PMID: 1683845Dec 1, 1991

Transglutaminases: multifunctional cross-linking enzymes that stabilize tissues

FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology
Charles S GreenbergRobert H Rice

Abstract

Transglutaminases catalyze the posttranslational modification of proteins by transamidation of available glutamine residues. This action results primarily in the formation of epsilon-(gamma-glutamyl)lysine cross-links but includes the incorporation of polyamines into suitable protein substrates as well. The covalent isopeptide crosslink is stable and resistant to proteolysis, thereby increasing the resistance of tissue to chemical, enzymatic, and mechanical disruption. The plasma transglutaminase, factor XIIIa, is formed at sites of blood coagulation and impedes blood loss by stabilizing the fibrin clot. The squamous epithelium constituting the protective callus layer of skin is formed by the action of keratinocyte transglutaminase (TGK) and epidermal transglutaminase (TGE). The tissue transglutaminase (TGC) is a cytoplasmic enzyme present in many cells including those in the blood vessel wall. TGC function is unknown, although it could function to stabilize intra- and extra-cellular molecules in a wide variety of physiologic or pathologic processes. The amino acid sequences of factor XIII, TGC, and TGK establish them as a homologous gene family and also reveal a striking homology to the erythrocyte membrane protein, band 4.2. ...Continue Reading

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Related Concepts

Factor XIII A-Chain
Glutamic Acids
Lysine Hydrochloride
Protein Conformation
Post-Translational Protein Processing
Transglutaminases
Homologous Sequences, Nucleic Acid
Drug or Chemical Tissue Distribution
Keratinocyte
Glutamic Acid, (D)-Isomer

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