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Biochemical Parameters: Childhood Diarrhea and Malabsorption Syndrome
Published in Anil Gupta, Biochemical Parameters and the Nutritional Status of Children, 2020
The tissue transglutaminase enzyme can stimulate the immuno-stimulatory effect of gluten through the process of deamidation. It also serves as target tissue antigen (autoantigen) to the immune system. The tissue transglutaminase enyme plays a significant role in the pathogenesis of celiac disease (Di Sabatino et al. 2012).
Mixed bullous disease
Published in Lionel Fry, Atlas of Bullous Diseases, 2020
The exception to a common antigen in the subepidermal bullous disorders is DH. The autoantigen in DH and celiac disease has now been defined as tissue-transglutaminase. However, the induction of antibodies to tissue-transglutaminase is due to an external factor, namely gluten, and the antibodies disappear with gluten withdrawal.
Lactic Acid Bacteria Application to Decrease Food Allergies
Published in Marcela Albuquerque Cavalcanti de Albuquerque, Alejandra de Moreno de LeBlanc, Jean Guy LeBlanc, Raquel Bedani, Lactic Acid Bacteria, 2020
Vanessa Biscola, Marcela Albuquerque Cavalcanti de Albuquerque, Tatiana Pacheco Nunes, Antonio Diogo Silva Vieira, Bernadette Dora Gombossy de Melo Franco
Celiac individuals develop an immune reaction mediated by T-cells against tissue transglutaminase, which is an enzyme located in the extracellular matrix. The reaction causes mucosal damage and, in some cases, intestinal villous atrophy. In general, peptides originating from the incomplete digestion of gliadin, such as the 33-mer peptide, reach the small intestine intact and cross the intestinal epithelium barrier, attaining the lamina propria, where they undergo a deamidation process. These peptides trigger an innate immune response, resulting in the activation of the adaptive immune response. Such a process stimulates the production of proinflammatory cytokines, which cause the inflammatory process of the small intestine mucosa. The inflammatory process compromises the cellular junctions from the intestinal epithelium, resulting in increased permeability of the gut membrane due to complete histological disorganization (Elli et al. 2015).
Comparative transcriptome analysis reveals the effects of different feeding times on the hepatopancreas of Chinese mitten crabs
Published in Chronobiology International, 2023
Yingkai Xu, Baoli Zhang, Changyue Yu, Ziwei Hung, Nan Hu, Yuqiao Cai, Yingdong Li
Transglutaminase is involved in blood coagulation, a defense mechanism of invertebrates. Previous studies have confirmed that the depletion of transglutaminase affects gene expression in shrimp and results in a significant decrease in crustacean and lysozyme (Huang et al. 2013). In this study, the pathway with the most enriched downregulated genes during the day was the lysosome pathway. Some GABA(A) receptor-associated proteins (GABARAPs) have been identified in different invertebrates, such as the Chinese mitten crab (Zhou et al. 2012). Additional studies have shown that GAB receptor trafficking and aggregation are involved in the process of autophagy, a component of the innate immune defense system against pathogens (Kabeya et al. 2004; Tanji et al. 2011). We speculate that a relationship between GABA(A) receptor-associated proteins and the innate immunity of Chinese mitten crabs. Interestingly, we identified this gene among those upregulated at night, which further indicated that feeding E. sinensis at night is more beneficial, to enhance its immune function, than feeding during the day. In a previous study, we analyzed the hemolymph transcriptome of Chinese mitten crabs at different time points of the day, and the results showed that the molting behavior was more active at night (Yu et al. 2022). However, in this study, the molting process of Chinese mitten crabs might have been accelerated by changes in the feeding time. Finally, the expression of molting-related genes was upregulated in daytime-fed crabs.
Exposure to emamectin benzoate confers cytotoxic effects on human molt-4 T-cells and possible ameliorative role of vitamin E and dithiothreitol
Published in Drug and Chemical Toxicology, 2023
Yongjun Chen, Xuefeng Liu, Dongmei Yan, Jialin Xu, Shaorong Luan, Ciying Xiao, Qingchun Huang
Transglutaminase activity was measured according to an established procedure using calorimetric hydroxamate, with minor modification (Folk and Cole 1966). After Molt-4 cells were exposed to EMB for 24 or 48 h, the cells were lysed in 0.2 M ice-cold Tris-acetate buffer (pH 6.0) containing 1.0 mM PMSF, 1.0 mM EDTA, 150 mM NaCl, 0.1% SDS, 1.0% sodium deoxycholate, and 1.0% Triton X-100. Cell lysates were centrifuged (10,000 g, 4 °C) for 10 min, and then 0.5 mL of the supernatant was collected and incubated with 0.5 mL of 0.2 M ice-cold Tris-acetate buffer (pH 6.0) containing 5 mM CaCl2, 10 mM GSH, 100 mM hydroxylamine and 30 mM CBZ-L-glutaminylglycine at 37 °C for 10 min. The reaction was terminated by the addition of 1.0 mL ferric chloride-trichloroacetic acid reagent, and the absorbance at 525 nm was measured. Protein content was determined by the Bradford method using bovine serum albumin as a standard (Bradford 1976). The enzyme activity is expressed as ΔOD525·min−1·mg−1 protein.
Transglutaminase 2 mediates lung inflammation and remodeling by transforming growth factor beta 1 via alveolar macrophage modulation
Published in Experimental Lung Research, 2021
Young Chan Kim, Jeonghyeon Kim, Subin Kim, Boram Bae, Ruth Lee Kim, Eui-Man Jeong, Sang-Heon Cho, Hye-Ryun Kang
Transglutaminase is a calcium-dependent enzyme that catalyzes protein cross-linking, polyamination, or deamidation at selective glutamine residues.11 Among the several types of TGs with a high degree of sequence similarity,12 TG2 is the enzyme most widely expressed in numerous cell types. It is localized to multiple cell compartments, including the cytosol, mitochondria, and cell surface.13 Since TGF-β1 is synthesized in an inactive form, activation of latent TGF-β1 is required to initiate TGF-β1 signaling.14 TG2 cross-links the N-terminal region of latent TGF-β binding protein 1 to ECM proteins,15 whereas TGF-β1 increases membrane-associated extracellular TG2 expression in idiopathic pulmonary fibrosis. In mice, TG2 deletion suppresses pulmonary fibrosis after bleomycin challenge, which normally induces the release of the active form of TGF-β1 by alveolar macrophages.16