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Transglutaminase 2 (TG2) is a ubiquitously expressed (intracellular as well as extracellular) protein, with multiple modes of Post-translational regulation, including an allosteric disulfide bond between Cys-370-Cys-371 that renders the enzyme inactive in the extracellular matrix.
Anti-transglutaminase antibodies are found in celiac disease and may play a role in the small bowel damage in response to dietary gliadin that characterises this condition. [2] In the related condition dermatitis herpetiformis , in which small bowel changes are often found and which responds to dietary exclusion of gliadin-containing wheat ...
Levels in cell membranes are increased by reduced glucose levels and decreased by increased glucose levels. GLUT1 expression is upregulated in many tumors. GLUT2: Is a bidirectional transporter, allowing glucose to flow in 2 directions. Is expressed by renal tubular cells, liver cells and pancreatic beta cells.
Gamma-glutamyltransferase (also γ-glutamyltransferase, GGT, gamma-GT, gamma-glutamyl transpeptidase; [1] EC 2.3.2.2) is a transferase (a type of enzyme) that catalyzes the transfer of gamma-glutamyl functional groups from molecules such as glutathione to an acceptor that may be an amino acid, a peptide or water (forming glutamate).
The components of bilayers are distributed unequally between the two surfaces to create asymmetry between the outer and inner surfaces. [2] This asymmetric organization is important for cell functions such as cell signaling. [3] The asymmetry of the biological membrane reflects the different functions of the two leaflets of the membrane. [4]
GLUT2 has high capacity for glucose but low affinity (high K M, ca. 15–20 mM) and thus functions as part of the "glucose sensor" in the pancreatic β-cells of rodents, though in human β-cells the role of GLUT2 seems to be a minor one. [8] It is a very efficient carrier for glucose.
A deficiency is associated with ichthyosis lamellaris. [11] Epidermal transglutaminase is the autoantigen, in humans, of dermatitis herpetiformis.. A study on the mutation of keratinocyte transglutaminase (TGK) came to conclude that those affected with ichthyosis lamellaris, present a substantial deficit in keratinocyte transglutaminase activity. [8]
Some studies have revealed that antibodies increase the activity of tTG, instead of inhibiting activity as is commonly encountered with function-altering antibodies. A recent study has shown that ATA also modify and increase replication in intestinal epithelial Cells, by apparently interacting with cell-surface transglutaminase. [22]