Effect of hUC-MSCs on the NLRP3/Caspase-1 Pathway in APP/PS1 Mice

[Objectives] To investigate the effect of human umbilical cord mesenchymal stem cells (hUC-MSCs) on the NOD-like receptor protein 3 (NLRP3)/cysteinyl aspartate specific proteinase (Caspase-1) pathway within the cerebral cortex of a mouse model of Alzheimer s disease (AD).[Methods] Twelve 6-month-old female APP/PS1 mice were randomly assigned to two groups: the model group (MOD, n =6) and the hUC-MSCs treatment group (MSC, n =6). Six 6-month-old C57BL/6N mice were utilized as a control group (CON, n =6). All mice underwent caudal vein injections of hUC-MSCs. Following a 4-week treatment, the mice from each group were euthanized. The expression levels of NLRP3, Caspase-1 protein, and mRNA in the cerebral cortex of each group were assessed using Western blotting and real-time fluorescence quantitative PCR assays.[Results] The results of immunoblotting showed that the expression levels of NLRP3 and Caspase-1 proteins in the MOD group were significantly higher than those observed in the CON group. Furthermore, the expression levels of NLRP3 and Caspase-1 proteins in the MSC group were found to be lower than those in the MOD group. Additionally, the findings from real-time fluorescence quantitative PCR assay demonstrated that the mRNA levels of NLRP3 and Caspase-1 in the MOD group were elevated compared to the CON group. Conversely, the mRNA levels of NLRP3 and Caspase-1 in the MSC group were reduced in comparison to the MOD group.[Conclusions] hUC-MSCs have the capacity to modulate the expression of the NLRP3/Caspase-1 pathway within the cerebral cortex of APP/PS1 mice. This modulation may be associated with the neuroinflammatory processes mediated by hUC-MSCs in the brains of APP/PS1 mice.

4.8 nm Concave {M_(72)}(M=Co,Ni,Fe) metal-organic polyhedra capped by 18 calixarenes

Three 4.8 nm isostructural{M_(72)}(M=Co^(Ⅱ) for CIAC-128,Ni^(Ⅱ) for CIAC-129,Fe^(Ⅱ) for CIAC-130) metal-organic polyhedra(MOPs) are constructed by eighteen M_(4)-p-tert-butylthiacalix[4]arene (M_(4)-TC4A) units bridged via sixteen four-connected 5,5′-(1H-1,2,4-triazole-3,5-diyl) diisophthalic acid (H_(4)TADIPA) linkers.These MOPs are featured with a rarely reported concave coordination cage,which can be simplified as a squeezed double-decker hexagonal prism pressed from the top and bottom hexagonal faces.Furthermore,CIAC-128,CIAC-129 and CIAC-130 are the highest nuclearity discrete clusters of Co,Ni and Fe reported so far.CIAC-128 has higher separation selectivity of C_(3)H_(8) than CH_(4) under ambient conditions,and also exhibits separation selectivity for C_(2)H_(6)/CH_(4),C_(2)H_(2)/CH_(4),and C_(2)H_(4)/CH_(4).In addition,CIAC-128 can provide the cavity for the confined synthesis of noble metal nanoclusters such as Pd nanoclusters and the resulting Pd@CIAC-128 hybrids show higher electrocatalytic activity than commercial Pt/C towards hydrogen evolution reaction (HER).

OsDMI3-mediated OsUXS3 phosphorylation improves oxidative stress tolerance by modulating OsCATB protein abundance in rice

Calcium(Ca^(2+))/calmodulin(CaM)-dependent protein kinase(CCaMK)is an important positive regulator of antioxidant defenses and tolerance against oxidative stress.However,the underlying molecular mechanisms are largely unknown.Here,we report that the rice(Oryza sativa)CCa MK(OsDMI3)physically interacts with and phosphorylates OsUXS3,a cytosol-localized UDP-xylose synthase.Genetic and biochemical evidence demonstrated that OsUXS3 acts downstream of OsDMI3 to enhance the oxidative stress tolerance conferred by higher catalase(CAT)activity.Indeed,OsUXS3 interacted with CAT isozyme B(OsCATB),and this interaction was required to increase OsCATB protein abundance under oxidative stress conditions.Furthermore,we showed that OsDMI3 phosphorylates OsUXS3 on residue Ser-245,thereby further promoting the interaction between OsUXS3 and OsCATB.Our results indicate that OsDMI3 promotes the association of OsUXS3 with OsCATB to enhance CAT activity under oxidative stress.These findings reveal OsUXS3 as a direct target of OsDMI3 and demonstrate its involvement in antioxidant defense.