Effect of beraprost sodium on renal function and p38MAPK signaling pathway in rats with diabetic nephropathy

Purpose: To investigate the effect of beraprost sodium (BPS) on renal function and P38MAPK pathway in diabetic nephropathy (DN) rats.Methods: Sprague Dawley (SD) rats (n = 30) were randomly divided into three groups, viz, normal control (NC), diabetic nephropathy (DN) and beraprost sodium (BPS). Creatinine (Cr), blood urea nitrogen (BUN) and fasting blood glucose (FBG), were determined by Hitachi 7020 automatic biochemical analyzer, while low-density lipoprotein cholesterol (LDL-C), high-density lipoprotein cholesterol (HDL-C), triglycerides (TG) and total cholesterol (TC) were measured by Olympus 400 automatic biochemical analyzer. Western blot analysis was performed to examine protein expression. Interleukin-6 (IL-6), hs-CRP, and TNF-α levels were evaluated using enzyme linked immunosorbent assay (ELISA).Results: After 8 weeks of treatment, renal function indices (urine output, KW/BW, UAlb/24 h, Cr and BUN), blood lipid indices (FBG, LDL-C, TG and TC) and inflammatory factors levels (IL-6, hs-CRP and TNF-α) in DN group were higher than NC group (p < 0.05). In BPS group, renal function and blood lipid indices and inflammatory factor levels decreased when compared to DN group (p < 0.05). Furthermore, BPS inhibited the protein expression of p-P38MAPK, TGF-β1 and COX-2.Conclusion: Beraprost sodium improves renal function in DN rats by inhibiting P38MAPK signalingpathway

Multispecies Adulteration Detection of Camellia Oil by Chemical Markers

Adulteration of edible oils has attracted attention from more researchers and consumers in recent years. Complex multispecies adulteration is a commonly used strategy to mask the traditional adulteration detection methods. Most of the researchers were only concerned about single targeted adulterants, however, it was difficult to identify complex multispecies adulteration or untargeted adulterants. To detect adulteration of edible oil, identification of characteristic markers of adulterants was proposed to be an effective method, which could provide a solution for multispecies adulteration detection. In this study, a simple method of multispecies adulteration detection for camellia oil (adulterated with soybean oil, peanut oil, rapeseed oil) was developed by quantifying chemical markers including four isoflavones, trans-resveratrol and sinapic acid, which used liquid chromatography tandem mass spectrometry (LC-MS/MS) combined with solid phase extraction (SPE). In commercial camellia oil, only two of them were detected of daidzin with the average content of 0.06 ng/g while other markers were absent. The developed method was highly sensitive as the limits of detection (LODs) ranged from 0.02 ng/mL to 0.16 ng/mL and the mean recoveries ranged from 79.7% to 113.5%, indicating that this method was reliable to detect potential characteristic markers in edible oils. Six target compounds for pure camellia oils, soybean oils, peanut oils and rapeseed oils had been analyzed to get the results. The validation results indicated that this simple and rapid method was successfully employed to determine multispecies adulteration of camellia oil adulterated with soybean, peanut and rapeseed oils

Single-Cell Transcriptomics Reveals the Difference of Aortic Atherosclerosis Response to Phytosterols and Oxidation Products of Sterols

ScopePhytosterols (PS) and sterol oxidation products are key dietary factors influencing atherosclerosis besides cholesterol, although the mechanisms remain elusive. Recently, single-cell RNA sequencing (scRNA-seq) has revealed the heterogeneity of multiple cell types associated with complex pathogenesis in atherosclerosis development. Methods and resultsHere, scRNA-seq is performed to investigate the alterations in the aortic cells from ApoE(-/-) mice induced by diet-derived PS or two sterol oxidation products, phytosterols oxidation products (POPs), and cholesterol oxidation products (COPs). The study identifies four fibroblast subpopulations with different functions, and immunofluorescence demonstrates their spatial heterogeneity, providing evidence that suggests the transformation of smooth muscle cells (SMCs) and fibroblasts in atherosclerosis. The composition and gene expression profiles of aortic cells change broadly in response to PS/COPs/POPs exposure. Notably, PS exhibits an atheroprotective effect where different gene expressions are mainly found in B cells. Exposure to COPs accelerates atherosclerosis and results in marked alternations in myofibroblast subpopulations and T cells, while POPs only alter fibroblast subpopulations and B cells. ConclusionThe data elucidate the effects of dietary PS/COPs/POPs on aortic cells during atherosclerosis development, especially on the newly identified fibroblast subpopulations

Data Comparison and Cross-Calibration between Level 1 Products of DPC and POSP Onboard the Chinese GaoFen-5(02) Satellite

The Polarization CrossFire (PCF) suite onboard the Chinese GaoFen-5(02) satellite has been sophisticatedly composed by the Particulate Observing Scanning Polarimeter (POSP) and the Directional Polarimetric Camera (DPC). Among them, DPC is a multi-angle sequential measurement polarization imager, while POSP is a cross-track scanning simultaneous polarimeter with corresponding radiometric and polarimetric calibrators, which can theoretically be used for cross comparison and calibration with DPC. After the data preprocessing of these two sensors, we first select local homogeneous cluster scenes by calculating the local variance-to-mean ratio in DPC’s Level 1 product projection grids to reduce the influence of scale differences and geometry misalignment between DPC and POSP. Then, taking the observation results after POSP data quality assurance as the abscissa and taking the DPC observation results under the same wavelength band and geometric conditions as the same ordinate, a two-dimensional radiation/polarization feature space is established. Results show that the normalized top of the atmosphere (TOA) radiances of DPC and POSP processed data at the nadir are linearly correlated. The normalized TOA radiance root mean square errors (RMSEs) look reasonable in all common bands. The DPC and POSP normalized radiance ratios in different viewing zenith angle ranges at different times reveal the temporal drift of the DPC relative radiation response. The RMSEs, mean absolute errors (MAEs), relative errors (REs), and scatter percentage of DPC degree of linear polarization (DoLP) falling within the expected error (EE = ±0.02) of POSP measured DoLP are better than 0.012, 0.009, 0.066, and 91%, respectively

Construction and Deciphering of Human Phosphorylation-Mediated Signaling Transduction Networks

Protein phosphorylation is the most abundant reversible covalent modification. Human protein kinases participate in almost all biological pathways, and approximately half of the kinases are associated with disease. PhoSigNet was designed to store and display human phosphorylation-mediated signal transduction networks, with additional information related to cancer. It contains 11 976 experimentally validated directed edges and 216 871 phosphorylation sites. Moreover, 3491 differentially expressed proteins in human cancer from dbDEPC, 18 907 human cancer variation sites from CanProVar, and 388 hyperphosphorylation sites from PhosphoSitePlus were collected as annotation information. Compared with other phosphorylation-related databases, PhoSigNet not only takes the kinase–substrate regulatory relationship pairs into account, but also extends regulatory relationships up- and downstream (e.g., from ligand to receptor, from G protein to kinase, and from transcription factor to targets). Furthermore, PhoSigNet allows the user to investigate the impact of phosphorylation modifications on cancer. By using one set of in-house time series phosphoproteomics data, the reconstruction of a conditional and dynamic phosphorylation-mediated signaling network was exemplified. We expect PhoSigNet to be a useful database and analysis platform benefiting both proteomics and cancer studies

Construction and Deciphering of Human Phosphorylation-Mediated Signaling Transduction Networks

Protein phosphorylation is the most abundant reversible covalent modification. Human protein kinases participate in almost all biological pathways, and approximately half of the kinases are associated with disease. PhoSigNet was designed to store and display human phosphorylation-mediated signal transduction networks, with additional information related to cancer. It contains 11 976 experimentally validated directed edges and 216 871 phosphorylation sites. Moreover, 3491 differentially expressed proteins in human cancer from dbDEPC, 18 907 human cancer variation sites from CanProVar, and 388 hyperphosphorylation sites from PhosphoSitePlus were collected as annotation information. Compared with other phosphorylation-related databases, PhoSigNet not only takes the kinase–substrate regulatory relationship pairs into account, but also extends regulatory relationships up- and downstream (e.g., from ligand to receptor, from G protein to kinase, and from transcription factor to targets). Furthermore, PhoSigNet allows the user to investigate the impact of phosphorylation modifications on cancer. By using one set of in-house time series phosphoproteomics data, the reconstruction of a conditional and dynamic phosphorylation-mediated signaling network was exemplified. We expect PhoSigNet to be a useful database and analysis platform benefiting both proteomics and cancer studies

Construction and Deciphering of Human Phosphorylation-Mediated Signaling Transduction Networks

Protein phosphorylation is the most abundant reversible covalent modification. Human protein kinases participate in almost all biological pathways, and approximately half of the kinases are associated with disease. PhoSigNet was designed to store and display human phosphorylation-mediated signal transduction networks, with additional information related to cancer. It contains 11 976 experimentally validated directed edges and 216 871 phosphorylation sites. Moreover, 3491 differentially expressed proteins in human cancer from dbDEPC, 18 907 human cancer variation sites from CanProVar, and 388 hyperphosphorylation sites from PhosphoSitePlus were collected as annotation information. Compared with other phosphorylation-related databases, PhoSigNet not only takes the kinase–substrate regulatory relationship pairs into account, but also extends regulatory relationships up- and downstream (e.g., from ligand to receptor, from G protein to kinase, and from transcription factor to targets). Furthermore, PhoSigNet allows the user to investigate the impact of phosphorylation modifications on cancer. By using one set of in-house time series phosphoproteomics data, the reconstruction of a conditional and dynamic phosphorylation-mediated signaling network was exemplified. We expect PhoSigNet to be a useful database and analysis platform benefiting both proteomics and cancer studies