Comparative effects of experimental lead poisoning on enzymatic activities of kidney and liver in rat

Iannaccone, A; Boscolo, P; Bombardieri, G.

doi:10.1016/0024-3205(76)90049-7

Cited by 19 publications

(7 citation statements)

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“…Our results are in agreement with the biochemical findings of Nehru and Kaushal,6) where SDH was significantly inhibited following lead poisoning but in dispute with the findings of some biochemical studies where lead exposure had no influence on succinate dehydrogenase activity in the liver and kidney homogenates of rats fed for 6 months with 1 per cent lead acetate diet. 16,33,34) Similar results were obtained in the heart tissue. 35) The reduction in the activity of malate dehydrogenase due to lead intoxication seen in the present histochemical results is in agreement with the results of biochemical investigation on the activity of this enzyme in the kidney homongenate, and muscle fibres of intoxicated rats.…”

Section: Discussionsupporting

confidence: 82%

“…Lactate dehydrogenase playes an important role in the intermediary metabolism as a link between amino acid metabolism and the citric acid cycle where it converts lactate into pyruvate. The increase in the activity of this enzyme due to lead intoxication in the present study is in agreement with the biochemical findings of Secchi 37) but in contradiction with the findings of Iannaccone et al, 33) where the activity of lactate dehydrogenase was unmodified in the kidney homogenate of rats fed for 6 months with 0.1 per cent lead acetate diet and of Yagminas et al,38) where the activity of this enzyme was lowered in the kidney of lead acetate treated rats. The varieties in the activity of renal dehydrogenases due to lead intoxication obtained by different investigators could be due to the variations in the experimental conditions such as the level of exposure, duration, route of administration and animal species used in the experiment.…”

Section: Discussionsupporting

confidence: 81%

“…35) The reduction in the activity of malate dehydrogenase due to lead intoxication seen in the present histochemical results is in agreement with the results of biochemical investigation on the activity of this enzyme in the kidney homongenate, and muscle fibres of intoxicated rats. 33,36) Malate dehydrogenase converts malate to oxaloacetate, the final reaction in the Krebs cycle.…”

Section: Discussionmentioning

confidence: 99%

“…33,37) NAD-dependent isocitrate dehydrogenase is structuraly bounded to the mitochondria and participates in the Krebs cycle. It has been reported that the activity of this enzyme was increased in the muscle fibers of lead intoxicated rats.…”

Section: Discussionmentioning

confidence: 99%

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Histochemical Demonstration of the Alterations in the Renal Dehydrogenases Activities Induced by Lead in Wistar Albino Rats (Rattus norvegicus).

Jarrar

Mahmoud

2002

JOURNAL OF HEALTH SCIENCE

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A total of 112 male albino rats (Rattus norvegicus) were divided into seven groups and exposed to lead acetate trihydrate (0, 0.125, 0.25, 0.5, 1.0, 2.0 and 4 per cent for 1 to 8 months) in drinking water to investigate possible histochemical changes of nine renal dehydrogenases due to lead intoxication. A marked increase in the activity of lactate-, glucose-6-phosphate-, α-glycerophosphate-, reduced nicotinamide adenine dinucleotide (NAD)-and reduced nicotinamide adenine dinucleotide phosphate (NADP) dehydrogenase was observed while significant reduction was recorded in the activity of succinate-, malate-, isocitrate-and glutamate dehydrogenase. Changes in the activity of renal dehydrogenases were seen mainly in the pars recta and to a lesser extent in the pars convoluta and the ascending thick segment of the loop of Henle while the other medullary portions of the renal tubule were less affected. These histochemical findings led us to conclude that such changes in the renal dehydrogenases activities were due to chronic lead exposure and could be an adaptation to the metabolic, structural and functional alterations in the organelles of the renal cells especially the mitochondria.

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Section: Discussionsupporting

confidence: 82%

Section: Discussionsupporting

confidence: 81%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Histochemical Demonstration of the Alterations in the Renal Dehydrogenases Activities Induced by Lead in Wistar Albino Rats (Rattus norvegicus).

Jarrar

Mahmoud

2002

JOURNAL OF HEALTH SCIENCE

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“…Heavy metals are capable of combining with a variety of organic molecules and interacting with sulfhydryl, carboxyl, amino and phosphoryl groups (23). Lead may cause direct inhibition of enzymatic activity by such interactions (16,32), although decreased synthesis of enzymes has also been suggested (25). An attempt at further clarification of the effects of lead on enzymatic activity is noted in recent studies of hepatic biotransformation of drugs, hormones, and other chemicals mediated through the mixed function oxidase system in the liver.…”

Section: Discussionmentioning

confidence: 99%

Effect of Lead Exposure on the Activity of Some Hepatic Enzymes in the Rat

et al. 1979

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SummarySeven-day-old rats were fed 1% lead acetate tetrahydrate solution for 2,4, or 7 days. Adult rats were fed the same lead solution for 6-8 wk. In the newborn rats, hepatic UDP-bilirubin glucuronyl transferase (GT) and gamma glutamyl transpeptidase (GGTP) activities were markedly increased. GT activity was increased after 4 days as compared to the controls (6.3 f 0.3 vs. 4.3 f 0.3, P < 0.001), and was maximal after 7 days of treatment (7.5 f 0.4 vs. 4.6 f 0.4, P < 0.001). GGTP activity was already maximally increased after 2 days of lead treatment (1.4 rt: 0.2 vs. 0.4 f 0.1, P < 0.001). Hepatic GT and GGTP activities were similarly increased in adult rats (7.9 f 0.3 vs. 5.1 f 0.1, P < 0.001, and 0.7 f 0.1 vs. 0.4 f 0.1, P < 0.005, respectively). In vitro studies adding lead citrate to liver homogenates did not produce any direct effect on GT and GGTP activities. SpeculationThe increase in hepatic GT and GGTP activities in lead treated animals appears to be a response to lead induced cellular damage or may result from interference with regulatory mechanisms responsible for production of these enzymes and not related to hepatic enzyme induction. The hepatic metabolism of drugs ingested by children with an increased lead burden may, therefore, be significantly altered.While lead remains one of the more important industrial and environmental toxins, and a series of recent factors have reduced the incidence of lead exposure and toxicity (1 I), its affect on the liver has received relatively little attention when compared to its impact on hematopoietic and neuromuscular systems. Lead administration to animals causes changes in the liver (12, 14) visible by light and electron microscopy. Additionally, it increases the concentrations of enzymes in serum released from damaged hepatocytes, and produces alterations in hepatocyte function as manifested by decreased bilirubin clearance and enhanced bromosulfophthalein retention (8,31). Recently, inhibition of the microsoma1 hepatic cytochrome P-450 dependent mixed function oxidase system has been reported (3, 26) in lead intoxicated animals and humans, suggesting the possibility of an alteration in hepatic drug metabolism. In order to explore further the effects of lead on hepatic enzyme activity, microsomal, noncytochrome P-450 dependent systems were studied in rats previously shown to be poisoned by lead (17). MATERIALS A N D METHODSanimals and littermate controls at 2,4, and 7 days were 12, 10; 8, 6; and 20, 18, respectively. All animals were killed by decapitation 24 hr after the last dose. The livers were removed, weighed, and the activity of UDP-bilirubin GT (EC 2.4.1.17), GGTP (EC 2.3.2.2), and hepatic protein content were determined. CHRONIC ADULT EXPOSUREFifteen adult male Sprague Dawley rats weighing 200-250 g were given a 1% lead acetate tetrahydrate solution in their daily drinking water for 6-8 wk. The lead solution was offered ad libitum. At the end of the treatment period, the rats were killed by decapitation, the livers were removed, weighed, GT and GGTP ...

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Lead and the terminal mitochondrial enzymes of haem biosynthesis

Rossi¹,

Taketani²,

Garcia-Webb³

1993

Biomedical Chromatography

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Lead exposure causes increases in urinary coproporphyrin excretion and the accumulation of zinc protoporphyrin in red cells. In the conventional view of the effect of lead on haem biosynthesis, the accumulation of these metabolites results from lead inhibition of two of the mitochondrial enzymes of haem biosynthesis, coproporphyrinogen oxidase (EC 1.3.3.3) and ferrochelatase (EC 4.99.1.1). This review critically assesses the evidence for the inhibition of these enzymes. We consider this evidence to be inconclusive and alternative explanations for the increased concentrations of coproporphyrin and zinc protoporphyrin are proposed.

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Comparative effects of experimental lead poisoning on enzymatic activities of kidney and liver in rat

Cited by 19 publications

References 13 publications

Histochemical Demonstration of the Alterations in the Renal Dehydrogenases Activities Induced by Lead in Wistar Albino Rats (Rattus norvegicus).

Histochemical Demonstration of the Alterations in the Renal Dehydrogenases Activities Induced by Lead in Wistar Albino Rats (Rattus norvegicus).

Effect of Lead Exposure on the Activity of Some Hepatic Enzymes in the Rat

Lead and the terminal mitochondrial enzymes of haem biosynthesis

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