Murine Antithrombin Matched Antibody Pair

Moutan Cortex charcoal has been used to ameliorate blood heat symptoms and treat pathologic hemorrhage down the ages. Although well known as an agent with the effect of astringency and hemostasis, its active ingredients and action mechanism remain unclear. In the present study, molecular docking technology was employed to screen the potential hemostatic compounds in Moutan Cortex charcoal and their target proteins. Protein protein-interaction (PPI) analysis was performed to explain the functions and enrichment pathways of the target proteins. The results showed that a total of 25 compounds were estimated as active constituents targeting multiple proteins related to hemostatic diseases, including 5 proteins (SERPINC1, FVIII, FX, FII and FXII) that were considered as the key targets. Then the drug-target (D-T) network was constructed to analyze the underlying hemostatic mechanism of Moutan Cortex charcoal, followed by a hierarchical cluster analysis (HCA) for compounds clustering, and a coagulation screening test for compound verification on their coagulation activities, with the results indicating that M15 (5-Tetradecenoic acid) and M31 (1-Monolinolein) might be the key compounds contributing to the hemostasis effect of Moutan Cortex charcoal by involving in the pathways related to complement, coagulation cascades and the platelet activation, particularly by activating FVIII, FX, FII and FXII and inhibiting SERPINC1. This study has demonstrated that Moutan Cortex charcoal may work as a hemostatic through the interaction between multiple-compounds and multiple-proteins, which provides the basis for further researches on the hemostasis mechanism of Moutan Cortex charcoal.

The aim of the study was to compare proteomic data on the effects of spaceflight factors on the human body, including both real space missions and ground-based experiments. LC-MS/MS-based proteomic analysis of blood plasma samples obtained from 13 cosmonauts before and after long-duration (169-199 days) missions on the International Space Station (ISS) and for five healthy men included in 21-day-long head-down bed rest (HDBR) and dry immersion experiments were performed. The semi-quantitative label-free analysis revealed significantly changed proteins: 19 proteins were significantly different on the first (+1) day after landing with respect to background levels; 44 proteins significantly changed during HDBR and 31 changed in the dry immersion experiment. Comparative analysis revealed nine common proteins (A1BG, A2M, SERPINA1, SERPINA3, SERPING1, SERPINC1, HP, CFB, TF), which changed their levels after landing, as well as in both ground-based experiments. Common processes, such as platelet degranulation, hemostasis, post-translational protein phosphorylation and processes of protein metabolism, indicate common pathogenesis in ground experiments and during spaceflight. Dissimilarity in the lists of significantly changed proteins could be explained by the differences in the dynamics of effective development in the ground-based experiments. Data are available via ProteomeXchange using the identifier PXD013305.