[The application of rapid rehabilitation model of multidisciplinary cooperation in cesarean section and the evaluation of health economics].

Objective: To explore the application value of multiple disciplinary team Enhanced recovery after surgery (MDT-ERAS) in cesarean section and evaluate its health economic benefits. Methods: A total of 572 cases of pregnant women undergoing cesarean section in obstetrics department of Jiaxing Maternity and Child Health Care Hospital from March 2018 to March 2019 were selected and randomly divided into experimental group and control group, 286 cases in each group. The control group was treated with traditional rehabilitation mode, and the experimental group was treated with MDT-ERAS intervention to compare the difference of rehabilitation index and health economics index between the two groups, and to evaluate the application value and health economics benefit of MDT-ERAS. Results: The VAS scores of the two groups at 1 day after operation were higher than those at the time of returning to the ward after operation(1.81±0.40 VS. 1.58±0.39, 3.78±0.89 VS. 3.22±0.83, all P<0.05). The VAS scores at 2 days and 3 days after operation were lower than those at the time of returning to the ward(0.58±0.09 VS. 1.58±0.39, 1.02±0.15 VS. 1.58±0.39; 1.88±0.37 VS. 3.22±0.83, 2.67±0.44 VS. 3.22±0.83, all P<0.05). The VAS scores of the experimental group at each time point after operation were lower than those of the control group(1.58±0.39 VS. 3.22±0.83, 1.81±0.40 VS. 3.78±0.89, 1.02±0.15 VS. 2.67±0.44, 0.58±0.09 VS. 1.88±0.37), and these differences were statistically significant (P<0.05). The anal exhaust time, indwelling catheterization time, first time out of bed and first time eating time of the experimental group were lower than those of the control group, with statistical significance (P<0.05). Postpartum hemorrhage rate and neonatal milk addition rate in the experimental group were significantly lower than those in the control group (all P<0.05). The hospitalization time and hospitalization expenses of the experimental group were lower than those of the control group(all P<0.05), and the health economics benefit of the experimental group was significantly higher than that of the latter (P<0.05). Conclusion: MDT-ERAS can effectively improve the recovery rate of the parturient after cesarean section, ensure the analgesic effect and improve the maternal and infant outcomes, and has higher health and economic benefits, which is worthy of promotion.

[Diagnostic values of mitral inflow and mitral annulus diastolic velocity for heart failure with preserved ejection fraction].

OBJECTIVE: To explore the diagnostic values of ratios of early diastolic peak transmitral velocity(E) to late velocity(A) (E/A) and E to early diastolic peak mitral annulus velocity (E/E') for heart failure patients with preserved ejection fraction (HF-PEF). METHODS: Two hundred and sixteen healthy people were divided into <50 years, 50-59 years, 60-69 years, and ≥70 years groups to clarify the impact of aging on E/A and E/E'. Two hundred and two newly diagnosed consecutive in-patients with HF-PEF and 221 age- and sex-matched non-heart-failure subjects with risk factors of HF-PEF (negative controls) were enrolled.The diagnostic values and cutoff points of E/A and E/E' for HF-PEF were derived from receiver operating characteristic curve (ROC) analysis. RESULTS: E/A and E/E' were significantly different among age groups in healthy controls (all P<0.01). Compared with <50 years group, average E/A was lower and average E/E' was higher in ≥70 years group(both P<0.01). E/A ratio was less than 1 in 68%(71/105), E/E' was >8 cm/s in 48% (50/105)healthy people with age≥60 years. Neither E/A nor E/E' of HF-PEF patients was statistically different regarding to NYHA classification (grade Ⅱ, Ⅲ, Ⅳ), but NT-proBNP value increased in proportion to higher NYHA classification(P<0.01). The area of E/E' under ROC for diagnosing HF-PEF was 0.839(P<0.01), and the corresponding cutoff point was 9.5 with a sensitivity of 86% and a specificity of 69%. The areas of E/A (larger value or smaller value indicating positive) under ROC for diagnosing HF-PEF were 0.469 and 0.531, respectively(all P>0.05). CONCLUSIONS: Aging exerts significant impacts on both E/A and E/E'. E/E' has moderate diagnostic accuracy while E/A is of limited value for diagnosing HF-PEF.

Prognostic value of neutrophil-lymphocyte ratio in critically ill patients with cancer: a propensity score matching study.

BACKGROUND: Neutrophil-lymphocyte ratio (NLR) has shown a good prognostic value in many different type of malignancies. The purpose of this study was to investigate the relationship between NLR and the outcome of critically ill patients with cancer. METHODS: We performed a single-institution, retrospective study of 1317 adult critically ill patients with cancer and determined the optimal cut-off for NLR by X-tile software. Propensity score matching (PSM) and inverse probabilities of treatment weighting (IPTW) were performed to control confounders. Cox proportional hazards model was used to evaluate the relationship between NLR and 28-day, 6-month and 1-year all-cause mortality. Kaplan-Meier method, subgroup analysis, and receiver operating characteristics (ROC) analysis were applied to assess the prognostic value of NLR. RESULTS: The cut-off value for NLR was 17.6. Cox proportional hazards model demonstrated that high NLR (> 17.6) was independently associated with 28-day, 6-month and 1-year all-cause mortality with hazard ratio (HR) of 1.58 (1.29, 1.94), 1.51 (1.28, 1.77) and 1.45 (1.25, 1.69), respectively. The results were consistent with survival analyses (p < 0.001, log-rank test). The ROC analyses showed that the discrimination abilities of NLR were better than other blood-based biomarkers. CONCLUSION: NLR is a promising prognostic indicator of survival in unselected critical ill patients with cancer.

Characterization and optical transition in tb-doped 12CaO x 7Al2O3 powders.

Tb-doped 12CaO x 7Al2O3 (C12A7:Tb3+) powders with strong green emission were prepared using the sol-gel method. X-ray diffraction, micro-Raman spectra, scanning electron microscopy and absorption spectra showed that C12A7:Tb3+ powders with grain size of 200-300 nm were synthesized. Porous powders could be formed as the concentration of Tb3+ was 5 at%. The absorption band around 209 nm was attributed to the host lattice absorption, and the bands around 255 nm and 274 nm were related to the 4f-5d transitions of Tb3+. The absorption intensity of the visible region was enhanced due to the presence of one 100 nm-diameter hole in every grain of C12A7:Tb3+ powders. The emission spectra showed noticeable influence of Tb-Tb cross relaxation, which favored the green photoluminescence (PL) over the blue PL. The study on the concentration quenching indicated that the energy transfers depopulating the 5D3 and 5D4 levels were assigned to the mechanisms of electric dipole-dipole and exchange interaction, respectively.

Long non-coding RNA PICART1 inhibits cell proliferation by regulating the PI3K/AKT and MAPK/ERK signaling pathways in gastric cancer.

OBJECTIVE: Gastric cancer (GC) is one of the most frequent malignancies and the second leading cause of cancer-related death in the world. The aim of this work was to illustrate the functional role of long non-coding RNA (lnRNA)-PICART1 (p53-inducible cancer-associated RNA transcript 1) in GC, thereby providing novel insights into biomarkers and therapeutic strategies in GC. PATIENTS AND METHODS: The relative expression level of lncRNA-PICART1 was evaluated by quantitative Real Time-Polymerase Chain Reaction (qRT-PCR). Cell counting kit-8 (CCK-8) assay and colony formation assay were used to determine the ability of cell proliferation. Flow cytometric analysis was performed to detect cell cycle and cell apoptosis. The protein expressions of ERK, p-ERK, AKT and p-AKT were detected by Western blotting. Furthermore, the transfected cells were used to perform tumor xenograft formation assay. RESULTS: LncRNA-PICART1 was lowly expressed in both GC tissues and cell lines. CCK-8 assay, colony formation assay and flow cytometric analysis validated that up-regulated lncRNA-PICART1 significantly suppressed cell proliferation, whereas promoted cell apoptosis. Besides, the over-expression of lncRNA-PICART1 remarkably inhibited the PI3K/AKT and ERK/MAPK signaling pathways. Tumor xenograft formation assay indicated that lncRNA-PICART1 overexpression significantly inhibited tumor formation. CONCLUSIONS: Our research illustrated that lncRNA-PICART1 functioned as a tumor suppressor in GC. The regulation of the PI3K/AKT and ERK/MAPK signaling pathways might be the underlying mechanism of the tumor suppressor role of lncRNA-PICART1. In addition, our study might bring novel insights into biomarkers and therapeutic strategies for GC.

The effect of mutation at valine-45 on the stability and redox potentials of trypsin-cleaved cytochrome b5.

In an attempt to elucidate the determinants of redox potential and protein stability in cytochrome b5, three mutants at a highly conserved residue Val45, which is a member of heme hydrophobic pocket residues have been characterized. The V45Y mutant was designed to introduce a bulkier residue and a hydroxyl group to the heme pocket. The mutants V45H and V45E were constructed to test the effect of positive and negative charge on the stability and redox potential of proteins. The influence of these mutants on the protein stability towards thermal, urea, acid, ethanol and on the redox potential were studied. It is concluded that the decrease of hydrophobic free energy and the larger volume of the tyrosine make the phenylhydroxyl group of tyrosine still sitting inside the hydrophobic pocket, while the side chain of the mutant V45E and V45H shift away from the heme pocket. The redox potentials of mutants V45Y, V45H, V45E and wild-type of cytochrome b5 are -35 mV, 8 mV, -26 mV and -3 mV, respectively. The bigger change of the V45Y on redox potential is due to the close contact between the hydroxyl group and the heme, while the changes of the V45E and V45H result from the alteration of charge density and distribution around the heme. Different relative stability of these mutants towards heat have been observed with the order: WT > V45Y-V45H > V45E being both in the oxidized and reduced state. The relative stability induced by addition of urea decreases in the order: WT > V45Y > V45H > V45E. These results suggest that the difference in the hydrophobic free energy is a major factor contributing to the stability of the Val45 mutants. Also the loose of the helix III in the mutant V45E makes it more unstable. These results indicate that residue Val45 plays an important role in the stability and redox potential of the protein.

Crystal structure of recombinant trypsin-solubilized fragment of cytochrome b(5) and the structural comparison with Val61His mutant.

The crystal structure of the recombinant trypsin-solubilized fragment of the microsomal cytochrome b(5) from bovine liver has been determined at 1.9 A resolution and compared with the reported crystal structure of the lipase-solubilized fragment of the membrane protein cytochrome b(5). The two structures are similar to each other. However, some detailed structural differences are observed: the conformation of the segment Asn16-Ser20 is quite different, some helices around the heme and some segments between the helices are shifted slightly, the heme is rotated about the normal of the mean plane of heme, one of the propionates of the heme exhibits a different conformation. The average coordination distances between the iron and the two nitrogen atoms of the imidazole ligands are the same in the two structures. Most of the structural differences can be attributed to the different intermolecular interactions which result from the crystal packing. The wild-type protein structure is also compared with its Val61His mutant, showing that the heme binding and the main chain conformations are basically identical with each other except for the local area of the mutation site. However, when Val61 is mutated to histidine, the large side chain of His61 is forced to point away from the heme pocket toward the solvent region, disturbing the micro-environment of the heme pocket and influencing the stability and the redox potential of the protein.

Effect of mutation at valine 61 on the three-dimensional structure, stability, and redox potential of cytochrome b5.

To elucidate the role played by Val61 of cytochrome b(5), this residue of the tryptic fragment of bovine liver cytochrome b(5) was chosen for replacement with tyrosine (Val61Tyr), histidine (Val61His), glutamic acid (Val61Glu), and lysine (Val61Lys) by means of site-directed mutagenesis. The mutants Val61Tyr, Val61Glu, Val61His, and Val61Lys exhibit electronic spectra identical to that of the wild type, suggesting that mutation at Val61 did not affect the overall protein structure significantly. The redox potentials determined by differential pulse voltammetry were -10 (wild type), -25 (Val61Glu), -33 (Val61Tyr), 12 (Val61His), and 17 mV (Val61Lys) versus NHE. The thermal stabilities and urea-mediated denaturation of wild-type cytochrome b(5) and its mutants were in the following order: wild type > Val61Glu > Val61Tyr > Val61His > Val61Lys. The kinetics of denaturation of cytochrome b(5) by urea was also analyzed. The first-order rate constants of heme transfer between cytochrome b(5) and apomyoglobin at 20 +/- 0.2 degrees C were 0.25 +/- 0.01 (wild type), 0.42 +/- 0.02 (Val61Tyr), 0.93 +/- 0.04 (Val61Glu), 2.88 +/- 0.01 (Val61His), and 3.88 +/- 0.02 h(-)(1) (Val61Lys). The crystal structure of Val61His was determined using the molecular replacement method and refined at 2.1 A resolution, showing that the imidazole side chain of His61 points away from the heme-binding pocket and extends into the solvent, the coordination distances from Fe to NE2 atoms of two axial ligands are approximately 0.6 A longer than the reported value, and the hydrogen bond network involving Val61, the heme propionates, and three water molecules no longer exists. We conclude that the conserved residue Val61 is located at one of the key positions, the "electrostatic potential" around the heme-exposed area and the hydrophobicity of the heme pocket are determinant factors modulating the redox potential of cytochrome b(5), and the hydrogen bond network around the exposed heme edge is also an important factor affecting the heme stability.