Phycobiliprotein Peptide Extracts from Arthrospira platensis Ameliorate Nonalcoholic Fatty Liver Disease by Modulating Hepatic Lipid Profile and Strengthening Fat Mobilization.

Arthrospira platensis phycobiliprotein peptide extracts (PPEs) exhibit potential mitigative effects on hepatic steatosis. However, the precise role of PPEs in addressing high-fat-induced nonalcoholic fatty liver disease (NAFLD), as well as the underlying mechanism, remains to be elucidated. In this study, NAFLD was induced in rats through a high-fat diet (HFD), and the rats were subsequently treated with PPEs for a duration of 10 weeks. The outcomes of this investigation demonstrate that PPE supplementation leads to a reduction in body weight gain, a decrease in the accumulation of lipid droplets within the liver tissues, alterations in hepatic lipid profile, regulation of lipolysis-related gene expression within white adipose tissues and modulation of intestinal metabolites. Notably, PPE supplementation exhibits a potential to alleviate liver damage by manipulating neutral lipid metabolism and phospholipid metabolism. Additionally, PPEs appear to enhance fat mobilization by up-regulating the gene expression levels of key factors such as HSL, TGL, UCP1 and UCP2. Furthermore, PPEs impact intestinal metabolites by reducing the levels of long-chain fatty acids while concurrently increasing the levels of short-chain fatty acids. The findings from this study unveil the potential of PPE intervention in ameliorating NAFLD through the modulation of hepatic lipid profile and the reinforcement of the fat mobilization of intestinal metabolites. Thus, PPEs exhibit noteworthy therapeutic effects in the context of NAFLD.

Reconfiguration of Gut Microbiota and Reprogramming of Liver Metabolism with Phycobiliproteins Bioactive Peptides to Rehabilitate Obese Rats.

Phycobiliproteins (derived from Arthrospira platensis) bioactive peptide extracts (PPE) possess multiple pharmacological effects in the mitigation of human metabolic disorders. The role of PPE in the treatment of diet-induced obesity and the understanding of the underlying mechanism between the gut microbiome and metabolic blood circulation for obese patients remains poorly understood. In this study, we showed that PPE attenuated obesity by reducing body weight, and ameliorated glucose and lipid indexes in serum. In particular, PPE is postulated to mitigate liver steatosis and insulin resistance. On the other hand, dietary treatment with PPE was found to "reconfigure" the gut microbiota in the way that the abundances were elevated for Akkermansia_muciniphila, beneficial Lactobacillus and Romboutsia, SCFA-producing species Faecalibacterium prausnitzii, Lachnospiraceae_bacterium, Clostridiales_bacterium, probiotics Clostridium sp., Enterococcus faecium, and Lactobacillus_johnsonii, while the abundance of Firmicutes was reduced and that of Bacteroidetes was increased to reverse the imbalance of Firmicutes/Bacteroidetes ratio. Finally, the metabolomics of circulating serum using UHPLC-MS/MS illustrated that PPE supplementation indeed promoted lipid metabolism in obese rats. As summary, it was seen that PPE reprogrammed the cell metabolism to prevent the aggravation of obesity. Our findings strongly support that PPE can be regarded as a potential therapeutic dietary supplement for obesity.

InlB-mediated Listeria monocytogenes internalization requires a balanced phospholipase D activity maintained through phospho-cofilin.

Internalization of Listeria monocytogenes into non-phagocytic cells is tightly controlled by host cell actin dynamics and cell membrane alterations. However, knowledge about the impact of phosphatidylcholine cleavage driven by host cell phospholipase D (PLD) on Listeria internalization into epithelial cells is limited. Here, we report that L. monocytogenes activates PLD in Vero cells during the internalization. With immunostaining it was shown that both PLD1 and PLD2 surrounded partially or completely the phagocytic cup of most L. monocytogenes. Either up- or down-regulation of PLD expression (activity) diminished Listeria internalization. Both PLD1 and PLD2 in Vero cells were required for efficient Listeria internalization, and could substitute for each other in the regulation of Listeria internalization. Further, exogenous InlB activated host cell PLD1 and PLD2 via the Met receptor, and restored host PLD activation by InlB-deficient L. monocytogenes. InlB-induced PLD activation and Listeria internalization were tightly controlled by phospho-cycling of cofilin. PLD1, but not PLD2, was involved in cofilin-mediated PLD activation and Listeria internalization. These data indicate that cofilin-dependent PLD activation induced by InlB may represent a novel regulation mechanism for efficient Listeria internalization into epithelial cells.

ß-1,3-Glucan-induced host phospholipase D activation is involved in Aspergillus fumigatus internalization into type II human pneumocyte A549 cells.

The internalization of Aspergillus fumigatus into lung epithelial cells is a process that depends on host cell actin dynamics. The host membrane phosphatidylcholine cleavage driven by phospholipase D (PLD) is closely related to cellular actin dynamics. However, little is known about the impact of PLD on A. fumigatus internalization into lung epithelial cells. Here, we report that once germinated, A. fumigatus conidia were able to stimulate host PLD activity and internalize more efficiently in A549 cells without altering PLD expression. The internalization of A. fumigatus in A549 cells was suppressed by the downregulation of host cell PLD using chemical inhibitors or siRNA interference. The heat-killed swollen conidia, but not the resting conidia, were able to activate host PLD. Further, ß-1,3-glucan, the core component of the conidial cell wall, stimulated host PLD activity. This PLD activation and conidia internalization were inhibited by anti-dectin-1 antibody. Indeed, dectin-1, a ß-1,3-glucan receptor, was expressed in A549 cells, and its expression profile was not altered by conidial stimulation. Finally, host cell PLD1 and PLD2 accompanied A. fumigatus conidia during internalization. Our data indicate that host cell PLD activity induced by ß-1,3-glucan on the surface of germinated conidia is important for the efficient internalization of A. fumigatus into A549 lung epithelial cells.