Utilizing Wheel Washing Machine Sludge as a Cement Substitute in Repair Mortar: An Experimental Investigation into Material Characteristics.

The construction industry strives for sustainable solutions to tackle environmental challenges and optimize resource use. One such focus area is the management of industrial byproducts and waste materials, including fugitive dust control through wheel washers. While wheel washers play a pivotal role in dust management, they generate a challenging byproduct known as wheel washer sludge (WWS). The disposal of WWS is complicated due to its composition and potential hazards. Recent research explores reusing WWS in construction materials, particularly in repair mortar, aiming for sustainability and circular economy principles. This study investigates the incorporation of WWS into repair mortar formulations, evaluating mechanical properties, durability, and environmental implications. Results show that WWS enhances workability but prolongs setting time. Mechanical strength tests reveal improvements with WWS addition, especially when pretreated. Water absorption rates decrease with pretreated WWS, indicating enhanced durability. Chemical attack tests demonstrate resistance to carbonation and chloride penetration, especially with modified WWS. Freeze-thaw tests reveal improved resistance with WWS addition, particularly modified. Microstructure analysis confirms hydration products and denser matrices with WWS inclusion. Environmental hazard analysis shows WWS contains no harmful heavy metals, indicating its suitability for use in repairs. Overall, this study highlights the technical feasibility and environmental benefits of incorporating WWS into repair mortar, contributing to sustainable construction practices.

Machine Learning-Based Simulation of the Air Conditioner Operating Time in Concrete Structures with Bayesian Thresholding.

Efficient energy use is crucial for achieving carbon neutrality and reduction. As part of these efforts, research is being carried out to apply a phase change material (PCM) to a concrete structure together with an aggregate. In this study, an energy consumption simulation was performed using data from concrete mock-up structures. To perform the simulation, the threshold investigation was performed through the Bayesian approach. Furthermore, the spiking part of the spiking neural network was modularized and integrated into a recurrent neural network (RNN) to find accurate energy consumption. From the training-test results of the trained neural network, it was possible to predict data with an R2 value of 0.95 or higher through data prediction with high accuracy for the RNN. In addition, the spiked parts were obtained; it was found that PCM-containing concrete could consume 32% less energy than normal concrete. This result suggests that the use of PCM can be a key to reducing the energy consumption of concrete structures. Furthermore, the approach of this study is considered to be easily applicable in energy-related institutions and the like for predicting energy consumption during the summer.

Telmisartan Inhibits TNFα-Induced Leukocyte Adhesion by Blocking ICAM-1 Expression in Astroglial Cells but Not in Endothelial Cells.

Telmisartan is an angiotensin-II receptor blocker and acts as a selective modulator of peroxisome proliferator-activated receptor gamma (PPARγ). Several studies have demonstrated that telmisartan ameliorates depression and memory dysfunction and reduces brain inflammation. We hypothesized that the beneficial effects of telmisartan on brain could be due to modulation of the blood-brain barrier (BBB) function. Here, we examined the effect of telmisartan on tumor necrosis factor alpha (TNF-α)-induced expression of intercellular adhesion molecule 1 (ICAM-1) which plays an important role in leukocyte transcytosis through the BBB. Telmisartan blocked TNF-α-induced ICAM-1 expression and leukocyte adhesion in U87MG human glioma cells but showed no effect on human brain microvascular endothelial cells. In U87MG cells, a PPAR antagonist, GW9662 did not block the effect of telmisartan on ICAM1 expression but rather potentiated. Moreover, GW9662 caused no change in TNF-α-induced ICAM-1 expression, suggesting no implication of PPARγ in the telmisartan effect. Further studies showed that telmisartan blocked TNF-α- induced activation of c-Jun N-terminal kinase (JNK), extracellular signal-regulated kinase 1/2 (ERK1/2), p38, and nuclear factorkappa B (NF-κB). In contrast, inhibitors of JNK, ERK1/2 and NF-κB but not p38, blocked ICAM-1 expression induced by TNF-α. Thus, our findings suggest that the beneficial effect of telmisartan is likely due to the reduction of astrocytic ICAM1 expression and leukocytes adhesion to astrocytes, and that this response was mediated by the inhibition of JNK/ERK1/2/NF-κB activation and in the PPAR-independent manner. In conclusion, this study enhances our understanding of the mechanism by which telmisartan exerts the beneficial brain function.

Aß-induced degradation of BMAL1 and CBP leads to circadian rhythm disruption in Alzheimer's disease.

BACKGROUND: Patients with Alzheimer's disease (AD) frequently experience disruption of their circadian rhythms, but whether and how circadian clock molecules are perturbed by AD remains unknown. AD is an age-related neurological disorder and amyloid-ß (Aß) is one of major causative molecules in the pathogenesis of AD. RESULTS: In this study, we investigated the role of Aß in the regulation of clock molecules and circadian rhythm using an AD mouse model. These mice exhibited altered circadian behavior, and altered expression patterns of the circadian clock genes, Bmal1 and Per2. Using cultured cells, we showed that Aß induces post-translational degradation of the circadian clock regulator CBP, as well as the transcription factor BMAL1, which forms a complex with the master circadian transcription factor CLOCK. Aß-induced degradation of BMAL1 and CBP correlated with the reduced binding of transcription factors to the Per2 promoter, which in turn resulted in disruptions to PER2 protein expression and the oscillation of Per2 mRNA levels. CONCLUSIONS: Our results elucidate the underlying mechanisms for disrupted circadian rhythm in AD.

Calsenilin regulates presenilin 1/γ-secretase-mediated N-cadherin ε-cleavage and ß-catenin signaling.

Presenilin 1 (PS1) is a component of the γ-secretase complex that cleaves a variety of type I membrane proteins, including the ß-amyloid precursor protein (ß-APP), Notch, and neuronal (N)- and epithelial (E)-cadherins. N-cadherin is an essential adhesion molecule that forms a complex with, and is cleaved by, PS1/γ-secretase and ß-catenin in the plasma membrane. The purpose of this study was to determine whether calsenilin, a presenilin-interacting protein, has a functional role in PS1/γ-secretase-mediated N-cadherin ε-cleavage using Western blot analysis, RT-PCR, immunoprecipitation, subcellular fractionation, biotinylation, and a luciferase reporter assay in SH-SY5Y neuroblastoma cells. Here, we demonstrate that the expression of calsenilin leads to a disruption of PS1/γ-secretase-mediated ε-cleavage of N-cadherin, which results in the significant accumulation of N-cadherin C-terminal fragment 1 (Ncad/CTF1), the reduction of cytoplasmic Ncad/CTF2 release, and a deceleration of PS1-CTF delivery to the cell surface. Interestingly, we also found that the expression of calsenilin is associated with the redistribution of ß-catenin from the cell surface to a cytoplasmic pool, as well as with the negative regulation of genes that are targets of T-cell factor/ß-catenin nuclear signaling. Taken together, our findings suggest that calsenilin is a novel negative regulator of N-cadherin processing that plays an important role in ß-catenin signaling.

Calsenilin is degraded by the ubiquitin-proteasome pathway.

Calsenilin, a neuronal calcium binding protein that has been shown to have multiple functions in the cell, interacts with presenilin 1 (PS1) and presenilin 2 (PS2), represses gene transcription and binds to A-type voltage-gated potassium channels. In addition, increased levels of calsenilin are observed in the brains of Alzheimer's disease and epilepsy patients. The present study was designed to investigate the molecular mechanism of calsenilin degradation pathways in cultured cells. Here, we demonstrate that inhibition of the ubiquitin-proteasomal pathway (UPP) but not lysosomal pathway markedly increased the expression levels of calsenilin. Immunofluorescence analysis revealed that following proteasomal inhibition calsenilin accumulated in the endoplasmic reticulum (ER) and Golgi, while lysosomal inhibition had no effect on calsenilin localization. In addition, we found the change of subcellular localization of PS1 from diffuse pattern to punctuate staining pattern in the ER and perinuclear region in the presence of calsenilin. These findings suggest that calsenilin degradation is primarily mediated by the UPP and that impairment in the UPP may contribute to the involvement of calsenilin in disease-associated neurodegeneration.