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( A ) Binding affinity ( K D ) of <t>the</t> <t>anti-uPAR</t> mAb to human uPAR assessed by SPR. ( B and C ) IF (B) and immunoelectron microscopy (C) analysis of anti-uPAR binding to uPAR-expressing HEK-293T cells. DAPI, 4′,6-diamidino-2-phenylindole. ( D and E ) Detection of different forms of uPAR by the anti-uPAR mAb shown by FCM (D) and Western blotting (E). MFI, mean fluorescence intensity. ( F ) Competitive binding assay showing the ability of anti-uPAR to inhibit <t>uPA</t> binding to uPAR, as shown by FCM. ( G ) Western blotting of phosphorylated ERK ( p -ERK) and total ERK (T-ERK) in SNU-216 cells pretreated with anti-uPAR or CTRL mAb after pro-uPA stimulation. ( H to K ) Growth curves (H and I), transwell invasion assay (J), and cell adhesion assay (K) of AGS and SNU-216 cells treated with anti-uPAR or CTRL mAb. Data are expressed as means ± SEM (* P < 0.05, ** P < 0.01, and *** P < 0.001).
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recombinant human pro upas356a upa  (Sino Biological)
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( A ) Binding affinity ( K D ) of <t>the</t> <t>anti-uPAR</t> mAb to human uPAR assessed by SPR. ( B and C ) IF (B) and immunoelectron microscopy (C) analysis of anti-uPAR binding to uPAR-expressing HEK-293T cells. DAPI, 4′,6-diamidino-2-phenylindole. ( D and E ) Detection of different forms of uPAR by the anti-uPAR mAb shown by FCM (D) and Western blotting (E). MFI, mean fluorescence intensity. ( F ) Competitive binding assay showing the ability of anti-uPAR to inhibit <t>uPA</t> binding to uPAR, as shown by FCM. ( G ) Western blotting of phosphorylated ERK ( p -ERK) and total ERK (T-ERK) in SNU-216 cells pretreated with anti-uPAR or CTRL mAb after pro-uPA stimulation. ( H to K ) Growth curves (H and I), transwell invasion assay (J), and cell adhesion assay (K) of AGS and SNU-216 cells treated with anti-uPAR or CTRL mAb. Data are expressed as means ± SEM (* P < 0.05, ** P < 0.01, and *** P < 0.001).
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( A ) Binding affinity ( K D ) of <t>the</t> <t>anti-uPAR</t> mAb to human uPAR assessed by SPR. ( B and C ) IF (B) and immunoelectron microscopy (C) analysis of anti-uPAR binding to uPAR-expressing HEK-293T cells. DAPI, 4′,6-diamidino-2-phenylindole. ( D and E ) Detection of different forms of uPAR by the anti-uPAR mAb shown by FCM (D) and Western blotting (E). MFI, mean fluorescence intensity. ( F ) Competitive binding assay showing the ability of anti-uPAR to inhibit <t>uPA</t> binding to uPAR, as shown by FCM. ( G ) Western blotting of phosphorylated ERK ( p -ERK) and total ERK (T-ERK) in SNU-216 cells pretreated with anti-uPAR or CTRL mAb after pro-uPA stimulation. ( H to K ) Growth curves (H and I), transwell invasion assay (J), and cell adhesion assay (K) of AGS and SNU-216 cells treated with anti-uPAR or CTRL mAb. Data are expressed as means ± SEM (* P < 0.05, ** P < 0.01, and *** P < 0.001).
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( A ) Binding affinity ( K D ) of <t>the</t> <t>anti-uPAR</t> mAb to human uPAR assessed by SPR. ( B and C ) IF (B) and immunoelectron microscopy (C) analysis of anti-uPAR binding to uPAR-expressing HEK-293T cells. DAPI, 4′,6-diamidino-2-phenylindole. ( D and E ) Detection of different forms of uPAR by the anti-uPAR mAb shown by FCM (D) and Western blotting (E). MFI, mean fluorescence intensity. ( F ) Competitive binding assay showing the ability of anti-uPAR to inhibit <t>uPA</t> binding to uPAR, as shown by FCM. ( G ) Western blotting of phosphorylated ERK ( p -ERK) and total ERK (T-ERK) in SNU-216 cells pretreated with anti-uPAR or CTRL mAb after pro-uPA stimulation. ( H to K ) Growth curves (H and I), transwell invasion assay (J), and cell adhesion assay (K) of AGS and SNU-216 cells treated with anti-uPAR or CTRL mAb. Data are expressed as means ± SEM (* P < 0.05, ** P < 0.01, and *** P < 0.001).
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( A ) Binding affinity ( K D ) of <t>the</t> <t>anti-uPAR</t> mAb to human uPAR assessed by SPR. ( B and C ) IF (B) and immunoelectron microscopy (C) analysis of anti-uPAR binding to uPAR-expressing HEK-293T cells. DAPI, 4′,6-diamidino-2-phenylindole. ( D and E ) Detection of different forms of uPAR by the anti-uPAR mAb shown by FCM (D) and Western blotting (E). MFI, mean fluorescence intensity. ( F ) Competitive binding assay showing the ability of anti-uPAR to inhibit <t>uPA</t> binding to uPAR, as shown by FCM. ( G ) Western blotting of phosphorylated ERK ( p -ERK) and total ERK (T-ERK) in SNU-216 cells pretreated with anti-uPAR or CTRL mAb after pro-uPA stimulation. ( H to K ) Growth curves (H and I), transwell invasion assay (J), and cell adhesion assay (K) of AGS and SNU-216 cells treated with anti-uPAR or CTRL mAb. Data are expressed as means ± SEM (* P < 0.05, ** P < 0.01, and *** P < 0.001).
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( A ) Binding affinity ( K D ) of <t>the</t> <t>anti-uPAR</t> mAb to human uPAR assessed by SPR. ( B and C ) IF (B) and immunoelectron microscopy (C) analysis of anti-uPAR binding to uPAR-expressing HEK-293T cells. DAPI, 4′,6-diamidino-2-phenylindole. ( D and E ) Detection of different forms of uPAR by the anti-uPAR mAb shown by FCM (D) and Western blotting (E). MFI, mean fluorescence intensity. ( F ) Competitive binding assay showing the ability of anti-uPAR to inhibit <t>uPA</t> binding to uPAR, as shown by FCM. ( G ) Western blotting of phosphorylated ERK ( p -ERK) and total ERK (T-ERK) in SNU-216 cells pretreated with anti-uPAR or CTRL mAb after pro-uPA stimulation. ( H to K ) Growth curves (H and I), transwell invasion assay (J), and cell adhesion assay (K) of AGS and SNU-216 cells treated with anti-uPAR or CTRL mAb. Data are expressed as means ± SEM (* P < 0.05, ** P < 0.01, and *** P < 0.001).
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Image Search Results


( A ) Binding affinity ( K D ) of the anti-uPAR mAb to human uPAR assessed by SPR. ( B and C ) IF (B) and immunoelectron microscopy (C) analysis of anti-uPAR binding to uPAR-expressing HEK-293T cells. DAPI, 4′,6-diamidino-2-phenylindole. ( D and E ) Detection of different forms of uPAR by the anti-uPAR mAb shown by FCM (D) and Western blotting (E). MFI, mean fluorescence intensity. ( F ) Competitive binding assay showing the ability of anti-uPAR to inhibit uPA binding to uPAR, as shown by FCM. ( G ) Western blotting of phosphorylated ERK ( p -ERK) and total ERK (T-ERK) in SNU-216 cells pretreated with anti-uPAR or CTRL mAb after pro-uPA stimulation. ( H to K ) Growth curves (H and I), transwell invasion assay (J), and cell adhesion assay (K) of AGS and SNU-216 cells treated with anti-uPAR or CTRL mAb. Data are expressed as means ± SEM (* P < 0.05, ** P < 0.01, and *** P < 0.001).

Journal: Science Advances

Article Title: Therapeutic strategies targeting uPAR potentiate anti–PD-1 efficacy in diffuse-type gastric cancer

doi: 10.1126/sciadv.abn3774

Figure Lengend Snippet: ( A ) Binding affinity ( K D ) of the anti-uPAR mAb to human uPAR assessed by SPR. ( B and C ) IF (B) and immunoelectron microscopy (C) analysis of anti-uPAR binding to uPAR-expressing HEK-293T cells. DAPI, 4′,6-diamidino-2-phenylindole. ( D and E ) Detection of different forms of uPAR by the anti-uPAR mAb shown by FCM (D) and Western blotting (E). MFI, mean fluorescence intensity. ( F ) Competitive binding assay showing the ability of anti-uPAR to inhibit uPA binding to uPAR, as shown by FCM. ( G ) Western blotting of phosphorylated ERK ( p -ERK) and total ERK (T-ERK) in SNU-216 cells pretreated with anti-uPAR or CTRL mAb after pro-uPA stimulation. ( H to K ) Growth curves (H and I), transwell invasion assay (J), and cell adhesion assay (K) of AGS and SNU-216 cells treated with anti-uPAR or CTRL mAb. Data are expressed as means ± SEM (* P < 0.05, ** P < 0.01, and *** P < 0.001).

Article Snippet: One group (1 × 10 6 cells in 100 μl of staining buffer) was treated with 1 μg of His-tagged pro-uPA (Sino Biological, 10815-H08H) plus 1 μg of the anti-uPAR mAb in the dark at 4°C for 30 min.

Techniques: Binding Assay, Immuno-Electron Microscopy, Expressing, Western Blot, Fluorescence, Competitive Binding Assay, Transwell Invasion Assay, Cell Adhesion Assay

We identify uPAR as an immune-related cell surface protein that is specifically overexpressed in DGC with a relatively high positivity rate and a promising therapeutic potential. Our anti-uPAR mAb targets the DII-DIII region of uPAR and blocks uPA binding to its receptor, thereby inhibiting uPAR-dependent ERK activation and downstream signalings involved in cell proliferation, migration, and adhesion. Moreover, the anti-uPAR mAb stimulates infiltration of cytotoxic CD8 + T cells, induces robust ADCC and CDC, and augments the antitumor efficacy of PD-1 blockade therapy.

Journal: Science Advances

Article Title: Therapeutic strategies targeting uPAR potentiate anti–PD-1 efficacy in diffuse-type gastric cancer

doi: 10.1126/sciadv.abn3774

Figure Lengend Snippet: We identify uPAR as an immune-related cell surface protein that is specifically overexpressed in DGC with a relatively high positivity rate and a promising therapeutic potential. Our anti-uPAR mAb targets the DII-DIII region of uPAR and blocks uPA binding to its receptor, thereby inhibiting uPAR-dependent ERK activation and downstream signalings involved in cell proliferation, migration, and adhesion. Moreover, the anti-uPAR mAb stimulates infiltration of cytotoxic CD8 + T cells, induces robust ADCC and CDC, and augments the antitumor efficacy of PD-1 blockade therapy.

Article Snippet: One group (1 × 10 6 cells in 100 μl of staining buffer) was treated with 1 μg of His-tagged pro-uPA (Sino Biological, 10815-H08H) plus 1 μg of the anti-uPAR mAb in the dark at 4°C for 30 min.

Techniques: Binding Assay, Activation Assay, Migration