Transglutaminase-mediated transamidation of serotonin, dopamine and noradrenaline to fibronectin: evidence for a general mechanism of monoaminylation

The activity of some small GTPases is regulated by covalent transamidation of serotonin (5-hydropxytryptamien) to glutamine residues of the enzymes. This process is mediated by transglutaminase (TGase) and is termed “serotonylation”. In addition, serotonylation of neural proteins and proteins of the...

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Hauptverfasser: Hummerich, René (VerfasserIn) , Thumfart, Jörg Oliver (VerfasserIn) , Findeisen, Peter (VerfasserIn) , Bartsch, Dusan (VerfasserIn) , Schloss, Patrick (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 31 July 2012
In: FEBS letters
Year: 2012, Jahrgang: 586, Heft: 19, Pages: 3421-3428
ISSN:1873-3468
DOI:10.1016/j.febslet.2012.07.062
Online-Zugang:Verlag, Volltext: http://dx.doi.org/10.1016/j.febslet.2012.07.062
Verlag, Volltext: http://febs.onlinelibrary.wiley.com/doi/abs/10.1016/j.febslet.2012.07.062
Volltext
Verfasserangaben:René Hummerich, Jörg-Oliver Thumfart, Peter Findeisen, Dusan Bartsch, Patrick Schloss
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Zusammenfassung:The activity of some small GTPases is regulated by covalent transamidation of serotonin (5-hydropxytryptamien) to glutamine residues of the enzymes. This process is mediated by transglutaminase (TGase) and is termed “serotonylation”. In addition, serotonylation of neural proteins and proteins of the extracellular matrix such as fibronectin has been demonstrated. Here we show that the catecholamines dopamine (DA) and noradrenaline (NA) inhibit serotonylation of fibronectin and that DA and NA themselves can be selectively transamidated into fibronectin by TGase. All three biogenic monoamines also block TGase-mediated transamidation of another monoamine, monodansylacadaverine, into fibronectin, suggesting a general mechanism of TGase-mediated “monoaminylation”.
Beschreibung:Gesehen am 30.07.2018
Available online 31 July 2012
First published: 30 July 2012
Beschreibung:Online Resource
ISSN:1873-3468
DOI:10.1016/j.febslet.2012.07.062