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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946 Citations
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946 Citations

Transglutaminases: nature's biological glues.
TLDR
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. -. Chen, K. Mehta
  • Biology, Chemistry
    The international journal of biochemistry & cell biology
  • 1999
"Tissue" transglutaminase in animal development.
TLDR
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.
TLDR
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
TLDR
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
TLDR
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
TLDR
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
TLDR
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
TLDR
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
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TLDR
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TLDR
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TLDR
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