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

Abstract

Ectonucleotidase ADA Acetylcholinesterase a b s t r a c t Ginger and turmeric rhizomes are used in folk medicine for the treatment of several cerebrovascular diseases with limited scientific basis for their action. Hence, in this study, we investigate the effects of two Zingiberaceae varieties (ginger and turmeric) on ectonucleotidases (NTPDase and 5 0 -nucleotidase), adenosine deaminase (ADA) and acetylcholinesterase (AChE) activities in synaptosomes of cerebral cortex from L-NAME induced hypertensive rats. The animals were divided into seven groups (n = 10): normotensive control rats; hypertensive rats; hypertensive rats treated with atenolol; normotensive and hypertensive rats treated with 4% supplementation of turmeric and ginger rhizomes, respectively. After 14 days of pre-treatment with both rhizomes the animals were induced with hypertension by oral administration of L-NAME. The results revealed an increase of ATP and AMP hydrolysis as well as ADA and AChE activities of cerebral cortex synaptosomes in induced rats when compared with the control. The supplementation of both rhizomes prevented these alterations by decreasing ATP and AMP hydrolysis and ADA and AChE activities in cerebral cortex. In conclusion, this study demonstrated that both rhizomes Please cite this article in press as: Akinyemi, A.J., et al., 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.

Functional Oil from Black Seed Differentially Inhibits Aldose-reductase and Ectonucleotidase Activities by Up-regulating Cellular Energy in Haloperidol-induced Hepatic Toxicity in Rat Liver

“…Additionally, the current investigation shows that differential pre, co and EO treatments upregulated the activity of LDH-marker of ATP production in liver when compared with HAL induced liver toxicity group. The hepatic high activity of LDH can be a consequence of the luteolin and quercetin action from the oil in the cell, preventing ATP hydrolysis or blocking the breakdown of the liver tissue as well as depleting eco-5 1 -nucleotidase activity 32,33 . This finding supports the previous discovery that patients with hepatic dysfunctions displayed low level of ATP molecules 2 .…”

Stem Bark Extract from Alstonia boonei attenuates Cholesterol, Triglyceride and Oxidative Damage via Low Immunohistochemical Expression in Small Intestinal Tract of Male Rats

“…Absolutely, pre-treatment with SBEAB is most efficacious to safeguard intestinal cells in diabetic rat followed post-treatment and anti-diabetic drug (METAG) respectively. This action may be linked to the synergistic, competitive and mutual functionality of the PUFAs in the stem bark of Alstonia boonei [47].…”

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. …”

“…The design of CAIs as therapeutic agents is related to the large number of isoforms in humans, their rather diffuse localization in many tissues or organs and the lack of isoenzyme selectivity of the presently available inhibitors [55][56][57][58][59] . 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] .…”

“…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.…”