Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.6.5.2 (NQO1)
 6,196 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The response of rat gastrocnemius muscle fibers to chronic streptozotocindiabetes was studied. Transverse sections of this muscle from normal and diabetic rats were histochemically assayed for reduced diphosphopyridine nucleotide-diaphorase, myofibrillar adenosine triphosphatase, mitochondrial alpha-glycerophosphate dehydrogenase, beta-hydroxybutyrate dehydrogenase, and alkaline phosphatase activities. Cross-sectional areas of the fiber types were measured, and fiber capillarization and populations estimated. Chemically-induced diabetes appeared to have little effect on the metabolic or morphological properties of slow-twitch fibers. However, a general dedifferentiation occurred in the 2 fast-twitch fiber populations. There was a loss of oxidative potential in the fast-twitch-oxidative-glycolytic fibers, and a significant decrease in size in the fast-twitch-glycolytic fibers. No change in the proportions of slow- and fast-twitch fibers in the muscles of diabetic rats occurred. It is concluded that hypoinsulinism has differential effects on the 3 fiber types in heterogeneous rat skeletal muscle, and that slow-twitch fibers are least affected by the diabetic condition.
 ...
PMID:Histochemical properties of skeletal muscle fibers in streptozotocin-diabetic rats. 12 6

Quantitative histochemical assays of several enzymes (succinic, lactic, beta-hydroxybutyrate, alpha-glycerophosphate, and glucose-6-phosphate dehydrogenases, NAD diaphorase, and phosphorylase) in the myocardium of persons who had died suddenly with postinfarctional cardiosclerosis have failed to reveal any changes specific for this patient group. Direct correlations were established between the enzyme activities assayed, on the one hand, and the extent of myocardial hypertrophy and the signs of chronic heart failure, on the other. The activities of beta-hydroxybutyrate dehydrogenase and glucose-6-phosphate dehydrogenase, which are involved in fatty acid utilization and in the pentose phosphate pathway, were elevated in cases of moderate hypertrophy, as were those of all redox enzymes in cases of strongly marked hypertrophy, although they were reduced in cases with signs of chronic cardiac failure despite the presence of considerable myocardial hypertrophy. Areas of acute myocardial ischemia were discovered in 45% of the cases.
 ...
PMID:[Histochemical study of the enzyme activity of the myocardium of sudden death victims with postinfarct cardiosclerosis]. 296 Feb 98

NADH-diaphorase, succinate dehydrogenase (SDH), beta-hydroxybutyrate dehydrogenase (beta-HBDH), malate dehydrogenase (MDH) and cytochrome oxidase (CytO) were demonstrated histochemically in isolated perfused rat hearts during global ischaemia from 0 to 12 hours. The corresponding enzyme activities were measured when possible. The histochemically demonstrable activities of NADH-diaphorase and MDH decreased during the first hour of ischaemia. The time course of inactivation of biochemically detectable NADH-ferricyanide oxidoreductase was much the same as that of NADH-diaphorase. Both histochemically and biochemically detectable beta-HBDH gradually decreased by about 6 h of ischaemia. NADH-diaphorase but not MDH itself proved to be the rate-limiting factor when demonstrating MDH histochemically with nitroblue tetrazolium (NBT), whereas in the case of beta-HBDH the situation was probably the reverse. CytO and SDH activities did not change during the experimental period. Histochemistry clearly demonstrated ischaemic cellular injury, even though no significant diagnostic changes of ischaemia were visible by light microscopy. Even though this shows that enzyme-histochemical methods can be sensitive indicators of early ischaemic injury, in practice the time between the onset of injury and death as well as between death and autopsy must be taken into consideration when interpreting the results.
 ...
PMID:Correlations between enzyme histochemical reactions and respective enzyme activities in global ischaemic rat hearts. 300 15

To evaluate the diagnostic role of histochemically demonstrated aerobic dehydrogenases in ischemic myocardial injury NADH-diaphorase, succinate dehydrogenase (SDH), beta-hydroxybutyrate dehydrogenase (HBDH) and malate dehydrogenase (MDH) were demonstrated histochemically and the corresponding enzyme activities were measured biochemically in isolated perfused rats hearts after global ischemia from 0 to 12 h. The present data show that the enzyme-histochemical methods when used properly are more sensitive indicators of early ischemic injury than classical histological staining procedures. From the enzymes tested here the histochemical demonstration of HBDH turned out to be best suited for use when suspecting ischemic myocardial injury at autopsy.
 ...
PMID:Oxidative enzyme activities and respective histochemical reactions in ischemic rat myocardium. 342 4

Histochemical study of enzymatic activity in the myocardium was performed in sudden cardiac death. Human hearts in which there were no macroscopic and histological focal or diffuse changes served as material. The following enzymes were studied in the anterior or posterior walls of the left ventricle or in the interventricular septum: succinate dehydrogenase, lactate dehydrogenase (LDH), beta-hydroxybutyrate dehydrogenase (OHBDH), alpha-glycerophosphate- and glucose-6-phosphate dehydrogenase, NAD-diaphorase and phosphorylase. Increased activity of OHBDH and LDH was found: 36,0 and 22,6% higher than in trauma and brain hemorrhage that served as control. These alterations seem to be connected with the increase of blood content of fatty acids, and lactate as a response to the catecholamine excess. Foci of an acute ischemia were found in the interventricular septum in 80% of cases in which phosphorylase was revealed. The appearance of the ischemic foci was obviously due to the coronary arteries contraction.
 ...
PMID:[Histoenzymological characteristics of the myocardium in sudden cardiac death]. 405 12

A histochemical study of the metabolism of rat renal arteries and arterioles. Rat renal arteries and arterioles were examined histochemically to determine their metabolic profiles. Succinate, malate and NAD-isocitrate dehydrogenase, cytochrome oxidase and ubiquinone were assessed to determine aerobic metabolism. Glucose-6-phosphate dehydrogenase and DPN diaphorase were evaluated to determine hexose-monophosphate-shunt activity. Anaerobic metabolism was evaluated via lactate dehydrogenase, and the substrate, glycogen. Gomori's lipase, beta-hydroxybutyrate dehydrogenase and amounts of neutral fat and free fatty acids were assessed as indicators of lipid utilization. Myosin ATPase activity was evaluated as an index of ATP utilization for contraction. Deoxyribonucleic and ribonucleic acids were appraised as indicators of protein synthesis. In general, the oxidative enzymes and myosin ATPase demonstrate considerable activity in renal arteries and arterioles which suggests aerobic metabolism and ATP usage. Renal arteries and arterioles also appear capable of anaerobic metabolism as indicated by strong lactate dehydrogenase reactivity and by the presence of slight to moderate quantities of glycogen, while high levels of glucose-6-phosphate dehydrogenase and moderate amounts of deoxyribonucleic acid suggest a potential for beta-hydroxybutyrate dehydrogenase, minimal lipase activity, and the absence of fatty acids with substantial amounts of neutral fat, indicate limited lipid catabolism.
 ...
PMID:A histochemical study of the metabolism of rat renal arteries and arterioles. 620 11

The profiles of fiber types in hindlimb muscles from the tree shrew (Tupaia glis), lesser bushbaby (Galago senegalensis), and the slow loris (Nycticebus coucang) were determined using histochemical techniques. Fibers were classified as fast-twitch oxidative-glycolytic (FOG), fast-twitch glycolytic (FG), slow-twitch oxidative (SO), or fast-twitch oxidative (FO), according to reactions for alkaline-stable ATPase, acid-stable ATPase, alpha-glucan phosphorylase, reduced nicotinamide adenine dinucleotide diaphorase, succinate dehydrogenase, mitochondrial alpha-glycerophosphate dehydrogenase (MaGPDH), and beta-hydroxybutyric dehydrogenase, as well as glycogen staining by the periodic acid-Schiff technique. Prolonged dissection of numerous muscles was carried out on hindlimbs submersed in cold Tyrode's solution; such treatment had no qualitative effect on enzyme staining reactions, but it is not a suitable procedure if one wishes to stain for glycogen. Fast-twitch oxidative (FO) fibers are alkaline-stable ATPase-positive and possess low MalphaGPDH enzyme activity. These fibers have not been reported previously in any hindlimb muscles. No muscles of any species studies were homogeneous with respect to fiber type. Slow loris muscles lacked FG fibers. The majority of the muscles of the slow loris contained numerous SO fibers. The relationship between enzyme activities and locomotor pattern is discussed.
 ...
PMID:Comparative histochemical study of prosimian primate hindlimb muscles. I. Muscle fiber types. 645 15

The present investigation concerning the histochemical demonstration of DPN diaphorase follows the development of a new reagent, Nitro-BT, which has already been used successfully for the cytochemical localization of the succinic dehydrogenase system. The most consistently favorable results were obtained with the lactate-lactic dehydrogenase system buffered at pH 7.4. Using sections of rat kidney and stomach, it was found that the intensity of stain was optimal after 15 minutes incubation at 37 degrees C., conducted aerobically. By appropriate variations in the substrate mixture it was possible to selectively demonstrate the histochemical distribution of certain DPN-linked dehydrogenases in addition to DPN diaphorase. This was made possible by the special distribution of some of these dehydrogenases which distinguished them from one another. Of the dehydrogenases studied the distribution pattern of beta-hydroxybutyric dehydrogenase was the most singular. In the gastric mucosa beta-hydroxybutyric dehydrogenase was restricted to the cells of the mucous lining epithelium and the gland necks; and in the kidney the enzyme was limited to the cells of the proximal convoluted tubule and thick limbs of Henle's loop. In contrast, lactic dehydrogenase like DPN diaphorase was demonstrable in almost all cytologic elements of both the stomach and the kidney.
 ...
PMID:A histochemical method for the demonstration of diphosphopyridine nucleotide diaphorase. 1350 25

Several different epithelial elements that have intense active transport or protein secretory functions were histochemically assayed in several dehydrogenase media by a recently perfected method. The mitochondria represented the only site of activity, not only when tested in the succinate and D-beta-hydroxybutyrate media, but also when tested in the lactate, malate, and isocitrate media. The reaction for D-beta-hydroxybutyric dehydrogenase in the mouse kidney was curiously limited to the mitochondria of the distal segment of the proximal convoluted tubule, a finding that most convincingly shows that dehydrogenase activity may be differentiated in certain instances from diaphorase activity by the ditetrazole methods and that D-beta-hydroxybutyric dehydrogenase is not present in all mitochondria. Tetranitro-BT is favored over nitro-BT in studies conducted on most organs prepared without fixation and on formalin-fixed tissues that consist of lipid-containing or active transport cells.
 ...
PMID:A survey of dehydrogenases in various epithelial cells in the rat. 1399 76

A newly synthesized substrate, 3-hydroxybutyrylglycyl-glycyl-glycine (3HB-GGG), was applied to the assay of ACE-inhibiting activity to overcome the smaller selectivity and sensitivity of the conventional method. In this study, an ACE-inhibiting assay was improved by the use of a water-soluble tetrazolium salt, 4-[3-(4-iodophenyl)-2-(4-nitrophenyl)-2H-5-tetrazolio]-1,3-benzene disulfonate sodium salt (WST-1), for the detection of 3-hydroxybutyrate, derived from 3HB-GGG. The optimized conditions were as follows: 0.333 mM NAD(+), 0.333 mM WST-1, 0.1 mM EDTA, 0.633 U ml(-1) diaphorase, and 0.700 U ml(-1) 3-hydroxybutyrate dehydrogenase. The developed assay was efficiently applicable to evaluate the ACE-inhibiting activity of practical ACE inhibitors.
 ...
PMID:Assay of angiotensin I-converting enzyme-inhibiting activity based on the detection of 3-hydroxybutyrate with water-soluble tetrazolium salt. 1868 50


1