Zobrazeno 1 - 10
of 41
pro vyhledávání: '"Nikos E. Tsopanoglou"'
Autor:
Dimitrios Dougenis, Nikos E. Tsopanoglou, Panagiotis Alexopoulos, Efstratios Koletsis, George Vogiatzis, Konstantina Panoutsopoulou
Publikováno v:
Journal of Cardiovascular Pharmacology. 70:34-41
Exenatide and cyclosporine A have been shown to moderately protect against myocardial reperfusion injury leading to reduction of infarct size in patients. Our objective was to investigate whether the combined treatment with exenatide (glucagon-like p
Autor:
M. Teresa García-López, Pilar Ventosa-Andrés, Nikos E. Tsopanoglou, Rosario Herranz, Ioannis Pappos, Ángel M. Valdivielso
Publikováno v:
European Journal of Medicinal Chemistry. 58:98-111
By applying a diversity oriented synthesis strategy for the search of new antagonists of the thrombin receptor PAR1, a series of peptide-based ureas and thioureas, including analogues of the PAR1 reference antagonist RWJ-58259, has been designed and
Autor:
Helen A. Papadaki, Dimitrios Siamblis, Konstantinos Katsanos, Evangelos Liatsikos, Dimitrios Karnabatidis, Athanasios Diamantopoulos, George Loudos, Iason Kyriazis, Nikos E. Tsopanoglou, Katerina Geronatsiou, George C. Kagadis
Publikováno v:
American Journal of Nephrology. 36:278-286
Background/Aims: Parstatin is a 41-mer peptide formed by proteolytic cleavage on activation of the protease-activated receptor 1. Parstatin was recently found to be cardioprotective against myocardial ischemia/reperfusion (IR) injury. In the present
Publikováno v:
European Cytokine Network. 20:171-179
A plethora of endogenous modulators of angiogenesis have been identified and their roles in the molecular and cellular events that mediate and regulate angiogenesis have been proposed. In this review, we summarize the recent findings on the role of t
Autor:
Jidong Su, John E. Baker, Michael E. Widlansky, Anna Hsu, Jingli Wang, Nikos E. Tsopanoglou, Jennifer L. Strande, Kasi V. Routhu
Publikováno v:
Cardiovascular Research. 83:325-334
Aims Thrombin activates protease-activated receptor 1 by proteolytic cleavage of the N-terminus. Although much research has focused on the activated receptor, little is known about the 41-amino acid N-terminal peptide (parstatin). We hypothesized tha
Autor:
Dimitrios Karnabatidis, Athanasios Diamantopoulos, Nikos E. Tsopanoglou, George Nikiforidis, Panagiota Ravazoula, Dimitrios Siablis, Konstantinos Katsanos, George C. Kagadis
Publikováno v:
Journal of Vascular Surgery. 49:1000-1012
BackgroundCompared with angiogenesis, arteriogenesis is a distinct process based on the remodeling and maturation of pre-existing arterioles into large conductance arteries. Therapeutic angiogenesis has been proposed as a potential treatment for isch
Autor:
Despina Gourni, Nikos E. Tsopanoglou, Panagiota Zania, Christodoulos S. Flordellis, Alfred C. Aplin, Michael E. Maragoudakis, Roberto F. Nicosia
Publikováno v:
Journal of Pharmacology and Experimental Therapeutics. 328:378-389
The proteolytic activation by thrombin of the proteinase-activated receptor 1 unveils the tethered peptide ligand and cleaves a 41-amino acid peptide. In this report, we show that this peptide, which we have designated as "parstatin," is a potent inh
Autor:
Panagiota Zania, Christodoulos S. Flordellis, M. E. Papaconstantinou, Michael E. Maragoudakis, Nikos E. Tsopanoglou
Publikováno v:
American Journal of Physiology-Cell Physiology. 294:C1215-C1226
Thrombin has been reported to play a pivotal role in the initiation of angiogenesis by indirectly regulating and organizing a network of angiogenic molecules. In addition, it has been proposed that thrombin can directly activate endothelial cell prol
Autor:
Christodoulos S. Flordellis, P. Tone, N. Zacharakis, Nikos E. Tsopanoglou, Michael E. Maragoudakis
Publikováno v:
Journal of Cellular and Molecular Medicine
Angiogenesis is the process of generating new blood vessels from preexisting vessels and is considered essential in many pathological conditions. The purpose of the present study was to evaluate the effect of methylene blue in chick chorioallantoic m
Autor:
Agustin O. Pineda, Christodoulos S. Flordellis, F. Scott Mathews, Michael E. Maragoudakis, Nikos E. Tsopanoglou, M. E. Papaconstantinou, Christopher J. Carrell, Kevin M. Bobofchak, Enrico Di Cera
Publikováno v:
Journal of Biological Chemistry. 280:29393-29396
Previous studies have suggested that thrombin interacts with integrins in endothelial cells through its RGD (Arg-187, Gly-188, Asp-189) sequence. All existing crystal structures of thrombin show that most of this sequence is buried under the 220-loop