Tissue transglutaminase is expressed, active, and directly involved in rat dermal wound healing and angiogenesis

Haroon, Zishan A.; Hettasch, Joann M.; Lai, Thung S.; Dewhirst, Mark W.; Greenberg, Charles S.

doi:10.1096/fasebj.13.13.1787

Cited by 232 publications

(214 citation statements)

References 38 publications

(38 reference statements)

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“…Moreover, GTP and ATP act as non-competitive inhibitors for TGase5 transamidating activity. Therefore, under physiological conditions, TGase5-transamidating activity appears to be regulated by local concentrations of calcium and nucleotides (GTP, GDP, GMP and ATP), as previously proposed for TGase2 [6].…”

Section: Resultssupporting

confidence: 57%

“…TGase2 is involved in both intracellular and extracellular biological processes such as receptor-mediated endocytosis, cell adhesion, apoptosis and wound healing [4][5][6]. Several reports indicate that TGase2 activation can be associated with apoptosis (although recent evidence would suggest that involvement of TGase2 in apoptosis is indirect [7,8]) or with anti-apoptotic effects mediated by Rb [9].…”

Section: Introductionmentioning

confidence: 99%

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Transglutaminase 5 is regulated by guanine–adenine nucleotides

Candi

Paradisi

Terrinoni

et al. 2004

Biochemical Journal

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Transglutaminases (TGases) are Ca 2+ -dependent enzymes capable of catalysing transamidation of glutamine residues to form intermolecular isopeptide bonds. Nine distinct TGases have been described in mammals, and two of them (types 2 and 3) are regulated by GTP/ATP. TGase2 hydrolyses GTP and is therefore a bifunctional enzyme. In the present study, we report that TGase5 is also regulated by nucleotides. We have identified the putative TGase5 GTP-binding pocket by comparative amino acid sequence alignment and homology-derived three-dimensional modelling. GTP and ATP inhibit TGase5 cross-linking activity in vitro, and Ca 2+ is capable of completely reversing this inhibition. In addition, TGase5 mRNA is not restricted to epidermal tissue, but is also present in different adult and foetal tissues, suggesting a role for TGase5 outside the epidermis. These results reveal the reciprocal actions of Ca 2+ and nucleotides with respect to TGase5 activity. Taken together, these results indicate that TGases are a complex family of enzymes regulated by calcium, with at least three of them, namely TGase2, TGase3 and TGase5, also being regulated by ATP and GTP.

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Section: Resultssupporting

confidence: 57%

Section: Introductionmentioning

confidence: 99%

Transglutaminase 5 is regulated by guanine–adenine nucleotides

Candi

Paradisi

Terrinoni

et al. 2004

Biochemical Journal

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“…Human transglutaminase (TG2) enhances angiogenesis and wound healing in a rat dorsal skin flap chamber 155 . However, there has also been a report of an inhibitory effect of TG2 on angiogenesis (156).…”

Section: Transglutaminase Activity and Angiogenesismentioning

confidence: 99%

Roles of transglutaminases in cardiac and vascular diseases

Sane

Kontos²,

Greenberg³

2007

Front Biosci

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All transglutaminases share the common enzymatic activity of transamidation, or the cross-linking of glutamine and lysine residues to form N epsilon (gamma-glutamyl) lysyl isopeptide bonds. The plasma proenzyme factor XIII is responsible for stabilizing the fibrin clot against physical and fibrinolytic disruption. Another member of the transglutaminase family, tissue transglutaminase or TG2 is abundantly expressed in cardiomyocytes, vascular cells and macrophages. The transglutaminases have a variety of functions independent of their transamidating activity. For example, TG2 binds and hydrolyzes GTP, thereby fostering signal transduction by several G protein coupled receptors. Accumulating evidence points to novel roles for factor XIII and TG2 in cardiovascular biology including: (a) modulating platelet activity, (b) regulating glucose control, (c) contributing to the development of hypertension, (d) influencing the progression of atherosclerosis, (e) regulating vascular permeability and angiogenesis (f) and contributing to myocardial signaling, contractile activity and ischemia/reperfusion injury. In this review, we summarize the cardiovascular biology of two members of the family of transglutaminases, Factor XIII and TG2.

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“…We are currently investigating the significance of this finding in relationship to mechanisms of angiogenesis. Tissue transglutaminase is thought to mediate angiogenesis by crosslinking the extracellular matrix (Haroon et al, 1999).…”

Section: Angiocidin Binds Ubiquitinated Proteins In Vivo and In Vitromentioning

confidence: 99%

Endothelial apoptotic activity of angiocidin is dependent on its polyubiquitin binding activity

et al. 2005

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We recently cloned the full-length cDNA of a tumour-associated protein. The recombinant protein expressed in bacteria and referred to as angiocidin has potent antitumour activity in vivo and in vitro. Angiocidin inhibits tumour growth and angiogenesis by inducing apoptosis in endothelial cells. Based on the sequence similarity of angiocidin to S5a, one of the major polyubiquitin recognition proteins in eukaryotic cells, we postulated that the antiendothelial activity of angiocidin could be due in part to its polyubiquitin binding activity. In support of this hypothesis, we show that angiocidin binds polyubiquitin in vivo with high affinity and colocalises with ubiquitinated proteins on the surface of endothelial cells. Binding is blocked with an antiubiquitin antibody. Angiocidin treatment of endothelial cells transfected with a proteasome fluorescent reporter protein showed a dose-dependent inhibition of proteasome activity and accumulation of polyubiquitinated proteins. Full-length angiocidin bound polyubiquitin while three angiocidin recombinant proteins whose putative polyubiquitin binding sites were mutated either failed to bind polyubiquitin or had significantly diminished binding activity. The in vitro apoptotic activity of these mutants correlated with their polyubiquitin binding activity. These data strongly argue that the apoptotic activity of angiocidin is dependent on its polyubiquitin binding activity.

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Tissue transglutaminase is expressed, active, and directly involved in rat dermal wound healing and angiogenesis

Cited by 232 publications

References 38 publications

Transglutaminase 5 is regulated by guanine–adenine nucleotides

Transglutaminase 5 is regulated by guanine–adenine nucleotides

Roles of transglutaminases in cardiac and vascular diseases

Endothelial apoptotic activity of angiocidin is dependent on its polyubiquitin binding activity

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