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1.
Braz. j. med. biol. res ; 33(11): 1369-77, Nov. 2000. tab, graf
Article in English | LILACS | ID: lil-273214

ABSTRACT

The effects of transient forebrain ischemia, reperfusion and ischemic preconditioning on rat blood platelet ATP diphosphohydrolase and 5'-nucleotidase activities were evaluated. Adult Wistar rats were submitted to 2 or 10 min of single ischemic episodes, or to 10 min of ischemia 1 day after a 2-min ischemic episode (ischemic preconditioning) by the four-vessel occlusion method. Rats submitted to single ischemic insults were reperfused for 60 min and for 1, 2, 5, 10 and 30 days after ischemia; preconditioned rats were reperfused for 60 min 1 and 2 days after the long ischemic episode. Brain ischemia (2 or 10 min) inhibited ATP and ADP hydrolysis by platelet ATP diphosphohydrolase. On the other hand, AMP hydrolysis by 5'-nucleotidase was increased after 2, but not 10, min of ischemia. Ischemic preconditioning followed by 10 min of ischemia caused activation of both enzymes. Variable periods of reperfusion distinctly affected each experimental group. Enzyme activities returned to control levels in the 2-min group. However, the decrease in ATP diphosphohydrolase activity was maintained up to 30 days of reperfusion after 10-min ischemia. 5'-Nucleotidase activity was decreased 60 min and 1 day following 10-min ischemia; interestingly, enzymatic activity was increased after 2 and 5 days of reperfusion, and returned to control levels after 10 days. Ischemic preconditioning cancelled the effects of 10-min ischemia on the enzymatic activities. These results indicate that brain ischemia and ischemic preconditioning induce peripheral effects on ecto-enzymes from rat platelets involved in nucleotide metabolism. Thus, ATP, ADP and AMP degradation and probably the generation of adenosine in the circulation may be altered, leading to regulation of microthrombus formation since ADP aggregates platelets and adenosine is an inhibitor of platelet aggregation


Subject(s)
Animals , Rats , Male , 5'-Nucleotidase/metabolism , Apyrase/metabolism , Blood Platelets/chemistry , Brain Ischemia/enzymology , Analysis of Variance , Ischemic Preconditioning , Rats, Wistar , Time Factors
2.
Braz. j. med. biol. res ; 32(6): 761-6, Jun. 1999. tab
Article in English | LILACS | ID: lil-233709

ABSTRACT

The purpose of the present study was to investigate the in vitro and in vivo effects of aluminum sulfate on delta-aminolevulinic acid dehydratase (ALA-D) activity from the brain, liver and kidney of adult mice (Swiss albine). In vitro experiments showed that the aluminum sulfate concentration needed to inhibit the enzyme activity was 1.0-5.0 mM (N = 3) in brain, 4.0-5.0 mM (N = 3) in liver and 0.0-5.0 mM (N = 3) in kidney. The in vivo experiments were performed on three groups for one month: 1) control animals (N = 8); 2) animals treated with 1 g per cent (34 mM) sodium citrate (N = 8) and 3) animals treated with 1 g per cent (34 mM) sodium citrate plus 3.3 g per cent (49.5 mM) aluminum sulfate (N = 8). Exposure to aluminum sulfate in drinking water inhibited ALA-D activity in kidney (23.3 + ou - 3.7 per cent, mean + ou - SEM, P<0.05 compared to control), but enhanced it in liver (31.2 + ou - 15.0 per cent, mean + ou - SEM, P<0.05). The concentrations of aluminum in the brain, liver and kidney of adult mice were determined by graphite furnace atomic absorption spectrometry. The aluminum concentrations increased significantly in the liver (527 + ou - 3.9 per cent, mean + ou - SEM, P<0.05) and kidney (283 + ou - 1.7 per cent, mean + ou - SEM, P<0.05) but did not change in the brain of aluminum-exposed mice. One of the most important and striking observations was the increase in hepatic aluminum concentration in the mice treated only with 1 g per cent sodium citrate (34 mM) (217 + ou - 1.5 per cent, mean + ou - SEM, P<0.05 compared to control). These results show that aluminum interferes with delta-aminolevulinate dehydratase activity in vitro and in vivo. The accumulation of this element was in the order: liver > kidney > brain. Furthermore, aluminum had only inhibitory properties in vitro, while in vivo it inhibited or stimulated the enzyme depending on the organ studied.


Subject(s)
Animals , Mice , Male , Female , Aluminum/pharmacology , Brain/enzymology , Kidney/enzymology , Liver/enzymology , Porphobilinogen Synthase/metabolism , Sulfates/pharmacology , Brain/drug effects , Citrates , Kidney/drug effects , Liver/drug effects , Porphobilinogen Synthase/antagonists & inhibitors
3.
Braz. j. med. biol. res ; 31(12): 1529-32, Dec. 1998. graf
Article in English | LILACS | ID: lil-224836

ABSTRACT

Adenosine 5',5'''-P1,P4-tetraphosphate (Ap4A) and adenosine 5',5'''-P1,P5-pentaphosphate (Ap5A) are stored in and released from rat brain synaptic terminals. In the present study we investigated the hydrolysis of dinucleotides (Ap4A and Ap5A) in synaptosomes from the cerebral cortex of adult rats. Ap4A and Ap5A, but not Ap3A, were hydrolyzed at pH 7.5 in the presence of 20 mM Tris/HCl, 2.0 mM MgCl2, 10 mM glucose and 225 mM sucrose at 37oC. The disappearance of the substrates measured by FPLC on a mono-Q HR column was both time and protein dependent. Since synaptosome integrity was at least 90 percent at the end of the assay, hydrolysis probably occurred by the action of an ecto-enzyme. Extracellular actions of adenine dinucleotides at central nervous system terminate due to the existence of ecto-nucleotidases which specifically cleave these dinucleotides. These enzymes in association with an ATP diphosphohydrolase and a 5'-nucleotidase are able to promote the complete hydrolysis of dinucleotides to adenosine in the synaptic cleft


Subject(s)
Male , Animals , Rats , Acid Anhydride Hydrolases/analysis , Adenosine Triphosphate/metabolism , Cerebral Cortex/enzymology , Dinucleoside Phosphates/metabolism , Synaptosomes/enzymology , Acid Anhydride Hydrolases/physiology , Adenosine Triphosphate/analysis , Cerebral Cortex/chemistry , Chromatography, High Pressure Liquid , Rats, Wistar , Synaptosomes/chemistry
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