Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.6.99.3 (diaphorase)
 5,903 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effects of an oral administration of carbon tetrachloride on various liver microsomal and supernatant components were studied 1hr. and 2hr. after dosing. The modifications of such early changes resulting from a concomitant administration of promethazine together with the carbon tetrachloride were also investigated. The microsomal components studied were: cytochromes P-450 and b(5); inorganic pyrophosphatase; NADH- and NADPH-cytochrome c reductases; NADH- and NADPH-neotetrazolium reductases; a lipid-peroxidation system associated with the oxidation of NADPH and stimulated by ADP and Fe(2+). NAD- and NADP- DT-diaphorases were measured in the supernatant solution remaining after isolation of liver microsomes, and the distribution of RNA phosphorus between the microsomes and supernatant solution was also determined. Carbon tetrachloride produced a rapid fall in inorganic pyrophosphatase activity, a rather slower decrease in cytochrome P-450 content of the microsomes and small increases in the activities of NADH-cytochrome c reductase and neotetrazolium reductases. The activities of NADPH-cytochrome c reductase, the NADPH-ADP/Fe(2+)-linked lipid-peroxidation system, DT-diaphorases and the content of cytochrome b(5) in the microsomes were unchanged. There was also a loss of RNA phosphorus from the microsomes into the supernatant solution. The RNA phosphorus redistribution, the decrease in inorganic pyrophosphatase and the increases in neotetrazolium reductase activities were at least partially prevented by a concomitant dosing with promethazine. However, the decrease in cytochrome P-450 was not affected by promethazine treatment. These early changes are discussed in terms of the liver necrosis produced by carbon tetrachloride and which is greatly retarded in its onset by the administration of promethazine.
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PMID:The effects of carbon tetrachloride on rat liver microsomes during the first hour of poisoning in vivo, and the modifying actions of promethazine. 576 54

A proteomic study of Cunninghamella echinulata recovery during exposure to tributyltin was conducted with 2-D SDS-PAGE protein separation and profiling, MALDI-TOF/TOF protein identification, and PCA analysis. The presence of TBT resulted in an upregulation of enzymes related to energy production via cellular respiration. The unique overexpression of NADH dehydrogenase and mitochondrial malate dehydrogenase, together with an increased level of cytochrome c oxidase, ATP synthase subunits, and inorganic pyrophosphatase, indicates a strong energy deficit in the cells, leading to an increase in the ATP production. The overexpression of Prohibitin-1, a multifunctional protein associated with the proper functioning of mitochondria, was observed as well. The data also revealed oxidative stress condition. Among reactive oxygen species (ROS)-scavenging enzymes, only superoxide dismutase (SOD) showed active response against oxidative stress induced by the xenobiotic. The induction of a series of ROS-scavenging enzymes was supported by a microscopic analysis revealing a considerably large concentration of ROS in the hyphae. The overexpression of cytoskeleton-related proteins in the TBT presence was also noticed. The obtained results allow explaining the recovery strategy of the fungus in response to the energy depletion caused by TBT.
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PMID:A proteomic study of Cunninghamella echinulata recovery during exposure to tributyltin. 3162 17