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Pectic oligosaccharides (POS), small molecular polymers, can be prepared from pectin by different methods. Compared with natural pectin, POS have lower molecular mass, better water solubility, higher bioavailability, and more diverse biological activities. A series of POS with different molecular masses and structures can be obtained under different preparation conditions. In addition, the biological activities of POS are closely related to their molecular mass and structures. This review aims to comprehensively summarize the preparation, purification, structure analysis, and biological activity of POS, in order to provide some references for their applications as natural active substances in the fields of food, medicine, and health products.

In this study, starch extracted from lily bulbs were modified using an ultra‐high pressure (UHP) treatment at six different pressure levels (100, 200, 300, 400, 500, and 600 MPa). The effects of UHP treatment on the physicochemical and morphological properties of lily starch were investigated. The morphological observation revealed that UHP treatment led to particle expansion and aggregation. Compared with the native and lily starch treated at 100–500 MPa, the lily starch treated at 600 MPa exhibited almost completely disrupted morphology and a larger particle size, indicating nearly complete gelatinization of the starch. The relative crystallinity of the UHP‐treated starch remarkably reduced. Gelatinization temperatures via differential scanning calorimetry decreased with increasing pressure. The rapid viscoanalyzer results revealed that the lily starch treated with UHP at 600 MPa showed low values of peak viscosity, trough viscosity, breakdown, final viscosity, and setback. These results indicated that UHP was an effective physical modification method for lily starch, UHP treatment (600 MPa, 30 min) caused nearly complete gelatinization of lily starch, and lily starch modified using UHP might expand the application of lily in the food field. [ABSTRACT FROM AUTHOR]

In this study, the effects of grafting chlorogenic acid (CA) on the antioxidant and probiotic activities of curdlan oligosaccharides (CDOS) were investigated. CDOS with degrees of polymerization of 3-6 was first obtained by degradation of curdlan with hydrogen peroxide and then grafted with CA using a free radical-mediated method under an ultrasonication-assisted Fenton system. The thermal stability and antioxidant ability of CDOS were enhanced after grafting with CA. In vitro fermentation, supplementation of CDOS-CA stimulated the proliferation of Prevotella and Faecalibacterium while inhibiting the growth of harmful microbiota. Notably, the concentration of total short-chain fatty acids and the relative abundance of beneficial bacteria markedly increased after fermentation of CDOS-CA, indicating that CA grafting could improve the probiotic activity of CDOS. Overall, the covalent binding of CDOS and CA could enhance the antioxidant and probiotic activities of CDOS, suggesting potential improvements in gastrointestinal and colonic health., Competing Interests: The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (© 2023 The Author(s).)

Amiloride-sensitive epithelial sodium channel (ENaC) is a major sodium channel in the lung facilitating fluid absorption. ENaC is composed of alpha-, beta-, and gamma-subunits, and the alpha-subunit is indispensable for ENaC function in the lung. In human lungs, the alpha-subunit is expressed as various splice variants. Among them, alpha(1)- and alpha(2)-subunits are two major variants with different upstream regulatory sequences that possess similar channel characteristics when tested in Xenopus oocytes. Despite the importance of alpha-ENaC, little was known about the relative abundance of its variants in lung epithelial cells. Furthermore, lung infection and inflammation are often accompanied by reduced alpha-ENaC expression, oxidative stress, and pulmonary edema. However, it was not clear how oxidative stress affects expression of alpha-ENaC variants. In this study, we examined relative expression levels of alpha-subunit variants in four human lung epithelial cell lines. We also tested the hypothesis that oxidative stress inhibits alpha-ENaC expression. Our results show that both alpha(1)- and alpha(2)-ENaC variants are expressed in the cells we tested, but relative abundance varies. In the two monolayer-forming cell lines, H441 and Calu-3, alpha(2)-ENaC is the predominant variant. We also show that H(2)O(2) specifically suppresses alpha(1)- and alpha(2)-ENaC variant expression in H441 and Calu-3 cells in a dose-dependent fashion. This suppression is achieved by inhibition of their promoters and is attenuated by dexamethasone. These data demonstrate the importance of the alpha(2)-subunit variant and suggest that glucocorticoids and antioxidants may be useful in correcting infection/inflammation-induced lung fluid imbalance.

Vimentin is one of the mammalian intermediate filament proteins. It is expressed in cells of mesenchymal origin and is characteristic of proliferating cells at the fetal stage. During malignancy, vimentin expression is activated in certain lung epithelial cells. Examination of a group of lung cancer cells showed a marked difference in their vimentin expression. The difference in vimentin expression among lung cancer cells is due to differential regulation at the transcriptional level. Analysis of the vimentin promoter revealed a 102-bp promoter sequence that is important for promoter activity in a lung cancer cell line in which vimentin is strongly expressed. This promoter region interacts with poly(ADP-ribose) polymerase-1 (PARP-1), which is also a transcription regulator. Exogenous expression of PARP-1 increased vimentin promoter activity. A shortened PARP-1 without the COOH-terminal catalytic domain showed the same promoter activation effect. Treatment of cells with H(2)O(2) reduced PARP-1 and vimentin expression at the protein level. H(2)O(2) also dose dependently suppressed vimentin promoter activity in cells overexpressing PARP-1. These results demonstrate that vimentin expression in lung cancer cells is regulated at the transcriptional level and that PARP-1 binds and activates the vimentin promoter independent of its catalytic domain and may play a role in H(2)O(2)-induced inhibition of vimentin expression.