Fig. 5.
Fig. 5. Vitamin D3induction of activation of Smad2/Smad3 in HL-60 cells. / Vitamin D3 induces activation of Smad2/Smad3 in HL-60 cells in a TGF-β–dependent manner. (A) Western blot analysis of phosphorylation of endogenous Smad2 in HL-60 cells untreated or treated with 100 nM Vit D3 for 24 hours. (B) Immunohistochemical staining of Smad3 in HL-60 cells untreated (Control) or treated with 100 nM Vit D3 at 18 hours. Original magnification × 400. (C) TGF-β1–neutralizing antibodies block the phosphorylation of Smad2 induced by treatment of Hl-60 cells with either 10 ng/mL TGF-β or 100 nM Vit D3. Lysates from cells incubated in either the presence or absence of 12.5 μg/mL TGF-β1 control (12H5) or neutralizing (1D11) antibody at 2 hours or 24 hours were directly subjected to immunoblotting with antibodies against Smad2 (not shown) and phosphorylated Smad2.

Vitamin D3induction of activation of Smad2/Smad3 in HL-60 cells.

Vitamin D3 induces activation of Smad2/Smad3 in HL-60 cells in a TGF-β–dependent manner. (A) Western blot analysis of phosphorylation of endogenous Smad2 in HL-60 cells untreated or treated with 100 nM Vit D3 for 24 hours. (B) Immunohistochemical staining of Smad3 in HL-60 cells untreated (Control) or treated with 100 nM Vit D3 at 18 hours. Original magnification × 400. (C) TGF-β1–neutralizing antibodies block the phosphorylation of Smad2 induced by treatment of Hl-60 cells with either 10 ng/mL TGF-β or 100 nM Vit D3. Lysates from cells incubated in either the presence or absence of 12.5 μg/mL TGF-β1 control (12H5) or neutralizing (1D11) antibody at 2 hours or 24 hours were directly subjected to immunoblotting with antibodies against Smad2 (not shown) and phosphorylated Smad2.

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