Transglutaminases: multifunctional cross‐linking enzymes that stabilize tissues

  title={Transglutaminases: multifunctional cross‐linking enzymes that stabilize tissues},
  author={Charles S. Greenberg and Paul J. Birckbichler and Robert H. Rice},
  journal={The FASEB Journal},
  pages={3071 - 3077}
Transglutaminases catalyze the posttranslational modification of proteins by transamidation of available glutamine residues. This action results primarily in the formation of ∊‐(γ‐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… 

Transglutaminases: nature's biological glues.

The structural and regulatory features important in mammalian Tgases are detail, with particular focus on the ubiquitous type 2 tissue enzyme, and some of the present and future biotechnological applications are included.

Tissue transglutaminase: an enzyme with a split personality.

  • J. -. ChenK. Mehta
  • Biology, Chemistry
    The international journal of biochemistry & cell biology
  • 1999

"Tissue" transglutaminase in animal development.

An overview of the current knowledge on tTG expression and regulation in animal reproduction and development is presented and the data available so far further strengthen the relationship existing between t TG expression and the induction of PCD.

Roles of transglutaminases in cardiac and vascular diseases.

Accumulating evidence points to novel roles for factor XIII and TG2 in cardiovascular biology including: modulating platelet activity, regulating glucose control, contributing to the development of hypertension, and influencing the progression of atherosclerosis.

Transglutaminase Cross‐Linking of the τ Protein

These experiments demonstrate that the enzyme modifies τ at only one or a few discrete sites, primarily in the carboxyl half of the molecule, and provides evidence that the cross-linking reaction is specific, and requires that the substrates be appropriately associated for cross‐linking to occur.

“Activation of tissue tranglutsaminase by removal of carboxyl‐terminal peptides”

  • B. Fraij
  • Biology, Chemistry
    Journal of cellular biochemistry
  • 2011
Calcium or GTP was essential for activation of T GC cross‐linking activity by trypsin in membrane fractions from human RBC and was accompanied by the conversion of TGC to a smaller TG form, a condition that may be comparable to injury or wounds that lead to rapid enzymatic transamidation activation.

Mammalian transglutaminases

Data is reviewed on the properties of mammalian transglutaminases, particularly as regards their protein substrates and the relevance of transglUTaminase‐catalysed reactions in physiological and disease conditions.

379 Transglutaminases : Nature ’ s biological glues

Transglutaminases (Tgases) are a widely distributed group of enzymes that catalyse the post-translational modification of proteins by the formation of isopeptide bonds. This occurs either through

Characterisation of a novel cold‐adapted calcium‐activated transglutaminase: implications for medicine and food processing

The successful expression of recombinant transglutaminase protein from Atlantic cod (AcTG‐1) as a soluble protein upon induction at low temperature was confirmed by sodium dodecyl sulfate/polyacrylamide gel electrophoresis, immunoblotting and mass spectrometry analysis, offering advantages over commercially available enzymatic glues in the food industry.

Evidences for a role of protein cross-links in transglutaminase-related disease

A comprehensive review of recent insights into the pathophysiology of TGs related to their protein cross-linking activity is presented.



Transglutaminase-mediated cross-linking of proteins and cell ageing: the erythrocyte and lens models.

  • L. Lorand
  • Biology
    Advances in experimental medicine and biology
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The transglutaminase-mediated incorporation of amines “could produce modified body proteins which might interfere with enzymatic activities.....or might possess antigenic properties” gains some support from the high incidence of autoimmune diseases following treatment with isoniazid and hydralazine, two drugs which could conceivably provoke a breakdown of immune tolerance against the parent protein itself.

Covalent polyamine-protein conjugates: analysis and distribution.

Most suggestions as to the biological functions of the polyamines, putrescine, spermidine, and spermine, are based on the observed noncovalent binding of these polycations to nucleic acids, proteins,

Primary structure of keratinocyte transglutaminase.

Alignments of amino acid sequences show substantial similarity among the keratinocyte transglutaminase, human clotting factor XIII catalytic subunit, guinea pig liver tissue transglutanase, and the human erythrocyte band-4.2 protein.

Proteolytic release of keratinocyte transglutaminase.

Human keratinocytes express a particulate transglutaminase that can be released from the membrane by limited proteolysis with trypsin or plasmin to yield a form that is congruent to 80 kDa, and hydrodynamic measurements showed that the endogenously released enzyme was monomeric in solution, whereas that solubilized by hydroxylamine without proteolytic activity appeared dimeric.

Primary structure of blood coagulation factor XIIIa (fibrinoligase, transglutaminase) from human placenta.

The primary structure of human placental factor XIIIa, an enzyme that forms intermolecular isopeptide bonds between fibrin molecules as the last step in blood coagulation, is determined by homology to the high-affinity sites in calmodulins.

Amino acid sequence of guinea pig liver transglutaminase from its cDNA sequence.

The complete amino acid sequence of guinea pig liver transglutaminase, a typical tissue-type nonzymogenic transglutonase, was predicted by the cloning and sequence analysis of DNA complementary to its mRNA.