Journal: Animals : an Open Access Journal from MDPI

Article Title: Myeloperoxidase Inhibition Decreases the Expression of Collagen and Metallopeptidase in Mare Endometria under In Vitro Conditions

doi: 10.3390/ani11010208

Figure Lengend Snippet: Relative mRNA transcription of type I collagen ( COL1A2 ) ( A , B ) and relative abundance of COL1 protein ( C , D ) in mare endometrial explants from the follicular phase (FP) and the mid-luteal phase (MLP) treated with culture medium only (Control), myeloperoxidase (MPO: 0.5 μg/mL), 4-aminobenzoic hydrazide (ABAH: 10 μg/mL), or MPO (0.5 μg/mL) + ABAH (10 μg/mL) for 24 or 48 h. Results are presented as median with interquartile range. Significance was determined at p < 0.05. The differences among treatments with the same treatment time are signaled by distinct superscript letters (a,b—24 h; x,y—48 h). The differences among times of treatment for the identical treatment are shown by asterisks (* p < 0.05; ** p < 0.01).

Article Snippet: Afterwards, endometrial explants (FP: n = 8; MLP: n = 6 for all the performed treatments) were further treated in new culture medium for 24 h or 48 h with (i) vehicle (negative control)–culture medium alone; (ii) myeloperoxidase (MPO; 0.5 μg/mL; orb81997; Biorbyt, Cambridge, UK); (iii) 4-aminobenzoic hydrazide, an MPO inhibitor (ABAH; 10 μg/mL; C7H9N3O, sc-204107; Santa Cruz Biotechnology, Dallas, TX, USA); (iv) MPO (0.5 μg/mL) + ABAH (10 μg/mL); or (v) oxytocin (OXT; 10-7 M).

Techniques: Control

Journal: Animals : an Open Access Journal from MDPI

Article Title: Myeloperoxidase Inhibition Decreases the Expression of Collagen and Metallopeptidase in Mare Endometria under In Vitro Conditions

doi: 10.3390/ani11010208

Figure Lengend Snippet: Transcription of MMP2 ( A , B ) and MMP9 ( C , D ) relative mRNA in mare endometrial explants from the follicular phase (FP) and the mid-luteal phase (MLP) treated with culture medium only (Control), myeloperoxidase (MPO: 0.5 μg/mL), 4-aminobenzoic hydrazide (ABAH: 10 μg/mL), or MPO (0.5 μg/mL) + ABAH (10 μg/mL) for 24 or 48 h. Results are presented as median with interquartile range. Significance was determined at p < 0.05. The differences among treatments with the same treatment time are signaled by distinct superscript letters (a,b,c—24 h; x,y—48 h). The differences among times of treatment for the identical treatment are depicted by asterisks (*** p < 0.001).

Article Snippet: Afterwards, endometrial explants (FP: n = 8; MLP: n = 6 for all the performed treatments) were further treated in new culture medium for 24 h or 48 h with (i) vehicle (negative control)–culture medium alone; (ii) myeloperoxidase (MPO; 0.5 μg/mL; orb81997; Biorbyt, Cambridge, UK); (iii) 4-aminobenzoic hydrazide, an MPO inhibitor (ABAH; 10 μg/mL; C7H9N3O, sc-204107; Santa Cruz Biotechnology, Dallas, TX, USA); (iv) MPO (0.5 μg/mL) + ABAH (10 μg/mL); or (v) oxytocin (OXT; 10-7 M).

Techniques: Control

Journal: Animals : an Open Access Journal from MDPI

Article Title: Myeloperoxidase Inhibition Decreases the Expression of Collagen and Metallopeptidase in Mare Endometria under In Vitro Conditions

doi: 10.3390/ani11010208

Figure Lengend Snippet: Relative MMP-2 ( A , B ) and MMP-9 ( C , D ) gelatinolytic activities in mare endometrial explants from the follicular phase (FP) and the mid-luteal phase (MLP) treated with culture medium only (Control), myeloperoxidase (MPO: 0.5 μg/mL), 4-aminobenzoic hydrazide (ABAH: 10 μg/mL), or MPO (0.5 μg/mL) + ABAH (10 μg/mL) for 24 or 48 h. Data of the least square means ± SEM are shown in bars as percentage of change from control. Significance was determined at p < 0.05. The differences among treatments with the same treatment time are signaled by distinct superscript letters. The differences among times of treatment for the identical treatment and MMP form are presented by asterisks (* p < 0.05; ** p < 0.01).

Article Snippet: Afterwards, endometrial explants (FP: n = 8; MLP: n = 6 for all the performed treatments) were further treated in new culture medium for 24 h or 48 h with (i) vehicle (negative control)–culture medium alone; (ii) myeloperoxidase (MPO; 0.5 μg/mL; orb81997; Biorbyt, Cambridge, UK); (iii) 4-aminobenzoic hydrazide, an MPO inhibitor (ABAH; 10 μg/mL; C7H9N3O, sc-204107; Santa Cruz Biotechnology, Dallas, TX, USA); (iv) MPO (0.5 μg/mL) + ABAH (10 μg/mL); or (v) oxytocin (OXT; 10-7 M).

Techniques: Control

Journal: Parasites & vectors

Article Title: Pentatrichomonas hominis induces extracellular traps formation of macrophages via the TLR2/NADPH/PAD4 pathway.

doi: 10.1186/s13071-025-06840-w

Figure Lengend Snippet: Fig. 5 NADPH activation and ROS production were involved in the formation of P. hominis-induced METs. a, Macrophages (7.5 × 105 cells/ml) were pretreated with NADPH oxidase inhibitor (DPI) prior to P. hominis trophozoite stimulation for 30 min. b, ROS production was detected via DCFH-DA. Macrophages were pretreated or untreated with DPI. The macrophages stimulated with zymosan (1 mg/ml) were used as a positive control, and unstimulated macrophages were used as a negative control. c, Macrophages (7.5 × 105 cells/ml) were pretreated with MPO inhibitor (4-ABAH) prior to P. hominis trophozoite stimulation for 30 min. d, DNase I was added to the coincubated medium 15 min before the end of incubation. The dsDNA produced by METs in supernatants was stained with PicoGreen and detected. Bars represent the mean ± SD for the three experiments, ***P < 0.001, ****P < 0.0001

Article Snippet: In parallel experiments, macrophages were pretreated with 20 μM of NADPH oxidase inhibitor (diphenylene iodonium [DPI], Merck, D2926, USA), 100 μM of MPO inhibitor (4-aminobenzoic acid hydrazide [4-ABAH], Selleck, S9874, China), 50 μM of extracellular regulated protein kinase 1/2 (ERK1/2) inhibitor (U0126, Selleck, S1102, China), 10 μM of p38 MAPK inhibitor (SB202190, Selleck, S1077, China), 100 μM of TLR2 inhibitor (TLR2-IN-C29, Selleck, S6597, China), 100 μM of SOCE inhibitor (2-aminoethyl diphenylborinate [2-APB], Selleck, S6657, China), 10 μM of PAD4 inhibitor (GSK484 hydrochloride, MedChemExpress, HY-100514, USA), and 1 μM of cytochalasin D (Cyt D, APExBio, 22144-77- 0, USA) at 37 °C and 5% CO2 for 30 min. DNase I in 90 U/well (Thermo Scientific, EN0523, USA) was used to digest the MET structure for 15 min before the end of coincubation.

Techniques: Activation Assay, Positive Control, Negative Control, Incubation, Produced, Staining