Journal: Molecules (Basel, Switzerland)

Article Title: F4/80 + Kupffer Cell-Derived Oncostatin M Sustains the Progression Phase of Liver Regeneration through Inhibition of TGF-β2 Pathway.

doi: 10.3390/molecules26082231

Figure Lengend Snippet: Figure 6. The effects of depletion of F4/80+ KCs post-PHx on the TGF-β2/smad2 pathway during liver regeneration. (A) KEGG signal pathway enrichment scatter map. (B) ELISA assay of serum TGF-β2 in post-PHx α-F4/80-treated mice. (C) Western blot of TGF-β2/smad2 pathway in livers from (B), n = 3–5; * p < 0.05, ** p < 0.01.

Article Snippet: After blocking with 0.5% BSA, the membranes were incubated with primary antibodies at 4 ◦C overnight and then with secondary antibodies for at least 2 h. The primary antibodies used were as follows: TGFβ2 (1:1000, R&D Systems, Wiesbaden, Germany); CyclinD1 (1:1000, proteintech, Wuhan, China); PCNA (1:2000, proteintech, Wuhan, China); VEGFR2 (1:1000, Cell Signaling Technology, Danvers, MA, USA); HNF-4α, GAPDH, and CD31 (1:500, Abcam, Cambridge, MA, USA); and VEGFR2, Smad2, Smad3, and phospho-Smad2/3 (1:1000, Cell Signaling Technology, Danvers, MA, USA).

Techniques: Enzyme-linked Immunosorbent Assay, Western Blot

Journal: Molecules (Basel, Switzerland)

Article Title: F4/80 + Kupffer Cell-Derived Oncostatin M Sustains the Progression Phase of Liver Regeneration through Inhibition of TGF-β2 Pathway.

doi: 10.3390/molecules26082231

Figure Lengend Snippet: Figure 7. TGF-βRI treatment partially rescued the impaired proliferation of hepatocytes caused by depletion of F4/80+ KCs in post-PHx. (A) Phosphorylated and total protein levels of smad2 or smad3 in the post-PHx α-F4/80-treated groups in the absence or presence of TGF-βRI. Values represent the means ± SDs. (B) Liver/body weight ratios were analyzed in post-PHx α-F4/80-treated alone or that combined with TGF-βRI. (C) Representative photomicrographs of Ki67+ hepatocytes. Those relatively larger and rounder are considered hepatocytes. Quantification of the labeled cells at the lower left corner. (D) The protein levels of HNF-4α, PCNA, Cyclin D1, and GAPDH in livers (A). * p < 0.05, ** p < 0.01, n = 3.

Article Snippet: After blocking with 0.5% BSA, the membranes were incubated with primary antibodies at 4 ◦C overnight and then with secondary antibodies for at least 2 h. The primary antibodies used were as follows: TGFβ2 (1:1000, R&D Systems, Wiesbaden, Germany); CyclinD1 (1:1000, proteintech, Wuhan, China); PCNA (1:2000, proteintech, Wuhan, China); VEGFR2 (1:1000, Cell Signaling Technology, Danvers, MA, USA); HNF-4α, GAPDH, and CD31 (1:500, Abcam, Cambridge, MA, USA); and VEGFR2, Smad2, Smad3, and phospho-Smad2/3 (1:1000, Cell Signaling Technology, Danvers, MA, USA).

Techniques: Labeling

Journal: Molecules (Basel, Switzerland)

Article Title: F4/80 + Kupffer Cell-Derived Oncostatin M Sustains the Progression Phase of Liver Regeneration through Inhibition of TGF-β2 Pathway.

doi: 10.3390/molecules26082231

Figure Lengend Snippet: Figure 10. The effect of r-OSM reconstitution on hepatocyte proliferation and the TGF-β2/smad2 signaling pathway during the progression process of liver regeneration. (A) Representative photomicrographs and quantification of Ki67+ hepatocytes in α-F4/80 alone or combined with r-OSM-treated mice after PHx. (B) Expression of HNF-4α, PCNA, Cyclin D1, and GAPDH proteins in (A). (C) Expression of the TGF-β2/smad2 pathway-associated proteins in (A). n = 3–5, * p < 0.05, ** p < 0.01.

Article Snippet: After blocking with 0.5% BSA, the membranes were incubated with primary antibodies at 4 ◦C overnight and then with secondary antibodies for at least 2 h. The primary antibodies used were as follows: TGFβ2 (1:1000, R&D Systems, Wiesbaden, Germany); CyclinD1 (1:1000, proteintech, Wuhan, China); PCNA (1:2000, proteintech, Wuhan, China); VEGFR2 (1:1000, Cell Signaling Technology, Danvers, MA, USA); HNF-4α, GAPDH, and CD31 (1:500, Abcam, Cambridge, MA, USA); and VEGFR2, Smad2, Smad3, and phospho-Smad2/3 (1:1000, Cell Signaling Technology, Danvers, MA, USA).

Techniques: Expressing

Journal: Korean Journal for Food Science of Animal Resources

Article Title: Sensitivity of Pseudomonas syringae to Bovine Lactoferrin Hydrolysates and Identification of a Novel Inhibitory Peptide

doi: 10.5851/kosfa.2016.36.4.487

Figure Lengend Snippet: Separation and identification of antimicrobial peptides in bovine lactoferrin hydrolysates against P. syringae . Hydrolysates of bLf were confirmed using Tris tricine/SDS-PAGE (A). Reverse-phase HPLC purification of the antimicrobial peptide of bovine lactoferrin were fractionated on a column Asahipak C4P-50 (B), and antimicrobial activity of HPLC fractions was investigated using 96-well microplate method against P. syringae (C).

Article Snippet: Pseudomonas syringae DSM5175 and Pseudomonas fluorescens DSM 50090 were obtained as freeze-dried samples from the DSMZ-German Collection of Microorganisms and Cell Cultures (Germany).

Techniques: SDS Page, Purification, Activity Assay

Journal: Korean Journal for Food Science of Animal Resources

Article Title: Sensitivity of Pseudomonas syringae to Bovine Lactoferrin Hydrolysates and Identification of a Novel Inhibitory Peptide

doi: 10.5851/kosfa.2016.36.4.487

Figure Lengend Snippet: Crystal structure of bovine lactoferrin. The region contained in antimicrobial peptides against P. syringae is shown in red. The figure was constructed using RasWin molecular graphics (Protein Data Bank accession code 1BLF) ( Moore et al. , 1997 ).

Article Snippet: Pseudomonas syringae DSM5175 and Pseudomonas fluorescens DSM 50090 were obtained as freeze-dried samples from the DSMZ-German Collection of Microorganisms and Cell Cultures (Germany).

Techniques: Construct