Effects of EGIS-7229 (S 21407), a Novel Class III Antiarrhythmic Drug, on Myocardial Refractoriness to Electrical Stimulation In Vivo and In Vitro

2001 ◽  
Vol 37 (1) ◽  
pp. 78-88 ◽  
Author(s):  
Anikó Kovács ◽  
Ildikó Gyönös ◽  
János Magyar ◽  
Tamás Bányász ◽  
Péter P. Nánási ◽  
...  
Keyword(s):  
Electrical Stimulation ◽  
Antiarrhythmic Drug ◽  
Class Iii ◽  
Class Iii Antiarrhythmic Drug

Myocardial contractility after in Vitro treatment with class III antiarrhythmic drug Nibentan

2006 ◽  
Vol 141 (1) ◽  
pp. 81-83
Author(s):  
I. A. Latfullin ◽  
R. F. Gaifullina ◽  
R. K. Dzhordzhikiya ◽  
R. R. Nigmatullina
Keyword(s):  
Antiarrhythmic Drug ◽  
Myocardial Contractility ◽  
Class Iii ◽  
Class Iii Antiarrhythmic Drug ◽  
In Vitro Treatment

scholarly journals Depolarization and electrical stimulation enhance in vitro and in vivo sensory axon growth after spinal cord injury

2018 ◽  
Vol 300 ◽  
pp. 247-258 ◽  
Author(s):  
Ioana Goganau ◽  
Beatrice Sandner ◽  
Norbert Weidner ◽  
Karim Fouad ◽  
Armin Blesch
Keyword(s):  
Spinal Cord ◽  
Spinal Cord Injury ◽  
Electrical Stimulation ◽  
Axon Growth ◽  
Sensory Axon ◽  
Cord Injury

Sirtuin-dependent reversible lysine acetylation controls the activity of acetyl-Coenzyme A synthetase in Campylobacter jejuni

2021 ◽  
Author(s):  
Victoria L. Jeter ◽  
Jorge C. Escalante-Semerena
Keyword(s):  
Campylobacter Jejuni ◽  
Posttranslational Modifications ◽  
Active Site ◽  
Protein Function ◽  
Metabolic Enzyme ◽  
Lysine Acetylation ◽  
Class Iii ◽  
Acetyl Coa

Posttranslational modifications are mechanisms for rapid control of protein function used by cells from all domains of life. Acetylation of the epsilon amino group ( N ε ) of an active-site lysine of the AMP-forming acetyl-CoA synthetase (Acs) enzyme is the paradigm for the posttranslational control of the activity of metabolic enzymes. In bacteria, the alluded active-site lysine of Acs enzymes can be modified by a number of different GCN5-type N -acetyltransferases (GNATs). Acs activity is lost as a result of acetylation, and restored by deacetylation. Using a heterologous host, we show that Campylobacter jejuni NCTC11168 synthesizes enzymes that control Acs function by reversible lysine acetylation (RLA). This work validates the function of gene products encoded by the cj1537c , cj1715, and cj1050c loci, namely the AMP-forming acetate:CoA ligase ( Cj Acs), a type IV GCN5-type lysine acetyltransferase (GNAT, hereafter Cj LatA), and a NAD + -dependent (class III) sirtuin deacylase ( Cj CobB), respectively. To our knowledge, these are the first in vivo and in vitro data on C. jejuni enzymes that control the activity of Cj Acs. IMPORTANCE This work is important because it provides the experimental evidence needed to support the assignment of function to three key enzymes, two of which control the reversible posttranslational modification of an active-site lysyl residue of the central metabolic enzyme acetyl-CoA synthetase ( Cj Acs). We can now generate Campylobacter jejuni mutant strains defective in these functions, so we can establish the conditions in which this mode of regulation of Cj Acs is triggered in this bacterium. Such knowledge may provide new therapeutic strategies for the control of this pathogen.

scholarly journals Influence of dronedarone (a class III antiarrhythmic drug) on the anticonvulsant potency of four classical antiepileptic drugs in the tonic–clonic seizure model in mice

2018 ◽  
Vol 126 (2) ◽  
pp. 115-122 ◽  
Author(s):  
Katarzyna M. Sawicka ◽  
Agnieszka Wawryniuk ◽  
Jadwiga Daniluk ◽  
Sławomir Karwan ◽  
Magdalena Florek-Łuszczki ◽  
...  
Keyword(s):  
Antiepileptic Drugs ◽  
Antiarrhythmic Drug ◽  
Clonic Seizure ◽  
Tonic Clonic Seizure ◽  
Class Iii ◽  
Class Iii Antiarrhythmic Drug ◽  
Seizure Model
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