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Mn 0.5 Ti 2 (PO 4) 3 with a NASICON structural is used as an anode material in potassium-ion batteries due to its abundance of vacancies that can hold potassium ions. This characteristic not only contributes to its excellent stability but also results in a high specific capacity. However, the poor electrical conductivity of the polyanionic type structure limits the material's ability to fully utilize its capacity. In this paper, the conductivity and electrochemical stability of the Mn 0.5 Ti 2 (PO 4) 3 anode material are enhanced through composite formation with an F-doped carbon layer. The introduction of F into the carbon matrix creates a large number of vacancy defects and F active sites. The vacancies enhance the transport of potassium ions on the Mn 0.5 Ti 2 (PO 4) 3 material's surface, while the active sites exhibit strong electronegativity, improving the absorption of potassium ions. Therefore, the diffusion impedance of potassium ions is significantly reduced, leading to an increased diffusion rate of potassium ions. Attributing to the improved reaction kinetics, the Mn 0.5 Ti 2 (PO 4) 3 @F-doped carbon composite demonstrates a high specific capacity of 86 mA h g−1 at 10,000 mA g−1 when used as the anode for potassium-ion batteries. Even more, the specific capacity remains a capacity of 136 mA g−1 after 3000 cycles at 1000 mA h g−1. This study enhances our comprehension of material design by investigating the alteration of carbon matrix to promote the electrochemical characteristics of materials. [ABSTRACT FROM AUTHOR]

Cell proliferation and turnover are fueled by stem cells. In a previous study, we demonstrated that rat eccrine sweat glands contained abundant bromodeoxyuridine (BrdU)-label-retaining cells (LRCs). However, morphological observations showed that eccrine sweat glands usually show little or no signs of homeostatic change. In this study, we account for why the homeostatic change is rare in eccrine sweat glands based on cytokinetic changes in BrdU-LRC turnover, and also determine the BrdU-labeled cell type. Thirty-six newborn SD rats, were injected intraperitoneally with 50 mg/kg BrdU twice daily at a 2 h interval for 4 consecutive days. After a chase period of 4, 6, 8, 12, 24 and 32 weeks, rats were euthanized, and the hind footpads were removed and processed for BrdU immunostaining, and BrdU/α-SMA and BrdU/K14 double-immunostaining. BrdU-LRCs were observed in the ducts, secretory coils and mesenchymal cells at all survival time points. The percentage of BrdU + cells in rat eccrine sweat glands averaged 4.2 ± 1.2% after 4 weeks of chase, increased slightly by the 6th week, averaging 4.4 ± 0.9%, and peaked at 8 weeks, averaging 5.3 ± 1.0%. Subsequently, the average percentage of BrdU + cells declined to 3.2 ± 0.8% by the 32nd week. There was no difference in the percentage of BrdU-LRCs among the different survival time points except that a significant difference in the percentage of BrdU-LRCs detected at 24 weeks versus 8 weeks, and 32 weeks versus 8 weeks, was observed. We concluded that the BrdU-LRCs turnover is slow in eccrine sweat glands. [ABSTRACT FROM AUTHOR]

Superoxide dismutase (SOD, EC 1.15.1.1) is a member of metalloenzyme that plays a key role in protecting organisms from oxidative damage. A novel extracellular Cu Zn superoxide dismutase RESOD was identified from Rimicaris exoculata , a dominant species that lives in close proximity to the deep-sea hydrothermal vents. It encoded a protein consisting of 227 amino acids with a signal peptide of 22 amino acids. Sequence analysis revealed that it had the characteristics of Cu Zn superoxide dismutase, and had low homology with the known SODs. Then the recombinant RESOD was expressed successfully, and high-purity RESOD was obtained. The recombinant RESOD exhibited maximal activity and stability with a temperature range of 0 °C to 10 °C. And the optimal pH for the activity and stability was about 10. However, RESOD was sensitive to some metal ions, particularly calcium. Furthermore, the biological function of RESOD was investigated in HeLa cells. It was found that RESOD could reduce the level of oxidation, and decrease the apoptosis resulted from excessive oxidant challenge. In conclusion, a novel alkali-tolerant cold-active extracellular Cu Zn SOD was characterized. The characteristics make RESOD a good candidate in a wide range of applications. [ABSTRACT FROM AUTHOR]

High expression of Bacillus thuringiensis ( Bt ) protein in transgenic Bt crops has dramatically improved the resistance of crops to some insect pests. However, some Bt crops were reported to have poorer adaptabilities to abiotic stress environments compared to their non- Bt counterparts. The biological reasons for poorer adaptabilities were still unclear. A two-year field experiment was conducted to investigate yield and physiological response of newly bred Bt rice lines with different Bt protein expression levels [MH63 ( Cry1C* ), MH63 ( Cry2A* ) and MH63 ( Cry1Ab/Ac )] and their non- Bt counterpart MH63 to drought stress. MH63 ( Cry1C* ), MH63 ( Cry2A* ) and MH63 ( Cry1Ab/Ac ) all showed lower grain yields and lower biomass under drought treatment compared to MH63. The lower grain yields and lower biomass of Bt -MH63 were mainly due to the earlier leaf senescence associated with disorder in protein metabolism under drought treatment. These variations in Bt -MH63 were found to be correlated to the BT/SP (ratio of Bt protein to soluble protein) in Bt -MH63 leaves. The impact of drought on traits of Bt -MH63 was aggravated with increase of the Bt protein expression level in the plant. These results suggested that Bt -MH63 had poorer adaptabilities to drought stress compared to their non- Bt counterpart MH63. “Bio-burden” caused by the high expression of Bt protein in the plant was proposed to be one possible reason for the poorer adaptability, and BT/SP was estimated to be an indicator for the assessment of the “bio-burden”. [ABSTRACT FROM AUTHOR]

Eccrine sweat glands are comprised of secretory coils and ducts, which are distinct in morphology and function. To better understand the roles of the two parts in development, homeostasis, wound repair and regeneration of eccrine sweat glands, we must distinguish between them. In this study, the localization of keratins and alpha-SMA in human eccrine sweat glands was examined by immunofluorescence staining. Based on the differential localization of keratins and alpha-SMA in different cell types, four pairs of antibodies (K5/K7, K5/alpha-SMA, K14/K7 and K14/alpha-SMA) were used to differentiate secretory coils from ducts by double-immunofluorescence staining. Immunofluorescence staining showed that myoepithelial cells of secretory coils expressed K5, K14 and alpha-SMA, whereas secretory cells of secretory coils expressed K7, K8, K15, K18 and K19. Ductal cells expressed K5, K8, K14 and K19. Double-staining showed that the secretory coils were K5 + /K7 + , K5 + /alpha-SMA + , K14 + /K7 + and K14 + /alpha-SMA + , whereas ducts were K5 + /K7 − , K5 + /alpha-SMA − , K14 + /K7 − and K14 + /alpha-SMA − . In conclusion, by combining use of keratins and alpha-SMA antibodies, secretory coils can be easily differentiated from ducts in morphology. [ABSTRACT FROM AUTHOR]

The secretory portions of human eccrine sweat glands secrete isotonic fluid into the lumen and then the primary fluid is rendered hypotonic during its passage to the skin surface. During the processes of sweat secretion and absorption, many enzymes and proteins play important roles. In the study, the cellular localizations of Na + /H + exchanger 1 (NHE1), cystic fibrosis transmembrane conductance regulator (CFTR), potassium channel (KC), epithelial sodium channel γ (γENaC) and vacuolar-type H+-ATPase (V-ATPase) in human eccrine sweat glands and epidermis were detected using immunofluorescence labeling. The results revealed that in the secretory coils, the basolateral membranes showed evidence of CFTR, NHE1 and KC activities, the apical membranes showed the activities of KC and NHE1, and the nucleus showed γEaNC and V-ATPase activities; in the duct, the peripheral and luminal ductal cells showed evidence of CFTR, NHE1 and KC, the apical membranes showed the activities of CFTR and NHE1, and the nucleus showed γEaNC, V-ATPase and KC activities. The cellular localization of these proteins in eccrine sweat glands is helpful to better understand the mechanisms of sweat secretion and absorption. [ABSTRACT FROM AUTHOR]

In order to evaluate the function of the repaired or regenerated eccrine sweat glands, we must first localize the proteins involved in sweat secretion and absorption in normal human eccrine sweat glands. In our studies, the cellular localization of Na + –K + -ATPase α/β, Na + –K + –2Cl-cotransporter 1 (NKCC1) and aquaporin-5 (AQP5) in eccrine sweat glands were detected by immunoperoxidase labeling. The results showed that Na + –K + -ATPase α was immunolocalized in the cell membrane of the basal layer and suprabasal layer cells of the epidermis, the basolateral membrane of the secretory coils, and the cell membrane of the outer cells and the basolateral membrane of the luminal cells of the ducts. The localization of Na + –K + -ATPase β in the secretory coils was the same as Na + –K + -ATPase α, but Na + –K + -ATPase β labeling was absent in the straight ducts and epidermis. NKCC1 labeling was seen only in the basolateral membrane of the secretory coils. AQP5 was strongly localized in the apical membrane and weakly localized in the cytoplasm of secretory epithelial cells. The different distribution of these proteins in eccrine sweat glands was related to their functions in sweat secretion and absorption. [ABSTRACT FROM AUTHOR]