Transglutaminases: multifunctional cross‐linking enzymes that stabilize tissues

@article{Greenberg1991TransglutaminasesMC,
  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},
  year={1991},
  volume={5},
  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… 
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948 Citations

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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.

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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

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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.

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    Journal of cellular biochemistry
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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.

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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.

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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…

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

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TLDR
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.

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TLDR
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TLDR
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TLDR
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TLDR
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...