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)

Intraperitoneal injection of thyroxine (T4; 1 microgram/g body weight on alternate days, seven doses) to male garden lizards of three different age groups caused a stimulation of hepatic succinic dehydrogenase activity, the degree of response being higher in the old (63%) than in middle-aged (39%) and young (31%). Percent inhibition of enzyme activity following thiourea treatment (0.05 mg/g body weight on alternate days, three doses) was higher in middle-aged lizards (24%) than in young (10%) and old (12%) ones.
 ...
PMID:Age-related changes in the response of hepatic succinic dehydrogenase activity to thyroxine and thiourea in lizards. 314 Dec 48

The brain of the fishes (Channa punctatus) subjected to cold acclimation (15 +/- 1 degree) in darkness exhibited low succinic dehydrogenase (SDH) activity after 3 and 7 days and high protein content after 7 days when compared with their warm acclimated (32 +/- 1 degree) counterparts. In warm acclimated fishes maintained in complete darkness, T4 (0.5 micrograms/g body weight/day) depressed the enzyme activity after 5 and 7 days of treatment and reduced the protein content after 3 days. But neither in cold acclimated fishes maintained in darkness for 3, 5, and 7 days nor in warm acclimated fishes maintained in 12 hr dark and 12 hr daylight for the same periods did T4 induce a significant change in the same biochemical parameters. It appears that T4 action in this fish is dependent on acclimation temperature and light:dark regimes. When warm acclimated control fishes maintained in complete darkness were compared with those maintained in 12 hr dark and 12 hr daylight, the enzyme activity was found to be higher and the protein content lower in the former than in the latter. The results suggest that natural photoperiod regulates the thyroid activity in vivo. In vitro studies revealed that the presence of T4 (3.12 microM) in the incubating medium stimulated the enzyme activity of brain homogenates possibly due to direct action on mitochondria. Immersion of fishes in thiourea solution (1 mg/ml) for 3, 5, and 7 days resulted in enhancement of enzyme activity after 7 days of treatment and of protein content after 5 days of treatment. Thyroid hormones in vivo appear to have an inhibitory effect on the carbohydrate metabolism of the nervous tissue.
 ...
PMID:Thyroid hormones and carbohydrate metabolism of brain in the teleost, Channa punctatus. I. Effect of T4 and thiourea on succinic dehydrogenase (SDH) activity and protein content. 642 14

In a previous study, we found that treatment of rat heart mitochondria with H(2)O(2) resulted in a decline and subsequent recovery in the rate of state 3 NADH-linked respiration. These effects were shown to be mediated by reversible alterations in NAD(P)H utilization and in the activities of specific Krebs cycle enzymes alpha-ketoglutarate dehydrogenase (KGDH) and succinate dehydrogenase. The purpose of the current study was to examine potential mechanism(s) by which H(2)O(2) reversibly alters KGDH activity. We report here that inactivation is not simply due to direct interaction of H(2)O(2) with KGDH. In addition, incubation of mitochondria with deferroxamine, an iron chelator, or 1,3-dimethyl-2-thiourea, an oxygen radical scavenger, prior to addition of H(2)O(2) did not alter the rate or extent of inactivation. Thus, inactivation does not appear to involve a more potent oxygen radical formed upon metal-catalyzed oxidation. Inactive KGDH from H(2)O(2)-treated mitochondria was reactivated with dithiothreitol, implicating oxidation of a protein sulfhydryl(s). However, the thioredoxin system had no effect, indicating that enzyme inactivation is not due to the formation of intra- or intermolecular disulfide(s) or a sulfenic acid. Upon incubation of mitochondria with H(2)O(2), reduced GSH levels fell rapidly prior to enzyme inactivation but recovered at the same time as enzyme activity. Importantly, treatment of inactive KGDH with glutaredoxin facilitated the GSH-dependent recovery of KGDH activity. Glutaredoxin is characterized as a specific and efficient catalyst of protein deglutathionylation. Thus, the results of the current study indicate that KGDH activity appears to be modulated through enzymatic glutathionylation and deglutathionylation. These studies demonstrate a novel mechanism by which KGDH activity and mitochondrial function can be modulated by redox status.
 ...
PMID:Reversible inactivation of alpha-ketoglutarate dehydrogenase in response to alterations in the mitochondrial glutathione status. 1268 Jul 78

In this study, proteomes of two pathogenic Leptospira spp., namely L. interrogans, serogroup Icterohaemorrhagiae, serovar Copenhageni and L. borgpetersenii, serogroup Tarassovi, serovar Tarassovi, were revealed by using two dimensional gel electrophoresis (2DE)-based-proteomics. Bacterial cells were disrupted in a lysis buffer containing 30 mM Tris, 2 M thiourea, 7 M urea, 4% CHAPS, 2% IPG buffer pH 3-10 and protease inhibitors and then subjected to sonication in order to solubilize as much as possible the bacterial proteins. The 2DE-separated components of both Leptospira homogenates were blotted individually onto membranes and antigenic components (immunomes) were revealed by probing the blots with immune serum of a mouse readily immunized with the homogenate of L. interrogans, serogroup Icterohaemorrhagiae, serovar Copenhageni. The immunogenic proteins of the two pathogenic Leptospira spp. could be grouped into 10 groups. These are: 1) proteins involved in the bacterial transcription and translation including beta subunit transcription anti-termination protein of DNA polymerase III, elongation factors Tu and Ts, and tRNA (guanine-N1)-methyltransferase; 2) proteins functioning as enzymes for metabolisms and nutrient acquisition including acetyl-Co-A acetyltransferase, putative glutamine synthetase, glyceraldehyde-3-phospahte dehydrogenase, NifU-like protein, 3-oxoacyl-(acyl-carrier-protein) reductase, oxidoreductase, sphingomyelinase C precursor, spermidine synthase, beta subunit of succinyl-CoA synthetase, and succinate dehydrogenase iron-sulfur subunit; 3) proteins/enzymes necessary for energy and electron transfer, i.e. electron transfer flavoprotein, and proton-translocating transhydrogenase; 4) enzymes for degradation of misfolded proteins, i.e. ATP-dependent Clp protease; 5) molecular chaperone, i.e. 60 kDa chaperonin; 6) signal transduction system, i.e. response regulator; 7) protein involved in immune evasion in host, i.e. peroxiredoxin; 8) cell structure proteins including MreB (cytoskeletal) and flagellin/ periplasmic flagellin; 9) lipoproteins/outer membrane proteins: LipL32, LipL41, LipL45 and OmpL1; and 10) various hypothetical proteins. Many immunogenic proteins are common to both Leptospira spp. These proteins not only are the diagnostic targets but also have potential as candidates of a broad spectrum leptospirosis vaccine especially the surface exposed components which should be vulnerable to the host immune effector factors.
 ...
PMID:Proteome and immunome of pathogenic Leptospira spp. revealed by 2DE and 2DE-immunoblotting with immune serum. 1789 22