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mouse plau upa (MedChemExpress)

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MedChemExpress mouse plau upa
Mouse Plau Upa, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 91 stars, based on 1 article reviews

mouse plau upa - by Bioz Stars, 2026-06

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Sequences of the primers used for real-time RT-PCR.

Journal: Frontiers in Immunology

Article Title: Crucial Involvement of IL-6 in Thrombus Resolution in Mice via Macrophage Recruitment and the Induction of Proteolytic Enzymes

doi: 10.3389/fimmu.2019.03150

Figure Lengend Snippet: Sequences of the primers used for real-time RT-PCR.

Article Snippet: The following mAbs and polyclonal Abs (pAbs) were used for immunohistochemical and double-color immunofluorescence analyses: rat anti-mouse F4/80 mAb (Dainippon Pharmaceutical Company, Japan), mouse anti-IL-6 mAb (Santa Cruz Biotechnology, Dallas, Texas), rabbit anti-mouse IL-6 pAbs, rabbit anti-mouse CCL2 pAbs (Novus Biologicals, Centennial, CO), goat anti-mouse MMP-2 pAbs, goat anti-mouse MMP-9 pAbs (Santa Cruz Biotechnology, Dallas, Texas), rabbit anti-mouse PLAU (uPA) pAbs, rabbit anti-mouse tPA pAbs, rabbit anti-mouse PAI-1 pAbs (Santa Cruz Biotechnology, Dallas, TX), mouse anti-mouse Col1A2 mAb (Santa Cruz Biotechnology), rabbit anti-mouse myeloperoxidase (MPO) pAbs (Neomarkers, Fremont, CA), rabbit anti-mouse CD3 mAb (Abcam, Tokyo, Japan), cyanine dye 3-conjugated donkey anti-rat IgG pAbs, cyanine dye 3-conjugated donkey anti-goat IgG, fluorescein isothiocyanate (FITC)-conjugated donkey anti-rat IgG pAbs, and FITC-conjugated donkey anti-rabbit IgG pAbs (Jackson ImmunoResearch Laboratories, West Grove, PA).

Techniques: Sequencing

Intrathrombotic expression of IL-6 in wild-type (WT) mice after inferior vena cava (IVC) ligation. (A) Il6 gene expression was examined by real-time reverse transcription (RT)–PCR as described in section Materials and Methods. All values represent mean ± SEM ( n = 6). (B) Intrathrombotic IL-6 protein levels were determined by ELISA. All values represent mean ± SEM ( n = 6). (C) Immunohistochemical analysis of intrathrombotic IL-6 expression (original magnification, ×100, upper panel; ×400, lower panel). (D) A double-color immunofluorescence analysis of IL-6-expressing cells in the thrombus. The samples were immunostained with the combination of anti-F4/80 mAb and anti-IL-6 pAbs as described in section Materials and Methods. The fluorescent images were digitally merged in the right panel. Representative results from six independent experiments are shown here [original magnification, ×400; blue, nuclear staining by 4′,6-diamidino-2-phenylindole (DAPI)].

Journal: Frontiers in Immunology

Article Title: Crucial Involvement of IL-6 in Thrombus Resolution in Mice via Macrophage Recruitment and the Induction of Proteolytic Enzymes

doi: 10.3389/fimmu.2019.03150

Figure Lengend Snippet: Intrathrombotic expression of IL-6 in wild-type (WT) mice after inferior vena cava (IVC) ligation. (A) Il6 gene expression was examined by real-time reverse transcription (RT)–PCR as described in section Materials and Methods. All values represent mean ± SEM ( n = 6). (B) Intrathrombotic IL-6 protein levels were determined by ELISA. All values represent mean ± SEM ( n = 6). (C) Immunohistochemical analysis of intrathrombotic IL-6 expression (original magnification, ×100, upper panel; ×400, lower panel). (D) A double-color immunofluorescence analysis of IL-6-expressing cells in the thrombus. The samples were immunostained with the combination of anti-F4/80 mAb and anti-IL-6 pAbs as described in section Materials and Methods. The fluorescent images were digitally merged in the right panel. Representative results from six independent experiments are shown here [original magnification, ×400; blue, nuclear staining by 4′,6-diamidino-2-phenylindole (DAPI)].

Techniques: Expressing, Ligation, Gene Expression, Reverse Transcription, Reverse Transcription Polymerase Chain Reaction, Enzyme-linked Immunosorbent Assay, Immunohistochemical staining, Immunofluorescence, Staining

Intrathrombotic expression of proteolytic enzymes in wild-type (WT) and Il6 −/− mice. (A–C) A double-color immunofluorescence analysis of MMP-2-, MMP-9-, or PLAU-expressing cells in the thrombus. The fluorescent images were digitally merged in the right panel. Representative results from six independent experiments are shown here [original magnification, ×400; blue, nuclear staining by 4′,6-diamidino-2-phenylindole (DAPI)]. (D–F) Intrathrombotic gene expression of Mmp2 (D) , Mmp9 (E) , and Plau (F) after inferior vena cava (IVC) ligation. Each gene expression was determined by real-time reverse transcription (RT)–PCR as described in section Materials and Methods. All values represent the mean ± SEM ( n = 6 animals). * p < 0.05, ** p < 0.01, WT vs. Il6 −/− .

Journal: Frontiers in Immunology

Article Title: Crucial Involvement of IL-6 in Thrombus Resolution in Mice via Macrophage Recruitment and the Induction of Proteolytic Enzymes

doi: 10.3389/fimmu.2019.03150

Figure Lengend Snippet: Intrathrombotic expression of proteolytic enzymes in wild-type (WT) and Il6 −/− mice. (A–C) A double-color immunofluorescence analysis of MMP-2-, MMP-9-, or PLAU-expressing cells in the thrombus. The fluorescent images were digitally merged in the right panel. Representative results from six independent experiments are shown here [original magnification, ×400; blue, nuclear staining by 4′,6-diamidino-2-phenylindole (DAPI)]. (D–F) Intrathrombotic gene expression of Mmp2 (D) , Mmp9 (E) , and Plau (F) after inferior vena cava (IVC) ligation. Each gene expression was determined by real-time reverse transcription (RT)–PCR as described in section Materials and Methods. All values represent the mean ± SEM ( n = 6 animals). * p < 0.05, ** p < 0.01, WT vs. Il6 −/− .

Techniques: Expressing, Immunofluorescence, Staining, Gene Expression, Ligation, Reverse Transcription, Reverse Transcription Polymerase Chain Reaction

The effects of anti-IL-6 antibody (Ab) and recombinant murine IL-6 (rIL-6) in wild-type (WT) mice on thrombus resolution. (A–F) WT mice were intraperitoneally administered with anti-IL-6 as described in section Materials and Methods. (A) Macroscopic appearance of venous thrombi obtained from WT mice treated with anti-IL-6 Ab or control IgG at 10 days after inferior vena cava (IVC) ligation. Representative results from six independent animals are shown here. Thrombus weights (B) and thrombosed blood flow (C) were measured at 10 days after IVC ligation. All values represent the mean ± SEM ( n = 6 animals). * p < 0.05 vs. control IgG. (D–F) Intrathrombotic gene expression of Mmp2 (D) , Mmp9 (E) , and Plau (F) after IVC ligation. Each gene expression was determined by real-time reverse transcription (RT)–PCR as described in section Materials and Methods. All values represent the mean ± SEM ( n = 6 animals). * p < 0.05, ** p < 0.01, control Ig vs. anti-IL-6. (G–L) WT mice were intraperitoneally administered with rIL-6 as described in section Materials and Methods. (G) Macroscopic appearance of venous thrombi obtained from WT mice treated with rIL-6 or phosphate-buffered saline (PBS) at 10 days after IVC ligation. Representative results from six independent animals are shown here. Thrombus weights (H) and thrombosed blood flow (I) were measured at 10 days after IVC ligation. All values represent the mean ± SEM ( n = 6 animals). * p < 0.05, ** p < 0.01, PBS vs. rIL-6. (J–L) Intrathrombotic gene expression of Mmp2 (J) , Mmp9 (K) , and Plau (L) after IVC ligation. Each gene expression was determined by real-time RT-PCR as described in section Materials and Methods. All values represent the mean ± SEM ( n = 6 animals). * p < 0.05, ** p < 0.01, control PBS vs. rIL-6.

Journal: Frontiers in Immunology

Article Title: Crucial Involvement of IL-6 in Thrombus Resolution in Mice via Macrophage Recruitment and the Induction of Proteolytic Enzymes

doi: 10.3389/fimmu.2019.03150

Figure Lengend Snippet: The effects of anti-IL-6 antibody (Ab) and recombinant murine IL-6 (rIL-6) in wild-type (WT) mice on thrombus resolution. (A–F) WT mice were intraperitoneally administered with anti-IL-6 as described in section Materials and Methods. (A) Macroscopic appearance of venous thrombi obtained from WT mice treated with anti-IL-6 Ab or control IgG at 10 days after inferior vena cava (IVC) ligation. Representative results from six independent animals are shown here. Thrombus weights (B) and thrombosed blood flow (C) were measured at 10 days after IVC ligation. All values represent the mean ± SEM ( n = 6 animals). * p < 0.05 vs. control IgG. (D–F) Intrathrombotic gene expression of Mmp2 (D) , Mmp9 (E) , and Plau (F) after IVC ligation. Each gene expression was determined by real-time reverse transcription (RT)–PCR as described in section Materials and Methods. All values represent the mean ± SEM ( n = 6 animals). * p < 0.05, ** p < 0.01, control Ig vs. anti-IL-6. (G–L) WT mice were intraperitoneally administered with rIL-6 as described in section Materials and Methods. (G) Macroscopic appearance of venous thrombi obtained from WT mice treated with rIL-6 or phosphate-buffered saline (PBS) at 10 days after IVC ligation. Representative results from six independent animals are shown here. Thrombus weights (H) and thrombosed blood flow (I) were measured at 10 days after IVC ligation. All values represent the mean ± SEM ( n = 6 animals). * p < 0.05, ** p < 0.01, PBS vs. rIL-6. (J–L) Intrathrombotic gene expression of Mmp2 (J) , Mmp9 (K) , and Plau (L) after IVC ligation. Each gene expression was determined by real-time RT-PCR as described in section Materials and Methods. All values represent the mean ± SEM ( n = 6 animals). * p < 0.05, ** p < 0.01, control PBS vs. rIL-6.

Techniques: Recombinant, Control, Ligation, Gene Expression, Reverse Transcription, Reverse Transcription Polymerase Chain Reaction, Saline, Quantitative RT-PCR

The effects of recombinant murine IL-6 (rIL-6) on the gene expression of Mmp2, Mmp9 , and Plau and on Stat3 signaling in peritoneal macrophages. Peritoneal macrophages were obtained from wild-type (WT) mice and were stimulated as described in section Materials and Methods. The gene expression of Mmp2 (A) , Mmp9 (B) , and Plau (C) was analyzed by real-time reverse transcription (RT)–PCR. All values represent the mean ± SEM ( n = 6 independent experiments). * p < 0.05, vs. no stimulation. (D) Western blotting analysis using anti-GAPDH pAbs confirmed that an equal amount of protein was loaded onto each lane. Representative results from six independent experiments are shown here. (E) The ratios of p-Stat3/Stat3 were densitometrically determined and are shown. All values represent means ± SEM ( n = 4 independent experiments). (F–H) The effects of anti-IL-6 or Stattic on IL-6-induced gene expression of Mmp2 (F) , Mmp9 (G) , and Plau (H) . Each gene expression was analyzed by real-time RT-PCR. All values represent the mean ± SEM ( n = 4 independent experiments). * p < 0.05; ** p < 0.01, vs. no stimulation.

Journal: Frontiers in Immunology

Article Title: Crucial Involvement of IL-6 in Thrombus Resolution in Mice via Macrophage Recruitment and the Induction of Proteolytic Enzymes

doi: 10.3389/fimmu.2019.03150

Figure Lengend Snippet: The effects of recombinant murine IL-6 (rIL-6) on the gene expression of Mmp2, Mmp9 , and Plau and on Stat3 signaling in peritoneal macrophages. Peritoneal macrophages were obtained from wild-type (WT) mice and were stimulated as described in section Materials and Methods. The gene expression of Mmp2 (A) , Mmp9 (B) , and Plau (C) was analyzed by real-time reverse transcription (RT)–PCR. All values represent the mean ± SEM ( n = 6 independent experiments). * p < 0.05, vs. no stimulation. (D) Western blotting analysis using anti-GAPDH pAbs confirmed that an equal amount of protein was loaded onto each lane. Representative results from six independent experiments are shown here. (E) The ratios of p-Stat3/Stat3 were densitometrically determined and are shown. All values represent means ± SEM ( n = 4 independent experiments). (F–H) The effects of anti-IL-6 or Stattic on IL-6-induced gene expression of Mmp2 (F) , Mmp9 (G) , and Plau (H) . Each gene expression was analyzed by real-time RT-PCR. All values represent the mean ± SEM ( n = 4 independent experiments). * p < 0.05; ** p < 0.01, vs. no stimulation.

Techniques: Recombinant, Gene Expression, Reverse Transcription, Reverse Transcription Polymerase Chain Reaction, Western Blot, Quantitative RT-PCR

PAI-1 loss anticipates fibrosis and exacerbates muscle disease progression: Reversal by pharmacological and genetic interference with uPA in vivo. (A) Fibrosis quantification in diaphragms of PAI-1 +/+ and PAI-1 −/− mdx mice over time (*, P < 0.01 vs. age-matched PAI-1 +/+ mdx; means ± SEM; n = 5 for each group). (B) Quantitative PCR analysis of fibrosis-associated markers in diaphragm muscles of 3-mo-old PAI-1 +/+ and PAI-1 −/− mdx mice (*, P < 0.05 vs. PAI-1 +/+ mdx; means ± SEM; n = 5 for each group). (C) As in B, serum creatine kinase (CK) levels are shown (*, P < 0.01; means ± SEM; n = 5 for each group). (D) Representative Sirius red staining in diaphragm muscle sections of 3.5-mo-old PAI-1 +/+ and PAI-1 −/− mdx mice and PAI-1 −/− mdx mice treated with amiloride (a uPA inhibitor; see Fig. S3 for additional information). Bar, 25 µm. (E) Quantitative PCR analysis of PAI-1 expression in diaphragm muscle of mdx mice at the indicated ages; values are expressed as fold induction over WT (*, P < 0.01 vs. 1 mo; means ± SEM; n = 5 for each group). (F) Increased TGF-β1 active protein and miR-21 expression in the diaphragm muscle of PAI-1 −/− mdx mice compared with PAI-1 +/+ mdx mice, as measured by ELISA and quantitative PCR, respectively (*, P < 0.05; **, P < 001, means ± SEM; n = 4 for each group). (G, left) As in F, muscle samples were analyzed by Western blotting using antibodies against the proteins P-Smad2, total Smad2/3, and β-actin. (right) Quantification of P-Smad2 versus total Smad2/3 and normalized for β-actin levels is shown (*, P < 0.01; means ± SEM; n = 5 for each group). P-Smad2 levels in basal muscle of WT and PAI-1 −/− mice were undistinguishable (not depicted). (H) siRNA for uPA or a scrambled control oligomiR was delivered into gastrocnemius muscles of 3-mo-old PAI-1 −/− mdx mice every other day for 3 wk, and, after the treatment, muscles were analyzed for TGF-β1 active protein levels, collagen content, miR-21 expression, and Smad2 activity (P-Smad2; *, P < 0.05; **, P < 001, means ± SEM; n = 4 for each group). (I) siRNA for uPA or Scramble was delivered into the gastrocnemius muscle of 24-mo-old mdx mice every other day for an additional 1 mo. Then, muscles were analyzed for TGF-β1 activity, collagen content, and miR-21 expression (*, P < 0.01; means ± SEM; n = 5 for each group). (J) As in I, H/E staining is shown. Bar, 50 µm.

Journal: The Journal of Cell Biology

Article Title: PAI-1–regulated miR-21 defines a novel age-associated fibrogenic pathway in muscular dystrophy

doi: 10.1083/jcb.201105013

Figure Lengend Snippet: PAI-1 loss anticipates fibrosis and exacerbates muscle disease progression: Reversal by pharmacological and genetic interference with uPA in vivo. (A) Fibrosis quantification in diaphragms of PAI-1 +/+ and PAI-1 −/− mdx mice over time (*, P < 0.01 vs. age-matched PAI-1 +/+ mdx; means ± SEM; n = 5 for each group). (B) Quantitative PCR analysis of fibrosis-associated markers in diaphragm muscles of 3-mo-old PAI-1 +/+ and PAI-1 −/− mdx mice (*, P < 0.05 vs. PAI-1 +/+ mdx; means ± SEM; n = 5 for each group). (C) As in B, serum creatine kinase (CK) levels are shown (*, P < 0.01; means ± SEM; n = 5 for each group). (D) Representative Sirius red staining in diaphragm muscle sections of 3.5-mo-old PAI-1 +/+ and PAI-1 −/− mdx mice and PAI-1 −/− mdx mice treated with amiloride (a uPA inhibitor; see Fig. S3 for additional information). Bar, 25 µm. (E) Quantitative PCR analysis of PAI-1 expression in diaphragm muscle of mdx mice at the indicated ages; values are expressed as fold induction over WT (*, P < 0.01 vs. 1 mo; means ± SEM; n = 5 for each group). (F) Increased TGF-β1 active protein and miR-21 expression in the diaphragm muscle of PAI-1 −/− mdx mice compared with PAI-1 +/+ mdx mice, as measured by ELISA and quantitative PCR, respectively (*, P < 0.05; **, P < 001, means ± SEM; n = 4 for each group). (G, left) As in F, muscle samples were analyzed by Western blotting using antibodies against the proteins P-Smad2, total Smad2/3, and β-actin. (right) Quantification of P-Smad2 versus total Smad2/3 and normalized for β-actin levels is shown (*, P < 0.01; means ± SEM; n = 5 for each group). P-Smad2 levels in basal muscle of WT and PAI-1 −/− mice were undistinguishable (not depicted). (H) siRNA for uPA or a scrambled control oligomiR was delivered into gastrocnemius muscles of 3-mo-old PAI-1 −/− mdx mice every other day for 3 wk, and, after the treatment, muscles were analyzed for TGF-β1 active protein levels, collagen content, miR-21 expression, and Smad2 activity (P-Smad2; *, P < 0.05; **, P < 001, means ± SEM; n = 4 for each group). (I) siRNA for uPA or Scramble was delivered into the gastrocnemius muscle of 24-mo-old mdx mice every other day for an additional 1 mo. Then, muscles were analyzed for TGF-β1 activity, collagen content, and miR-21 expression (*, P < 0.01; means ± SEM; n = 5 for each group). (J) As in I, H/E staining is shown. Bar, 50 µm.

Article Snippet: For siRNA treatment in vivo, 5 μg in a volume of 10 μl of either siRNA uPA (Mouse PLAU; Thermo Fisher Scientific) or negative control was injected in the injured or dystrophic muscles.

Techniques: Biomarker Discovery, In Vivo, Real-time Polymerase Chain Reaction, Muscles, Staining, Expressing, Enzyme-linked Immunosorbent Assay, Western Blot, Control, Activity Assay

PAI-1 loss results in dysregulated miR-21 expression, which promotes AKT-mediated cell proliferation of skeletal muscle fibroblasts. (A) uPA activity (chromogenic assay), active TGF-β1 (ELISA), active TGF-β1 protein, and miR-21 expression (quantitative PCR) were analyzed in muscle fibroblasts from PAI-1 +/+ and PAI-1 −/− mice, either untreated or treated with recombinant PAI-1 (rPAI-1) and amiloride or transfected with siRNA for uPA or Scramble control, as indicated (*, P < 0.05; means ± SEM; n = 4 for each group). (B) PAI-1 +/+ and PAI-1 −/− muscle fibroblasts, transfected with Ant-miR-21 or Scramble oligomiR, were stimulated or not with 10 ng/ml TGF-β1, and the number of cells was counted at the indicated time points (means ± SEM; n = 4 for each group). (C) PAI-1 +/+ and PAI-1 −/− muscle fibroblasts, stimulated as in B, were analyzed for Coll I and TIMP-1 expression after TGF-β1 treatment (*, P < 0.05; means ± SEM; n = 4 for each group). (D) Extracts of PAI-1 +/+ and PAI-1 −/− muscle fibroblasts, stimulated or not with TGF-β1 for 24 h, were analyzed by Western blotting using antibodies for the proteins P-Smad2, total Smad2/3 protein, P-AKT, total AKT protein, PTEN, and β-actin; in lane 5, PAI-1 −/− muscle fibroblasts were incubated with 2 µM wortmannin (Wort) 30 min before the addition of TGF-β1. In lanes 6 and 7, PAI-1 −/− muscle fibroblasts were transfected with Scramble and siRNA uPA oligomiRs, respectively, before the addition of TGF-β1. (E) Western blotting analysis of muscle fibroblasts (left) or extracts of gastrocnemius muscles from 3-mo-old PAI-1 +/+ and PAI-1 −/− mdx mice (right) treated every other day for 1 mo with a scrambled oligomiR or Ant-miR-21 using antibodies for the proteins P-AKT, total AKT, PTEN, and β-actin.

Journal: The Journal of Cell Biology

Article Title: PAI-1–regulated miR-21 defines a novel age-associated fibrogenic pathway in muscular dystrophy

doi: 10.1083/jcb.201105013

Figure Lengend Snippet: PAI-1 loss results in dysregulated miR-21 expression, which promotes AKT-mediated cell proliferation of skeletal muscle fibroblasts. (A) uPA activity (chromogenic assay), active TGF-β1 (ELISA), active TGF-β1 protein, and miR-21 expression (quantitative PCR) were analyzed in muscle fibroblasts from PAI-1 +/+ and PAI-1 −/− mice, either untreated or treated with recombinant PAI-1 (rPAI-1) and amiloride or transfected with siRNA for uPA or Scramble control, as indicated (*, P < 0.05; means ± SEM; n = 4 for each group). (B) PAI-1 +/+ and PAI-1 −/− muscle fibroblasts, transfected with Ant-miR-21 or Scramble oligomiR, were stimulated or not with 10 ng/ml TGF-β1, and the number of cells was counted at the indicated time points (means ± SEM; n = 4 for each group). (C) PAI-1 +/+ and PAI-1 −/− muscle fibroblasts, stimulated as in B, were analyzed for Coll I and TIMP-1 expression after TGF-β1 treatment (*, P < 0.05; means ± SEM; n = 4 for each group). (D) Extracts of PAI-1 +/+ and PAI-1 −/− muscle fibroblasts, stimulated or not with TGF-β1 for 24 h, were analyzed by Western blotting using antibodies for the proteins P-Smad2, total Smad2/3 protein, P-AKT, total AKT protein, PTEN, and β-actin; in lane 5, PAI-1 −/− muscle fibroblasts were incubated with 2 µM wortmannin (Wort) 30 min before the addition of TGF-β1. In lanes 6 and 7, PAI-1 −/− muscle fibroblasts were transfected with Scramble and siRNA uPA oligomiRs, respectively, before the addition of TGF-β1. (E) Western blotting analysis of muscle fibroblasts (left) or extracts of gastrocnemius muscles from 3-mo-old PAI-1 +/+ and PAI-1 −/− mdx mice (right) treated every other day for 1 mo with a scrambled oligomiR or Ant-miR-21 using antibodies for the proteins P-AKT, total AKT, PTEN, and β-actin.

Techniques: Expressing, Activity Assay, Chromogenic Assay, Enzyme-linked Immunosorbent Assay, Real-time Polymerase Chain Reaction, Recombinant, Transfection, Control, Western Blot, Incubation, Muscles

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