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Image Search Results

Journal: The Journal of Experimental Medicine
Article Title: Tumor Necrosis Factor α Stimulates Osteoclast Differentiation by a Mechanism Independent of the Odf/Rankl–Rank Interaction
doi:
Figure Lengend Snippet: Expression of mRNAs of TNFR1, TNFR2, RANK, and c-Fms by M-BMMφ (A) and the effects of mouse and human TNF-α on the activation of NF-κB in M-BMMφ (B). (A) Total RNA was extracted from bone marrow cells, M-BMMφ, and purified osteoclasts of ddY mouse origin, and subjected to semiquantitative PCR analysis for TNFR1, TNFR2, RANK, c-Fms, and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) using the specific primer pairs described in Materials and Methods. PCR was performed under conditions determined to be in the linear range of product formation. (B) M-BMMφ were treated with sODF/sRANKL (100 ng/ml), mouse TNF-α (20 ng/ml), or human TNF-α (20 ng/ml) for 1 h. Nuclear extracts were prepared and analyzed by an electrophoretic mobility shift assay with an NF-κB–binding oligonucleotide probe as described in Materials and Methods. Similar results were obtained in two independent experiments.
Article Snippet: Recombinant proteins of mouse and human TNF-α, and human IL-1α were obtained from R & D Systems, Inc. Human M-CSF was obtained from Yoshitomi Pharmaceutical Co.
Techniques: Expressing, Activation Assay, Purification, Electrophoretic Mobility Shift Assay, Binding Assay
![TRAP-positive cell formation induced by mouse TNF-α in M-BMMφ requires both TNFR1- and TNFR2-mediated signals. (A) M-BMMφ prepared from ddY mice were further cultured for 3 d with sODF/sRANKL (100 ng/ml) (top) or mouse TNF-α (20 ng/ml) (bottom) in the presence of M-CSF (100 ng/ml). M-BMMφ were simultaneously treated with or without control IgG (30 μg/ml), anti–TNFR1 antibody (10 μg/ml), or anti–TNFR2 antibody (30 μg/ml). After culturing for an additional 3 d, cells were fixed and stained for TRAP. The number of TRAP-positive cells was scored. Results were expressed as the means ± SEM of three cultures. Similar results were obtained in three independent experiments. (B) M-BMMφ were prepared from normal C57BL/6J mice (wild type), TNFR1-deficient C57BL/6J mice [TNFR1(−/−)] or TNFR2-deficient C57BL/6J mice [TNFR2(−/−)]. M-BMMφ were further cultured with sODF/sRANKL (100 ng/ml) (top) or mouse TNF-α (20 ng/ml) in the presence of M-CSF (100 ng/ml) (bottom). After culturing for an additional 3 d, cells were fixed and stained for TRAP. The number of TRAP-positive cells was scored. Results were expressed as the means ± SEM of four mice in each group. *Significantly different from the control (A) or wild type (B); P < 0.01.](https://pub-med-central-images-cdn.bioz.com/pub_med_central_ids_ending_with_5746/pmc02195746/pmc02195746__JEM991127.f5.jpg)
Journal: The Journal of Experimental Medicine
Article Title: Tumor Necrosis Factor α Stimulates Osteoclast Differentiation by a Mechanism Independent of the Odf/Rankl–Rank Interaction
doi:
Figure Lengend Snippet: TRAP-positive cell formation induced by mouse TNF-α in M-BMMφ requires both TNFR1- and TNFR2-mediated signals. (A) M-BMMφ prepared from ddY mice were further cultured for 3 d with sODF/sRANKL (100 ng/ml) (top) or mouse TNF-α (20 ng/ml) (bottom) in the presence of M-CSF (100 ng/ml). M-BMMφ were simultaneously treated with or without control IgG (30 μg/ml), anti–TNFR1 antibody (10 μg/ml), or anti–TNFR2 antibody (30 μg/ml). After culturing for an additional 3 d, cells were fixed and stained for TRAP. The number of TRAP-positive cells was scored. Results were expressed as the means ± SEM of three cultures. Similar results were obtained in three independent experiments. (B) M-BMMφ were prepared from normal C57BL/6J mice (wild type), TNFR1-deficient C57BL/6J mice [TNFR1(−/−)] or TNFR2-deficient C57BL/6J mice [TNFR2(−/−)]. M-BMMφ were further cultured with sODF/sRANKL (100 ng/ml) (top) or mouse TNF-α (20 ng/ml) in the presence of M-CSF (100 ng/ml) (bottom). After culturing for an additional 3 d, cells were fixed and stained for TRAP. The number of TRAP-positive cells was scored. Results were expressed as the means ± SEM of four mice in each group. *Significantly different from the control (A) or wild type (B); P < 0.01.
Article Snippet: Recombinant proteins of mouse and human TNF-α, and human IL-1α were obtained from R & D Systems, Inc. Human M-CSF was obtained from Yoshitomi Pharmaceutical Co.
Techniques: Cell Culture, Staining

Journal: The Journal of Experimental Medicine
Article Title: Tumor Necrosis Factor α Stimulates Osteoclast Differentiation by a Mechanism Independent of the Odf/Rankl–Rank Interaction
doi:
Figure Lengend Snippet: Schematic representation of ligand-receptor systems in osteoclast differentiation and function regulated by TNF-α, ODF/RANKL, and IL-1α. TNF-α and ODF/RANKL independently stimulate osteoclast differentiation. Osteoclast differentiation induced by TNF-α occurs via TNFR1 and TNFR2 expressed by osteoclast precursors. ODF/RANKL induces osteoclast differentiation through RANK-mediated signals. M-CSF is a common factor required for both TNF-α– and ODF/RANKL-induced osteoclast differentiation. Activation of osteoclasts is induced by ODF/RANKL and IL-1α through RANK and type 1 IL-1 receptor, respectively. Common signaling cascades such as NF-κB and JNK activation may be involved in the differentiation and activation of osteoclasts induced by TNF-α, ODF/RANKL, and IL-1α.
Article Snippet: Recombinant proteins of mouse and human TNF-α, and human IL-1α were obtained from R & D Systems, Inc. Human M-CSF was obtained from Yoshitomi Pharmaceutical Co.
Techniques: Activation Assay