Exercise training prevents ecto-nucleotidases alterations in platelets of hypertensive rats

Abstract

In this study, we investigated the effect of 6 weeks of swimming training on the ecto-nucleotidase activities and platelet aggregation from rats that developed hypertension in response to oral administration of L-NAME. The rats were divided into four groups: control (n = 10), exercise (n = 10), L-NAME (n = 10), and exercise L-NAME (n = 10). The animals were trained five times per week in an adapted swimming system for 60 min with a gradual increase of the workload up to 5 % of animal's body weight. The results showed an increase in ATP, ADP, AMP, and adenosine hydrolysis, indicating an augment in NTPDase (from 35.3 ± 8.1 to 53.0 ± 15.1 nmol Pi/min/mg protein for ATP; and from 21.7 ± 7.0 to 46.4 ± 15.6 nmol Pi/min/mg protein for ADP as substrate), ecto-5'-nucleotidase (from 8.0 ± 5.7 to 28.1 ± 6.9 nmol Pi/min/mg protein), and ADA (from 0.8 ± 0.5 to 3.9 ± 0.8 U/L) activities in platelets from L-NAME-treated rats when compared to other groups (p < 0.05). A significant augment on platelet aggregation in L-NAME group was also observed. Exercise training was efficient in preventing these alterations in the exercise L-NAME group, besides showing a significant hypotensive effect. In conclusion, our results clearly indicated a protector action of moderate intensity exercise on nucleotides and nucleoside hydrolysis and on platelet aggregation, which highlights the exercise training effect to avoid hypertension complications related to ecto-nucleotidase activities.

Effect of dietary supplementation of ginger and turmeric rhizomes on ectonucleotidases, adenosine deaminase and acetylcholinesterase activities in synaptosomes from the cerebral cortex of hypertensive rats

“…This result is in agreement with previously described studied by Balbinott et al (2005). Also, many authors have reported the ability of the arginine analog, L-NAME, to induce systemic arterial hypertension (Furstenau et al, 2008(Furstenau et al, , 2010Cardoso et al, 2012Cardoso et al, , 2014, which probably occurs due to the capacity of L-NAME to inhibit the production of nitric oxide, a well known vasodilator molecule, by blocking nitric oxide synthase (NOS) activity (Moncada et al, 1991). However, dietary supplementation with both rhizomes and treatment with a positive control drug (atenolol) caused a significant reduction of SBP in the hypertensive rats (Fig.…”

“…3A and B and 4). Alterations in the activities of this enzyme complex have been verified in various studies in hypertensive patients (Schetinger et al, 2007;Lunkes et al, 2009;Bagattini et al, 2011;Cardoso et al, 2012). Regarding L-NAME-induced hypertension in rats, it has recently been demonstrated that ectonucleotidase activities are altered in these enzyme activities in different tissues (Furstenau et al, 2008(Furstenau et al, , 2010Cardoso et al, 2012).…”

“…The chronic inhibition of NO produces volumedependent elevation of blood pressure and its physiological and pathological characteristics resemble essential hypertension (Lerman et al, 2005;Cardoso et al, 2012Cardoso et al, , 2014. Several studies have administered in vivo an inhibitor of nitric oxide biosynthesis, the N-nitro-L-arginine methyl ester hydrochloride (L-NAME), which is an L-arginine analog, to induce hypertension in rats (Furstenau et al, 2008(Furstenau et al, , 2010Cardoso et al, 2012Cardoso et al, , 2014. The brain especially the cerebral cortex is a major target of the deleterious effects of hypertension and is responsible for a large portion of the related mortality and morbidity (Dahlof, 2007;Toth et al, 2015).…”

Synthesis of some tetrahydropyrimidine-5-carboxylates, determination of their metal chelating effects and inhibition profiles against acetylcholinesterase, butyrylcholinesterase and carbonic anhydrase

“…Synthesis of ethyl 1-(2-hydroxybutyl)-4-methyl-6-phenyl-2-thioxo-1,2,3,6-tetrahydropyrimidine-5-carboxylate (3) Ethyl 6-methyl-2-thioxo-4-(p-tolyl)-1,2,3,4-tetrahydropyrimidine-5-carboxylate (1.52 g, 0.02 mol) is dissolved in 2:1 ratio of acetylacetone and ethyl alcohol (12 mL:5 mL) and 1,2-epoxobutane (2.03 mL, 0.02 mol) is added on it drop by drop. After being dissolved in the stirrer for 30 min, 0.02 g AlCl 3 catalyst is added on it and mixed by heating at [60][61][62][63][64][65] C. …”

“…Acetylcholinesterase (AChE, E.C.3.1.1.7) enzyme, a serine hydrolase, is responsible for the degradation of ACh in the synaptic cleft of cholinergic synapses and neuromuscular junctions into inactive metabolites such as choline and acetate 9,60,61 . It has essential role in regulating many vital functions such as memory, learning, cortical organization of movement and cerebral blood flow control which demonstrates the high degree of importance of ACh as a neurotransmitter target for the study of cerebrovascular diseases associated with hypertension 60,[62][63][64] . On the other hand, butyrylcholinesterase (BChE, E.C.…”