cell adhesion with biotinylated cRGDfK), after neutravidin was washed out, 200 μL of biotinylated cRGDfK (1−150 nM in DNA origami buffer, Peptides International, PCI-3697-PI) was added on the glass-bottomed dish, and the mixture was incubated for 10 min. Unbound biotinylated cRGDfK was washed out using a DNA origami buffer.

Techniques: Fluorescence, Avidin-Biotin Assay, Standard Deviation

Journal: ACS nano

Article Title: A Programmable DNA Origami Nanospring That Reports Dynamics of Single Integrin Motion, Force Magnitude and Force Orientation in Living Cells.

doi: 10.1021/acsnano.2c12545

Figure Lengend Snippet: Figure 5. NS force sensor indicated dynamics of loaded force and single integrin motions in living cells. (a−c) Representative traces showing the length of the NS (top), loaded force on the NS (middle), and angle of the NS (bottom) for an integrin-bound NS. The force trace was calculated from the NS length. The thin lines indicate raw data; the bold lines indicate moving averages. (d, e) The colors of the traces correspond to (a−c), and the gradations of the colors correspond to the time course. Representative traces showing a single integrin motion tethered with an NS (d) and the force vector (e) in polar coordinates. Colors correspond to (a−c). (f) Histograms of the loaded force distributions for cRGDfK-labeled NS (red, n = 59 molecules; N = 23 cells) and cRGDfK-less NS (blue, n = 138 molecules; N = 24 cells) underneath the cells.

Article Snippet: For positive control experiments (cell adhesion with biotinylated cRGDfK), after neutravidin was washed out, 200 μL of biotinylated cRGDfK (1−150 nM in DNA origami buffer, Peptides International, PCI-3697-PI) was added on the glass-bottomed dish, and the mixture was incubated for 10 min. Unbound biotinylated cRGDfK was washed out using a DNA origami buffer.

Techniques: Plasmid Preparation, Labeling

Journal: Cell Adhesion & Migration

Article Title: Inhibition of Integrin α v β 3 -FAK-MAPK signaling constrains the invasion of T-ALL cells

doi: 10.1080/19336918.2023.2191913

Figure Lengend Snippet: The cell invasion of Jurkat cells with in vitro integrin β3 inhibition. (a) The transwell analysis of invasion of Jurkat cells treated with cyclo(rgdyk) in concentration ladder of 0, 0.2, 0.4, 0.6, 0.8, 1.0 mmol/L after 24 hours. The migrated cells were stained with crystal violet. (b) Column graph of invasive Jurkat cells treated with cyclo(rgdyk) in concentration ladder of 0, 0.2, 0.4, 0.6, 0.8, 1.0 mmol/L after 24 hours detected by transwell analysis. ***P<.01, ***P<.001. (c) The transwell analysis of invasion of control Jurkat cells(ctrl) and those treated with integrin αvβ3 specific antibodies(anti-ITGαvβ3). The migrated cells were stained with crystal violet. (d) Column graph of invasion of control Jurkat cells(ctrl) and those treated with integrin αvβ3 specific antibodies(anti-ITGαvβ3) detected by transwell analysis. **P<.001.

Article Snippet: The specific integrin inhibitor cyclo(Arg-Gly-Asp-d-Tyr-Lys) peptides (cyclo(RGDyK)(S7844; Selleck Chemicals) was used for disturbing the function of integrin.

Techniques: In Vitro, Inhibition, Concentration Assay, Staining, Control

Journal: Cell Adhesion & Migration

Article Title: Inhibition of Integrin α v β 3 -FAK-MAPK signaling constrains the invasion of T-ALL cells

doi: 10.1080/19336918.2023.2191913

Figure Lengend Snippet: Interference of ITGB3 expression decreased the invasiveness of Jurkat cells and Molt-4 cells.(a) the expression of ITGB3 mRNA in common Jurkat cells (ctrl), cells infected by scramble control RNAi virus (sh-NC) and ITGB3 RNAi virus interfered cells (sh-ITGB3). The relative expression level was presented as the ratio of integrin β3 and β-actin, which was applied as endogenous control. ***P<.001, ***P<.01. ( b ) The expression of ITGB3 mRNA in common MOLT-4 cells (ctrl), blank control cells infected by scramble control RNAi virus (sh-NC) and ITGB3 RNAi virus interfered cells (sh-ITGB3). The expression was **P<.001, ***P<.05. (c) The expression of integrin β3 in Jurkat(ctrl), sh-NC and sh-ITGB3 cells detected by Western blot. (d) The expression of integrin β3 in MOLT-4 (ctrl), sh-NC and sh-ITGB3 cells detected by Western blot. The expression of β-actin was used as internal control. (e) The migratory cell counts of Jurkat (ctrl), sh-NC and sh-ITGB3 cells in transwell assays. (f) The column graph of migratory cell counts of Jurkat, BC and shITGB3 cells. ***P<.001. (g) The migratory cell counts of MOLT-4 (ctrl), sh-NC and sh-ITGB3 cells in transwell assays. (h) The column graph of migratory cell counts of MOLT-4 (ctrl), sh-NC and sh-ITGB3 cells. ***P<.001.

Article Snippet: The specific integrin inhibitor cyclo(Arg-Gly-Asp-d-Tyr-Lys) peptides (cyclo(RGDyK)(S7844; Selleck Chemicals) was used for disturbing the function of integrin.

Techniques: Expressing, Infection, Control, Virus, Western Blot

Journal: Cell Adhesion & Migration

Article Title: Inhibition of Integrin α v β 3 -FAK-MAPK signaling constrains the invasion of T-ALL cells

doi: 10.1080/19336918.2023.2191913

Figure Lengend Snippet: Integrin αV not integrin α2b interact with integrin β3 to regulate the migration of T-ALL cells. (a) The transwell assays for T-ALL cell lines, Jurkat and Molt-4, treated with solution control (ctrl), anti-integrin αvβ3 antibodies (anti-itgαvβ3) and anti-integrin α2bβ3 antibodies (anti- itgα2bβ3), respectively. (b, c) The statistical comparison of migrated T-ALL cell count (B: Jurkat, C: Molt-4) between three groups in transwell assays in (A). ***P<.001. (d) Western blot for the immunoprecipitation of α chain integrin interact with integrin β3. IgG and input represent the negative and positive control, respectively.

Article Snippet: The specific integrin inhibitor cyclo(Arg-Gly-Asp-d-Tyr-Lys) peptides (cyclo(RGDyK)(S7844; Selleck Chemicals) was used for disturbing the function of integrin.

Techniques: Migration, Control, Comparison, Cell Counting, Western Blot, Immunoprecipitation, Positive Control