BACKGROUND/AIMS: The transglutaminases (TG2 and factor XIIIa) may contribute to the stability of arteries by cross-linking a variety of substrates, including extracellular matrix proteins and protease inhibitors. The preferred substrates have never been determined, however. METHODS: We used an amine donor, 5-biotinamidopentylamine, that is covalently linked to acceptor glutamine residues, to determine transglutaminase substrates in carotid endarterectomy tissue. RESULTS: The incorporation of 5-biotinamidopentylamine was calcium dependent, resulting in the labeling of several proteins that were detected by streptavidin-peroxidase and purified over a monomeric avidin affinity column. A major band of 42 kDa that was eluted from the column was sequenced along with 2 additional bands (80 and 65 kDa), revealing an internal fragment of vimentin, transferrin and albumin, respectively. Vimentin dimers were detected in 5 out of 5 carotid plaque homogenates. CONCLUSIONS: Vimentin is a major arterial substrate for transglutaminases. It has previously been shown that TG2 activity and vimentin contribute to vasomotor activity of arteries. Furthermore, transglutaminases (both TG2 and factor XIIIa), as well as vimentin, regulate structural alterations (inward remodeling) that occur in response to low flow states. Transglutaminase-mediated vimentin dimerization produces a novel unifying pathway by which vasodilatory and remodeling responses may be regulated. Copyright 2007 S. Karger AG, Basel.
BACKGROUND/AIMS: The transglutaminases (TG2 and factor XIIIa) may contribute to the stability of arteries by cross-linking a variety of substrates, including extracellular matrix proteins and protease inhibitors. The preferred substrates have never been determined, however. METHODS: We used an aminedonor, 5-biotinamidopentylamine, that is covalently linked to acceptor glutamine residues, to determine transglutaminase substrates in carotid endarterectomy tissue. RESULTS: The incorporation of 5-biotinamidopentylamine was calcium dependent, resulting in the labeling of several proteins that were detected by streptavidin-peroxidase and purified over a monomeric avidin affinity column. A major band of 42 kDa that was eluted from the column was sequenced along with 2 additional bands (80 and 65 kDa), revealing an internal fragment of vimentin, transferrin and albumin, respectively. Vimentin dimers were detected in 5 out of 5 carotid plaque homogenates. CONCLUSIONS:Vimentin is a major arterial substrate for transglutaminases. It has previously been shown that TG2 activity and vimentin contribute to vasomotor activity of arteries. Furthermore, transglutaminases (both TG2 and factor XIIIa), as well as vimentin, regulate structural alterations (inward remodeling) that occur in response to low flow states. Transglutaminase-mediated vimentin dimerization produces a novel unifying pathway by which vasodilatory and remodeling responses may be regulated. Copyright 2007 S. Karger AG, Basel.
Authors: D Henrion; F Terzi; K Matrougui; M Duriez; C M Boulanger; E Colucci-Guyon; C Babinet; P Briand; G Friedlander; P Poitevin; B I Lévy Journal: J Clin Invest Date: 1997-12-01 Impact factor: 14.808
Authors: Erik N T P Bakker; Adrian Pistea; Jos A E Spaan; Titia Rolf; Carlie J de Vries; Nico van Rooijen; Eleonara Candi; Ed VanBavel Journal: Circ Res Date: 2006-06-01 Impact factor: 17.367
Authors: Erik N T P Bakker; Carsten L Buus; Jos A E Spaan; Jop Perree; Anuradha Ganga; Titia M Rolf; Oana Sorop; Linda H Bramsen; Michael J Mulvany; Ed Vanbavel Journal: Circ Res Date: 2004-11-18 Impact factor: 17.367
Authors: Clare R Foster; Joanne L Robson; William J Simon; Jeremy Twigg; Derek Cruikshank; Robert G Wilson; Chris J Hutchison Journal: Nucleus Date: 2011-09-01 Impact factor: 4.197
Authors: Jocelyn A Silvester; Elizabeth A Faucher; Caitlin E McCarty; Adie Kalansky; Zackary J Hintze; Paul D Mitchell; Jeffrey D Goldsmith; Dascha C Weir; Alan M Leichtner Journal: J Pediatr Gastroenterol Nutr Date: 2019-02 Impact factor: 2.839