Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Succinates”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 55 records · Page 3Linked to original sources
PubMed2001

Crystallization, melting, and enzymatic degradation of biodegradable poly(butylene succinate-co-14 mol % ethylene succinate) copolyester.

The crystal structure and growth kinetics of melt-crystallized poly(butylene succinate-co-14 mol % ethylene succinate) [P(BS-co-14 mol % ES)] copolyester have been investigated at a wide crystallization temperature range of 30 to 90 degrees C. By means of wide-angle X-ray diffraction (WAXD), the copolyester composed of BS and ES units has been identified to have the same crystal structure with that of poly(butylene succinate) (PBS) homopolymer, suggesting that only PBS sequences crystallize while that the ES units are in an amorphous form. On the basis of secondary nucleation theory, two regimes of II and III have been observed and their transition temperature is around 80 degrees C. The spherulitic morphologies of P(BS-co-14 mol % ES) copolyester developed from banded spherulites to the normal ones without banding extinction patterns as the crystallization temperature increased. The melting behavior of P(BS-co-14 mol % ES) copolyester under different conditions has been studied by differential scanning calorimetry (DSC). Four melting peaks and one exothermal peak on the melting curves were observed during heating process, and their origination is discussed. The enzymatic degradation was carried out on the melt-crystallized P(BS-co-14 mol % ES) thin film by an extracellar PHB depolymerase from Pseudomonas stutzeri and the morphologies of lamellar crystals before and after degradation have been examined by atomic force microscopy (AFM). The results have indicated that enzymatically degradable ES units exist on the surface of lamellar crystals and are hydrolyzed by the enzyme, while that the crystalline cores composed of PBS chains are not degraded.

Absorbable Implants↗
PubMed2000

Effect of gene disruption of succinate dehydrogenase on succinate production in a sake yeast strain.

Succinate dehydrogenase (SDH) of Saccharomyces cerevisiae consists of four subunits encoded by the SDH1, SDH2, SDH3, and SDH4 genes. We determined the effect of SDH deficiency on the productivity of organic acids in a sake yeast strain Kyokai no. 9. The SDH activity of single disruptants was retained at 30-90% of that of the wild-type strain, but the activity disappeared in double disruptants of the SDH1 and SDH2 or SDH1b (the SDH1 homologue) genes. Two double disruptants showed no growth on a medium containing glycerol as the sole carbon source, while the single disruptants could utilize glycerol. These results indicate that double disruption of the SDH1 and SDH2 or SDH1b genes is required for complete loss of SDH activity and that the SDH1b gene compensates for the function of the SDH1 gene. The sdh1 sdh1b disruptant showed a marked increase in succinate productivity of up to 1.9-fold along with a decrease in malate productivity relative to the wild-type strains under shaking conditions. Under both static and sake brewing conditions, the productivity of these organic acids in the disruptants was virtually unchanged from that in the wild-type strain. Furthermore, SDH activity was undetectable in the wild-type and the disrupted strains under static conditions. These results suggest that SDH activity contributes to succinate production under shaking conditions, but not under static and sake brewing conditions.

Journal Article↗
PubMed2004

Chloramphenicol succinate, a competitive substrate and inhibitor of succinate dehydrogenase: possible reason for its toxicity.

From our previous study [Eur. J. Clin. Pharmacol. 56 (2000) 405] we hypothesized that chloramphenicol succinate (CAPS) may be a competitive substrate for succinate dehydrogenase (SDH). It may be oxidized by SDH to release chloramphenicol (CAP), which may inhibit SDH by feed back mechanism. The present ex-vivo/in vitro study was aimed to investigate this possibility by using human tissues (bone marrow and liver samples) and animal tissues (rat liver and kidney). The effect of different SDH activators and specific inhibitors was studied on CAPS metabolism by SDH. The metabolites and reduction products were detected by using HPLC. In marrow samples, CAPS was slowly oxidized to form CAP. The formation of CAP (oxidation product) was enhanced by FAD and low malonate and inhibited by high malonate and 3-NPA. Similar results were obtained with mitochondria from human and rat tissues. These studies suggest that CAPS could be a competitive oxidative substrate and the metabolite CAP could be an inhibitor at the reduction site. Therefore, SDH could be a target molecule responsible for CAPS induced toxicity.

Animals↗
PubMedDate not supplied

Molecular mobility and phase structure of biodegradable poly(butylene succinate) and poly(butylene succinate-co-butylene adipate).

Molecular mobility and phase structure of biodegradable poly(butylene succinate) (PBS) and poly(butylene succinate-co-20 mol % butylene adipate) [P(BS-co-20 mol % BA)] have been investigated by high-resolution solid-state (13)C NMR. For both samples, two components with different (13)C spin-lattice relaxation time (T(1C)) values have been observed in the crystalline region. The crystalline component with shorter T(1C) value is assignable to the interface near amorphous phase. The crystalline component with longer T(1C) value is ascribed to the inside of the crystalline region. On the basis of T(1C), it has been concluded that the BA units are not included in the crystalline region of P(BS-co-20 mol % BA). Molecular mobility and higher-ordered structure of amorphous phase have been also compared between the melt and solid state. Variable-temperature high-resolution (13)C NMR measurements for the amorphous phase have revealed the remarkable difference in dynamics and structure between the melt and solid state.

Adipates↗
PubMed2003

Novel roles for the rho subfamily of GTP-binding proteins in succinate-induced insulin secretion from betaTC3 cells: further evidence in support of the succinate mechanism of insulin release.

We have previously demonstrated regulatory roles for Rho subfamily of G-proteins in glucose- and calcium-induced insulin secretion. Herein, we examined regulation by these proteins of insulin secretion from betaTC3 cells elicited by mitochondrial fuels, such as the succinic acid methyl ester (SAME). Preincubation of these cells with Clostridium difficile toxin-B (200 ng/mL), which monoglucosylates and inactivates Cdc42 and Rac1, markedly decreased (> 70%) SAME-induced insulin secretion. Furthermore, exposure of betaTC3 cells to GGTI-2147 (20 microM), a selective inhibitor of the requisite prenylation of Rac1 and Cdc42, significantly reduced (> 80%) SAME-induced insulin release, suggesting that post-translational prenylation of these proteins is necessary for SAME-induced insulin release. Western blot analysis indicated localization of Cdc42, Rac1, and Ras in the beta cell mitochondrial fraction. Confocal microscopy revealed a modest, but inconsistent, increase in the association of either Rac1 or Cdc42 with Mitotracker, a mitochondrial marker, following exposure to SAME. These data suggest that activation of preexisting intramitochondrial Rac1 and Cdc42 may be sufficient to regulate SAME-induced insulin secretion. Together, our findings support a role for G-proteins in insulin secretion at a step dependent on mitochondrial metabolism. They also identify mevalonate-derived, isoprenoid modified Rho G-proteins as specific signaling molecules in recently proposed succinate mechanism of insulin release.

Animals↗
PubMed1987

Growth of Paracoccus denitrificans on [2,3-13C]succinate and [1,4-13C]succinate. II. Isoleucine biosynthesis.

Paracoccus denitrificans was grown on either [2,3-13C]succinate or [1,4-13C]succinate, and extracts were analysed by using gas chromatography-mass spectrometry. The distribution of label in isoleucine indicated that the 2-ketobutyrate required for isoleucine biosynthesis was mainly produced from pyruvate by 2-keto-acid chain elongation (i.e. the 'pyruvate elongation pathway'). Approximately 10% of isoleucine was produced by a second pathway involving propionyl CoA. Threonine and glutamate were not utilized by P. denitrificans as a source of 2-ketobutyrate production for isoleucine biosynthesis under the growth conditions used.

Carbon Isotopes↗
PubMed1986

Studies on analogues of succinic semialdehyde as substrates for succinate semialdehyde dehydrogenase from rat brain.

The methyl ester of succinic semialdehyde (SSA) was examined as a substrate for succinate semialdehyde dehydrogenase (SSADH) from rat brain. It was found that the ester can be oxidized by the enzyme. Values of Km for SSA-Me were higher than for those for SSA, and for this substrate the enzyme showed a substrate-dependent inhibition. This finding suggests that the carboxylate group of SSA is not essential in the process of inhibition of SSADH by the substrate. Cyclopropyl analogues of SSA, cis- and trans-1-formyl-cyclopropan-2-carboxylic acids, were also individually tested as substrates of SSADH. Only the trans isomer was found to be oxidized to the corresponding dicarboxylic acid; it inhibited the enzyme in the same range of concentrations as SSA. The above data suggest that, as for gamma-aminobutyric acid, SSA is present in an unfolded, transoid conformation at the active site of SSADH.

Aldehyde Oxidoreductases↗
PubMed1990

Molecular analysis of two genes of the Escherichia coli gab cluster: nucleotide sequence of the glutamate:succinic semialdehyde transaminase gene (gabT) and characterization of the succinic semialdehyde dehydrogenase gene (gabD).

We have characterized two genes of the Escherichia coli K-12 gab cluster, which encodes the enzymes of the 4-aminobutyrate degradation pathway. The nucleotide sequence of gabT, coding for glutamate:succinic semialdehyde transaminase (EC 2.6.1.19), alternatively known as 4-aminobutyrate transaminase, was determined. The structural gene consists of 1,281 nucleotides specifying a protein of 426 amino acids with a molecular mass of 45.76 kDa. The protein shows significant homologies to the ornithine transaminases from Saccharomyces cerevisiae and from rat and human mitochondria. Three functionally and structurally important amino acid residues of the transaminase were identified by sequence comparison studies, and evolutionary relationships of the aminotransferases are discussed. The gabD gene, encoding succinic semialdehyde dehydrogenase (EC 1.2.1.16), was cloned and shown to be located adjacent to the 5' end of gabT. Expression studies with subfragments of the initially cloned DNA region revealed a maximal size of 1.7 kb for gabD. Both genes are cotranscribed from a promoter located upstream of gabD.

4-Aminobutyrate Transaminase↗
PubMed2001

Biodegradation of poly(tetramethylene succinate-co-tetramethylene adipate) and poly(tetramethylene succinate) through water-soluble products.

Poly(tetramethylene succinate-co-tetramethylene adipate) (PBSA) and poly(tetramethylenesuccinate) (PBS) were hydrolyzed experimentally into water-soluble oligomers and monomers by Chromobacterium extracellular lipase. The oligomers were identified by high-performance liquid chromatography-mass spectrometry and 1H-nuclear magnetic resonance, which indicated that a total of 28 oligomer species were liberated from PBSA, and that 13 of them were identical to the hydrolysates from PBS. Moreover, 20 of the species were polyester-based compounds of monomer units, and the other 8 species were small amounts of diurethane compounds. Bis(hydroxybutyl) succinate (BSB) and bis(hydroxybutyl) hexamethylene dicarbamate (BHB) were the typical oligomers and were chemically synthesized. Biodegradability of BSB and BHB was examined for 28 d in the activated sludge, and analysis of the results of this study indicated that the final conversion rate of constituent carbon to carbon dioxide was estimated at 80 mol% for BSB and 10 mol% for BHB. The remaining amount of carbon in the undegraded BHB was 20 mol%. In the presence of BSB, the biodegradability of BHB was increased by about 1.5 times. The suggestion was made that BSB induced a growth of microorganisms and helped BHB degradation. This is consistent with the observation that the biodegradation of BHB in native soil for 60 d reached > 60%.

Adipates↗
PubMed1987

Urinary organic acids in succinic semialdehyde dehydrogenase deficiency: evidence of alpha-oxidation of 4-hydroxybutyric acid, interaction of succinic semialdehyde with pyruvate dehydrogenase and possible secondary inhibition of mitochondrial beta-oxidation.

In addition to the previously reported abnormalities, urine extracts from three cases of succinic semialdehyde dehydrogenase deficiency have shown consistently increased amounts of 2,4-dihydroxybutyric acid, and its lactone, and 3-hydroxypropionic acid, metabolites related to the alpha-oxidation of 4-hydroxybutyric acid. Threo- and erythro-4,5-dihydroxyhexanoic acids have also been identified for the first time and probably arise from the reaction of succinic semialdehyde with an intermediate in the pyruvate dehydrogenase pathway. Adipic acid excretion is also consistently raised, suggesting secondary interference with mitochondrial beta-oxidation. The presence of these metabolites could be a source of diagnostic confusion.

Adipates↗
PubMed1990

Comparative evaluation of the antioxidant activity of alpha-tocopherol, alpha-tocopherol polyethylene glycol 1000 succinate and alpha-tocopherol succinate in isolated hepatocytes and liver microsomal suspensions.

The antioxidant activity of alpha-tocopherol polyethylene glycol 1000 succinate (TPGS) and of alpha-tocopherol succinate (TS) has been examined in isolated hepatocytes and microsomal fractions from rat liver. Both TPGS and TS require esterase activity to yield free alpha-tocopherol and, hence, antioxidant activity. TPGS and TS consistently exerted a more effective antioxidant protection than an equivalent amount of directly-added free alpha-tocopherol. The low antioxidant efficiency of directly added free alpha-tocopherol in such water-based experimental systems as used here seems to be due to its extreme hydrophobicity. TPGS, on the other hand, is an extremely hydrophilic compound that is being examined as a useful source of alpha-tocopherol in certain clinical situations and is here shown to be a convenient and effective source for experimental studies into lipid peroxidation and antioxidant mechanisms.

Animals↗
PubMed2001

Synthesis of iron-crosslinked chitosan succinate and iron-crosslinked hydroxamated chitosan succinate and their in vitro evaluation as potential matrix materials for oral theophylline sustained-release beads.

Chitosan succinate (CS) and hydroxamated chitosan succinate (HCS) were prepared. The generated semisynthetic polymers were employed in the formation of drug-loaded, iron(III)-crosslinked polymeric beads. Infrared spectroscopy was employed to prove the crosslinking. The produced beads were evaluated in vitro as drug prolonging and potentially orally administered delivery system. Theophylline was used as the loaded model drug. The generated beads proved to be successful in prolonging drug release. Iron leaching from the generated beads was minimal (<2%), and it only took place under acidic conditions (pH 1).

Administration, Oral↗
PubMed2000

Vitamin E succinate induces apoptosis in human prostate cancer cells: role for Fas in vitamin E succinate-triggered apoptosis.

The apoptosis-triggering properties of vitamin E succinate (VES, RRR-alpha-tocopheryl succinate) for human LNCaP and PC-3 prostate carcinoma cells and normal PrEC human prostate epithelial cells were investigated. LNCaP and PC-3 cells were sensitive to VES-induced apoptosis, with 100% and 60% of cells undergoing apoptosis after three days of treatment with 10 micrograms of VES/ml, respectively. PrEC cells were resistant to VES-induced apoptosis. Treatment of prostate cells with agonistic anti-Fas antibody triggered apoptosis in approximately 50% of PC-3 cells within 48 hours, whereas LNCaP and PrEC cells were resistant. Prostate cells simultaneously treated with VES and agonistic anti-Fas antibodies revealed 1) no effect on PrEC cells, 2) an additive effect on Fas-sensitive PC-3 cells, and 3) a synergistic effect on LNCaP cells. VES treatment of LNCaP cells caused depletion of cytosolic 43-kDa Fas, enhanced membrane levels of 43-kDa Fas, and induced Fas sensitivity. PC-3 cells expressed high levels of membrane 43-kDa Fas that were enhanced by VES treatments. Fas ligand expression by LNCaP cells was enhanced by VES treatments. In summary, VES triggers apoptosis in human prostate carcinoma cells but not normal prostate cells in vitro, and VES modulates Fas signaling.

Apoptosis↗
PubMed1980

Influence of 6 alpha-methylprednisolone 21-sodium succinate on the pituitary, adrenal glands, and the gastrointestinal tract in rats. (Comparative toxicity study with hydrocortisone 21-sodium succinate).

A comparative toxicity study with 6 alpha-methylprednisolone 21-sodium succinate (MPS) and hydrocortisone 21-sodium succinate (HCS) was carried out on male rats of the Wistar strain. MPS and HCS were administered intravenously to rats in dose levels of 20 or 100 mg/kg/day for 14 days. There were no significant differences in the pituitary weights in MPS and HCS groups, but weight of the adrenal glands decreased with increasing dose levels of MPS and HCS. Histopathological examination of MPS and HCS treated rats revealed atrophy of the zona fasiculata in the adrenal cortex which correlated with dose levels. The decline of serum corticosterone levels in rats correlated with increasing dose levels of MPS and HCS. It can be concluded that the inhibitory effect of MPS on the pituitary-adrenal system in rats was the same as HCS. No ulceration was observed in the gastro-intestinal tract of MPS of HCS treated rats.

Adrenal Glands↗
PubMed2001

Enzyme electrokinetics: energetics of succinate oxidation by fumarate reductase and succinate dehydrogenase.

Protein film voltammetry is used to probe the energetics of electron transfer and substrate binding at the active site of a respiratory flavoenzyme--the membrane-extrinsic catalytic domain of Escherichia coli fumarate reductase (FrdAB). The activity as a function of the electrochemical driving force is revealed in catalytic voltammograms, the shapes of which are interpreted using a Michaelis-Menten model that incorporates the potential dimension. Voltammetric experiments carried out at room temperature under turnover conditions reveal the reduction potentials of the FAD, the stability of the semiquinone, relevant protonation states, and pH-dependent succinate--enzyme binding constants for all three redox states of the FAD. Fast-scan experiments in the presence of substrate confirm the value of the two-electron reduction potential of the FAD and show that product release is not rate limiting. The sequence of binding and protonation events over the whole catalytic cycle is deduced. Importantly, comparisons are made with the electrocatalytic properties of SDH, the membrane-extrinsic catalytic domain of mitochondrial complex II.

Flavin-Adenine Dinucleotide↗
PubMed1997

A pilot study to investigate the treatment of anogenital warts with Topical Lithium Succinate cream (8% lithium succinate, 0.05% zinc sulphate).

The incidence of anogenital warts (condyloma acuminatum) is rapidly increasing while there is still no totally satisfactory treatment available. In light of the emphasis of experimental approaches toward the prevention of viral replication and evidence of the antiviral action of lithium salts it was proposed to investigate the efficacy of Topical Lithium Succinate cream (LSC) in the treatment of anogenital warts. A total of 101 patients (42 women, 59 men) were randomized to receive either active or placebo treatment for a period of 4 weeks. Assessment of the number, location, size and area of coverage of the warts was made by the clinician at baseline, weeks 2, 4, 6 and 12. Compliance to the study protocol following cessation of treatment at week 4 was extremely poor. The high drop-out rate after this was felt to invalidate data collected after that point. It was therefore decided that the analysis should concentrate on the treatment period. Of 101 patients entering the trial 51 received active (30 male and 21 female) and 50 received placebo (29 male, 21 female). The primary efficacy variable was percentage change from baseline in the overall coverage of lesions. Over all patients LSC treatment resulted in a reduction of 42% (P<0.02) in the overall coverage of lesions. Separate analyses for male and female patients showed that for males there was a highly significant reduction in the coverage of lesions of 65% (P<0.02). However for females the reduction of 11% was not significant. A possible explanation for this difference between the sexes is that as many of the lesions in the female patients were internal therefore this could lead to difficulty in both application of the cream, and subsequent lesion assessment.

Administration, Topical↗
PubMed1989

One-step purification from Escherichia coli of complex II (succinate: ubiquinone oxidoreductase) associated with succinate-reducible cytochrome b556.

Complex II (succinate:ubiquinone oxidoreductase) is an important component of both the tricarboxylic acid cycle and of the aerobic respiratory chains of eukaryotic and prokaryotic organisms. The enzyme has been purified from numerous sources and appears to be highly conserved from considerations of both the amino acid sequences of the catalytic subunits and from the prosthetic groups associated with the enzyme. The sdh operon has been cloned and sequenced from Escherichia coli, but the enzyme from this source has, so far, resisted attempts at biochemical purification. In this work, a one-step purification of the enzyme is described which yields a stable four-subunit enzyme which has a high specific activity. This purification takes advantage of a strain which overproduces the enzyme by 10-fold due to the presence of a multicopy plasmid containing the cloned sdh operon. The purified complex II has one FAD, eight non-heme irons, seven acid-labile sulfides, and one protoheme IX per molecule. The enzyme has been reconstituted in phospholipid vesicles and demonstrated to reduce ubiquinone-8, the natural electron acceptor, at a high rate.

Cell Membrane↗