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The objective of this study was to determine the effects of growth-related myopathies, i.e., normal, wooden breast (WB), white striping (WS), and the combined lesions of WS and WB (WS + WB), on the molecular response of Caco-2 cells. A total of 24 cooked chicken breasts (n = 6 per myopathy) was subjected to an in vitro digestion using an enzymatic process mimicking human gastrointestinal digestion. Based on peptidomics, in vitro protein digestion of the abnormal samples, particularly WB meat, resulted in more peptides with lower molecular mass relative to those of normal samples. The cooked meat hydrolysates obtained at the end of the digestion were applied to a Caco-2 cell model for 4 h. The cell viability of treated normal and abnormal samples was not different (p ≥ 0.05). Absolute transcript abundances of genes associated with primary oxidative stress response, including nuclear factor erythroid 2 like 2, superoxide dismutase, and hypoxia-inducible factor 1 were determined using a droplet digital polymerase chain reaction. No significant differences in transcript abundance of those genes in Caco-2 cells were demonstrated between normal and the abnormal samples (p ≥ 0.05). Overall, the findings supported that, compared to normal meat, the cooked chicken meat with growth-related myopathies might be digested and absorbed to a greater extent. The cooked abnormal meat did not exert significant transcriptional impacts regarding oxidative stress on the human epithelial Caco-2 cells. [ABSTRACT FROM AUTHOR]

The study explored proteomics to better understand the relationship between type 2 diabetes (T2DM) and hypertension (HT) in Thai adults, using shotgun proteomics and bioinformatics analysis. Plasma samples were taken from 61 subjects: 14 healthy subjects (mean age = 40.85 ± 7.12), 13 with T2DM (mean age = 57.38 ± 6.03), 16 with HT (mean age = 66.87 ± 10.09), and 18 with coexisting T2DM/HT (mean age = 58.22 ± 10.65). Proteins were identified using liquid chromatography-tandem mass spectrometry (LC-MS/MS). Protein–protein interactions were analyzed using the Search Tool for the Retrieval of Interacting Genes/Proteins (STRING) version 11.5. We identified six unique proteins in T2DM patients, including translationally controlled 1 (TPT1) and nibrin (NBN), which are associated with the DNA damage response. In HT patients, seven unique proteins were identified, among them long-chain fatty acid-CoA ligase (ASCL), which functions in the stimulation of triacylglycerol and cholesterol synthesis, and NADPH oxidase activator 1 (NOXA1), which is involved in high blood pressure via angiotensin II-induced reactive oxygen species (ROS)-generating systems. In coexisting T2DM/HT patients, six unique proteins were identified, of which two—microtubule-associated protein 1A (MAP1A)—might be involved in dementia via RhoB-p53 and diacylglycerol kinase beta (DGKB), associated with lipid metabolism. This study identified new candidate proteins that are possibly involved in the pathology of these diseases. [ABSTRACT FROM AUTHOR]

Alzheimer's disease (AD) is a neurodegenerative disease that causes physical damage to neuronal connections, leading to brain atrophy. This disruption of synaptic connections results in mild to severe cognitive impairments. Unfortunately, no effective treatment is currently known to prevent or reverse the symptoms of AD. The aim of this study was to investigate the effects of three synthetic peptides, i.e., KLVFF, RGKLVFFGR and RIIGL, on an AD in vitro model represented by differentiated SH-SY5Y neuroblastoma cells exposed to retinoic acid (RA) and brain-derived neurotrophic factor (BDNF). The results demonstrated that RIIGL peptide had the least significant cytotoxic activity to normal SH-SY5Y while exerting high cytotoxicity against the differentiated cells. The mechanism of RIIGL peptide in the differentiated SH-SY5Y was investigated based on changes in secretory proteins compared to another two peptides. A total of 380 proteins were identified, and five of them were significantly detected after treatment with RIIGL peptide. These secretory proteins were found to be related to microtubule-associated protein tau (MAPT) and amyloid-beta precursor protein (APP). RIIGL peptide acts on differentiated SH-SY5Y by regulating amyloid-beta formation, neuron apoptotic process, ceramide catabolic process, and oxidative phosphorylation and thus has the potentials to treat AD. [ABSTRACT FROM AUTHOR]

An elevated sea temperature is considered a key abiotic stressor causing thermal stress to intertidal macroalgae and influencing their populations. Halimeda macroloba is an important CaCO3 producer that contributes to the carbonate budget in marine ecosystems. The population decline of this intertidal algal species could lead to considerable declines in both regional and global carbonate production. However, the impact of increasing temperature on the molecular mechanisms and protein profile of calcified H. macroloba is unclear and remains to be explored. In this study, H. macroloba was exposed to 30 °C and 35 °C for 7 days. The whole protein was then extracted using 0.5% SDS and digested using trypsin before an analysis using LC-MS. The protein profile of H. macroloba was characterized using the MaxQuant program aligned with the UniProt database. A total of 407 proteins were identified, and 12 proteins were found to be significantly upregulated or downregulated in response to the elevated temperature. Cell division protein, protein kinase domain-containing protein, phospholipid transport protein, and small ribosomal subunit protein were the significant proteins identified in our dataset. The proteins associated with cell division, cellular metabolic processes, localization, oxidoreductase activity, and biosynthetic process pathways were overexpressed with a more than 2-fold change at a high temperature. An interaction map generated using STITCH revealed that the significant protein change altered the other proteins related to abiotic stress, producing energy and inducing calcification. This information could be useful in understanding how H. macroloba responds to an elevated sea temperature. [ABSTRACT FROM AUTHOR]