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1
Zilda, Dewi Zeswita. "MICROBIAL TRANSGLUTAMINASE: SOURCE, PRODUCTION AND ITS ROLE TO IMPROVE SURIMI PROPERTIES." Squalen Bulletin of Marine and Fisheries Postharvest and Biotechnology 9, no. 1 (May 10, 2014): 35. http://dx.doi.org/10.15578/squalen.v9i1.82.
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Transglutaminases (EC 2.3.2.13) have attracted a wide interest from both scientific and appliedpoints of view due to their capacity to cross-link protein substrates. Obtaining transglutaminasesderived from animals are extremely high cost process, which has hampered its wider applicationuntil the discovery of transglutaminase produced by microorganisms. In the early 1990, sincemicrobial transglutaminase have been found, many transglutaminase-producing microbial strainshave been isolated and the enzyme production processes have been optimized. This resulted in the increased uses of transglutaminases in the food industries. In the fisheries industry, MTGasehas successfully been used to improve the mechanical properties of surimi from various fishes.
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Sidauruk, Santhy Wisuda, Tati Nurhayati, and Untung Trimo Laksono. "Characterization of Endogenous Transglutaminase Enzyme of Yellow Pike Conger’s Liver." Jurnal Pengolahan Hasil Perikanan Indonesia 20, no. 3 (December 25, 2017): 582. http://dx.doi.org/10.17844/jphpi.v20i3.19816.
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Transglutaminases have been found in various living organism, such as mammals, plants, <br />microorganisms, and marine organisms including fishes. Transglutaminases have many various functions<br />such as food properties, non-food properties and pharmacologies. This research aimed to characterize<br />transglutaminase that obtained from byproducts of yellow pike conger (Congresox talabon) such as<br />catadromous fish of yellow pike conger’s liver. The characteristic of transglutaminase had the possibility<br />to know the optimum condition in application of transglutaminase from liver of yellow pike conger such<br />as food processing industry, non-food industry and pharmacological application. A yield of yellow pike<br />conger’s liver was 0.88±0.11%. Specific activity of remang fish liver weighing 10 grams was 1,375 U/mg.<br />Characteristic crude transglutaminase from liver of yellow pike conger had optimum pH at 7.5; optimum<br />temperature at 50°C, transglutaminase activity increased on Mg<br />2+<br /> ion dependent and crude transglutaminase <br />had molecular weight of 27.48; 37.00; 69.51; 78.89; 88.18; 108.45; 134.10; dan 172.12 kDa.<br /><br />
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Martin, Antonio, Giulia De Vivo, and Vittorio Gentile. "Possible Role of the Transglutaminases in the Pathogenesis of Alzheimer's Disease and Other Neurodegenerative Diseases." International Journal of Alzheimer's Disease 2011 (2011): 1–8. http://dx.doi.org/10.4061/2011/865432.
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Transglutaminases are ubiquitous enzymes which catalyze posttranslational modifications of proteins. Recently, transglutaminase-catalyzed post-translational modification of proteins has been shown to be involved in the molecular mechanisms responsible for human diseases. Transglutaminase activity has been hypothesized to be involved also in the pathogenetic mechanisms responsible for several human neurodegenerative diseases. Alzheimer's disease and other neurodegenerative diseases, such as Parkinson's disease, supranuclear palsy, Huntington's disease, and other polyglutamine diseases, are characterized in part by aberrant cerebral transglutaminase activity and by increased cross-linked proteins in affected brains. This paper focuses on the possible molecular mechanisms by which transglutaminase activity could be involved in the pathogenesis of Alzheimer's disease and other neurodegenerative diseases, and on the possible therapeutic effects of selective transglutaminase inhibitors for the cure of patients with diseases characterized by aberrant transglutaminase activity.
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Sachslehner, Attila Placido, Marta Surbek, Bahar Golabi, Miriam Geiselhofer, Karin Jäger, Claudia Hess, Ulrike Kuchler, Reinhard Gruber, and Leopold Eckhart. "Transglutaminase Activity Is Conserved in Stratified Epithelia and Skin Appendages of Mammals and Birds." International Journal of Molecular Sciences 24, no. 3 (January 22, 2023): 2193. http://dx.doi.org/10.3390/ijms24032193.
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The cross-linking of structural proteins is critical for establishing the mechanical stability of the epithelial compartments of the skin and skin appendages. The introduction of isopeptide bonds between glutamine and lysine residues depends on catalysis by transglutaminases and represents the main protein cross-linking mechanism besides the formation of disulfide bonds. Here, we used a fluorescent labeling protocol to localize the activity of transglutaminases on thin sections of the integument and its appendages in mammals and birds. In human tissues, transglutaminase activity was detected in the granular layer of the epidermis, suprabasal layers of the gingival epithelium, the duct of sweat glands, hair follicles and the nail matrix. In the skin appendages of chickens, transglutaminase activity was present in the claw matrix, the feather follicle sheath, the feather sheath and in differentiating keratinocytes of feather barb ridges. During chicken embryogenesis, active transglutaminase was found in the cornifying epidermis, the periderm and the subperiderm. Transglutaminase activity was also detected in the filiform papillae on the tongue of mice and in conical papillae on the tongue of chickens. In summary, our study reveals that transglutaminase activities are widely distributed in integumentary structures and suggests that transglutamination contributes to the cornification of hard skin appendages such as nails and feathers.
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Indarto, Cahyo, Wahyu Prihanta, and Supriyanto. "The beginning study of transglutaminase from plant origin." E3S Web of Conferences 499 (2024): 01030. http://dx.doi.org/10.1051/e3sconf/202449901030.
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Texture is an important parameter in processed foods such as meatball, sausage and surimi, where it is affected by the protein gel strength. Sodium tripolyphosphate is often used to improve quality of food texture, and even borax which is harmful to health including causing severe dizziness and trouble breathing, is still widely used. This study aims to explore and characterize transglutaminase of plant origin which is safer than gelling chemicals agents in food products. Transglutaminase is an enzime that can modify protein into strong gel by creating cross-linkage among protein chains. Animal tissue is one source of transglutaminase but requires high costs for providing raw materials. While the search for transglutaminase source from microorganisms need many stages to ensure that transglutaminase meets safety standards, therefore transglutaminasefrom plant origin is an alternative. The method in this study was to identify and characterize transglutaminase extracted from iodine leaf (Jatropha multifida), including determining the optimum temperature, optimum pH as well as activator and inhibitor of transglutaminase extract from iodine leaf. The results showed that the optimum temperature for transglutaminase from iodine leaf is 40-60 oC; The optimum pH is in the range of 6-7. Unlike most transglutaminases derived from animal tissues, transglutaminase from iodine leaf does not depent on presence of Ca2+, however Zn2+ could be an inhibitor. Transglutaminase extract from iodine leaf has high activity, it will be a promising potential to be applied in food industry to improve texture quality.
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Cocuzzi, E., M. Piacentini, S. Beninati, and S. I. Chung. "Post-translational modification of apolipoprotein B by transglutaminases." Biochemical Journal 265, no. 3 (February 1, 1990): 707–13. http://dx.doi.org/10.1042/bj2650707.
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The major form of cross-link found in apolipoprotein B was identified as N1N12-bis-(gamma-glutamyl)spermine, a product known to be formed through the catalytic action of transglutaminases (EC 2.3.2.13). N1-(gamma-Glutamyl)spermine was present in a trace amount but epsilon-(gamma-glutamyl)lysine cross-links, which are formed during fibrin formation in plasma, were not detected. In the presence of catalytic amounts of plasma Factor XIIIa (a thrombin-dependent extracellular transglutaminase) or cellular transglutaminase (a cytosolic enzyme), apolipoprotein B and other plasma apolipoproteins (A-I, A-II and C) underwent covalently bridged polymerization and served as amine acceptor substrates. These results suggests that transglutaminases may participate in the covalent modification of apolipoproteins, either in the physiological state or during pathogenesis.
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Dadabay, C. Y., and L. J. Pike. "Purification and characterization of a cytosolic transglutaminase from a cultured human tumour-cell line." Biochemical Journal 264, no. 3 (December 15, 1989): 679–85. http://dx.doi.org/10.1042/bj2640679.
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Transglutaminases are a family of Ca2(+)-dependent enzymes that catalyse the formation of isopeptide bonds between the side chains of glutamine and lysine residues. The enzymes have been hypothesized to be involved in a wide range of cellular processes, including growth and differentiation and stabilization of the cytoskeleton. The human epidermal carcinoma-cell line, A431 cells, have relatively high amounts of a cytosolic transglutaminase activity that varies upon treatment of the cells with epidermal growth factor. We demonstrate here that this cytosolic activity has the biochemical and immunological properties of a tissue transglutaminase. We also report the purification of this enzyme to apparent homogeneity by a protocol which involves a novel affinity-elution step. Polyclonal antibodies to the transglutaminase were raised and used to identify the enzyme by Western blotting. The availability of purified transglutaminase and antitransglutaminase antibodies will permit further study of the role of this enzyme in the growth of this hormone-responsive human tumour-cell line.
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Lerner, Aaron, and Torsten Matthias. "Processed Food Additive Microbial Transglutaminase and Its Cross-Linked Gliadin Complexes Are Potential Public Health Concerns in Celiac Disease." International Journal of Molecular Sciences 21, no. 3 (February 8, 2020): 1127. http://dx.doi.org/10.3390/ijms21031127.
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Microbial transglutaminase (mTG) is a survival factor for microbes, but yeasts, fungi, and plants also produce transglutaminase. mTG is a cross-linker that is heavily consumed as a protein glue in multiple processed food industries. According to the manufacturers’ claims, microbial transglutaminase and its cross-linked products are safe, i.e., nonallergenic, nonimmunogenic, and nonpathogenic. The regulatory authorities declare it as “generally recognized as safe” for public users. However, scientific observations are accumulating concerning its undesirable effects on human health. Functionally, mTG imitates its family member, tissue transglutaminase, which is the autoantigen of celiac disease. Both these transglutaminases mediate cross-linked complexes, which are immunogenic in celiac patients. The enzyme enhances intestinal permeability, suppresses mechanical (mucus) and immunological (anti phagocytic) enteric protective barriers, stimulates luminal bacterial growth, and augments the uptake of gliadin peptide. mTG and gliadin molecules are cotranscytosed through the enterocytes and deposited subepithelially. Moreover, mucosal dendritic cell surface transglutaminase induces gliadin endocytosis, and the enzyme-treated wheat products are immunoreactive in CD patients. The present review summarizes and updates the potentially detrimental effects of mTG, aiming to stimulate scientific and regulatory debates on its safety, to protect the public from the enzyme’s unwanted effects.
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Watanabe, Yuko, Kazuho Okuya, Yuki Takada, Masato Kinoshita, Saori Yokoi, Shinichi Chisada, Yasuhiro Kamei, et al. "Gene disruption of medaka (Oryzias latipes) orthologue for mammalian tissue-type transglutaminase (TG2) causes movement retardation." Journal of Biochemistry 168, no. 3 (June 24, 2020): 213–22. http://dx.doi.org/10.1093/jb/mvaa038.
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Abstract Transglutaminases are an enzyme family that catalyses protein cross-linking essential for several biological functions. In the previous studies, we characterized the orthologues of the mammalian transglutaminase family in medaka (Oryzias latipes), an established fish model. Among the human isozymes, tissue-type transglutaminase (TG2) has multiple functions that are involved in several biological phenomena. In this study, we established medaka mutants deficient for the orthologue of human TG2 using the CRISPR/Cas9 and transcription activator-like effector nucleases systems. Although apparent morphological changes in the phenotype were not observed, movement retardation was found in the mutant fish when evaluated by a tank-diving test. Furthermore, comparative immunohistochemistry analysis using in this fish model revealed that orthologue of human TG2 was expressed at the periventricular layer of the optic tectum. Our findings provide novel insight for the relationship between tissue-type transglutaminase and the nervous system and the associated behaviour.
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Xavier, Janifer Raj, K. V. Ramana, and R. K. Sharma. "Screening and statistical optimization of media ingredients for production of microbial transglutaminase." Defence Life Science Journal 2, no. 2 (May 31, 2017): 216. http://dx.doi.org/10.14429/dlsj.2.11369.
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<p>Transglutaminase is a calcium dependent enzyme that catalyses acyl transfer reactions between primary amino groups and protein bound glutamine residues. Eighteen bacterial and twenty eight actinomycetes were screened for the presence of transglutaminase. Among the microbial cultures screened <em>Streptomyces</em> sp. D1, showed maximum transglutaminase activity. In this study characterization of transglutaminase and its application to modifying the properties of panner (Indian cottage cheese) in the form of cross linking was investigated. Optimum temperature and pH for enzyme was found to be at 50°C and 6.0, respectively. Optimization of media ingredients for maximizing the transglutaminase activity using <em>Streptomyces</em> sp. D1 was carried out using central composite design. Response surface methodology was employed to standardize the optimum media composition for maximum enzyme activity. Three factors such as carbon source, nitrogen source and pH were tested for the maximum enzyme activity as response. The optimized medium with sugarcane molasses as carbon source 6.0% (w/v), peptone as nitrogen source 1.75% (w/v) were found to be optimal at initial pH 6.5 and incubation temperature 30.0°C with agitation at 100 rpm for 96h. The enzyme activity of transglutaminase obtained from the optimized medium was found to be 4.1 (AU/ml). Low cost substrate such as sugarcane molasses in the form of a renewable substrate is proposed to be suitable even for scale-up production of enzyme and for industrial applications. The ethanol fractionated transglutaminse treated milk was found to produce more paneer with increased moisture content while reduction in cooking loss of the paneer prepared using enzyme treated milk is also reported.</p>
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Gün, Büşra, and Semih Yilmaz. "BACILLUS ORIGINATED TRANSGLUTAMINASE: PROPERTIES AND USAGE." Current Trends in Natural Sciences 11, no. 21 (July 31, 2022): 194–201. http://dx.doi.org/10.47068/ctns.2022.v11i21.022.
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Enzymes with very important duties, form part of our lives and are useful in various fields. Owing to both the intensity of use and the amount of effective production in standard conditions, the production and use of bacterial-originated enzymes are used continuously in agriculture, health, food and many other industrial areas. Among them, transglutaminases (EC 2.3.2.13) are both intracellular and extracellular enzymes included in the transferase group that catalyse cross-links between proteins. Microbial transglutaminase enzymes are frequently used in the food and pharmaceutical industries to change the functional properties of proteins since it increases viscosity, elasticity and water holding capacity. Particularly the positive effects in meat, dairy, and bakery products such as gelling, increasing mechanical strength, and reducing structural deformations, specifically the texture. It also contributes to reducing the use of additives in diets with low protein and fat content. Furthermore, it reduces the time for cooking processes as well as sensory properties enhancement. Transglutaminase enzymes are also being used in other fields such as tissue culture, biochemical and biomedical research, textile, and leather industries. In this review, a broad perspective is presented on the literature dealing with bacterial transglutaminase studies, especially those belonging to the genus Bacillus. In Bacillus spp., transglutaminase gene was mostly reported in B. subtilis, B. amyloliquefaciens, B. cereus, B. nakamura, B. circulans species and also recently in the whole genome of local Bacillus thuringiensis (Bt) SY49.1 strain (JAHKEZ010000474.1) using the RAST database. It was determined that the Bt transglutaminase gene was 93% identical to that of B. cereus species. The presence of transglutaminase gene in agriculturally indispensable Bt strain can confer them a superficial characteristic due to their water holding capacity in terms of increasing the yield and quality of plant products.
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Ichinose, Akitada. "Physiopathology and Regulation of Factor XIII." Thrombosis and Haemostasis 86, no. 07 (2001): 57–65. http://dx.doi.org/10.1055/s-0037-1616201.
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SummaryFactor XIII is a plasma transglutaminase. Transglutaminases are at least 8 enzymes which cross-link a number of proteins. This type of reaction not only enhances the original functions of substrate proteins, but also adds new functions to them. Factor XIII in plasma is a tetramer (A2B2), and the A subunit contains the active site. Although transglutaminases are homologous, the nucleotide sequences in their 5’-flanking region differ significantly. Accordingly, transcription factors play a major role in the cell type-specific expression of each transglutaminase. A variety of missense and nonsense mutations, and deletions/insertions with or without out-of-frame shift/premature termination and splicing abnormalities have been identified in the genes for A and B subunits in factor XIII deficiency. In some cases, the mRNA level of the A or B subunit was severely reduced. Molecular and cellular bases have also been explored by expression experiments and by molecular modeling. In most cases, impaired folding and/or conformational change of the mutant A or B subunit leads to both intra- and extra-cellular instability, which is responsible for factor XIII deficiency.
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Bergamini, C. M., and M. Signorini. "Studies on tissue transglutaminases: interaction of erythrocyte type-2 transglutaminase with GTP." Biochemical Journal 291, no. 1 (April 1, 1993): 37–39. http://dx.doi.org/10.1042/bj2910037.
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Ca2+ and GTP are the main modulators of type-2 transglutaminases. To study the interaction of the enzyme with GTP, we have employed periodate-oxidized GTP as an affinity-label probe. Dialdehyde GTP bound irreversibly to type-2 transglutaminase in a time-dependent way with 1:1 stoichiometry at complete modification. The reaction took place in the absence, but was more rapid in the presence, of cyanoborohydride. Native GTP prevented incorporation of dialdehyde GTP, and Ca2+ significantly slowed down the reaction rate. The modified enzyme displayed decreased sensitivity to Ca2+, with a sigmoid saturation curve. We conclude that type-2 transglutaminase has a single GTP-binding site, the modification of which by dialdehyde GTP mimics nucleotide binding to the enzyme.
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Castorena-Gonzalez, Jorge A., Marius C. Staiculescu, Christopher A. Foote, Luis Polo-Parada, and Luis A. Martinez-Lemus. "The obligatory role of the actin cytoskeleton on inward remodeling induced by dithiothreitol activation of endogenous transglutaminase in isolated arterioles." American Journal of Physiology-Heart and Circulatory Physiology 306, no. 4 (February 15, 2014): H485—H495. http://dx.doi.org/10.1152/ajpheart.00557.2013.
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Inward remodeling is the most prevalent structural change found in the resistance arteries and arterioles of hypertensive individuals. Separate studies have shown that the inward remodeling process requires transglutaminase activation and the polymerization of actin. Therefore, we hypothesize that inward remodeling induced via endogenous transglutaminase activation requires and depends on actin cytoskeletal structures. To test this hypothesis, isolated and cannulated rat cremaster arterioles were exposed to dithiothreitol (DTT) to activate endogenous transglutaminases. DTT induced concentration-dependent vasoconstriction that was suppressed by coincubation with cystamine or cytochalasin-D to inhibit tranglutaminase activity or actin polymerization, respectively. Prolonged (4 h) exposure to DTT caused arteriolar inward remodeling that was also blocked by the presence of cystamine or cytochalasin-D. DTT inwardly remodeled arterioles had reduced passive diameters, augmented wall thickness-to-lumen ratios and altered elastic characteristics that were reverted upon disruption of the actin cytoskeleton with mycalolide-B. In freshly isolated arterioles, exposure to mycalolide-B caused no changes in their passive diameters or their elastic characteristics. These results suggest that, in arterioles, the early stages of the inward remodeling process induced by prolonged endogenous transglutaminase activation require actin dynamics and depend on changes in actin cytoskeletal structures.
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Semkova, Mariya E., and J. Justin Hsuan. "Mass Spectrometric Identification of a Novel Factor XIIIa Cross-Linking Site in Fibrinogen." Proteomes 9, no. 4 (November 2, 2021): 43. http://dx.doi.org/10.3390/proteomes9040043.
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Transglutaminases are a class of enzymes that catalyze the formation of a protein:protein cross-link between a lysine and a glutamine residue. These cross-links play important roles in diverse biological processes. Analysis of cross-linking sites in target proteins is required to elucidate their molecular action on target protein function and the molecular specificity of different transglutaminase isozymes. Mass-spectrometry using settings designed for linear peptide analysis and software designed for the analysis of disulfide bridges and chemical cross-links have previously been employed to identify transglutaminase cross-linking sites in proteins. As no control peptide with which to assess and improve the mass spectrometric analysis of TG cross-linked proteins was available, we developed a method for the enzymatic synthesis of a well-defined transglutaminase cross-linked peptide pair that mimics a predicted tryptic digestion product of collagen I. We then used this model peptide to determine optimal score thresholds for correct peptide identification from y- and b-ion series of fragments produced by collision-induced dissociation. We employed these settings in an analysis of fibrinogen cross-linked by the transglutaminase Factor XIIIa. This approach resulted in identification of a novel cross-linked peptide in the gamma subunit. We discuss the difference in behavior of ions derived from different cross-linked peptide sequences and the consequent demand for a more tailored mass spectrometry approach for cross-linked peptide identification compared to that routinely used for linear peptide analysis.
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Noguchi, Kazuyoshi, Kohki Ishikawa, Kei-ichi Yokoyama, Tomoko Ohtsuka, Noriki Nio, and Ei-ichiro Suzuki. "Crystal Structure of Red Sea Bream Transglutaminase." Journal of Biological Chemistry 276, no. 15 (November 15, 2000): 12055–59. http://dx.doi.org/10.1074/jbc.m009862200.
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The crystal structure of the tissue-type transglutaminase from red sea bream liver (fish-derived transglutaminase, FTG) has been determined at 2.5-Å resolution using the molecular replacement method, based on the crystal structure of human blood coagulation factor XIII, which is a transglutaminase zymogen. The model contains 666 residues of a total of 695 residues, 382 water molecules, and 1 sulfate ion. FTG consists of four domains, and its overall and active site structures are similar to those of human factor XIII. However, significant structural differences are observed in both the acyl donor and acyl acceptor binding sites, which account for the difference in substrate preferences. The active site of the enzyme is inaccessible to the solvent, because the catalytic Cys-272 hydrogen-bonds to Tyr-515, which is thought to be displaced upon acyl donor binding to FTG. It is postulated that the binding of an inappropriate substrate to FTG would lead to inactivation of the enzyme because of the formation of a new disulfide bridge between Cys-272 and the adjacent Cys-333 immediately after the displacement of Tyr-515. Considering the mutational studies previously reported on the tissue-type transglutaminases, we propose that Cys-333 and Tyr-515 are important in strictly controlling the enzymatic activity of FTG.
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Lorand, Laszlo. "Transglutaminase." Neurochemistry International 40, no. 1 (January 2002): 7–12. http://dx.doi.org/10.1016/s0197-0186(01)00056-0.
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Akimov, Sergey S., and Alexey M. Belkin. "Cell-surface transglutaminase promotes fibronectin assembly via interaction with the gelatin-binding domain of fibronectin." Journal of Cell Science 114, no. 16 (August 15, 2001): 2989–3000. http://dx.doi.org/10.1242/jcs.114.16.2989.
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Assembly of fibronectin into a fibrillar matrix is critical for regulation of cell growth and migration, embryogenesis and wound healing. We have previously shown that cell-surface tissue transglutaminase serves as an integrin-binding adhesion coreceptor for fibronectin. Here we report that transglutaminase strongly promotes fibronectin assembly mediated byα5β1 integrin. This effect is independent from transglutaminase-mediated enzymatic crosslinking of fibronectin and separate from the ability of transglutaminase to stimulate cell spreading. Surface transglutaminase increases the binding of fibronectin to cells via interaction with its gelatin-binding domain that contains modules I6II1,2I7-9 and lacks integrin-binding motifs. The gelatin-binding fragment of fibronectin binds to surface transglutaminase on cells in suspension but does not interact with cell monolayers where surface transglutaminase is occupied by fibronectin. Surface transglutaminase colocalizes with growing fibronectin fibrils at early timepoints of matrix formation and remains codistributed with fibronectin matrices thereafter. The observed stimulation of matrix assembly by transglutaminase is blocked by the gelatin-binding fragment of fibronectin,but is not strongly perturbed by its N-terminal fragment consisting of modules I1-5. These results implicate an interaction between transglutaminase and the gelatin-binding domain of fibronectin in matrix assembly and suggest its role in initiation of fibrillogenesis. However,blocking antibodies against α5β1 integrin or the cell-binding fragment of fibronectin that contains modules III2-11 most strongly suppress matrix formation and abolish the effects of transglutaminase. Hence,transglutaminase cooperates with but can not substitute for α5β1 integrin in fibronectin assembly. Treatment of fibroblasts with transforming growth factor β (TGFβ) significantly increases surface expression of transglutaminase and its association with β1 integrins, but not withαVβ3 integrin. TGFβ enhances the binding of fibronectin to the cell surface and elevates matrix formation, whereas antibody against transglutaminase or the gelatin-binding fragment of fibronectin suppresses these effects, indicating an involvement of transglutaminase in TGFβ-dependent fibronectin assembly. Therefore, TGFβ-induced fibronectin matrix deposition during normal wound healing or fibrotic disorders may depend on upregulation of integrin-associated surface transglutaminase.
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Korponay–Szabó, Ilma R., Satu Sulkanen, Tuula Halttunen, Francesco Maurano, Mauro Rossi, Giuseppe Mazzarella, Kaija Laurila, Riccardo Troncone, and Markku Mäki. "Tissue Transglutaminase Is the Target in Both Rodent and Primate Tissues for Celiac Disease–Specific Autoantibodies." Journal of Pediatric Gastroenterology and Nutrition 31, no. 5 (November 2000): 520–27. http://dx.doi.org/10.1002/j.1536-4801.2000.tb07175.x.
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ABSTRACTBackgroundEndomysial antibodies have recently been shown to react with tissue transglutaminase. This study was undertaken to investigate whether the tissue distribution of transglutaminase is also compatible with reticulin, jejunal, and fibroblast autoantibody binding patterns.MethodsSera from patients with and without celiac disease, monoclonal tissue transglutaminase antibodies, and sera from mice parenterally immunized against commercially available tissue transglutaminase, transglutaminase complexed with gliadin, or gliadin were used in indirect immunofluorescence and double‐staining studies using both rodent and primate tissues as substrates. Also, antibody competition, affinity chromatography, and potassium thiocyanate extraction studies were undertaken.ResultsTissue transglutaminase antibody binding patterns were identical with the extracellular binding patterns seen with celiac patient sera. Human umbilical cord–derived fibroblasts exhibited both cytoplasmic and extracellular matrix staining. Double staining with patients' sera and tissue transglutaminase antibodies showed complete overlapping. Tissue transglutaminase effectively absorbed reticulin‐endomysial antibodies from celiac sera, and patients' sera blocked the staining of the monoclonal tissue transglutaminase antibodies. Potassium thiocyanate extraction abolished the staining patterns, but they were elicited again after readdition of tissue transglutaminase.ConclusionsReticulin, endomysial, and jejunal antibodies detect transglutaminase in both rodent and primate tissues, indicating that these tissue autoantibodies are identical.
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Delong, Thomas, Gene Barbour, Brenda Bradley, Nichole Reisdorph, and Kathryn Haskins. "An altered peptide of Chromogranin A is a potent antigen for the diabetogenic T cell clone BDC-2.5 (44.21)." Journal of Immunology 186, no. 1_Supplement (April 1, 2011): 44.21. http://dx.doi.org/10.4049/jimmunol.186.supp.44.21.
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Abstract Pathogenesis of type 1 diabetes is mediated by autoreactive T cells directed toward antigens in islet beta cells. We have recently identified Chromogranin A (ChgA) as the antigen target for three diabetogenic CD4+ T cell clones that were derived from the non-obese diabetic mouse, including the clone BDC-2.5. These clones respond to WE14, a natural cleavage product of ChgA, but only at very high peptide concentrations, suggesting that WE14 may not be the natural T cell ligand. Our question in this study was to determine whether a post-translational modification (PTM) could be involved in the formation of the natural ligand for the T cell clones. Although WE14 is expressed in beta cells, we were not able to identify the complete peptide sequence in purified antigenic fractions from beta cell tumors. Mass spectrometric analysis revealed the presence of an amino acid sequence corresponding only to the C-terminal region of WE14. Glutamine, which is in the N-terminal region of WE14, is a potential target for the enzyme transglutaminase. We treated the peptide WE14 with transglutaminase and demonstrated that this treatment significantly increased the antigenicity. Transglutaminases are known to deamidate or covalently crosslink proteins and we are currently investigating whether those modifications can be found in the natural antigen from beta cells. If transglutaminase is required for the generation of autoantigenic T cell epitopes, it could be an attractive therapeutic target.
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Sárdy, Miklós, Sarolta Kárpáti, Barbara Merkl, Mats Paulsson, and Neil Smyth. "Epidermal Transglutaminase (TGase 3) Is the Autoantigen of Dermatitis Herpetiformis." Journal of Experimental Medicine 195, no. 6 (March 18, 2002): 747–57. http://dx.doi.org/10.1084/jem.20011299.
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Gluten sensitivity typically presents as celiac disease, a common chronic small intestinal disorder. However, in certain individuals it is associated with dermatitis herpetiformis, a blistering skin disease characterized by granular IgA deposits in the papillary dermis. While tissue transglutaminase has been implicated as the major autoantigen of gluten sensitive disease, there has been no explanation as to why this condition appears in two distinct forms. Here we show that while sera from patients with either form of gluten sensitive disease react both with tissue transglutaminase and the related enzyme epidermal (type 3) transglutaminase, antibodies in patients having dermatitis herpetiformis show a markedly higher avidity for epidermal transglutaminase. Further, these patients have an antibody population specific for this enzyme. We also show that the IgA precipitates in the papillary dermis of patients with dermatitis herpetiformis, the defining signs of the disease, contain epidermal transglutaminase, but not tissue transglutaminase or keratinocyte transglutaminase. These findings demonstrate that epidermal transglutaminase, rather than tissue transglutaminase, is the dominant autoantigen in dermatitis herpetiformis and explain why skin symptoms appear in a proportion of patients having gluten sensitive disease.
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Alfayadh, Hassan Mahdi, Mohammed Latif Hamk, Kocher Jamal Ibrahim, and Jasim Mohammed Al-Saadi. "Effect of milk proteins aggregation using Transglutaminase and Maillard reaction on Ca2+ milk gel." Kurdistan Journal of Applied Research 3, no. 1 (June 11, 2018): 63–67. http://dx.doi.org/10.24017/science.2018.1.13.
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Effect of transglutaminase, Maillard reaction induced crosslinking and the combination of transglutaminase and Maillard reaction induced crosslinking between whey proteins and caseins in milk on calcium milk gel properties were investigated. Treatment of milk with transglutaminase, Maillard reaction, and transglutaminase + Maillard reaction cause to the appearance of new high MW protein bands. Water holding capacity, gel strength and sensory scores of gel samples increased and spontaneous whey separation decreased in calcium-induced milk gel made from transglutaminase and combination of transglutaminase and Maillard reaction treated milk compare with calcium-induced milk gel made from untreated milk alone.
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Kikuchi, Yoshimi, Masayo Date, Kei-ichi Yokoyama, Yukiko Umezawa, and Hiroshi Matsui. "Secretion of Active-Form Streptoverticillium mobaraense Transglutaminase by Corynebacterium glutamicum: Processing of the Pro-Transglutaminase by a Cosecreted Subtilisin-Like Protease from Streptomyces albogriseolus." Applied and Environmental Microbiology 69, no. 1 (January 2003): 358–66. http://dx.doi.org/10.1128/aem.69.1.358-366.2003.
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ABSTRACT The transglutaminase secreted by Streptoverticillium mobaraense is a useful enzyme in the food industry. A fragment of transglutaminase was secreted by Corynebacterium glutamicum when it was coupled on a plasmid to the promoter and signal peptide of a cell surface protein from C. glutamicum. We analyzed the signal peptide and the pro-domain of the transglutaminase gene and found that the signal peptide consists of 31 amino acid residues and the pro-domain consists of 45 residues. When the pro-domain of the transglutaminase was used, the pro-transglutaminase was secreted efficiently by C. glutamicum but had no enzymatic activity. However, when the plasmid carrying the S. mobaraense transglutaminase also encoded SAM-P45, a subtilisin-like serine protease derived from Streptomyces albogriseolus, the peptide bond to the C side of 41-Ser of the pro-transglutaminase was hydrolyzed, and the pro-transglutaminase was converted to an active form. Our findings suggest that C. glutamicum has potential as a host for industrial-scale protein production.
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Akimov, Sergey S., Dmitry Krylov, Laurie F. Fleischman, and Alexey M. Belkin. "Tissue Transglutaminase Is an Integrin-Binding Adhesion Coreceptor for Fibronectin." Journal of Cell Biology 148, no. 4 (February 21, 2000): 825–38. http://dx.doi.org/10.1083/jcb.148.4.825.
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The protein cross-linking enzyme tissue transglutaminase binds in vitro with high affinity to fibronectin via its 42-kD gelatin-binding domain. Here we report that cell surface transglutaminase mediates adhesion and spreading of cells on the 42-kD fibronectin fragment, which lacks integrin-binding motifs. Overexpression of tissue transglutaminase increases its amount on the cell surface, enhances adhesion and spreading on fibronectin and its 42-kD fragment, enlarges focal adhesions, and amplifies adhesion-dependent phosphorylation of focal adhesion kinase. These effects are specific for tissue transglutaminase and are not shared by its functional homologue, a catalytic subunit of factor XIII. Adhesive function of tissue transglutaminase does not require its cross-linking activity but depends on its stable noncovalent association with integrins. Transglutaminase interacts directly with multiple integrins of β1 and β3 subfamilies, but not with β2 integrins. Complexes of transglutaminase with integrins are formed inside the cell during biosynthesis and accumulate on the surface and in focal adhesions. Together our results demonstrate that tissue transglutaminase mediates the interaction of integrins with fibronectin, thereby acting as an integrin-associated coreceptor to promote cell adhesion and spreading.
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Aeschlimann, D., A. Wetterwald, H. Fleisch, and M. Paulsson. "Expression of tissue transglutaminase in skeletal tissues correlates with events of terminal differentiation of chondrocytes." Journal of Cell Biology 120, no. 6 (March 15, 1993): 1461–70. http://dx.doi.org/10.1083/jcb.120.6.1461.
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Calcifying cartilages show a restricted expression of tissue transglutaminase. Immunostaining of newborn rat paw bones reveals expression only in the epiphyseal growth plate. Tissue transglutaminase appears first intracellularly in the proliferation/maturation zone and remains until calcification of the tissue in the lower hypertrophic zone. Externalization occurs before mineralization. Subsequently, the enzyme is present in the interterritorial matrix during provisional calcification and in the calcified cartilage cores of bone trabeculae. In trachea, mineralization occurring with maturation in the center of the cartilage is accompanied by expression of tissue transglutaminase at the border of the hydroxyapatite deposits. Transglutaminase activity also shows a restricted distribution in cartilage, similar to the one observed for tissue transglutaminase protein. Analysis of tissue homogenates showed that the enzyme is present in growth plate cartilage, but not in articular cartilage, and recognizes a limited set of substrate proteins. Osteonectin is coexpressed with tissue transglutaminase both in the growth plate and in calcifying tracheal cartilage and is a specific substrate for tissue transglutaminase in vitro. Tissue transglutaminase expression in skeletal tissues is strictly regulated, correlates with chondrocyte differentiation, precedes cartilage calcification, and could lead to cross-linking of the mineralizing matrix.
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Mosesson, Michael, Claudia Gohr, Ikuko Masuda, David Heinkel, Kevin Seibenlist, and Ann Rosenthal. "Regulation of transglutaminase activity in articular chondrocytes through thrombin receptor-mediated factor XIII synthesis." Thrombosis and Haemostasis 91, no. 03 (2004): 558–68. http://dx.doi.org/10.1160/th03-07-0462.
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SummaryTransglutaminases are a family of enzymes that catalyze the formation of ɛ-(γ-glutamyl)lysine isopeptide bonds in proteins, an activity that has been implicated in the pathogenesis of cartilage matrix mineralization in degenerative arthritis. Type II transglutaminase and thrombin-activatable factor XIII have been identified in articular cartilage. Thrombin, a coagulation protease, is found in pathological synovial fluids, and is known to stimulate transglutaminase activity in non-articular tissues. We investigated the effects of thrombin on transglutaminase activity in porcine articular chondrocytes. Direct addition of thrombin to chondrocyte lysates resulted in increased transglutaminase activity due to proteolytic conversion of factor XIII to XIIIa. Thrombin-treated chondrocyte cultures (0.001 to 2.0U/ml) also showed increased transglutaminase activity. Thrombin treatment of chondrocyte cultures increased transglutaminase activity as early as 15 minutes after addition, an effect that we attributed to factor XIII activation. Additional stimulatory effects of thrombin were observed in cultured chondrocytes at 4 and 24 hours. A thrombin receptor agonist peptide (TRAP) which activates the PAR1 thrombin receptor mimicked these later effects. Thrombin treatment of chondrocyte cultures increased factor XIII mRNA and protein levels, without affecting levels of type II transglutaminase. Thus, thrombin stimulates transglutaminase activity in articular cartilage by directly cleaving factor XIII and by receptor-mediated upregulation of factor XIII synthesis. Such increases in potential transglutaminase activity may facilitate pathological matrix calcification in degenerative arthritis.
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F??s??s, L. "Tissue transglutaminase." Blood Coagulation & Fibrinolysis 3, no. 6 (December 1992): 805. http://dx.doi.org/10.1097/00001721-199212000-00020.
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Romijn, J. C. "Polyamines and transglutaminase actions: Polyamine und Transglutaminase-Wirkungen." Andrologia 22, S1 (April 27, 2009): 83–91. http://dx.doi.org/10.1111/j.1439-0272.1990.tb02074.x.
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Wang, Jian-Ying, Mary Jane Viar, Ji Li, Hui-Jun Shi, Anami R. Patel, and Leonard R. Johnson. "Differences in transglutaminase mRNA after polyamine depletion in two cell lines." American Journal of Physiology-Cell Physiology 274, no. 2 (February 1, 1998): C522—C530. http://dx.doi.org/10.1152/ajpcell.1998.274.2.c522.
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Polyamines serve as natural substrates for the transglutaminase that catalyzes covalent cross-linking of proteins and is involved in cellular adhesion and proliferation. This study tests the hypothesis that intracellular polyamines play a role in the regulation of transglutaminase expression in rat small intestinal crypt cells (IEC-6 cell line) and human colon carcinoma cells (Caco-2 cell line). Treatment with α-difluoromethylornithine (DFMO; a specific inhibitor of polyamine synthesis) significantly depleted the cellular polyamines putrescine, spermidine, and spermine in both cell lines. In IEC-6 cells, polyamine depletion was associated with a decrease in the levels of transglutaminase mRNA. In Caco-2 cells, however, polyamine depletion significantly increased the levels of transglutaminase mRNA and enzyme activity. In both cell lines, ornithine decarboxylase mRNA levels increased and protooncogene c- myc mRNA decreased in the presence of DFMO. Addition of polyamines to cells treated with DFMO reversed the effect of DFMO on the levels of mRNA for these genes in both lines. There was no significant change in the stability of transglutaminase mRNA between control and DFMO-treated IEC-6 cells. In contrast, the half-life of mRNA for transglutaminase in Caco-2 cells was dramatically increased after polyamine depletion. Spermidine, when given together with DFMO, completely prevented increased half-life of transglutaminase mRNA in Caco-2 cells. These results indicate that 1) expression of transglutaminase requires polyamines in IEC-6 cells but is inhibited by these agents in Caco-2 cells, 2) polyamines modulate transglutaminase expression at the level of mRNA through different pathways in these two cell lines, and 3) posttranscriptional regulation plays a major role in the induction of transglutaminase mRNA in polyamine-deficient Caco-2 cells.
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Dickey, William. "Symposium 1: Joint BAPEN and British Society of Gastroenterology Symposium on ‘Coeliac disease: basics and controversies’ Coeliac disease in the twenty-first century." Proceedings of the Nutrition Society 68, no. 3 (June 3, 2009): 234–41. http://dx.doi.org/10.1017/s0029665109001414.
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Coeliac disease (CD), traditionally perceived as a rare childhood condition presenting with malabsorption, is instead an autoimmune multisystem disorder usually presenting in adulthood, affecting ⩾1% of the population and linked to the genetic expression of human leucocyte antigens (HLA) DQ2 and DQ8. Presentation occurs most often in the 40–60 years age-group, but potentially at any age. Symptoms attributable to the gut or to malabsorption may be mild, non-specific or absent; under one-third of patients have diarrhoea and almost half are overweight. Histological diagnosis no longer requires small intestine villous atrophy. The Marsh classification recognizes increased intraepithelial lymphocytes and crypt hyperplasia with intact villi as part of the gluten enteropathy spectrum, while some individuals have more subtle abnormalities identified only on electron microscopy. Serological testing for CD autoantibodies (to endomysium and tissue transglutaminase) has revolutionized diagnosis, shifting the process towards primary care. However, a substantial number of patients with CD are seronegative, particularly those without villous atrophy. The autoantibody to endomysium may be produced before histological change. The immune response to transglutaminase is crucial to the disease process. An exciting new development is the link between antibodies to organ-specific transglutaminases and clinical presentation; transglutaminases 2 (gut), 3 (skin) and 6 (nervous system). Negative testing for CD does not preclude its development later and HLA testing may allow ‘once and for all’ exclusion. In conclusion, an increasing proportion of patients with CD do not meet the ‘classic’ picture of malabsorption, positive serological testing and villous atrophy. Insisting on all these criteria for diagnosis will result in under diagnosis.
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Gentile, V., V. Thomazy, M. Piacentini, L. Fesus, and P. J. Davies. "Expression of tissue transglutaminase in Balb-C 3T3 fibroblasts: effects on cellular morphology and adhesion." Journal of Cell Biology 119, no. 2 (October 15, 1992): 463–74. http://dx.doi.org/10.1083/jcb.119.2.463.
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Tissue transglutaminase is a cytosolic enzyme whose primary function is to catalyze the covalent cross-linking of proteins. To investigate the functions of this enzyme in physiological systems, we have established lines of Balb-C 3T3 fibroblasts stably transfected with a constitutive tissue transglutaminase expression plasmid. Several cell lines expressing high levels of catalytically active tissue transglutaminase have been isolated and characterized. Transglutaminase-transfected cells showed morphologic features quite distinct from their nontransfected counterparts. Many of the cells showed an extended and very flattened morphology that reflected increased adhesion of the cells to the substratum. Other cells, particularly those showing the highest levels of intracellular transglutaminase expression, showed extensive membrane blebbing and cellular fragmentation. The results of these experiments suggest that the induction and activation of tissue transglutaminase may contribute both to changes in cellular morphology and adhesiveness.
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Shi, Yan Guo, Lei Qian, Na Zhang, Chun Ran Han, Ying Liu, Yi Fang Zhang, and Yong Qiang Ma. "Study on Separation and Purification of the Transglutaminase." Applied Mechanics and Materials 121-126 (October 2011): 443–47. http://dx.doi.org/10.4028/www.scientific.net/amm.121-126.443.
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The transglutaminase was purified through alcohol precipitation, ammonium sulphate precipitation, ultrafiltration, gel layer chromatography, and the purified alkaline was demonstrated to be electrophoretic by SDS-PAGE. Using the activity of alkaline protease as indicators. the purification of transglutaminase was optimized.The results indicated that the enzyme activity of purified transglutaminase was 107.86 U•mg-1, final purification factor was 10.42, Activity recovery factor was 27.3%,The enzyme properties of transglutaminase were also studied, The optimal conditions of transglutaminase were as follows:pH6.0, 40°C.After incubation at 40°C for 2h,the residual activity of the enzyme was ablve 90%,and the enzyme was relatively stable at pH5~7.
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Kang, S. J., K. S. Shin, W. K. Song, D. B. Ha, C. H. Chung, and M. S. Kang. "Involvement of transglutaminase in myofibril assembly of chick embryonic myoblasts in culture." Journal of Cell Biology 130, no. 5 (September 1, 1995): 1127–36. http://dx.doi.org/10.1083/jcb.130.5.1127.
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Involvement of transglutaminase in myofibrillogenesis of chick embryonic myoblasts has been investigated in vitro. Both the activity and protein level of transglutaminase initially decreased to a minimal level at the time of burst of myoblast fusion but gradually increased thereafter. The localization of transglutaminase underwent a dramatic change from the whole cytoplasm in a diffuse pattern to the cross-striated sarcomeric A band, being strictly colocalized with the myosin thick filaments. For a brief period prior to the appearance of cross-striation, transglutaminase was localized in nonstriated filamental structures that coincided with the stress fiber-like structures. When 12-o-tetradecanoyl phorbol acetate was added to muscle cell cultures to induce the sequential disassembly of thin and thick filaments, transglutaminase was strictly colocalized with the myosin thick filaments even in the myosacs, of which most of the thin filaments were disrupted. Moreover, monodansylcadaverine, a competitive inhibitor of transglutaminase, reversibly inhibited the myofibril maturation. In addition, myosin heavy chain behaved as one of the potential intracellular substrates for transglutaminase. The cross-linked myosin complex constituted approximately 5% of the total Triton X-100-insoluble pool of myosin molecules in developing muscle cells, and its level was reduced to below 1% upon treatment with monodansylcadaverine. These results suggest that transglutaminase plays a crucial role in myofibrillogenesis of developing chick skeletal muscle.
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HITOMI, Kiyotaka, Koji IKURA, and Masatoshi MAKI. "GTP, an Inhibitor of Transglutaminases, is Hydrolyzed by Tissue-type Transglutaminase (TGase 2) but not by Epidermal-type Transglutaminase (TGase 3)." Bioscience, Biotechnology, and Biochemistry 64, no. 3 (January 2000): 657–59. http://dx.doi.org/10.1271/bbb.64.657.
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Korner, G., D. E. Schneider, M. A. Purdon, and T. D. Bjornsson. "Bovine aortic endothelial cell transglutaminase. Enzyme characterization and regulation of activity." Biochemical Journal 262, no. 2 (September 1, 1989): 633–41. http://dx.doi.org/10.1042/bj2620633.
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Bovine aortic endothelial cells contain Ca2+-dependent tissue-type transglutaminase. Its activity in these cells was high, with apparent Km and Vmax. values with respect to putrescine of 0.203 mM and 18.5 nmol/min per mg of protein, and its activity was inhibited by the three competitive inhibitors dansylcadaverine, spermine and methylamine. The molecular mass of endothelial cell transglutaminase estimated by gel filtration chromatography was 88 kDa and it was immunoprecipitated by rabbit monospecific antiserum raised against rat liver transglutaminase. Its enzymic activity rose when the cell cultures reached confluence, and was further increased when their proliferation was arrested (synchronized at G0/G1 phase). Most of the enzymic activity was found in the 15,000 g soluble fraction, with only 4-22% of the activity found in the particulate fraction, depending on the state of cell proliferation. Examination of these cellular fractions by SDS/polyacrylamide-gel electrophoresis and immunoblotting revealed that at confluence endothelial cells have accumulated transglutaminase antigen in their 15,000 g particulate fraction. A series of experiments demonstrated the existence of a latent transglutaminase form in non-proliferating cells, and suggested that this might involve the formation of an inhibitory complex. Treatment of cell lysates and the 15,000 g particulate fraction with high salt concentration showed a significant increase in transglutaminase activity. Mixing experiments using the 100,000 g particulate fraction or purified rat liver transglutaminase on one hand and the cytosolic fraction on the other showed dose-dependent inhibition of the transglutaminase activity of the latter. It is concluded that endothelial cells contain a particulate fraction-residing inhibitor of transglutaminase which interacts via ionic interaction with the enzyme.
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Yashkin, A. I., and V. B. Mazalevskij. "EFFECT OF TRANSGLUTAMINASE TREATMENTON TRANSITION OF SOLIDS FROM MILK TO CHEESE." Innovations and Food Safety, no. 2 (August 6, 2021): 15–23. http://dx.doi.org/10.31677/2072-6724-2021-32-2-15-23.
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Transglutaminase is an enzyme that forms cross-links between protein molecules and affects such protein properties as the ability to gel, thermal stability, water retention, etc. One of the important tasks of the food industry is to increase the yield of products, in particular soft cheeses, in the production of which a significant part of the whey with dissolved substances is separated from milk. Therefore, the aim of the work was to study the effect of transglutaminase on the transition of milk solids to cheese, depending on the stage of application of the enzyme. Transglutaminase in an amount of 0.05% by weight of milk (1.6 units in terms of 1 g of protein) was introduced in two versions: simultaneously with the milk-clotting enzyme and after cutting the clot. It was found that the use of transglutaminase does not affect the duration of acid-rennet coagulation of milk. The data obtained indicate that when transglutaminase is introduced into milk simultaneously with the milk-converting enzyme, the transition of milk solids to cheese increases by 5.15%, including fat by 3.07%, compared to samples without transglutaminase. When transglutaminase is added at the stage of processing the clot, a denser consistency of cheese is formed.
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Battaglia, D. E., and B. M. Shapiro. "Hierarchies of protein cross-linking in the extracellular matrix: involvement of an egg surface transglutaminase in early stages of fertilization envelope assembly." Journal of Cell Biology 107, no. 6 (December 1, 1988): 2447–54. http://dx.doi.org/10.1083/jcb.107.6.2447.
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The involvement of transglutaminase activity in fertilization envelope (FE) formation was investigated using eggs from the sea urchin, Strongylocentrotus purpuratus. Eggs fertilized in the presence of the transglutaminase inhibitors, putrescine and cadaverine, had disorganized and expanded FEs with inhibition of the characteristic I-T transition. The permeability of the FE was increased by these agents, as revealed by the loss of proteins from the perivitelline space and the appearance of ovoperoxidase activity in supernates from putrescine-treated eggs. [3H]putrescine was incorporated into the FE during fertilization in a reaction catalyzed by an egg surface transglutaminase that could also use dimethylcasein as a substrate in vitelline layer-denuded eggs. Egg secretory products alone had no transglutaminase activity. The cell surface transglutaminase activity was transient and maximal within 4 min of activation. The enzyme was Ca2+ dependent and was inhibited by Zn2+. We conclude that sea urchin egg surface transglutaminase catalyzes an early step in a hierarchy of cross-linking events during FE assembly, one that occurs before ovoperoxidase-mediated dityrosine formation (Foerder, C. A., and B. M. Shapiro. 1977. Proc. Natl. Acad. Sci. USA. 74:4214-4218). Thus it provides a graphic example of the physiological function of a cell surface transglutaminase.
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Sitorasmi, Puspita Hapsari, Yuniar Sarah Ningtiyas, Indri Wahyuni, and Yulia Primitasari. "Safety of transglutaminase-induced corneal collagen cross-linking on the central cornea thickness and intraocular pressure in vivo." F1000Research 12 (January 12, 2023): 48. http://dx.doi.org/10.12688/f1000research.129694.1.
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Background: Corneal collagen cross-linking (CXL) is a procedure for making bonds that connect polymer chains to one another. Corneal CXL aims to slow or stop the progression of keratoconus by using photooxidative therapy so as to increase stromal rigidity. Transglutaminase enzymes are currently widely used in the food industry. Recent studies have shown that mRNA, fibronectin, and transglutaminase were found to be more abundant in human corneal keratocytes treated with UVA and riboflavin. Transglutaminase is considered to reduce discomfort caused by UVA irradiation. Methods: A total of 21 white New Zealand rabbits were divided into three groups, namely, transglutaminase-induced CXL group, epithelial-off CXL group, and transepithelial CXL group. The ocular surface was treated with a 1 U/mL microbial transglutaminase solution, and both the epithelial-off and transepithelial groups were exposed to clinical ultraviolet A-riboflavin (UVA/RF). The efficacy of each group was evaluated on the 14th day after the procedures. The central corneal thickness (CCT) and intraocular pressure (IOP) were evaluated using Corneal Visualization Scheimpflug Technology (Corvis ST). Results: The transglutaminase-induced CXL group exhibited the highest mean CCT (370.14 ± 38.85) in comparison with the UVA/RF epithelial-off group (368.00 ± 25.48) and the UVA/RF transepithelial group (369.86 ± 23.43). The transglutaminase-induced CXL group had the highest IOP mean (8.50 ± 3.02) compared with the UVA/RF epithelial-off (6.50 ± 3.07) and UVA/RF transepithelial groups (7.00 ± 1.90). There were no significant differences in CCT (p = 0.990) or IOP (p = 0.563) between the groups. Conclusions: The findings of this study suggest that there are no significant differences between the transglutaminase-induced CXL group and the UVA/RF CXL group. The safety of transglutaminase-induced CXL could be comparable to that of UVA/RF CXL in terms of altering CCT and IOP, which are two factors contributing to corneal rigidity.
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Akiyama, M., Soo-Youl Kim, Kozo Yoneda, and Hiroshi Shimizu. "Expression of transglutaminase 1 (transglutaminase K) in harlequin ichthyosis." Archives of Dermatological Research 289, no. 2 (January 28, 1997): 116–19. http://dx.doi.org/10.1007/s004030050165.
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JOHNSON, Timothy S., Claire I. SCHOLFIELD, James PARRY, and Martin GRIFFIN. "Induction of tissue transglutaminase by dexamethasone: its correlation to receptor number and transglutaminase-mediated cell death in a series of malignant hamster fibrosarcomas." Biochemical Journal 331, no. 1 (April 1, 1998): 105–12. http://dx.doi.org/10.1042/bj3310105.
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Treatment of the hamster fibrosarcoma cell lines (Met B, D and E) and BHK-21 hamster fibroblast cells with the glucocorticoid dexamethasone led to a powerful dose-dependent mRNA-synthesis-dependent increase in transglutaminase activity, which can be correlated with dexamethasone-responsive receptor numbers in each cell line. Increasing the number of dexamethasone-responsive receptors by transfection of cells with the HG1 glucocorticoid receptor protein caused an increase in transglutaminase activity that was proportional to the level of transfected receptor. In all experiments the levels of the tissue transglutaminase-mediated detergent-insoluble bodies was found to be comparable with increases in transglutaminase activity. Despite an increase in detergent-insoluble body formation, an increase in apoptosis as measured by DNA fragmentation was not found. Incubation of cells with the non-toxic competitive transglutaminase substrate fluorescein cadaverine led to the incorporation of this fluorescent amine into cellular proteins when cells were damaged after exposure to trypsin during cell passage. These cross-linked proteins containing fluorescein cadaverine were shown to be present in the detergent-insoluble bodies, indicating that the origin of these bodies is via activation of tissue transglutaminase after cell damage by trypsinization rather than apoptosis per se,since Met B cells expressing the bcl-2 cDNA were not protected from detergent-insoluble body formation. We describe a novel mechanism of cell death related to tissue transglutaminase expression and cell damage.
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Bogdanova, L., E. Efimova, E. Dmitruk, and S. Virina. "STUDY OF TECHNOLOGICAL FEATURES OF USE OF ACYLTRANSFERASE IN THE PRODUCTION OF DAIRY PRODUCTS." Topical issues of processing of meat and milk raw materials, no. 14 (December 14, 2020): 123–31. http://dx.doi.org/10.47612/2220-8755-2019-14-123-131.
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The article presents the results of studies on the effect of transglutaminase on the technological process of dairy production. An increase in the duration of fermentation and a slowdown in the increase in acidity with the addition of transglutaminase have been established. The higher viscosity of dairy products produced using transglutaminase and a lower increase in titratable acidity during storage were determined.
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Bogdanova, L., E. Efimova, E. Dmitruk, and S. Virina. "STUDY OF TECHNOLOGICAL FEATURES OF USE OF ACYLTRANSFERASE IN THE PRODUCTION OF DAIRY PRODUCTS." Topical issues of processing of meat and milk raw materials, no. 14 (December 14, 2020): 123–31. http://dx.doi.org/10.47612/8755-2019-14-123-131.
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The article presents the results of studies on the effect of transglutaminase on the technological process of dairy production. An increase in the duration of fermentation and a slowdown in the increase in acidity with the addition of transglutaminase have been established. The higher viscosity of dairy products produced using transglutaminase and a lower increase in titratable acidity during storage were determined.
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Alam Ali, Nur, Wadli, and Muhamad Hasdar. "PENGARUH KOMBINASI BAKSO DAGING IKAN LELE DAN DAGING AYAM DENGAN PENAMBAHAN ENZIM TRANSGLUTAMINASE." Journal of Technology and Food Processing (JTFP) 3, no. 01 (January 31, 2023): 16–24. http://dx.doi.org/10.46772/jtfp.v3i01.1108.
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harganya murah rasanya pun juga enak, penelitian ini bertujuan untuk mendapatkan hasil perlakuan terbaik dan mutu sesuai Setandar Nasional Indonesia (SNI) dari kombinasi daging ikan lele dan ayam yang ditambahkan enzim transglutaminase. Metode penelitian menggunakan Rancangan Acak Lengkap (RAL) dengan lima perlakuan dan tiga ulangan yaitu: PB1: (Daging ikan lele 200 gram Daging ayam 0 gram dan ditambah Enzim transglutaminase 6 gram), PB2 : (Daging ikan lele 150 gram Daging ayam 50 gram dan ditambah Enzim transglutaminase 6 gram), PB3 : (Daging ikan lele 100 gram Daging ayam 100 gram dan ditambah Enzim transglutaminase 6 gram), PB4 : (Daging ikan lele 50 gram Daging ayam 150 gram dan ditambah Enzim transglutaminase 6 gram), dan PB5 : (Daging ikan lele 0 gram Daging ayam 200 gram dan ditambah Enzim transglutaminase 6 gram). Parameter yang diuji adalah uji organoleptik meliputi warna, aroma, rasa, tekstur, uji lipat dan uji pH. Data hasil pengujian dianalisis menggunakan analisis sidik ragam atau (ANOVA) dan uji lanjut Duncan,s Multiple Range Test (DMRT). Hasil penelitian menunjukkan bahwa uji organoleptik, uji lipat dan uji pH, hasil beda nyata dan masih memenuhi syarat mutu bakso daging sapi SNI 01-3818-1995.
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Juprelle-Soret, M., S. Wattiaux-De Coninck, and R. Wattiaux. "Subcellular localization of transglutaminase. Effect of collagen." Biochemical Journal 250, no. 2 (March 1, 1988): 421–27. http://dx.doi.org/10.1042/bj2500421.
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1. The subcellular distribution of transglutaminase was investigated by using the analytical approach of differential and isopycnic centrifugation as applied to three organs of the rat: liver, kidney and lung. After differential centrifugation by the method of de Duve, Pressman, Gianetto, Wattiaux & Appelmans [(1955) Biochem. J. 63, 604-617], transglutaminase is mostly recovered in the unsedimentable fraction S and the nuclear fraction N. After isopycnic centrifugation of the N fraction in a sucrose density gradient, a high proportion of the enzyme remains at the top of the gradient; a second but minor peak of activity is present in high-density regions, where a small proportion of 5′-nucleotidase, a plasma-membrane marker, is present together with a large proportion of collagen recovered in that fraction. 2. Fractions where a peak of transglutaminase was apparent in the sucrose gradient were examined by electron microscopy. The main components are large membrane sheets with extracellular matrix and free collagen fibers. 3. As these results seem to indicate that some correlation exists between particulate transglutaminase distribution and those of collagen and plasma membranes, the possible binding of transglutaminase by collagen (type I) and by purified rat liver plasma membrane was investigated. 4. The binding studies indicated that collagen is able to bind transglutaminase and to make complexes with plasma-membrane fragments whose density is higher than that of plasma-membrane fragments alone. Transglutaminase cannot be removed from such complexes by 1% Triton X-100, but can be to a relatively large extent by 0.5 M-KCl and by 50% (w/v) glycerol. 5. Such results suggest that the apparent association of transglutaminase with plasma membrane originates from binding in vitro of the cytosolic enzyme to plasma membrane bound to collagen, which takes place during homogenization of the tissue, when the soluble enzyme and extracellular components are brought together.
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Nunes, Irene, Pierre-Emmanuel Gleizes, Christine N. Metz, and Daniel B. Rifkin. "Latent Transforming Growth Factor-β Binding Protein Domains Involved in Activation and Transglutaminase-dependent Cross-Linking of Latent Transforming Growth Factor-β." Journal of Cell Biology 136, no. 5 (March 10, 1997): 1151–63. http://dx.doi.org/10.1083/jcb.136.5.1151.
Full textAbstract:
Transforming growth factor-β (TGF-β) is secreted by many cell types as part of a large latent complex composed of three subunits: TGF-β, the TGF-β propeptide, and the latent TGF-β binding protein (LTBP). To interact with its cell surface receptors, TGF-β must be released from the latent complex by disrupting noncovalent interactions between mature TGF-β and its propeptide. Previously, we identified LTBP-1 and transglutaminase, a cross-linking enzyme, as reactants involved in the formation of TGF-β. In this study, we demonstrate that LTBP-1 and large latent complex are substrates for transglutaminase. Furthermore, we show that the covalent association between LTBP-1 and the extracellular matrix is transglutaminase dependent, as little LTBP-1 is recovered from matrix digests prepared from cultures treated with transglutaminase inhibitors. Three polyclonal antisera to glutathione S–transferase fusion proteins containing amino, middle, or carboxyl regions of LTBP-1S were used to identify domains of LTBP-1 involved in crosslinking and formation of TGF-β by transglutaminase. Antibodies to the amino and carboxyl regions of LTBP-1S abrogate TGF-β generation by vascular cell cocultures or macrophages. However, only antibodies to the amino-terminal region of LTBP-1 block transglutaminase-dependent cross-linking of large latent complex or LTBP-1. To further identify transglutaminase-reactive domains within the amino-terminal region of LTBP-1S, mutants of LTBP-1S with deletions of either the amino-terminal 293 (ΔN293) or 441 (ΔN441) amino acids were expressed transiently in CHO cells. Analysis of the LTBP-1S content in matrices of transfected CHO cultures revealed that ΔN293 LTBP-1S was matrix associated via a transglutaminasedependent reaction, whereas ΔN441 LTBP-1S was not. This suggests that residues 294–441 are critical to the transglutaminase reactivity of LTBP-1S.
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Tamada, Y., H. Takama, T. Kitamura, T. Ikeya, and T. Yokochi. "Expression of transglutaminase I in human anagen hair follicles." Acta Dermato-Venereologica 75, no. 3 (May 1, 1995): 190–92. http://dx.doi.org/10.2340/0001555575190192.
Full textAbstract:
The expression of the transglutaminase I in human anagen hair follicles was studied by an immunohistochemical staining. In the bulbar and suprabulbar portions of anagen hair follicles, transglutaminase I was detected on the hair cuticle and the three layers of the inner root sheath. Subsequently, the positive staining became translocated to the inner site of the outer root sheath in the middle part of the hair follicle. In the upper portion of the hair follicle transglutaminase I was detected in the internal part of the outer root sheath and the surface epidermis. Therefore, it was suggested that the expression of transglutaminase I might be closely associated with the terminal keratinization in the anagen hair follicles.
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Gebhardt, Ronald, Sahel Khanna, Jann Schulte, and Md Asaduzzaman. "Effect of Transglutaminase Post-Treatment on the Stability and Swelling Behavior of Casein Micro-Particles." International Journal of Molecular Sciences 23, no. 19 (October 5, 2022): 11837. http://dx.doi.org/10.3390/ijms231911837.
Full textAbstract:
Casein microparticles are produced by flocculation of casein micelles due to volume exclusion of pectin and subsequent stabilization by film drying. Transglutaminase post-treatment alters their stability, swelling behavior, and internal structure. Untreated particles sediment due to their size and disintegrate completely after the addition of sodium dodecyl sulfate. The fact that transglutaminase-treated microparticles only sediment at comparable rates under these conditions shows that their structural integrity is not lost due to the detergent. Transglutaminase-treated particles reach an equilibrium final size after swelling instead of decomposing completely. By choosing long treatment times, swelling can also be completely suppressed as experiments at pH 11 show. In addition, deswelling effects also occur within the swelling curves, which enhance with increasing transglutaminase treatment time and are ascribed to the elastic network of cross-linked caseins. We propose a structural model for transglutaminase-treated microparticles consisting of a core of uncross-linked and a shell of cross-linked caseins. A dynamic model describes all swelling curves by considering both casein fractions in parallel. The characteristic correlation length of the internal structure of swollen casein microparticles is pH-independent and decreases with increasing transglutaminase treatment time, as observed also for the equilibrium swelling value of uncross-linked caseins.
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Floyd, E. E., and A. M. Jetten. "Regulation of type I (epidermal) transglutaminase mRNA levels during squamous differentiation: down regulation by retinoids." Molecular and Cellular Biology 9, no. 11 (November 1989): 4846–51. http://dx.doi.org/10.1128/mcb.9.11.4846-4851.1989.
Full textAbstract:
Squamous differentiation of rabbit tracheal epithelial cells is accompanied by an approximately 50-fold increase in the activity of type I (epidermal) transglutaminase, while the levels of type II (tissue) transglutaminase remain almost undetectable. To identify a cDNA encoding type I transglutaminase, we screened a library of cDNA clones prepared from poly(A)+ RNA isolated from squamous-differentiated rabbit tracheal epithelial cells. Four overlapping clones (represented by clone pTG-7) which span a range of 2.8 kilobases were identified; partial sequencing of pTG-7 indicated that it encodes a transglutaminaselike protein. pTG-7 hybridized to a 3.6-kilobase mRNA which is distinct from that for type II transglutaminase. pTG-7 mRNA levels were low in proliferative cells, increased dramatically in squamous-differentiated cells, and could be further enhanced by growth of the cells in high concentrations (2 mM) of calcium ions. Retinoic acid, which blocks the expression of the squamous phenotype, prevented this increase in pTG-7 mRNA levels. These changes in levels of pTG-7 mRNA parallel the changes in type I transglutaminase activity observed under similar culture conditions. These data indicate that pTG-7 encodes the mRNA for transglutaminase type I and that expression of this mRNA is negatively regulated by retinoic acid.
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Floyd, E. E., and A. M. Jetten. "Regulation of type I (epidermal) transglutaminase mRNA levels during squamous differentiation: down regulation by retinoids." Molecular and Cellular Biology 9, no. 11 (November 1989): 4846–51. http://dx.doi.org/10.1128/mcb.9.11.4846.
Full textAbstract:
Squamous differentiation of rabbit tracheal epithelial cells is accompanied by an approximately 50-fold increase in the activity of type I (epidermal) transglutaminase, while the levels of type II (tissue) transglutaminase remain almost undetectable. To identify a cDNA encoding type I transglutaminase, we screened a library of cDNA clones prepared from poly(A)+ RNA isolated from squamous-differentiated rabbit tracheal epithelial cells. Four overlapping clones (represented by clone pTG-7) which span a range of 2.8 kilobases were identified; partial sequencing of pTG-7 indicated that it encodes a transglutaminaselike protein. pTG-7 hybridized to a 3.6-kilobase mRNA which is distinct from that for type II transglutaminase. pTG-7 mRNA levels were low in proliferative cells, increased dramatically in squamous-differentiated cells, and could be further enhanced by growth of the cells in high concentrations (2 mM) of calcium ions. Retinoic acid, which blocks the expression of the squamous phenotype, prevented this increase in pTG-7 mRNA levels. These changes in levels of pTG-7 mRNA parallel the changes in type I transglutaminase activity observed under similar culture conditions. These data indicate that pTG-7 encodes the mRNA for transglutaminase type I and that expression of this mRNA is negatively regulated by retinoic acid.
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Odii, Benedict Onyekachi, and Peter Coussons. "Biological Functionalities of Transglutaminase 2 and the Possibility of Its Compensation by Other Members of the Transglutaminase Family." Scientific World Journal 2014 (2014): 1–13. http://dx.doi.org/10.1155/2014/714561.
Full textAbstract:
Transglutaminase 2 (TG2) is the most widely distributed and most abundantly expressed member of the transglutaminase family of enzymes, a group of intracellular and extracellular proteins that catalyze the Ca2+-dependent posttranslational modification of proteins. It is a unique member of the transglutaminase family owing to its specialized biochemical, structural and functional elements, ubiquitous tissue distribution and subcellular localization, and substrate specificity. The broad substrate specificity of TG2 and its flexible interaction with numerous other gene products may account for its multiple biological functions. In addition to the classic Ca2+-dependent transamidation of proteins, which is a hallmark of transglutaminase enzymes, additional Ca2+-independent enzymatic and nonenzymatic activities of TG2 have been identified. Many such activities have been directly or indirectly implicated in diverse cellular physiological events, including cell growth and differentiation, cell adhesion and morphology, extracellular matrix stabilization, wound healing, cellular development, receptor-mediated endocytosis, apoptosis, and disease pathology. Given the wide range of activities of the transglutaminase gene family it has been suggested that, in the absence of active versions of TG2, its function could be compensated for by other members of the transglutaminase family. It is in the light of this assertion that we review, herein, TG2 activities and the possibilities and premises for compensation for its absence.