BCAA insufficiency leads to premature ovarian insufficiency via ceramide-induced elevation of ROS.

Premature ovarian insufficiency (POI) is a disease featured by early menopause before 40 years of age, accompanied by an elevation of follicle-stimulating hormone. Though POI affects many aspects of women's health, its major causes remain unknown. Many clinical studies have shown that POI patients are generally underweight, indicating a potential correlation between POI and metabolic disorders. To understand the pathogenesis of POI, we performed metabolomics analysis on serum and identified branch-chain amino acid (BCAA) insufficiency-related metabolic disorders in two independent cohorts from two clinics. A low BCAA diet phenotypically reproduced the metabolic, endocrine, ovarian, and reproductive changes of POI in young C57BL/6J mice. A mechanism study revealed that the BCAA insufficiency-induced POI is associated with abnormal activation of the ceramide-reactive oxygen species (ROS) axis and consequent impairment of ovarian granulosa cell function. Significantly, the dietary supplement of BCAA prevented the development of ROS-induced POI in female mice. The results of this pathogenic study will lead to the development of specific therapies for POI.

Rice proteins and cod proteins forming shared microstructures with enhanced functional and nutritional properties.

Low water solubility strictly limits the potential applications of plant or animal proteins such as rice proteins (RPs) and cod proteins (CPs). In this study, nanoscale hydrophilic colloidal co-assemblies (80 ~ 150 nm) with excellent water solubility were prepared by hydrating RPs and CPs at pH 12 combined with neutralization. The solubility of RPs was boosted to over 90% (w/v), while most of the subunits in CPs became fully soluble. Structural analysis revealed that RPs and CPs non-covalently reacted, which triggered sheet-helix transitions and formed a compact core of RPs coated by a layer of CPs. Both proteins exposed significant hydrophilic motifs and buried hydrophobic moieties, contributing to the high water-dispersibility of their co-assemblies. Moreover, the co-assembled proteins acquired leveraged amino acid compositions between RPs and CPs. This study will enrich the processing technology of protein components, customizing their structural and nutritional characteristics.