Recent advances in the development of tissue transglutaminase (TG2) inhibitors
48
Citation
50
Reference
10
Related Paper
Citation Trend
Keywords:
Tissue transglutaminase
An αs1-casein film prepared using transglutaminase was applied as a support for immobilized enzymes. That is, the enzyme, to be immobilized was added to a mixture of 5% αs1-casein and transglutaminase. Before gelation by means of the transglutaminase-reaction, the reaction mixture was quickly spread on a horizontal plate. The immobilized enzyme film was removed from the plate after air-drying. Attempts were made to immobilize several enzymes, such as β-glucosidase, α-amannosidase, β-galactosidase and glucose oxidase. None of the immobilized enzymes lost activity on repeated usage. The enzymes tested were evidently immobilized through entrapment in the lattice of the protein film. Some enzymic characteristics of the immobilized enzymes showed that this new technique was as good as other known immobilization methods.
Tissue transglutaminase
Glucose oxidase
Cite
Citations (25)
Celiac disease (CD) is an intestinal malabsorption characterized by intolerance to cereal proteins accompanied by immunological responses to dietary gliadins and tissue transglutaminase, an autoantigen located in the endomysium. Tissue transglutaminase belongs to the family of enzymes that catalyze protein cross-linking reactions and is constitutively expressed in many tissues as well as being activated during apoptosis. The role of gliadins in eliciting the immune response in CD and how transglutaminase is linked to the primary reaction are still unclear. In this work, we report the production and analysis of six phage Ab libraries from the peripheral and intestinal lymphocytes of three CD patients. We were able to isolate Abs to transglutaminase from all intestinal lymphocytes libraries but not from those obtained from peripheral lymphocytes. This is in contrast to Abs against gliadin, which could be obtained from all libraries, indicating that the humoral response against transglutaminase occurs at the local level, whereas that against gliadin occurs both peripherally and centrally. Abs from all three patients recognized the same transglutaminase epitopes with a bias toward the use of the V(H)5 Ab variable region family. The possible role of these anti-transglutaminase Abs in the onset of CD and associated autoimmune pathologies is discussed.
Tissue transglutaminase
Gliadin
Cite
Citations (186)
Tissue transglutaminase
Cite
Citations (4)
This chapter contains sections titled: Physiological Functions of Transglutaminases Transglutaminase and the Formation of the Cross-Linked Envelope of Terminally Differentiated Keratinocytes Substrates of Keratinocyte Transglutaminase Proteins With Abnormally Long Polyglutamine As Substrates of Neuronal Transglutaminases in Genetic Diseases of the Central Nervous System Transglutaminase in Alzheimer's Disease Transglutaminase in Parkinson's Disease What Makes a Good Transglutaminase Substrate? Features Shared by Transglutaminase Substrates and Proteins Associated With Diseases of Polyglutamine Expansion Perspectives Acknowledgements References
Tissue transglutaminase
Epidermis (zoology)
Cite
Citations (5)
Tissue transglutaminase
Cite
Citations (170)
Celiac disease is an intestinal malabsorption characterized by an intolerance to cereal proteins accompanied by immunological responses to dietary gliadins and an autoantigen located in the endomysium. The latter has been identified as the enzyme tissue transglutaminase which belongs to a family of enzymes that catalyze protein cross‐linking reactions and is constitutively expressed in many tissues as well as being activated during apoptosis. In a recent paper, we described the selection and characterization of anti‐transglutaminase Igs from phage antibody libraries created from intestinal lymphocytes from celiac disease patients. In this work, using transglutaminase gene fragments, we identify a region of tissue transglutaminase recognized by these antibodies as being conformational and located in the core domain of the enzyme. This is identical to the region recognized by anti‐transglutaminase Igs found in the serum of celiac disease patients.
Tissue transglutaminase
Cite
Citations (65)
Tissue transglutaminase
Cite
Citations (34)
Tissue transglutaminase
Specific activity
Heat stability
Cite
Citations (10)
An αsl-casein film prepared using transglutaminase was applied as a support for immobilized enzymes. That is, the enzyme, to be immobilized was added to a mixture of 5% ocsl-casein and transglutaminase. Before gelation by means of the transglutaminase-reaction, the reaction mixture was quickly spread on a horizontal plate. The immobilized enzyme film was removed from the plate after air-drying. Attempts were made to immobilize several enzymes, such as β-glucosidase, α- mannosidase, ß-galactosidase and glucose oxidase. None of the immobilized enzymes lost activity on repeated usage. The enzymes tested were evidently immobilized through entrapment in the lattice of the protein film. Some enzymic characteristics of the immobilized enzymes showed that this new technique was as good as other known immobilization methods.
Tissue transglutaminase
Glucose oxidase
Cite
Citations (2)
The celiac disease screening with IgA tissue transglutaminase antibodies depends on the cut-off reaction, therefore many patients with values less but close to the cut-off may be undiagnosed. Material and Method. We conducted the CD screening with IgA tissue transglutaminase antibodies in a group of 1616 children during 2014 at a cut-off of 25 U/ml and at a cut-off of 10 U/ml. We also wanted to compare our results with IgA tissue transglutaminase antibodies prevalence from other countries. Results. We found a IgA tissue transglutaminase antibodies prevalence rate of 3% for values higher 25 U/ml and a IgA tissue transglutaminase antibodies prevalence rate of 1.6% for values between 10-25 U/ml. A prevalence of 13.6% for IgA tissue transglutaminase antibodies was observed in , and . Conclusions. We observed a 4.6% IgA tissue transglutaminase antibodies prevalence at a cut-off of 10 U/ml. Prevalence of IgA tissue transglutaminase antibodies from Romania is lowered compared with other European countries.
Tissue transglutaminase
Specific antibody
Immunoglobulin A
Cite
Citations (1)