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PubMed1983

Influence of treatment with prostaglandin synthesis inhibitor or progesterone on cytotoxic activity and progesterone binding capacity of lymphocytes during pregnancy.

Cytotoxic activity and progesterone binding capacity of lymphocytes obtained from women with threatened preterm labour were tested before and during treatment with acetylsalicylic acid or 17-hydroxyprogesterone caproate. Cytotoxic activity of the lymphocytes significantly decreased (p less than 0.001), while progesterone binding capacity significantly increased (p less than 0.001) following the introduction of the treatments. No changes in these parameters were observed on lymphocytes of untreated women. Preterm delivery occurred more frequently among untreated women than among women treated with acetylsalicylic acid (p less than 0.01) or those treated with 17-hydroxyprogesterone caproate (p less than 0.05).

17-alpha-Hydroxyprogesterone↗
PubMed1984

Inhibitory effect of saturated fatty acids on the mutagenicity of N-nitrosodimethylamine.

Saturated fatty acids, C5-C12, inhibited the mutagenic activity of N-nitrosodimethylamine (NDMA) in E. coli WP2 uvrA/pKM101. The inhibition by laurate (C12) was due to the suppression of the enzymatic demethylation of NDMA, whereas that by caprate (C10) was simply due to the bactericidal effect of the fatty acid. Caproate (C6) did not affect the NDMA-demethylase, and evidence is presented to show that the inhibition of mutagenesis by caproate was a result of its interference with the uptake of NDMA metabolites into bacterial cells. Possible biological significance of the inhibition is discussed.

Animals↗
PubMed2006

The role of pH in the fermentative H2 production from an acidogenic granule-based reactor.

The role of pH in the fermentative H(2) production from an upflow acidogenic granule-based reactor was investigated in this study. Experimental results show that all H(2) partial pressure, H(2) production rate and H(2) yield were pH-dependent, in the range of 2.8 x 10(4)-5.2 x 10(4)Pa, 61-145 ml-H(2)l(-1)h(-1) and 0.68-1.61 mol-H(2)mol-glucose(-1), respectively. The maximum H(2) partial pressure was observed at pH 3.4, while both maximum H(2) production rate and H(2) yield were found at pH 4.2. Acetate, propionate, butyrate, i-butyrate, valerate, caporate and ethanol were present in the effluent of this UASB reactor, and their distribution was also pH-dependent. As pH was decreased from 4.2 to a lower level of 3.4 or increased to a higher level of 6.3, the fermentative type of this H(2)-producing reactor would shift from butyrate-type to caporate- or ethanol-type. Thermodynamic analysis was performed to explore the possible metabolic pathways of caproate and valerate formation. The metabolic pathway of caproate formation was pH-dependent, while that of valerate formation was pH-independent. A neural network model was designed, trained and validated. It was able to successfully describe the daily variations of H(2) partial pressure and H(2) yield of the reactor, and to predict its steady state performance at various pHs.

Anaerobiosis↗
PubMed2006

A novel esterase from Ralstonia sp. M1: gene cloning, sequencing, high-level expression and characterization.

A newly isolated gene from Ralstonia sp. M1, encoding an esterase, was cloned in Escherichia coli and its nucleotide sequence determined. The 1.6kb insert revealed one complete open reading frame, predicted to encode an esterase (320 aa, 34.1kDa) with a pI of 9.86. EstR contained a putative oxyanion hole H36G37, a conserved pentapeptide G103HSLG107 and a conserved catalytic His265 and Asp237. The EstR sequence shared 64-70 and 44-48% identity with the hydrolases/acyltransferases from Burkholderia strains and from Ralstonia strains, respectively, 44 and 38% identity with the lactone-specific esterase from Pseudomonas fluorescens and Mesorhizobium loti, respectively. The esterase EstR was expressed with a high level of 41mg/g wet cells. The Ni-NTA-purified esterase EstR showed an optimal activity in the temperature range 60-65 degrees C and pH range 7.5-9.0 towards p-nitrophenyl caproate. The enzyme was found to be highly resistant to many organic solvents especially induced by ethanolamine. Metal ions showed slight effect on esterase activity. The inhibitor phenylmethanesulfonyl fluoride inhibited strongly the esterase. Triton X-45 induced the activation of EstR, but other detergents slightly to strongly decreased or completely inhibited. Among tested p-NP esters, caproate was the most preferential substrate of this esterase.

Amino Acid Sequence↗
PubMed1994

Effects of various salts and pH on the stability of the nucleosome in chromatin fragments.

The stability of nucleosomes in long chromatin fragments was observed by differential scanning calorimetry over a wide range of solution conditions. The thermal denaturation of chromatin was characterized in general as three major transitions, although the process clearly is more complex. The three major transitions were (1) denaturation of the nucleosome, (2) base unstacking of DNA in the resulting denatured nucleoprotein, and (3) base unstacking of naked DNA. In very low salt concentrations (e.g., 2 mM sodium cacodylate), these three processes were essentially coincident (near 76 degrees C), but in medium salt concentrations (e.g., 100 mM NaCl) the nucleosome denaturation occurred first at about 69 degrees C and then base unstacking occurred at 85 degrees C. As [NaCl] was increased, all three processes were resolved with the observation of increasing amounts of naked DNA being melted, until at 2000 mM NaCl the calorimetric profile showed mainly the melting of DNA. The transition temperature for nucleosome denaturation decreased from 76 to 63 degrees C as the salt concentration increased from 1 to 600 mM. Destabilization of the nucleosome by increasing [NaCl] was also evident above 100 mM as a decrease in enthalpic change attributable to nucleosome denaturation. Similarly, as [NaCl] was increased above 100 mM, less and less denatured nucleoprotein was evident as more and more of the DNA melted as naked DNA. The fatty acid salts, sodium valerate and sodium caproate, destabilized the nucleosome but not the denatured nucleoprotein that resulted from the collapse of the nucleosome. In the series acetate, butyrate, valerate, caproate, it was clear that destabilization of the nucleosome increased as hydrophobicity (chain length) increased.(ABSTRACT TRUNCATED AT 250 WORDS)

Calorimetry, Differential Scanning↗
PubMed2003

Regulation of glucose-6-phosphatase gene expression in cultured hepatocytes and H4IIE cells by short-chain fatty acids: role of hepatic nuclear factor-4alpha.

Mechanisms underlying dietary nutrient regulation of glucose-6-phosphatase (Glc-6-Pase) gene expression are not well understood. Here we investigated the effects of short-chain fatty acids on the expression of this gene in primary cultures of rat hepatocytes and H4IIE hepatoma cells. Propionate, butyrate, valerate, and caproate induced severalfold increases in the expression of Glc-6-Pase mRNA. In reporter gene assays, propionate, valerate, caproate, and also octanoate increased Glc-6-Pase promoter activity by 6-16-fold. Butyrate, by itself, had little or no effect on promoter activity, but it induced a robust increase (45-fold) in promoter activity in cells co-transfected with a plasmid expressing the transcription factor HNF-4alpha (alpha isoforms of hepatic nuclear factor 4). HNF-4alpha also enhanced promoter activity induced by other short-chain fatty acids. A dominant negative form of HNF-4alpha abrogated the fatty acid-induced promoter activity, a finding that accentuates a role for HNF-4alpha in the transcription process studied here. In cells transfected with HNF-4alpha, short-chain fatty acids and trichostatin A, an inhibitor of histone deacetylase, synergistically enhanced promoter activity, suggesting that hyperacetylation of histones is an important component of the transactivation of the Glc-6-Pase gene promoter by HNF-4alpha. Region-751/-466 of this promoter contains seven putative HNF-4alpha-binding motifs. Binding of HNF-4alpha to this region was confirmed by electrophoretic mobility shift and chromatin immunoprecipitation assays, indicating that HNF-4alpha is recruited to the Glc-6-Pase gene promoter during short-chain fatty acid-induced transcription from this promoter.

Amino Acid Motifs↗
PubMed2001

Food aroma partition between packaging materials and fatty food simulants.

By means of thermal desorption experiments, the partition equilibrium (partition coefficient, K) was analysed for six food aroma components (d-limonene, n-decane, ethyl caproate, phenylethanol, n-hexanol and hexanal) between three sealable pollymer films suitable for direct food contact (ultra-low density polyethylene, ULDPE; ionomer, ION; and polyester, PET) and four fatty food simulants (ethanol 95%, EtOH; sunflower oil, Oil; n-heptane, HEP, and iso-octane, OCT). The results showed that aroma scalping is highly dependent on the fatty food simulant utilized. Polar aroma components were more sorbed into polymers in the presence of a non-polar fatty food simulant, and vice versa. K values in the presence of Oil were always between those in EtOH and in HEP or OCT. In general, PET was the packaging film which showed the lowest partition coeffecient for non-polar components while ULDPE showed the lowest partition for polar aromas. The partition equilibrium of mixed d-limonene, ethyl caproate, and n-hexanol was also determined. The differences in K values between isolated aromas and mixed aromas were small. In general, the most sorbed aroma showed increased partition by mixture while the partition of the least sorbed was reduced.

Fats↗
PubMed1994

Retinyl ester hydrolytic activity associated with human intestinal brush border membranes.

Hydrolysis of retinyl esters in the lumen of the small intestine is required before absorption. Previously, rat brush border membranes (BBMs) were found to contain a pancreatic-derived esterase preferring retinyl esters with short fatty acyl chains and an intrinsic esterase preferring esters with long fatty acyl chains. Here, similar activities were found for preparations of human BBMs. Long-chain ester hydrolysis was stimulated best by deoxycholate, a dihydroxy bile salt, whereas short-chain ester hydrolysis was stimulated best by taurocholate, a trihydroxy bile salt. A 10-fold difference in KM values for retinyl palmitate (0.53 mumol/L) and caproate (5.5 mumol/L) also indicated distinguishable long-chain and short-chain activities. Differences between retinyl butyrate and retinyl caproate hydrolysis suggested the possible presence of two short-chain esterase activities associated with both rat and human BBMs, in addition to the long-chain activity. Similarities between human BBM retinyl ester hydrolytic activities and those observed for rat BBMs suggest that the rat is a good model for humans in this step of vitamin A metabolism.

Adult↗
PubMed1984

Turn-over of phospholipids in Selenomonas ruminantium.

The particulate enzyme prepared from Selenomonas ruminantium subsp. lactilytica catalyzed the formation of phosphatidylserine (PS) from CDP-diglyceride and serine, and phosphatidylethanolamine (PE) from PS. This indicates that PS and PE in this organism are synthesized through a similar pathway to that in Escherichia coli. In turn-over experiments with [32P]orthophosphate and [14C]caproate, a rapid turn-over of PE was observed, while ethanolamine plasmalogen was relatively stable. The decrease of 14C-radioactivity in PE side-chains was accompanied by an increase of 14C-radioactivity in side-chains of ethanolamine plasmalogen. In pulse label-chase experiments with [32P]orthophosphate, significant amounts of 32P-radioactivities were incorporated into plasmalogens at the beginning of the chase and a precursor product relationship was observed between serine plasmalogen and ethanolamine plasmalogen. On the contrary, in pulse-label-chase experiments using [14C]caproate and [3H]glycerol, no significant radioactivity was incorporated into plasmalogens at the beginning of the chase and radioactivities in plasmalogens slowly increased during the chase. These results indicate that 1-O-alk-1'-enyl-2-acyl-glycerol moieties of plasmalogens are derived from a large precursor pool, but the phosphorous moiety is not. This concept was supported by the fact that synthesis of plasmalogens occurred in the absence of fatty acid synthesis. We wish to propose the possibility that 1-O-alk-1'-enyl-2-acyl-glycerol moieties of plasmalogens are derived from the diglyceride moieties of diacyl phospholipids.

CDPdiacylglycerol-Serine O-Phosphatidyltransferase↗
PubMed2004

Metabolic properties of Eubacterium pyruvativorans, a ruminal 'hyper-ammonia-producing' anaerobe with metabolic properties analogous to those of Clostridium kluyveri.

Eubacterium pyruvativorans I-6(T) is a non-saccharolytic, amino-acid-fermenting anaerobe from the rumen, isolated by its ability to grow on pancreatic casein hydrolysate (PCH) as sole C source. This study investigated its metabolic properties and its likely ecological niche. Additional growth was supported by pyruvate, vinyl acetate, and, to a lesser extent, lactate and crotonate, and also by a mixture of amino acids (alanine, glycine, serine and threonine) predicted to be catabolized to pyruvate. No single amino acid supported growth, and peptides were required for growth on amino acids. Alanine, followed by leucine, serine and proline, were used most extensively during growth, but only alanine and asparate were extensively modified before incorporation. Growth on PCH, but not on pyruvate, was increased by the addition of acetate, propionate and butyrate. l-Lactate was fermented incompletely, mainly to acetate, but no lactate-C was incorporated. Propionate and butyrate were utilized during growth, forming valerate and caproate, respectively. Labelling experiments suggested a metabolic pattern where two C atoms of butyrate, valerate and caproate were derived from amino acids, with the others being formed from acetate, propionate and butyrate. The metabolic strategy of E. pyruvativorans therefore resembles that of Clostridium kluyveri, which ferments ethanol only when the reaction is coupled to acetate, propionate or butyrate utilization. The fermentative niche of E. pyruvativorans appears to be to scavenge amino acids, lactate and possibly other metabolites in order to generate ATP via acetate formation, using volatile fatty acid elongation with C(2) units derived from other substrates to dispose of reducing equivalents.

Adenosine Triphosphate↗
PubMed1984

Isolation and partial characterization of bacteria in an anaerobic consortium that mineralizes 3-chlorobenzoic Acid.

A methanogenic consortium able to use 3-chlorobenzoic acid as its sole energy and carbon source was enriched from anaerobic sewage sludge. Seven bacteria were isolated from the consortium in mono- or coculture. They included: one dechlorinating bacterium (strain DCB-1), one benzoate-oxidizing bacterium (strain BZ-2), two butyrate-oxidizing bacteria (strains SF-1 and NSF-2), two H(2)-consuming methanogens (Methanospirillum hungatei PM-1 and Methanobacterium sp. strain PM-2), and a sulfate-reducing bacterium (Desulfovibrio sp. strain PS-1). The dechlorinating bacterium (DCB-1) was a gram-negative, obligate anaerobe with a unique "collar" surrounding the cell. A medium containing rumen fluid supported minimal growth; pyruvate was the only substrate found to increase growth. The bacterium had a generation time of 4 to 5 days. 3-Chlorobenzoate was dechlorinated stoichiometrically to benzoate, which accumulated in the medium; the rate of dechlorination was ca. 0.1 pmol bacterium day. The benzoate-oxidizing bacterium (BZ-2) was a gram-negative, obligate anaerobe and could only be grown as a syntroph. Benzoate was the only substrate observed to support growth, and, when grown in coculture with M. hungatei, it was fermented to acetate and CH(4). One butyrate-oxidizing bacterium (NSF-2) was a gram-negative, non-sporeforming, obligate anaerobe; the other (SF-1) was a gram-positive, sporeforming, obligate anaerobe. Both could only be grown as syntrophs. The substrates observed to support growth of both bacteria were butyrate, 2-dl-methylbutyrate, valerate, and caproate; isobutyrate supported growth of only the sporeforming bacterium (SF-1). Fermentation products were acetate and CH(4) (from butyrate, isobutyrate, or caproate) or acetate, propionate, and CH(4) (from 2-dl-methylbutyrate or valerate) when grown in coculture with M. hungatei. A mutualism among at least the dechlorinating, benzoate-oxidizing, and methane-forming members was apparently required for utilization of the 3-chlorobenzoate substrate.

Journal Article↗
PubMed2004

Polyhydroxyalkanoate (PHA) accumulation in sulfate-reducing bacteria and identification of a class III PHA synthase (PhaEC) in Desulfococcus multivorans.

Seven strains of sulfate-reducing bacteria (SRB) were tested for the accumulation of polyhydroxyalkanoates (PHAs). During growth with benzoate Desulfonema magnum accumulated large amounts of poly(3-hydroxybutyrate) [poly(3HB)]. Desulfosarcina variabilis (during growth with benzoate), Desulfobotulus sapovorans (during growth with caproate), and Desulfobacterium autotrophicum (during growth with caproate) accumulated poly(3HB) that accounted for 20 to 43% of cell dry matter. Desulfobotulus sapovorans and Desulfobacterium autotrophicum also synthesized copolyesters consisting of 3-hydroxybutyrate and 3-hydroxyvalerate when valerate was used as the growth substrate. Desulfovibrio vulgaris and Desulfotalea psychrophila were the only SRB tested in which PHAs were not detected. When total DNA isolated from Desulfococcus multivorans and specific primers deduced from highly conserved regions of known PHA synthases (PhaC) were used, a PCR product homologous to the central region of class III PHA synthases was obtained. The complete pha locus of Desulfococcus multivorans was subsequently obtained by inverse PCR, and it contained adjacent phaE(Dm) and phaC(Dm) genes. PhaC(Dm) and PhaE(Dm) were composed of 371 and 306 amino acid residues and showed up to 49 or 23% amino acid identity to the corresponding subunits of other class III PHA synthases. Constructs of phaC(Dm) alone (pBBRMCS-2::phaC(Dm)) and of phaE(Dm)C(Dm) (pBBRMCS-2::phaE(Dm)C(Dm)) in various vectors were obtained and transferred to several strains of Escherichia coli, as well as to the PHA-negative mutants PHB(-)4 and GPp104 of Ralstonia eutropha and Pseudomonas putida, respectively. In cells of the recombinant strains harboring phaE(Dm)C(Dm) small but significant amounts (up to 1.7% of cell dry matter) of poly(3HB) and of PHA synthase activity (up to 1.5 U/mg protein) were detected. This indicated that the cloned genes encode functionally active proteins. Hybrid synthases consisting of PhaC(Dm) and PhaE of Thiococcus pfennigii or Synechocystis sp. strain PCC 6308 were also constructed and were shown to be functionally active.

Acyltransferases↗
PubMed2002

Regulation of nap gene expression and periplasmic nitrate reductase activity in the phototrophic bacterium Rhodobacter sphaeroides DSM158.

Bacterial periplasmic nitrate reductases (Nap) can play different physiological roles and are expressed under different conditions depending on the organism. Rhodobacter sphaeroides DSM158 has a Nap system, encoded by the napKEFDABC gene cluster, but nitrite formed is not further reduced because this strain lacks nitrite reductase. Nap activity increases in the presence of nitrate and oxygen but is unaffected by ammonium. Reverse transcription-PCR and Northern blots demonstrated that the napKEFDABC genes constitute an operon transcribed as a single 5.5-kb product. Northern blots and nap-lacZ fusions revealed that nap expression is threefold higher under aerobic conditions but is regulated by neither nitrate nor ammonium, although it is weakly induced by nitrite. On the other hand, nitrate but not nitrite causes a rapid enzyme activation, explaining the higher Nap activity found in nitrate-grown cells. Translational nap'-'lacZ fusions reveal that the napK and napD genes are not efficiently translated, probably due to mRNA secondary structures occluding the translation initiation sites of these genes. Neither butyrate nor caproate increases nap expression, although cells growing phototrophically on these reduced substrates show a very high Nap activity in vivo (nitrite accumulation is sevenfold higher than in medium with malate). Phototrophic growth on butyrate or caproate medium is severely reduced in the NapA(-) mutants. Taken together, these results indicate that nitrate reduction in R. sphaeroides is mainly regulated at the level of enzyme activity by both nitrate and electron supply and confirm that the Nap system is involved in redox balancing using nitrate as an ancillary oxidant to dissipate excess reductant.

Arabidopsis Proteins↗
PubMed1993

Preparation and evaluation of fatty acid esters of 2-(4-hydroxyphenyl)-4,5-diphenylimidazole as fluorescent substrates for measurement of lipase activity.

A series of four aliphatic carboxylic acid esters (acetate, caproate, laurate and palmitate) of 2-(4-hydroxyphenyl)-4,5-diphenylimidazole (HDPI) was prepared. Usefulness of these esters as fluorescent substrates for the measurement of lipase activity was evaluated using a high performance liquid chromatographic method. The hydrolysate, HDPI, could be well separated from each substrate by a reversed-phase column and detected at 440 nm emission (cutoff-filter) with 360 nm excitation. Lipase from Candida cylindracea was used for the investigation. From their kinetic parameters, the caproate and laurate were found to be suitable for the lipase. Using the laurate, from 5 to 500 mU per assay tube of the lipase was determined.

Candida↗
PubMed1999

Characterization of a thermostable esterase activity from the moderate thermophile Bacillus licheniformis.

A new esterase activity from Bacillus licheniformis was characterized from an Escherichia coli recombinant strain. The protein was a single polypeptide chain with a molecular mass of 81 kDa. The optimum pH for esterase activity was 8-8.5 and it was stable in the range 7-8.5. The optimum temperature for activity was 45 degrees C and the half-life was 1 h at 64 degrees C. Maximum activity was observed on p-nitrophenyl caproate with little activity toward long-chain fatty acid esters. The enzyme had a KM of 0.52 mM for p-nitrophenyl caproate hydrolysis at pH 8 and 37 degrees C. The enzyme activity was not affected by either metal ions or sulfydryl reagents. Surprisingly, the enzyme was only slightly inhibited by PMSF. These characteristics classified the new enzyme as a thermostable esterase that shared similarities with lipases. The esterase might be useful for biotechnological applications such as ester synthesis.

Bacillus↗
PubMed2004

Progesterone treatment to prevent preterm birth.

The publication in 2003 of two large randomised trials of progesterone therapy to prevent preterm delivery has generated renewed interest in this treatment and has added substantial numbers of subjects to previously published small trials. The randomised trials of progestogens have generally shown efficacy in reducing the rate of recurrent preterm delivery in women with singleton pregnancies who were at high risk for preterm labour and delivery. Most of the successful trials have employed 17alpha-hydroxyprogesterone caproate, and one trial has reported positive results using progesterone vaginal suppositories. The administration of 17alpha-hydroxyprogesterone caproate or progesterone suppositories to women with these high-risk pregnancies showed a significant protective effect for preterm birth in six of the seven published trials. No successful trials of progestogens have been reported for women at risk for preterm delivery because of multiple gestations. Trials of progestogens after the occurrence of symptoms of labour have shown them to be ineffective in prolonging pregnancy.

Female↗
PubMedDate not supplied

[Effect of thiochrome capronate on lipid metabolism in rats].

Thiochrome caproate modified by the oxyethyl radical of the thiochrome derivative was studied for its effect on different indices of lipid metabolism in the liver and blood of albino rats. It was shown that when animals were fed on a standard laboratory diet, thiochrome caproate changed the amount of total and free fatty acids in the studied tissues and the fatty acid composition in the liver to a greater extent than thiochrome and hydroxythiamine.

Animals↗
PubMedDate not supplied

[Hormonal regulation of uterine contraction].

A personal method has been used to study spontaneous kinetic activity of the uterus in 50 women during puerperium following miscarriage between the VIIIth and XIIth weeks. Modifications induced were evaluated in several sessions (510 recordings) and at various periods of time, following administration of: 50 mg of 17B oestradiol, 200 mg natural progesterone, 500 mg of natural progesterone, 250 mg of 17 hydroxyprogesterone caproate and 500 mg of 17 hydroxyprogesterone caproate. In the case of some of the patients, hysterotonometry was evaluated following intravenous oxytocin loading. The results pointed to an activation of the uterine pacemaker after oestrogenic loading, and a clear-cut progestinic block of contractile activity.

Abortion, Spontaneous↗