Advances in diagnosis and treatment of mechanical hemolysis following percutaneous interventional for valvular heart diseases. / å¿ƒè„ç“£è†œç— ä»‹å ¥æ²»ç–—æœ¯åŽæœºæ¢°æ€§æº¶è¡€è¯Šç–—è¿›å±•.

Valvular heart disease is one of the common heart diseases in clinical practice, characterized by valve stenosis and/or incomplete closure. At present, drug therapy, surgery, and emerging percutaneous intervention therapy are the main treating methods for heart valve disease. Although the research and development of percutaneous intervention therapy devices is relatively mature, there are still problems such as postoperative mechanical hemolysis. The occurrence of mechanical hemolysis is associated with factors such as excessive shear stress experienced by red blood cells, direct interaction between red blood cells and the heart and valve surfaces, and thrombus formation. Furthermore, the presence of postoperative infection and other hemolytic diseases can also affect the occurrence of mechanical hemolysis. Although most patients are asymptomatic when hemolysis occurs, there are still critical cases. This type of hemolysis can accelerate the deterioration of the condition, and even endanger life in severe cases. Therefore, elucidating the background, pathogenesis, epidemiology, and related clinical research progress of mechanical hemolysis after percutaneous intervention therapy for valvular heart disease is of great significance for guiding the standardized diagnosis and treatment of the disease.

Interaction of Pyrogallol-Containing Polyphenols with Mucin Reinforces Intestinal Mucus Barrier Properties.

High consumption of polyphenol-rich green tea, coffee, fruits, and vegetables is associated with a low risk of human chronic diseases. Recent studies highlight the relevance of polyphenol-mediated gut microbiota modulation and its impact on mucus barrier. Herein, we study the direct interaction of epicatechin (EC), epigallocatechin gallate (EGCG), and tannic acid (TA) with intestinal mucin by isothermal titration calorimetry and multiple particle tracking and the impact on mucus barrier using ex vivo mucus and Caco-2/HT29-MTX cocultures. Results show that pyrogallol-containing polyphenols EGCG and TA exhibit strong binding to intestinal mucin and reinforce mucus barrier, whereas EC does not. ECGG and TA also mitigate gliadin-mediated cytotoxicity and inflammation. The chemical binding of EGCG and TA to the nucleophilic thiol groups of mucins shows their roles as cross-linkers of mucin networks. These results bring a novel understanding of the health benefits of polyphenols and provide support for the consumption of pyrogallol-containing beverages like green tea as a potential dietary therapy for gluten-related disorders.

Undigestible Gliadin Peptide Nanoparticles Penetrate Mucus and Reduce Mucus Production Driven by Intestinal Epithelial Cell Damage.

Wheat protein is the most consumed plant protein in our diet, and there is an increased prevalence of wheat/gluten intolerance and adherence to a gluten-free diet in many countries. Despite the known immunodominant effect of undigested gliadin peptides responsible for gluten-related intolerance, it remains unclear if and how gliadin peptides self-assemble into ordered nanostructures during gastrointestinal digestion, as well as their biological impact on the mucus barrier function. In this study, we purified undigestible gliadin peptide nanoparticles (UGPNs) by ultracentrifugation and characterized their structural and physiochemical properties. The results demonstrate that the UGPNs are self-assembled nanostructures generated by cationic amino acids (Lys and Arg)-capped surfactant-like peptides (SLPs), mainly derived from γ-gliadin and α-gliadin. SLPs trigger the concentration-dependent self-assembly driven by ß-sheet conformational transitions above their critical aggregation concentration (cac, ∼0.1 mg/mL). UGPNs can easily penetrate the mucus layer in Caco-2/HT29-MTX cocultures with a high Papp value (∼5.7 × 10-6 cm/s) and reduce the production and thickness of the mucus layer driven by intestinal epithelial cell damage. Isothermal titration calorimetry and Langmuir monolayer studies indicate that the self-assembled state of UGPNs significantly affects their binding to DPPC/DOPE lipid membrane models. These results highlight the relevance of the self-assembly of gliadin peptides as a trigger of mucosal inflammation-related wheat/gluten intolerance.