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Expression of neural <t>glyco-epitope</t> <t>HNK-1</t> in cultured cells and their sEVs. A , schematic drawing of HNK-1 biosynthesis and two antibodies that react with HNK-1 and its non-sulfated form. B , B16 cells were co-transfected with the plasmids for expressing GlcAT-P and HNK-1ST or the empty vector (−). Cells were lysed and subjected to western blotting with anti-GlcAT-P, anti-GFP, anti-GAPDH, M6749 mAb, and HNK-1 mAb. C , B16 cells were transfected with the plasmids for expressing GlcAT-P-myc, GlcAT-S-myc, or the empty vector (mock). Cells were lysed and subjected to Western blotting with anti-myc, anti-GAPDH, and M6749 mAb. The signal intensity of the bands blotted with M6749 was quantified in the right graph ( n = 3, mean ± SD, ∗∗: p < 0.01, unpaired t test). D , B16 cells were transfected with the plasmid for expressing GlcAT-P or the empty vector (mock). The sEV fractions were collected from the culture media by ultracentrifugation, and the sEV proteins were subjected to western blotting with anti-CD81 and M6749 mAb.
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Expression of neural <t>glyco-epitope</t> <t>HNK-1</t> in cultured cells and their sEVs. A , schematic drawing of HNK-1 biosynthesis and two antibodies that react with HNK-1 and its non-sulfated form. B , B16 cells were co-transfected with the plasmids for expressing GlcAT-P and HNK-1ST or the empty vector (−). Cells were lysed and subjected to western blotting with anti-GlcAT-P, anti-GFP, anti-GAPDH, M6749 mAb, and HNK-1 mAb. C , B16 cells were transfected with the plasmids for expressing GlcAT-P-myc, GlcAT-S-myc, or the empty vector (mock). Cells were lysed and subjected to Western blotting with anti-myc, anti-GAPDH, and M6749 mAb. The signal intensity of the bands blotted with M6749 was quantified in the right graph ( n = 3, mean ± SD, ∗∗: p < 0.01, unpaired t test). D , B16 cells were transfected with the plasmid for expressing GlcAT-P or the empty vector (mock). The sEV fractions were collected from the culture media by ultracentrifugation, and the sEV proteins were subjected to western blotting with anti-CD81 and M6749 mAb.
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Expression of neural <t>glyco-epitope</t> <t>HNK-1</t> in cultured cells and their sEVs. A , schematic drawing of HNK-1 biosynthesis and two antibodies that react with HNK-1 and its non-sulfated form. B , B16 cells were co-transfected with the plasmids for expressing GlcAT-P and HNK-1ST or the empty vector (−). Cells were lysed and subjected to western blotting with anti-GlcAT-P, anti-GFP, anti-GAPDH, M6749 mAb, and HNK-1 mAb. C , B16 cells were transfected with the plasmids for expressing GlcAT-P-myc, GlcAT-S-myc, or the empty vector (mock). Cells were lysed and subjected to Western blotting with anti-myc, anti-GAPDH, and M6749 mAb. The signal intensity of the bands blotted with M6749 was quantified in the right graph ( n = 3, mean ± SD, ∗∗: p < 0.01, unpaired t test). D , B16 cells were transfected with the plasmid for expressing GlcAT-P or the empty vector (mock). The sEV fractions were collected from the culture media by ultracentrifugation, and the sEV proteins were subjected to western blotting with anti-CD81 and M6749 mAb.
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The two-dimensional (2D) structure of <t>Honokiol</t> (A), and 3D structure of Bax (B).
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The two-dimensional (2D) structure of <t>Honokiol</t> (A), and 3D structure of Bax (B).
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Expression of neural glyco-epitope HNK-1 in cultured cells and their sEVs. A , schematic drawing of HNK-1 biosynthesis and two antibodies that react with HNK-1 and its non-sulfated form. B , B16 cells were co-transfected with the plasmids for expressing GlcAT-P and HNK-1ST or the empty vector (−). Cells were lysed and subjected to western blotting with anti-GlcAT-P, anti-GFP, anti-GAPDH, M6749 mAb, and HNK-1 mAb. C , B16 cells were transfected with the plasmids for expressing GlcAT-P-myc, GlcAT-S-myc, or the empty vector (mock). Cells were lysed and subjected to Western blotting with anti-myc, anti-GAPDH, and M6749 mAb. The signal intensity of the bands blotted with M6749 was quantified in the right graph ( n = 3, mean ± SD, ∗∗: p < 0.01, unpaired t test). D , B16 cells were transfected with the plasmid for expressing GlcAT-P or the empty vector (mock). The sEV fractions were collected from the culture media by ultracentrifugation, and the sEV proteins were subjected to western blotting with anti-CD81 and M6749 mAb.

Journal: The Journal of Biological Chemistry

Article Title: A neural glycan HNK-1 is transferred to recipient cells via small extracellular vesicles

doi: 10.1016/j.jbc.2026.111144

Figure Lengend Snippet: Expression of neural glyco-epitope HNK-1 in cultured cells and their sEVs. A , schematic drawing of HNK-1 biosynthesis and two antibodies that react with HNK-1 and its non-sulfated form. B , B16 cells were co-transfected with the plasmids for expressing GlcAT-P and HNK-1ST or the empty vector (−). Cells were lysed and subjected to western blotting with anti-GlcAT-P, anti-GFP, anti-GAPDH, M6749 mAb, and HNK-1 mAb. C , B16 cells were transfected with the plasmids for expressing GlcAT-P-myc, GlcAT-S-myc, or the empty vector (mock). Cells were lysed and subjected to Western blotting with anti-myc, anti-GAPDH, and M6749 mAb. The signal intensity of the bands blotted with M6749 was quantified in the right graph ( n = 3, mean ± SD, ∗∗: p < 0.01, unpaired t test). D , B16 cells were transfected with the plasmid for expressing GlcAT-P or the empty vector (mock). The sEV fractions were collected from the culture media by ultracentrifugation, and the sEV proteins were subjected to western blotting with anti-CD81 and M6749 mAb.

Article Snippet: The following antibodies were used: mouse anti-GAPDH (Merck Millipore; MAB374), mouse HNK-1 mAb (ATCC; clone Leu7), rabbit anti-FLAG (Cell Signaling Technologies; 14,793), rabbit anti-GFP (MBL; 598), mouse anti-CD81 (Santa Cruz; sc-166029), mouse anti-myc (millipore; 05–724), rabbit anti-TSG101 (abcam; ab125011), HRP-anti-mouse IgG (GE Healthcare; NA931 V), HRP-anti-rabbit IgG (GE Healthcare; NA934 V), HRP-anti-mouse IgM (Invitrogen; 62–6802), Alexa546-anti-rabbit IgG (Invitrogen; A10040), and Alexa488-anti-mouse IgM (Invitrogen; A21042).

Techniques: Expressing, Cell Culture, Transfection, Plasmid Preparation, Western Blot

The two-dimensional (2D) structure of Honokiol (A), and 3D structure of Bax (B).

Journal: Poultry Science

Article Title: Honokiol antagonizes cadmium-induced ultrastructural nuclear variation and mitochondrial dysfunction of hepatocytes through targeting Bax protein

doi: 10.1016/j.psj.2026.106557

Figure Lengend Snippet: The two-dimensional (2D) structure of Honokiol (A), and 3D structure of Bax (B).

Article Snippet: Honokiol (HNK) was procured from Shanghai Yuanye Technology Co., Ltd (Shanghai, China), while cadmium chloride (CdCl 2 ) was supplied by Sigma-Aldrich (St. Louis, USA).

Techniques: