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)

Histochemical studies have been made of the isocitrate dehydrogenase, succinic dehydrogenase, malate dehydrogenase, glutamate dehydrogenase, DPN diaphorase, TPN diaphorase, delta 5-3 beta-hydroxysteroid dehydrogenase and monoamine oxidase in the caput, corpus and cauda epididymides of normal and alpha chlorohydrin (6.5 mg/kg/9 days) treated rats. Administration of alpha chlorohydrin in a low dose caused a conspicuous decrease in all these enzymes except delta 5-3 beta-HSD, in various cell types of epididymal epithelium and sperms. Biochemical estimations of isocitrate dehydrogenase, succinic dehydrogenase, malate dehydrogenase and delta 5-3 beta-HSD have further supported and confirmed these histochemical observations. These changes in enzyme activities after treatment with low dose of alpha chlorohydrin strongly suggest that TCA cycle and amino acid metabolism of epididymis become defective, much earlier before any histological damage to the epididymis becomes visible.
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PMID:Effects of low doses of alpha chlorohydrin on the dehydrogenases and oxidases of rat epididymal epithelium and sperms: a correlative histochemical and biochemical study. 694 44

Androgen level and the activity of lactate dehydrogenase, succinic dehydrogenase, 17 beta-hydroxysteroid dehydrogenase and NADP-diaphorase was studied in cultured Leydig cells obtained from testes of male mice from inbred strains KP and CBA following a single injection of cadmium chloride. Mice from CBA strain, known to be resistant to the toxic effects of cadmium showed no differences in the enzyme activity and endocrine function of gonads, as compared with control animals. In KP mice, sensitive to cadmium, a marked decrease of activity of all studied dehydrogenases, as well as a fall of androgen level was observed following cadmium administration. The decrease of hormone secretion occurred on the 2nd day of tissue culture and showed a correlation with the 17 beta-hydroxysteroid dehydrogenase activity.
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PMID:Effect of cadmium on androgen level and oxidoreductive enzymes activity in cultured leydig cells of KP and CBA mice. 694 54

The quantitative cytochemical investigation of the prodigiozan effect on the enzymatic activity of the peritoneal macrophages was performed on mice. The drug was administered in a single dose of 150 microgram/kg 24 hours before the specimen collection. Prodigiozan promoted a reliable increase in the activity of the enzymes participating in glycolysis (lactate and cytoplasmic alpha-glycerophosphate dehydrogenases), hexoso-monophosphatic pathway of glucose oxidation (glucoso-6-phosphate dehydrogenase), succinate dehydrogenase, NADP. N-diaphorase and lysosomal enzymes, such as acid phosphatase and non-specific alpha-naphthyl acetate esterase. The changes indicate that activation of the macrophages is one of the significant mechanisms of increasing the host nonspecific resistance with prodigiozan.
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PMID:[Prodigiozan as an activator of peritoneal macrophages]. 727 Dec 60

Cytochemical reactions for mitochondrial NADH-dependent dehydrogenases (diaphorase/NADH which is related to flavoprotein), NAD-dependent dehydrogenases (isocitrate, malate) and succinate dehydrogenase were carried out in rat spermatozoa. In addition to a morphological evaluation, the intensity of the reactions was assessed using a computer image analysing system (Quantimet 600 S). The intensity of the reactions was examined in sperm midpieces by measuring integrated optical density (IOD) and mean optical density (MOD). The activity of mitochondrial respiratory chain complexes was also analysed using the polarographic method. In the population of spermatozoa studied, all whole spermatozoa midpieces were completely filled with formazans, the product of the cytochemical reaction. These morphological findings corresponded to the values obtained for IOD and MOD for the given enzymes. In the oxygraphic studies, the spermatozoa demonstrated consumption of oxygen in the presence of substrates for I, II and IV complexes and their mitochondria revealed normal integrity and sensitivity to the substrates and inhibitors. However, the oxygraphic studies revealed differences between the sperm and somatic cells. These differences concerned the stimulation of pyruvate oxidation by malate, the lack of an effect of malonic acid on phenazine methosulphate (an acceptor of electrons) oxidation and the lack of an effect of cytochrome c on ascorbate oxidation. The cytochemical method, together with densitometric measurements, enables: (1) the reaction intensity to be determined objectively; (2) subtle and dramatic differences in reaction intensity to be revealed between spermatozoa that do not differ under morphological evaluation of the intensity; (3) possible defects within the mitochondrial sheath to be located and assessed in a large number of spermatozoa. This method can be used as a screening method alongside the routine morphological examination of spermatozoa. On the other hand, the oxygraphic method in the inner membrane of mitochondria can reveal functional changes which are related to the action of respiratory chain complexes and display characteristic features of mitochondria energy metabolism. The methods used are complementary and allow the complex evaluation of mitochondria in spermatozoa. Both methods can be used in experimental and clinical studies.
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PMID:Computerized analysis of cytochemical reactions for dehydrogenases and oxygraphic studies as methods to evaluate the function of the mitochondrial sheath in rat spermatozoa. 1116 13

Nitric oxide synthase-1 (NOS-1) is found in high concentrations in skeletal muscles, where its synthesis product nitric oxide (NO) is reported to be involved in a number of processes, including the modulation of the oxidative metabolism of myofibers. Performing immunoblot analysis and quantification of formazan produced by its specific NADPH diaphorase activity, we found NOS-1 to be enriched in rat skeletal muscles with a high proportion of fast-twitch myofibers. Since these myofibers represent a metabolically heterogeneous subpopulation, we extended our investigation to the level of individual myofibers. Using serial sections we combined myosin heavy chain-based fiber-typing with quantitative succinate dehydrogenase histochemistry to determine three groups of fiber-types, comprising fast-oxidative, fast-glycolytic and slow-oxidative myofibers. Image analysis showed that NOS-1 diaphorase activity is significantly enriched in fast-oxidative myofibers compared with fast-glycolytic and slow-oxidative ones. In order to characterize potential biological effects of the fiber-type-specific enrichment of NOS-1, we performed cytochrome oxidase histochemistry in the presence of the NO donors NOC-9 and SNAP. Both NO donors reduced cytochrome oxidase activity in all myofibers investigated with almost identical semi-maximal inhibition rates, although fast-oxidative and slow-oxidative myofibers contained twice as much basal catalytic activity than fast-glycolytic ones. In summary, we suggest that the NOS-1/NO system of skeletal muscles exerts its biological role especially in fast-oxidative myofibers, since these myofibers express more NOS-1 than fast-glycolytic or slow-oxidative ones and also contain the highest concentrations of cytochrome oxidases as potential target molecules of NO.
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PMID:Nitric oxide synthase-1 is enriched in fast-twitch oxidative myofibers. 1170 44

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.
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PMID:A histochemical method for the demonstration of diphosphopyridine nucleotide diaphorase. 1350 25

THE ALDEHYDES INTRODUCED IN THIS PAPER AND THE MORE APPROPRIATE CONCENTRATIONS FOR THEIR GENERAL USE AS FIXATIVES ARE: 4 to 6.5 per cent glutaraldehyde, 4 per cent glyoxal, 12.5 per cent hydroxyadipaldehyde, 10 per cent crotonaldehyde, 5 per cent pyruvic aldehyde, 10 per cent acetaldehyde, and 5 per cent methacrolein. These were prepared as cacodylate- or phosphate-buffered solutions (0.1 to 0.2 M, pH 6.5 to 7.6) that, with the exception of glutaraldehyde, contained sucrose (0.22 to 0.55 M). After fixation of from 0.5 hour to 24 hours, the blocks were stored in cold (4 degrees C) buffer (0.1 M) plus sucrose (0.22 M). This material was used for enzyme histochemistry, for electron microscopy (both with and without a second fixation with 1 or 2 per cent osmium tetroxide) after Epon embedding, and for the combination of the two techniques. After fixation in aldehyde, membranous differentiations of the cell were not apparent and the nuclear structure differed from that commonly observed with osmium tetroxide. A postfixation in osmium tetroxide, even after long periods of storage, developed an image that-notable in the case of glutaraldehyde-was largely indistinguishable from that of tissues fixed under optimal conditions with osmium tetroxide alone. Aliesterase, acetylcholinesterase, alkaline phosphatase, acid phosphatase, 5-nucleotidase, adenosine triphosphatase, and DPNH and TPNH diaphorase activities were demonstrable histochemically after most of the fixatives. Cytochrome oxidase, succinic dehydrogenase, and glucose-6-phosphatase were retained after hydroxyaldipaldehyde and, to a lesser extent, after glyoxal fixation. The final product of the activity of several of the above-mentioned enzymes was localized in relation to the fine structure. For this purpose the double fixation procedure was used, selecting in each case the appropriate aldehyde.
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PMID:Cytochemistry and electron microscopy. The preservation of cellular ultrastructure and enzymatic activity by aldehyde fixation. 1397 66

The effect of environmental ion concentration on the enzyme activity of astrocytes was investigated in tissue cultures of rat cerebral cortex. It was found that the oxidative enzymatic activity (succinic dehydrogenase, DPN-diaphorase, and several other enzymes) of astrocytes depended on the concentration of NaCl in the environment. This response was not specific for NaCl, but was also elicited by MgCl(2) and LiCl; the response was less consistent, and often questionable for KCl. However, only NaCl could elicit enzymatic changes in astrocytes at concentrations known to be present in a living organism. Astrocytes were the only cells which responded this way; it appeared that the foot-plates were particularly involved in the response since increase of enzyme activity occurred earlier in the foot-plates than in the perikarya. It was concluded that astrocytes are metabolically involved in the maintenance of the ionic and osmotic environment of the central nervous system, particularly in regard to the active transport of sodium.
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PMID:THE ENZYMATIC RESPONSE OF ASTROCYTES TO VARIOUS IONS IN VITRO. 1410 17

The photoreducible cytochrome (Cyt) b from Dictyostelium discoideum was purified by differential precipitation with ammonium sulfate and chromatography over Sephadex G-100, diethylaminoethyl-cellulose, and calcium phosphate. The purified Cyt is composed of a single subunit of 15,000 daltons including a noncovalently bound protohaem, and exhibits in the reduced form alpha absorption bands at 555.5 and 560 nm at room temperature and 551 and 558.5 nm at 77 K. This Cyt is similar in some respects to Cyt b(557.5) from complex II of beef heart mitochondria, and to Cyt b(555) from the microsomal fraction of mung bean seedlings. Photoreduction by blue light of the purified Cyt b requires the addition of flavin; flavoprotein isolated from D. discoideum was the most active of four flavoproteins tested in catalyzing the photoreduction while diaphorase and l-amino-acid oxidase were inactive.
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PMID:Purification and Characterization of the Photoreducible b-type Cytochrome from Dictyostelium discoideum. 1666 Apr 35

The aim of the present investigation was to detect the regularities of postnatal development of "motor end-plate-muscle fiber (MF)-vascular network" system in different calf muscles of intact albino rats. Gastrocnemius, plantaris and soleus muscles were studied in 72 albino rats aged from 14 to 180 days. Identification of MF type was performed on the basis of succinate dehydrogenase and NADH-diaphorase activity. Cholinesterase activity of the neuro-muscular synapse (NMS) and alkaline phosphatase activity in the vascular endothelium were demonstrated using a combined histochemical method. The diameter of vascular network and the number of enzyme-active zones (EAZ) per one MF were the earliest parameters to be stabilized (before day 30). Histochemical profile of skeletal muscle was stabilized by the end of day 60. Dynamics of MF diameter and EAZ in NMS, vessel diameter and numbers per one MF is characterized by the periods of active changes (days 14-30), decrease (days 30-60) and stabilization (after day 60) of variance rate. The association between the level of oxidative metabolism and MF diameter was demonstrated.
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PMID:[Differentiation of calf skeletal muscles in the postnatal period of ontogenesis]. 2096 Jul 12


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