Research conducted previously has demonstrated that apoptosis significantly influences the chicken quality. While ROS are acknowledged as significant activators of apoptosis, the precise mechanism by which they influence muscle cell apoptosis in the post-mortem remains unclear. In this study, chicken samples were treated with rosemarinic acid and H2O2 to induce varying ROS levels, and the ROS-triggered apoptosis mechanism in chicken muscle cells in post-mortem was analyzed. The TUNEL results revealed that elevated ROS levels in chicken were associated with a greater degree of muscle cell apoptosis. Western-blot results suggested that sarcoplasmic ROS could initiate apoptosis through the mitochondrial pathway by activating the MAPK-JNK signaling pathway. Moreover, TEM and shear force results demonstrated that muscle cell apoptosis initiates myofiber fragmentation and structural damage to sarcomeres, ultimately reducing chicken tenderness. This study enhances our understanding of post-mortem muscle cell apoptosis, providing valuable insights for regulating chicken quality.

While calpain\'s role in myofibrillar protein degradation is well-established, its impact on post-mortem apoptosis remains fully elucidated. This study aimed to examine how calpain influences the mitochondrial apoptotic pathway in post-mortem muscle cells and assess its potential impact on chicken tenderness. The findings indicate that the calpain inhibitor treatment could decelerate the rate of lysosome destruction in post-mortem chicken, which is a crucial factor in delaying the mitochondrial apoptotic pathway. Subsequently, this inhibition enhanced the mitochondrial membrane\'s stability and suppressed the apoptosis-inducing factor Cyt c release into the sarcoplasm. The Western blot results in a greater myofibrillar protein degradation degree in the caspase inhibitor samples compared to the calpain inhibitor samples. Interestingly, the two groups had no significant difference in shear force. Based on these reasons, a novel perspective was introduced in this paper: Calpain could affect the change in meat tenderness by regulating mitochondrial apoptosis in the post-mortem period.

Myofibril proteins degradation constitutes an important factor in quality deterioration, procedural activation or inhibition of endogenous protease potential regulates autolytic proteolysis-induced softening of post mortem fish muscle. Based on the brief introduction of myofibril proteins degradation in fish skeletal muscle, a detailed description of the main myofibril degradation properties and the distinct role played by endogenous proteases were proposed, which reflects the limitations and challenges of the current research on myofibril hydrolysis mechanisms based on the varied surrounding conditions. In addition, the latest researches on the evaluation method of myofibril proteins degradation were comprehensively reviewed. The potential use of label-free proteomics combined with bioinformatics was also emphasized and has become an important means to in-depth understand protein degradation mechanism.

Neuroinflammatory mechanisms with glial cell activation have been implicated in the pathogenic process of Alzheimer\'s disease (AD). Activation of the NLRP3 inflammasome is an essential component of the neuroinflammatory response. A role for NLRP3 activation in AD is supported by both in vitro and in vivo preclinical studies with little direct investigation of AD brain tissue. RNA expression of genes of three glial cell markers, HLA-DRA, AIF-1 and GFAP; the components of the NLRP3 inflammasome NLRP3, ASC, and caspase-1; and downstream pre-inflammatory cytokines IL-1 β and IL-18, were investigated in the temporal cortex of AD patients and age- and sex-matched controls. Protein expression of GFAP was also assessed. Increases in both mRNA and protein expression were observed for GFAP in AD. There were no significant changes in other NLRP3 activation markers between groups. Our results indicate the involvement of astrocyte activation in AD, particularly in more severe patients. We found no evidence for the specific involvement of the NLRP3 inflammasome.

The cathode/anode-electrolyte interfaces in lithium/sodium ion batteries act as the \"gate\" for the ion exchange between the solid electrode and liquid electrolyte. Understanding the interfacial properties of these solid-liquid interfaces is essential for better design high-performance lithium/sodium ion batteries. Here, we provide a novel method for studying solid-liquid interfacial properties of battery materials through combining physical vapor deposition (PVD) and beam-exit cross-sectional polishing (BEXP) followed by controlled environment multifunctional Scanning Probe Microscope (SPM). In this method, commercial battery materials can be either directly grown on the current collector substrates, or polished by obliqued Ar-ion beams to get a nanoscale flat surface which allows the multifunctional SPM to study sample directly in the liquid electrolyte or in protective oxygen/H2O free environment. This approach allows to investigate wide range of interfacial properties, including surface morphology, internal cracks, mechanical properties, electronic/ionic conductivity and surface potential, with nanoscale resolution in-operando during the battery cycles as well as post-mortem.•PVD and novel BEXP methods were introduced to prepare battery powder materials as perfect specimens for nanoscale SPM characterization.•Various physical/chemical properties of battery materials can be probed on the as-prepared specimens under liquid electrolyte using in situ/operando SPM techniques.•Ex situ/post-mortem analyses based on the controlled environment multifunction SPM characterizations can be achieved in the BEXP polished degradation battery electrodes.

We investigated ten pale, soft, and exudative (PSE), and ten normal meat samples from pig carcasses. The meat quality at 0, 5, 12, and 24 h post-mortem and the key enzyme activities at 0 and 24 h post-mortem were determined. We selected three PSE and three normal samples for proteomics analysis at 0 h and 24 h post-mortem. No remarkable differences in pyruvate kinase (PK) and lactate dehydrogenase (LDH) activity were observed between samples at 0 h post-mortem; however, creatine kinase (CK) activity was significantly higher in PSE meat. Hexokinase (HK) activity in PSE samples was higher than that in normal samples at 24 h post-mortem. Bioinformatics analysis of the proteome showed that PSE was related to glycolysis, TCA cycle, oxidative phosphorylation, muscle tissue structure, signal transduction, and molecular chaperones. This research found that proteins such as troponin T slow skeletal muscle isoform X, GADPH, L-lactate dehydrogenase A chain, and gamma-enolase isoform X1 might be responsible for PSE.

The relationship between glycogen phosphorylase activity and phosphorylation levels in the longissimus thoracis muscle post-mortem was studied. Sixty lamb samples were collected at 0.5 h, 2 h, 6 h, 12 h, 24 h, 48 h, and 72 h post-mortem and divided into three groups (n = 6) with different glycolytic rates (fast, intermediate, and slow) according to the pH at 6 h post-mortem. The phosphorylation level and activity and expression of glycogen phosphorylase were determined. The results showed that the phosphorylation level and activity of glycogen phosphorylase in the slow pH decline group was lower than that in the fast pH decline group during 24 h post-mortem (P < .05). There was a significant positive correlation between the glycogen phosphorylase activity and the phosphorylation level. In conclusion, these data demonstrated that the glycogen phosphorylase activity in lambs was affected by phosphorylation levels and postmortem duration.

Poisoning by organophosphorus insecticides such as methamidophos makes up a significant portion of forensic identification cases in China. Stability of methamidophos during specimen storage remains largely unknown. This study aimed to examine the long-term stability of methamidophos in postmortem specimens. Three experimental dogs after oral administration of methamidophos were sacrificed, and blood and liver specimens were collected and stored at various conditions. Gas chromatography-mass spectrometry (GC/MS) was used to measure the methamidophos concentrations after 0, 4, 7, 12, 16, 60, and 180 days of storage. The results showed that methamidophos was not stable and followed first-order degradation kinetics at all storage conditions investigated. The degradation half-life in blood was 12.2, 16.9, 11.0, and 1.0 days when the samples were stored at room temperature (RT, 20 °C), 4 °C, -20 °C, and at RT with 1 % sodium fluoride (NaF), respectively. The degradation half-life in liver was 4.1, 9.8, 17.8, and 2.0 days when the samples were stored at RT, 4 °C, -20 °C, and at RT with liver fixed in 10 % formaldehyde solution, respectively. These findings are significant in guiding sample storage and data interpretation. Specimens containing methamidophos should be stored at -20 °C and analyzed as early as possible. Addition of NaF in blood and fixation of liver in formaldehyde should be avoided due to the accelerated degradation of methamidophos under these conditions. The preliminary study suggests that it might be possible to calculate methamidophos concentration at the time of death based on its first-order degradation kinetic under specific storage conditions.