Transglutaminase

Transglutaminase is an enzyme that catalyzes the formation of isopeptide bonds between proteins. It is also known as protein-glutamine γ-glutamyltransferase. The primary function of transglutaminase is to stabilize protein structures, but it also plays a role in various biological processes.

Function

Transglutaminase catalyzes the formation of an isopeptide bond between the γ-carboxamide group of a protein-bound glutamine and the ε-amino group of a protein-bound lysine, forming a cross-link that stabilizes the protein structure. This reaction is calcium-dependent.

In addition to its role in protein stabilization, transglutaminase is involved in various biological processes. It plays a role in the formation of the skin barrier, wound healing, and apoptosis. It is also involved in the pathogenesis of several diseases, including celiac disease, neurodegenerative diseases, and cancer.

Types

There are eight known types of transglutaminase, which are classified based on their tissue distribution and sequence homology. These include tissue transglutaminase (tTG), factor XIIIa, epidermal transglutaminase (TGase 3), and keratinocyte transglutaminase (TGase 1).

Clinical significance

Transglutaminase has been implicated in a number of diseases. In celiac disease, tTG modifies gluten peptides, which leads to an immune response that damages the small intestine. Transglutaminase is also involved in the aggregation of proteins in neurodegenerative diseases such as Alzheimer's disease and Parkinson's disease. In cancer, transglutaminase can contribute to tumor progression by promoting cell survival and metastasis.

See also

• Glutamine
• Isopeptide bond
• Celiac disease
• Alzheimer's disease
• Parkinson's disease
• Cancer

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