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Journal articles on the topic 'Transglutaminase'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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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 (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 transglutamin

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2

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 (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 tra

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3

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 char

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4

Sachslehner, Attila Placido, Marta Surbek, Bahar Golabi, et al. "Transglutaminase Activity Is Conserved in Stratified Epithelia and Skin Appendages of Mammals and Birds." International Journal of Molecular Sciences 24, no. 3 (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 i

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5

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. Anima

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6

Cocuzzi, E., M. Piacentini, S. Beninati, and S. I. Chung. "Post-translational modification of apolipoprotein B by transglutaminases." Biochemical Journal 265, no. 3 (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,

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7

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 (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 immu

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8

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 (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

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9

Watanabe, Yuko, Kazuho Okuya, Yuki Takada, et al. "Gene disruption of medaka (Oryzias latipes) orthologue for mammalian tissue-type transglutaminase (TG2) causes movement retardation." Journal of Biochemistry 168, no. 3 (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 ap

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10

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 (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 enz

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11

Gün, Büşra, and Semih Yilmaz. "BACILLUS ORIGINATED TRANSGLUTAMINASE: PROPERTIES AND USAGE." Current Trends in Natural Sciences 11, no. 21 (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

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12

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

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13

Bergamini, C. M., and M. Signorini. "Studies on tissue transglutaminases: interaction of erythrocyte type-2 transglutaminase with GTP." Biochemical Journal 291, no. 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 sa

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14

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 (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 concentratio

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15

Semkova, Mariya E., and J. Justin Hsuan. "Mass Spectrometric Identification of a Novel Factor XIIIa Cross-Linking Site in Fibrinogen." Proteomes 9, no. 4 (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 i

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16

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 (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 do

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17

Lorand, Laszlo. "Transglutaminase." Neurochemistry International 40, no. 1 (2002): 7–12. http://dx.doi.org/10.1016/s0197-0186(01)00056-0.

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18

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 (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 f

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19

Korponay–Szabó, Ilma R., Satu Sulkanen, Tuula Halttunen, et al. "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 (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‐staini

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20

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 (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 rel

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21

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 (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 transg

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22

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 (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

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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 (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

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Guadalupe, Concepción Rodríguez-Castillejos, Josias Téllez-Luis Simón, Vázquez-Vázquez Manuel, Aurelio Lois-Correa Jorge, Alberto Ramírez de León José, and Alvarado-Reyna Sofía. "Evaluation of alternative microbial transglutaminase production from sorghum grain and distilled dried grains with solubles using computational simulation." Revista Facultad de Ingeniería -redin-, no. 80 (September 15, 2016): 48–55. https://doi.org/10.17533/udea.redin.n80a06.

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 Microbial transglutaminase (MTGase) is widely used as an additive in the food industry for improving the mechanical properties and texture of foods. The enzyme production process is expensive due to the cost of the components of the fermentation medium used, therefore, it was evaluated the possibility of using inexpensive raw materials for <em>Streptomyces mobaraensis </em>growth. An economic study of microbial transglutaminase (MTGase) production with a variety of raw materials would be a long process. The software <em>SuperPro Designer</em>® <em>v7.5 </em>was used, based on data ob

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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 (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

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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 (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

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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

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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 (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 I

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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 (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

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Shi, Yan Guo, Lei Qian, Na Zhang, et al. "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

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F??s??s, L. "Tissue transglutaminase." Blood Coagulation & Fibrinolysis 3, no. 6 (1992): 805. http://dx.doi.org/10.1097/00001721-199212000-00020.

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32

Romijn, J. C. "Polyamines and transglutaminase actions: Polyamine und Transglutaminase-Wirkungen." Andrologia 22, S1 (2009): 83–91. http://dx.doi.org/10.1111/j.1439-0272.1990.tb02074.x.

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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 (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 sm

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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 (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 nonst

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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 (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

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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 amou

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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 (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 th

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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 (2000): 657–59. http://dx.doi.org/10.1271/bbb.64.657.

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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 whit

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Minh, N. P. "Synergistic effect of transglutaminase and salt on physical properties of fishballs from snakeskin gourami (Trichopodus pectoralis)." Food Research 9, no. 3 (2025): 359–63. https://doi.org/10.26656/fr.2017.9(3).5-118.

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The snakeskin gourami has been a favorite consumed due to its high commercial meat yield. Farming of snakeskin gourami has been recently extended in the Mekong Delta, Vietnam. Hence, it is essential to have a proper processing method to improve its marketable value. Transglutaminase enzyme has the potential to create good gelation with desirable rheological attributes while limiting the requirement of salt and phosphate. This research evaluated the production of fishballs prepared from snakeskin gourami. Fish paste was individually treated with transglutaminase (0-0.4%), salt (0-2.0%) or in co

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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 (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 th

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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 (1997): 116–19. http://dx.doi.org/10.1007/s004030050165.

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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 (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 ditamb

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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 (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 sec

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Nunes, Irene, Pierre-Emmanuel Gleizes, Christine N. Metz та 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, № 5 (1997): 1151–63. http://dx.doi.org/10.1083/jcb.136.5.1151.

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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 transgluta

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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 (1995): 190–92. http://dx.doi.org/10.2340/0001555575190192.

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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 t

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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 (2022): 11837. http://dx.doi.org/10.3390/ijms231911837.

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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 equi

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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 (1989): 4846–51. http://dx.doi.org/10.1128/mcb.9.11.4846-4851.1989.

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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

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