Transglutaminases: nature's biological glues.

Area of Science:

• Biochemistry
• Enzymology
• Molecular Biology

Background:

• Transglutaminases (Tgases) catalyze protein post-translational modifications via isopeptide bond formation.
• These modifications include protein cross-linking and amine incorporation, yielding stable, high-molecular-mass products.
• Tgase activity is vital in tissues like skin and hair, and processes such as blood clotting and wound healing.

Purpose of the Study:

• To review the structural and regulatory features of mammalian transglutaminases, with emphasis on the type 2 tissue enzyme.
• To discuss the physiological roles and substrates of Tgases.
• To explore the involvement of Tgases in human diseases and their biotechnological applications.

Main Methods:

• Literature review focusing on mammalian transglutaminases.
• Analysis of structural and regulatory features.
• Discussion of physiological roles, substrates, and disease pathogenesis.
• Exploration of current and future biotechnological applications.

Main Results:

• Transglutaminases form epsilon-(gamma-glutamyl)lysine bonds or incorporate primary amines into proteins.
• Accumulation of cross-linked products is observed in tissues and processes requiring mechanical strength and resistance to degradation.
• Deregulation of Tgase activity is implicated in chronic neurodegeneration, neoplastic diseases, autoimmune disorders, fibrosis, and skin diseases.

Conclusions:

• Mammalian transglutaminases, particularly type 2, play critical roles in protein structure and function.
• Understanding Tgase function and regulation is key to elucidating disease pathogenesis.
• The unique protein-modifying capabilities of Tgases present significant biotechnological opportunities.