Datasheet1_Inspiratory muscle training to reduce risk of pulmonary complications after coronary artery bypass grafting: a systematic review and meta-analysis.docx

BackgroundPulmonary complications occur in a substantial proportion of patients who undergo coronary artery bypass grafting. Inspiratory muscle training (IMT), a simple, well-tolerated physical therapy, has been proposed to reduce the risk of complications, but its efficacy remains controversial.MethodRandomized controlled trials (RCTs) examining the influence of IMT on the risk of pulmonary complications after coronary artery bypass grafting were identified from PubMed, Embase, CENTRAL, CINAL, and Web of Science through March 2023. Data were meta-analyzed for the primary outcomes of pulmonary complications, defined as pneumonia, pleural effusion, and atelectasis; and in terms of the secondary outcomes of maximum inspiratory pressure, maximum expiratory pressure, length of hospitalization, 6 min walk test, and peak expiratory flow and other outcomes. Risk of bias and quality of evidence assessments were carried out using the RoB 2.0 and Grading of Recommendations Assessment, Development and Evaluation (GRADE) applied to primary outcomes of pulmonary complications.ResultsData from eight RCTs involving 755 patients were meta-analyzed. IMT was associated with a significantly lower risk of postoperative pneumonia [relative risk (RR) 0.39, 95% confidence interval (CI) 0.25–0.62, P 2O, 95% CI 13.86–19.24, P 2O, 95% CI 2.39–15.60, P = 0.008) and maximum expiratory pressure (MD 7.15 cmH2O, 95% CI: 1.52–12.79, P = 0.01), and with significantly shorter hospitalization (MD −1.71 days, 95% CI −2.56 to −0.87, P ConclusionsThe available evidence from medium and high quality trials suggests that IMT can significantly decrease the risk of pneumonia and atelectasis after coronary artery bypass grafting while shortening hospitalization and improving the strength of respiratory muscles.Systematic Review Registrationhttps://www.crd.york.ac.uk/prospero/, identifier: CRD42023415817.</p

NMR Solution Structure of ATT_p, an <i>Arabidopsis thaliana</i> Trypsin Inhibitor^†^,^‡

The three-dimensional structure of the precursor form of the Arabidopsis thaliana trypsin inhibitor (ATTp, GenBank entry Z46816), a 68-residue (∼7.5 kDa) rapeseed class proteinase inhibitor, has been determined in solution at pH 5.0 and 25 °C by multinuclear magnetic resonance spectroscopy. The protein contains one α-helix and two strands of antiparallel β-sheet, with a type IV β-turn connecting the two strands. The α-helix and the inhibitory loop are connected to the β-sheet through three disulfide bridges; a fourth disulfide bridge connects the N- and C-termini. The overall structural topology of ATTp is similar to those of the sweet tasting protein brazzein (rmsd of 3.0 Å) and the antifungal protein Rs-Afp1 [a knottin protein from radish (Raphanus sativus), rmsd of 2.7 Å]. The precursor segment in ATTp is disordered, as visualized by the final 20-conformer ensemble and as confirmed by 15N heteronuclear NOE analysis. The overall fold of ATTp is distinct from those of other classes of serine proteinase inhibitors except in the inhibitor loop; therefore, it represents a new inhibitor fold

Table1_Inspiratory muscle training to reduce risk of pulmonary complications after coronary artery bypass grafting: a systematic review and meta-analysis.docx

BackgroundPulmonary complications occur in a substantial proportion of patients who undergo coronary artery bypass grafting. Inspiratory muscle training (IMT), a simple, well-tolerated physical therapy, has been proposed to reduce the risk of complications, but its efficacy remains controversial.MethodRandomized controlled trials (RCTs) examining the influence of IMT on the risk of pulmonary complications after coronary artery bypass grafting were identified from PubMed, Embase, CENTRAL, CINAL, and Web of Science through March 2023. Data were meta-analyzed for the primary outcomes of pulmonary complications, defined as pneumonia, pleural effusion, and atelectasis; and in terms of the secondary outcomes of maximum inspiratory pressure, maximum expiratory pressure, length of hospitalization, 6 min walk test, and peak expiratory flow and other outcomes. Risk of bias and quality of evidence assessments were carried out using the RoB 2.0 and Grading of Recommendations Assessment, Development and Evaluation (GRADE) applied to primary outcomes of pulmonary complications.ResultsData from eight RCTs involving 755 patients were meta-analyzed. IMT was associated with a significantly lower risk of postoperative pneumonia [relative risk (RR) 0.39, 95% confidence interval (CI) 0.25–0.62, P 2O, 95% CI 13.86–19.24, P 2O, 95% CI 2.39–15.60, P = 0.008) and maximum expiratory pressure (MD 7.15 cmH2O, 95% CI: 1.52–12.79, P = 0.01), and with significantly shorter hospitalization (MD −1.71 days, 95% CI −2.56 to −0.87, P ConclusionsThe available evidence from medium and high quality trials suggests that IMT can significantly decrease the risk of pneumonia and atelectasis after coronary artery bypass grafting while shortening hospitalization and improving the strength of respiratory muscles.Systematic Review Registrationhttps://www.crd.york.ac.uk/prospero/, identifier: CRD42023415817.</p

Tribological Properties of Alkylphenyl Diphosphates as High-Performance Antiwear Additive in Lithium Complex Grease and Polyurea Grease for Steel/Steel Contacts at Elevated Temperature

The alkylphenyl diphosphates pentaerythritol tetrakis­(diphenyl phosphate) (PDP) and trimethylolpropane tris­(diphenyl phosphate) (TDP) were evaluated as the antiwear additives in lithium complex grease and polyurea grease at 200 °C. The results indicated that both additives may effectively reduce the sliding friction and wear as compared to the base greases. The tribological performances were generally better than the normally used molybdenum disulfide (MoS₂)-based additive package in lithium complex grease and also in polyurea grease. Boundary lubrication films composed of Fe­(OH)­O, Fe₃O₄, FePO₄, and compounds containing the P–O bonds were formed on the worn surface, which resulted in excellent friction reduction and antiwear performance

FLS2 does not regulate CALK and IFT but suppresses CrKinesin13 phosphorylation independently of FLS1.

(A) CALK phosphorylation is not affected in fls2. WT and fls2 cells were treated with NaPPi for ciliary disassembly. Cell lysates at the indicated time were analyzed by immunoblotting with CALK antibody. CALK underwent phosphorylation with slower gel migration, which were not affected in fls2. (B) FLS2 does not affect increasing transport of IFT proteins in cilia. WT or fls2 Cells were treated with or without 20 mM NaPPi for 10 min followed by cilia isolation and immunoblotting. IFT121, a subunit of IFT-A and IFT46, a subunit of IFT-B were analyzed. α-tubulin was used as a loading control. (C) Loss of FLS2 does not affect ciliary transport of CrKinesin13 but induces earlier onset of its phosphorylation. WT or fls2 cells were treated with NaPPi for the indicated times followed by cilia isolation and immunoblotting. The slower migration form of CrKinesin13 is due to phosphorylation as demonstrated previously. (D) The kinase activity of FLS2 is required for suppression of earlier onset of CrKinesin13 phosphorylation. Isolated cilia from cell samples that were treated with or without NaPPi for 10 min were subjected to immunoblot analysis with the indicated antibodies. (E) FLS1 phosphorylation is not altered in fls2. Cell samples as indicated were analyzed by immunoblotting with FLS1 antibody. (F) FLS2 phosphorylation is not altered in fls1. fls1 or fls2 cells expressing FLS2-HA were treated for the indicated times followed by Phos-tag immunoblotting. FLS2 phosphorylation as evidenced by patterns of gel migration was similar between fls1 and fls2 cells. (G) Generation of an fls1-kd/fls2 strain by RNAi depletion of FLS1 in fls2 cells. Cell samples as indicated were subjected to immunoblotting with anti-FLS1 antibody. (H) CrKinesin13 phosphorylation in fls1-kd/fls2 cells. Cilia were isolated from cell samples that were treated with NaPPi for 10 min and were then subjected to immunoblotting. (I) fls1-kd/fls2 cells show more severe defect in ciliary disassembly. Cells as indicated were induced for ciliary disassembly followed by ciliary length measurement at the indicated times. Bars indicate SD.</p

Venn diagram showing genes expressed in <i>Brassica</i> hexaploid and its parents.

<p>A, <i>B</i><i>. rapa</i>; B, <i>B</i><i>. carinata</i>; C, <i>Brassica</i> hexaploid.</p

Use of Pollen Solid-Phase Extraction for the Determination of <i>trans</i>-Resveratrol in Peanut Oils

In this study, a simple and convenient method for the determination of <i>trans</i>-resveratrol (TRA) in peanut oils based on pollen grain solid-phase extraction (SPE) was developed. Pollen grains were used as normal-phase SPE sorbent to separate TRA from peanut oils for the first time. As a naturally occurring material, pollen grains exhibited an excellent adsorption capacity for polyphenolic compounds due to their particular functional structures such as hydroxyl groups, saturated and unsaturated aliphatic chains with aromatics. Their stable compositions as well as adequate particle size (30–40 μm) also make them suitable for SPE. Several parameters influencing extraction performance were investigated. Coupled with high-performance liquid chromatography-ultraviolet detection (HPLC-UV), a green purification method for fast determination of TRA in peanut oils using pollen grain cartridges as sorbents was established. The linearity range of the proposed method was 10–2500 ng·g^–1 with a satisfactory correlation coefficient (<i>r</i>²) of 0.9999. The limit of detection (LOD) for TRA in peanut oils was 2.7 ng·g^–1, and the recoveries in spiked oil samples were from 70.2% to 98.4% with the relative standard deviations (RSDs) less than 4.9% (intraday) and 5.2% (interday). This method was successfully applied to the analysis of TRA in several peanut oils with different brands from local market as well as other kinds of vegetable oils

Increased ciliary trafficking of FLS2 upon induction of ciliary disassembly.

(A) FLS2 is a cell body protein and transported to cilia during ciliary disassembly as examined by immunostaining. fls2 cells expressing FLS2-HA were treated with or without NaPPi for 10 min followed by immunostaining with HA and α-tubulin antibodies. WT cells were used as control. Bar, 5 μm. (B) Analysis of ciliary transport of FLS2 by immunoblotting. fls2 cells expressing FLS2-HA were separated into cell bodies (CB) and cilia (C) fractions after treatment with or without NaPPi for 10 min followed by immunoblotting. WC, whole cells. (C) Ciliary FLS2 is associated with the axonemes. Cilia isolated from cells treated with or without NaPPi for 10 min were fractionated into membrane matrix (M+M) and axonemal fractions followed by immunoblotting with the indicated antibodies. FMG1, a ciliary membrane protein was used as a control for M+M fractions. (D) FLS2 is transported to cilia during ciliary disassembly in zygote development. Immunostaining analysis of FLS2 in mt+ and mt- gametes (G+ and G-), 0.5 hr (Z0.5h) and 2.5 hr (Z2.5h) zygotes. Bar, 5 μm. (E) FLS2 in cilia undergoes dephosphorylation during ciliary disassembly but its levels are unchanged. Cilia were isolated from cells treated with NaPPi for 10 or 120 min. The isolated cilia were treated with or without phosphatase (Ptase) followed by phos-tag immunoblotting. Please note that FLS2 in the 10 min sample without phosphatase treatment exhibited slower gel motility shift relative to other samples. (F) The kinase activity of FLS2 is not required for its ciliary transport. Whole cells (WC) or isolated cilia from kinase-dead K33R mutant cells treated with or without NaPPi for 10 min were subjected to immunoblot analysis. (G) FLS1 does not affect ciliary transport of FLS2. Cilia isolated from fls1 cells expressing FLS2-HA treated with or without NaPPi were analyzed by phos-tag immunoblotting. fls2 cells expressing FLS2-HA were used as control. Ciliary transport as well as gel mobility of FLS2 expressed in fls1 were similar to the control.</p

FLS2 is a cargo of IFT70 for ciliary transport.

(A) Ciliary transport of FLS2 depends on IFT. Temperature sensitive mutant fla10-1 cells expressing FLS2-HA were incubated at the indicated temperatures for 1h followed by treatment with NaPPi or not for 10 min. The cilia were then isolated for immunoblotting with the indicated antibodies. (B) FLS2 interacts with IFT70 shown in yeast two-hybrid assays. Subunits of IFT-B or IFT-A were transformed respectively into yeast cells with FLS2, followed by growth on selection medium lacking Leu and Trp (-2) or Leu, Trp, His and Ade (-4). (C-D) The C-terminal non-kinase region of FLS2 is required for its interaction with IFT70. Full-length FLS2 and its deletion variants were assayed for their interaction with IFT70 in yeast two-hybrid assays (C). A GST pull-down assay of bacterial expressed FLS2-CT and IFT70 (D). (E) Co-immunoprecipitation of FLS2 and IFT70. Cilia were isolated from control cells (WT) or fls2 cells expressing FLS2-HA during ciliary disassembly followed by immunoprecipitation with anti-HA antibody and immunoblotting. (F-G) TPR1-3 of IFT70 is essential for its interaction with FLS2. Full-length of IFT70 and its various segments (E) or various TPR deletion mutants (F) were subjected to yeast two-hybrid assays with FLS2.</p

The C-terminal non-kinase region of FLS2 is required for its ciliary transport and proper ciliary disassembly.

(A) Deletion of TPR1, TPR2 or TPR3 of IFT70 abrogates its interaction with IFT52-IFT88 dimer. Cell lysates from bacterial cells expressing His-tagged full-length IFT70 and its various deletion mutants (IFT70*-His) were mixed, respectively, with cell lysates from cells expressing GST-IFT52 and IFT88-His followed by GST pull-down assay. His and GST antibodies were used for immunoblotting. (B) Expression of C-terminal deletion mutant of FLS2 in fls2 cells. fls2 cells expressing HA-tagged full-length (FL) FLS2 or its C-terminal deletion mutants (ΔCT) (three strains 11, 109, 191) were analyzed by immunoblotting. fls2 cells were used as a negative control. (C) The C-terminal region of FLS2 is required for its ciliary transport. Cilia were isolated from fls2 cells expressing full-length FLS2 or ΔCT mutant that were treated with or without NaPPi for 10 min followed by immunoblot analysis. (D) The C-terminal region of FLS2 does not affect its kinase activity. FLS2 was immunoprecipitated with anti-HA from cell samples as indicated and subjected to immunoblot analysis and in vitro kinase assay. In vitro kinase assay was performed as shown in Fig 3C. (E-F) Failed ciliary transport of FLS2 by C-terminal deletion induces CrKinesin13 phosphorylation and impairs ciliary disassembly. Cilia isolated from cell samples as indicated were analyzed by immunoblotting (E). fls2 cells expressing full-length (FL) FLS2 or ΔCT mutant were induced for ciliary disassembly by NaPPi treatment followed by ciliary length measurement at the indicated times. fls2 cells were used as control. Bars indicate SD.</p