Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.3.5.1 (succinate dehydrogenase)
 8,177 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Significant increase in the activity of liver succinate dehydrogenase (SDH) was observed in male Wistar rats, fed Aroclor 1260 (PCB; polychlorinated biphenyl) at 50 and 100 ppm level for 120 days. Lactate dehydrogenase (LDH) activity increased in 50 ppm PCB fed animals and decreased in 100 ppm PCB fed rats. On the other hand, enzymes like alanine and aspartate aminotransferase, alkaline and acid phosphatase showed remarkable decrease in activity in PCB fed animals. Slab gel electrophoresis of LDH isozymes showed remarkable increase in LDH2 and LDH3 and to some extent increase in LDH1 isozymes of livers of 50 ppm PCB fed animals but not in 100 ppm PCB fed groups as compared to controls. In both the PCB fed groups, liver showed centrilobular hypertrophy, hepatocellular damage, hyperplasia, karyolysis and karyorrhexis.
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PMID:Effect of feeding polychlorinated biphenyl (Aroclor 1260) on hepatic enzymes of rats. 216 95

Acephate, an organophosphorus insecticide (60 mg/day/rat) disturbed the carbohydrate metabolism in albino rats (wt. between 100-150 gms). Changes in the enzyme activities in the liver were estimated in the rats after oral administration of Acephate. The specific activities of succinic dehydrogenase was decreased in experimental rats than control. A gradual decrease in blood and liver glutathione was also observed. Increase in total lactate dehydrogenase was also noted. It has been observed that in the liver homogenate of treated rats, the isoenzymes LDH4+5 were increased, LDH1+2 were decreased while LDH3 remain unchanged with respect to control value.
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PMID:Changes in the activity of some hepatic enzymes during organophosphorus insecticide-acephate (orthene) treatment in albino rats. 715 41

Cadmium is known to be an environmental and industrial pollutant. Exposure to cadmium is known to affect various tissues. The purpose of this study is to determine the toxic effects of cadmium on lactate dehydrogenase (LDH) isoenzymes. Administration of cadmium chloride (3 mg kg(-1)) resulted in the reduction of LDH4 fraction of liver tissue indicating the inhibitory effect of cadmium. The LDH1 LDH3 and LDH5 fractions showed decreasing trend initially but there was a significant increase later In contrast the LDH2 fraction showed increasing trend after 24 hr from the last dosage it was elevated after 30 days. The total activity of LDH in liver showed gradual reduction in both groups. The activity of succinate dehydrogenase (SDH) the mitochondrial enzyme has been observed to be inhibited by cadmium with the possibility of interfering with energy transport mechanism. Na(+)- K(+)-ATPase activity of liver also showed similar decrease after cadmium administration which may lead to general deficit in cell membrane transport. As cadmium shows drastic decrease in all the enzymes studied, the LDH2 fraction which sharply rises from the control may be used as a marker enzyme to asses the liver injury.
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PMID:Effect of cadmium on lactate dehyrogenase isoenzyme, succinate dehydrogenase and Na(+)-K(+)-ATPase in liver tissue of rat. 2014 25

l-lactate formation occurs via the reduction of pyruvate catalyzed by lactate dehydrogenase. l-lactate removal takes place via its oxidation into pyruvate, which may be oxidized or converted into glucose. Pyruvate oxidation involves the cooperative effort of pyruvate dehydrogenase, the tricarboxylic acid cycle, and the mitochondrial respiratory chain. Enzymes of the gluconeogenesis pathway sequentially convert pyruvate into glucose. In addition, pyruvate may undergo reversible transamination to alanine by alanine aminotransferase. Enzymes involved in l-lactate metabolism are crucial to diabetes pathophysiology and therapy. Elevated plasma alanine aminotransferase concentration has been associated with insulin resistance. Polymorphisms in the G6PC2 gene have been associated with fasting glucose concentration and insulin secretion. In diabetes patients, pyruvate dehydrogenase is down-regulated and the activity of pyruvate carboxylase is diminished in the pancreatic islets. Inhibitors of fructose 1,6-bisphosphatase are being investigated as potential therapy for type 2 diabetes. In addition, enzymes implicated in l-lactate metabolism have revealed to be important in cancer cell homeostasis. Many human tumors have higher LDH5 levels than normal tissues. The LDHC gene is expressed in a broad range of tumors. The activation of PDH is a potential mediator in the body response that protects against cancer and PDH activation has been observed to reduce glioblastoma growth. The expression of PDK1 may serve as a biomarker of poor prognosis in gastric cancer. Mitochondrial DNA mutations have been detected in a number of human cancers. Genes encoding succinate dehydrogenase have tumor suppressor functions and consequently mutations in these genes may cause a variety of tumors.
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PMID:Enzymes involved in l-lactate metabolism in humans. 2402 12