Transglutaminases and disease: lessons from genetically engineered mouse models and inherited disorders - PubMed (original) (raw)
Review
. 2009 Jul;89(3):991-1023.
doi: 10.1152/physrev.00044.2008.
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- PMID: 19584319
- DOI: 10.1152/physrev.00044.2008
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Review
Transglutaminases and disease: lessons from genetically engineered mouse models and inherited disorders
Siiri E Iismaa et al. Physiol Rev. 2009 Jul.
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Abstract
The human transglutaminase (TG) family consists of a structural protein, protein 4.2, that lacks catalytic activity, and eight zymogens/enzymes, designated factor XIII-A (FXIII-A) and TG1-7, that catalyze three types of posttranslational modification reactions: transamidation, esterification, and hydrolysis. These reactions are essential for biological processes such as blood coagulation, skin barrier formation, and extracellular matrix assembly but can also contribute to the pathophysiology of various inflammatory, autoimmune, and degenerative conditions. Some members of the TG family, for example, TG2, can participate in biological processes through actions unrelated to transamidase catalytic activity. We present here a comprehensive review of recent insights into the physiology and pathophysiology of TG family members that have come from studies of genetically engineered mouse models and/or inherited disorders. The review focuses on FXIII-A, TG1, TG2, TG5, and protein 4.2, as mice deficient in TG3, TG4, TG6, or TG7 have not yet been reported, nor have mutations in these proteins been linked to human disease.
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