Journal: Chemical Biology & Drug Design

Article Title: Investigation on the antipyretic mechanism of Chaiqin Qingning capsule for the treatment of fever based on network pharmacology, molecular docking, and in vitro experimental validation

doi: 10.1111/cbdd.14451

Figure Lengend Snippet: FIGURE 7 Western blot detection of CQQNC on the expression of COX-1, COX-2, cAMP, EP3, and mPGES1. Statistical significance: ∆∆∆∆p < .0001, ∆∆p < .01, and ∆p < .05 represents IL-1β group versus control group. ****p < .0001, **p < .01, and *p < .05 represent CQQNC group versus IL-1β group (n = 3).

Article Snippet: AntiCOX- 1 (batch number: 00100314), COX- 2 (batch number: 10027896), EP3 (batch number: 00071265), mouse and rabbit GAPDH (batch number: 10021642 and 0013796) antibody were purchased from Proteintech.

Techniques: Western Blot, Expressing, Control

Journal: Cardiovascular research

Article Title: Involvement of COX-2 in VEGF-induced angiogenesis via P38 and JNK pathways in vascular endothelial cells.

doi: 10.1016/j.cardiores.2005.09.019

Figure Lengend Snippet: Fig. 1. Effects of U0126, SB203580 and SP600125 on VEGF-induced COX-2 expression in HUVEC. (A) HUVEC cells were pre-treated with U0126 (10 AM), SB203580 (20 AM) and SP600125 (20 AM) for 1 h before incubating with VEGF (20 ng/ml) for 3 h. The activation states of COX-1 and COX-2 were then determined by Northern blot (up panel) and Western blot (low panel) analyses. VEGF-induced COX-2 expression was blocked by p38 and JNK inhibitors but not by ERK1/2 inhibitor. Autoradiographic signals were quantified by densitometry using ImageQuant software. Quantitative analyses are shown on lower panel that the ration of COX-2 RNA vs. 28S (left) and level of COX-2 protein vs. h-actin (right). (B) HUVEC cells were pre-treated with SB203580 and SP600125 at indicated doses for 1 h, and then VEGF was added and continue to incubate cells for another 3 h. COX-2 expression was determined by Northern blot. VEGF-induced COX-2 expression blocked by both p38 and JNK inhibitors show dose dependent patterns.

Article Snippet: The following antibodies were applied to the study: AntiCOX-1 (Calbiochem, La Jolla, CA), COX-2 (Cayman Chemical, Ann Arbor, MI), p38 MAP kinase, phospho-p38 MAP kinase, SAPK/JNK and phospho-SAPK/JNK (Cell Signaling Technology), as well as h-actin (Santa Cruz Biotechnology, Santa Cruz, CA) antibodies.

Techniques: Expressing, Activation Assay, Northern Blot, Western Blot, Software

Journal: Cardiovascular research

Article Title: Involvement of COX-2 in VEGF-induced angiogenesis via P38 and JNK pathways in vascular endothelial cells.

doi: 10.1016/j.cardiores.2005.09.019

Figure Lengend Snippet: Fig. 2. VEGF-induced p38 MAP kinase and JNK phosphorylation in HUVEC. HUVEC cells were treated with VEGF at a time-dependent manner and the cell lysate was prepared by sampling buffer (1SDS, 10 mM sodium fluoride, 10 mM sodium vanadate) and then subject to Western blot analysis with antibodies against phospho-and nonphospho-forms of p38 or phospho- and nonphospho-form of JNK MAPK. Autoradiographic signals were quantified by densitometry using ImageQuant software. Quantitative analyses are shown on lower panel phopho-p38 vs. p38 (left) and phospho-JNK vs. JNK (right) with adjusted by the ratio of density of h-action. Note VEGF stimulates both p38 and JNK phosphorylation at 10 and 20 min. in HUVEC cells.

Article Snippet: The following antibodies were applied to the study: AntiCOX-1 (Calbiochem, La Jolla, CA), COX-2 (Cayman Chemical, Ann Arbor, MI), p38 MAP kinase, phospho-p38 MAP kinase, SAPK/JNK and phospho-SAPK/JNK (Cell Signaling Technology), as well as h-actin (Santa Cruz Biotechnology, Santa Cruz, CA) antibodies.

Techniques: Phospho-proteomics, Sampling, Western Blot, Software

Journal: Cardiovascular research

Article Title: Involvement of COX-2 in VEGF-induced angiogenesis via P38 and JNK pathways in vascular endothelial cells.

doi: 10.1016/j.cardiores.2005.09.019

Figure Lengend Snippet: Fig. 4. VEGF-induced tube-like formation in HUVECs with COX-2 overexpression and COX-2 silencing RNA (siRNA). COX-2O/E, COX-2/siRNA and empty vector (pEGFP-N1) were transiently transfected into HUVEC cells. Six hours after transfection, cells (5105 cells/well) were transferred into 24-well plate that was pre-coated with Matrigel (100 ul/well), and incubated without or with VEGF (20 ng/ml) for another 24 h. (a and b) pEGFP-N1, empty vector- transfected HUVEC without (A) or with (B) VEGF stimulation; (C and D) COX-2/siRNA transfected HUVEC without (C) or with (D) VEGF stimulation; (E and F) COX-2/pEGFP-N1 transfected HUVEC without (E) or with (F) VEGF stimulation. Photos were taken at 10 magnification. Note that ring and cord formation was observed in VEGF-treated HUVEC cells but neither in the HUVEC cells treated with p38 and JNK inhibitors nor with COX-siRNA. The quantitative tube formation assays derived from 3D cultures are shown on lower panel. The average numbers of tubule branch points in randomly selected 5 high-power field (40) views of assays derived from 3D cultures were quantified. *p <0.05.

Article Snippet: The following antibodies were applied to the study: AntiCOX-1 (Calbiochem, La Jolla, CA), COX-2 (Cayman Chemical, Ann Arbor, MI), p38 MAP kinase, phospho-p38 MAP kinase, SAPK/JNK and phospho-SAPK/JNK (Cell Signaling Technology), as well as h-actin (Santa Cruz Biotechnology, Santa Cruz, CA) antibodies.

Techniques: Over Expression, Plasmid Preparation, Transfection, Incubation, Derivative Assay