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PubMedDate not supplied

[Multiplication of Listeria in milk products].

The results of the evaluation of the multiplication dynamics of Listeria cells in milk and Bifidok, a lactic acid product, are presented. The samples were inoculated on thioglycol agar and studied at different exposure time after incubation at 37 degrees C, 20 degrees C and 4 degrees C. The study revealed the intensive multiplication of Listeria cells in milk, also during storage in a household refrigerator. The presence of bifidobacteria mixed with kefir-producing culture in dairy products was shown to essentially inhibit the growth of Listeria cells which were not detected by bacteriological techniques on day 7.

Bifidobacterium↗
PubMed1974

Cultivation and maintenance of Sphaerophorus necrophorus. I. An anaerobic medium for aerobic incubation.

Out of 185 media formulated and studied for the growth of Sphaerophorus necrophorus, ten were selected for intensive investigation. Their ability to promote growth was compared photometrically. Medium 156 made up of Brewer's thioglycollate broth, yeast extract, L-cystine, and ascorbic acid, was found to yield a very heavy growth. The viability of S. necrophorus was maintained indefinitely by weekly subcultures. When not subcultured, all isolates remained viable for fifteen weeks and some isolates for 30 weeks at 37 degrees C.Twenty-nine isolates were tested. No variation in maximum growth was noticed. Medium 156 is an optimum medium for S. necrophorus. It can be incubated aerobically without interfering with maximum growth. The medium does not deteriorate when stored for at least 12 weeks at room temperature.

Aerobiosis↗
PubMed1997

(-)-Epigallocatechin-3-gallate blocks the induction of nitric oxide synthase by down-regulating lipopolysaccharide-induced activity of transcription factor nuclear factor-kappaB.

Nitric oxide (NO) plays an important role in inflammation and multiple stages of carcinogenesis. We investigated the effect of various tea polyphenols and caffeine on the induction of NO synthase (NOS) in thioglycollate-elicited and lipopolysaccharide (LPS)-activated peritoneal macrophages. Gallic acid (GA), (-)-epigallocatechin (EGC), and (-)-epigallocatechin-3-gallate (EGCG), the major tea catechin, were found to inhibit inducible NOS (iNOS) protein in activated macrophages. EGCG, a potent antitumor agent with anti-inflammatory and antioxidant properties, inhibited NO generation, as measured by the amount of nitrite released into the culture medium. Inhibition of NO production was observed when cells were cotreated with EGCG and LPS. iNOS activity in soluble extracts of lipopolysaccharide-activated macrophages treated with EGCG (5 and 10 microM) for 6-24 hr was significantly lower than that in macrophages without EGCG treatment. Western blot, reverse transcription-polymerase chain reaction, and Northern blot analyses demonstrated that significantly reduced 130-kDa protein and 4.5-kb mRNA levels of iNOS were expressed in lipopolysaccharide-activated macrophages with EGCG compared with those without EGCG. Electrophoretic mobility shift assay indicated that EGCG blocked the activation of nuclear factor-kappaB, a transcription factor necessary for iNOS induction. EGCG also blocked disappearance of inhibitor kappaB from cytosolic fraction. These results suggest that EGCG decreases the activity and protein levels of iNOS by reducing the expression of iNOS mRNA and the reduction could occur through prevention of the binding of nuclear factor-kappaB to the iNOS promoter, thereby inhibiting the induction of iNOS transcription.

Animals↗
PubMed1965

Separation of acid and neutral proteinases of brain.

1. Cerebral proteinases were separated on Sephadex G-100 columns into acid and neutral fractions free from cross-contamination. Acid proteinases were more stable and were purified by additional steps with salt and pH5.0 precipitations, column chromatography on DEAE- or CM-cellulose and free-flow electrophoresis. 2. The separation made it possible to study the properties of the partially purified enzyme fractions. Some of these properties, such as K(m) with selected protein substrates, pH optima and temperature-dependence in the presence and absence of substrates, are described. 3. No requirement for metal ions or added cofactors was demonstrated. Neutral-proteinase activity was more sensitive to inhibition by heavy-metal ions; its activity could be increased by thioglycollate and glutathione, and inhibited by thiol reagents. Neutral and acid proteinases were inhibited by the chymotrypsin inhibitor chloromethyl l-2-phenyl-1-toluene-p-sulphonamidoethyl ketone. 4. In the presence of the appropriate synthetic substrates no cathepsin A activity was found, and only trace quantities of cathepsin B or C activities, which were more than 50-fold less than cathepsin D-like activity.

Journal Article↗
PubMed2000

Involvement of resident macrophages and mast cells in the writhing nociceptive response induced by zymosan and acetic acid in mice.

Intraperitoneal administration of zymosan and acetic acid induced a dose-dependent nociceptive writhing response in mice. Lavage of the peritoneal cavities with saline reduced the number of total resident peritoneal cells and caused a proportional decrease in the nociceptive responses induced by these stimuli. Furthermore, the specific reduction of the peritoneal mast cell population by intraperitoneal administration of compound 48/80 also reduced the nociceptive responses induced by zymosan and acetic acid. In contrast, enhancement of the peritoneal macrophage population by pretreatment of the cavities with thioglycollate caused an increase in the number of writhes induced by both stimuli. These data suggest that the nociceptive responses induced by zymosan and acetic acid are dependent upon the peritoneal resident macrophages and mast cells. These cells modulate the nociceptive response induced by zymosan and acetic acid via release of tumour necrosis factor alpha (TNF-alpha), interleukin 1beta and interleukin 8. This suggestion is supported by the following observations: (a) pretreatment of the peritoneal cavities with antisera against these cytokines reduced the nociceptive responses induced by these stimuli; (b) peritoneal cells harvested from cavities injected with zymosan or acetic acid released both interleukin 1beta and TNF-alpha; (c) although individual injection of TNF-alpha, interleukin 1beta or interleukin 8 did not induce the nociceptive effect, intraperitoneal injection of a mixture of these three recombinant cytokines caused a significant nociceptive writhing response. In conclusion, our results suggest that the nociceptive activity of zymosan and acetic acid in the writhing model is due to the release of TNF-alpha, interleukin 1beta and interleukin 8 by resident peritoneal macrophages and mast cells.

Acetic Acid↗
PubMed1975

Conversion of agroclavine to setoclavine and isosetoclavine in cell-free extracts from Claviceps sp. SD 58 and in a thioglycolate-iron (II) system.

Agroclavine was converted to setoclavine and isosetoclavine in crude extracts from Claviceps sp. SD 58. The ratio of setoclavine to isosetoclavine was 0.95. The conversion with boiled crude extract was 68% of the conversion with unboiled extract. In a thioglycolate-iron (II) system at 40 degrees for 5 hr, 45.5% of agroclavine was converted to setoclavine and isosetoclavine. At 70 degrees for 4 hr in the thioglycolate-iron (II) system, 4% of 4-dimethylallyltryptophan was converted to clavicipitic acid.

Alkaloids↗
PubMed1992

Modulation of macrophage procoagulant activity by arachidonic acid metabolites.

Macrophage (M phi)-mediated fibrin deposition via induction of procoagulant activity (PCA) is an important component of the host response during various infections. While endotoxin (LPS) is a well-known stimulus of PCA, the factors modulating its activity within the inflammatory microenvironment are unknown. The purpose of these studies was to determine the relative roles of two pathways of arachidonic acid metabolism, i.e., the cyclooxygenase (CO) and 5-lipoxygenase (5-LO) pathways, in modulating M phi PCA induction by LPS. Thioglycolate-elicited murine peritoneal M phi were treated with the CO inhibitor indomethacin (INDO), the 5-LO inhibitor nordihydroguaiaretic acid (NDGA), or control vehicle for 15 min prior to a 4-hr exposure to LPS (10 micrograms/ml). The ability of M phi to shorten the clotting time of plasma (i.e., PCA) was measured and clotting times were converted to PCA units via a thromboplastin standard. While CO blockade had no effect on PCA induction by LPS (without INDO 30 microM 446 +/- 131, with INDO 30 microM 546 +/- 193, mU/2 x 10(6) cells, n = 4), NDGA caused a dose-dependent inhibition (IC50 = 3 microM) without affecting cell viability (without NDGA 3 microM 446 +/- 131, with NDGA 3 microM 191 +/- 67, mU/2 x 10(6) cells, n = 6, P less than 0.05). Induction of PCA by Escherichia coli was similarly inhibited (E. coli 10(6) alone = 518 +/- 130; with NDGA 3 microM = 234 +/- 100, n = 2). Combined NDGA/INDO reduced PCA comparable to NDGA alone, ruling out the possibility that NDGA acted through generation of inhibitory prostanoids like PGE2.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1979

Insensitivity of the ferritin iron core to heat treatment.

To test whether the reactivity of ferritin iron is affected by the heat treatment used in ferritin isolation, we prepared ferritin from the same horse spleen with or without heating. Both samples exhibited similar reactivity upon reduction or chelation of iron.

Animals↗
PubMed2002

Egg-based media for delayed processing of nasopharyngeal swabs in colonization studies of Streptococcus pneumoniae.

This report describes the development and evaluation of a selective egg-based medium for ambient-temperature storage and transport of nasopharyngeal (NP) swabs in colonization studies of Streptococcus pneumoniae. Egg-thioglycolate-antibiotic (ETA) medium is based on Dorset's egg medium but made with thioglycolate broth and the addition of gentamicin (3 mg/l), nalidixic acid (15 mg/l), and amphotericin B (2.5 mg/l). Laboratory studies were conducted using mock swabs from 34 NP samples with known colony counts of pneumococci, which had previously been frozen in STGG (skim milk, tryptone, glucose, glycerol) broth. ETA facilitated better recovery of pneumococci than did either Stuart's or Amies' transport media. In a field study of 117 children, NP swabs were placed in ETA, after being vortexed in STGG and direct-plated for colony counts. Of 52 swabs that were culture positive for pneumococci, all 52 grew pneumococci after 4 days of storage in ETA, and 49 isolates were recovered after 7 days. Transport media such as Stuart's and Amies' require the processing of swabs within about 24 h, and storage in STGG broth requires freezing at -70 degrees C. ETA should be a useful addition to the storage media available for use in epidemiological studies of pneumococcal colonization, especially in situations where prompt processing, rapid transport, or low-temperature storage are not possible.

Anti-Bacterial Agents↗
PubMed1995

Determinant of bacterial translocation in the newborn: small bowel versus large bowel colonization.

This study investigated the relationship between bacterial translocation (BT) and small and large bowel bacterial colonization in the neonatal rabbit. The authors have previously shown that spontaneous BT occurs in rabbits during the first week of life, but is less frequent before the third day of life. The authors have also shown that bacterial colonization of the small bowel, is delayed until 3 to 5 days of age, and is preceded by colonization of the large bowel. Therefore, the authors hypothesizes that BT is dependent on small bowel, not large bowel, colonization. New Zealand White rabbit pups (n = 255) were divided into four groups, formula-fed (FF), formula-fed plus antibiotic (FFAB), breast-fed (BF) and unfed controls (UC). Animals from each group were killed on day 1 to 4 of life. Small bowel (SB) and large bowel (LB) specimens, mesenteric lymph nodes (MLN), spleen (SPL), and liver (LIV) were obtained from each rabbit, incubated for 24 hours in thioglycolate broth, and plated on both MacConkey and Colistin Naladixic Acid media in an aerobic environment. After 24 hours, growth on either plate was recorded. Bacterial colonization was significantly greater in FF versus UC, BF, and FFAB rabbit groups. In addition, large bowel colonization was significantly increased compared with small bowel colonization in all feeding groups (P < .05). Bacterial translocation to MLN, SPL, and LIV ranged from 10% to 27% in all groups. Gram-negative bacteria predominated over gram-positive bacteria in translocation to the various tissues sampled.(ABSTRACT TRUNCATED AT 250 WORDS)

Age Factors↗
PubMed2005

Neutrophil accumulation promotes intimal hyperplasia after photochemically induced arterial injury in mice.

The role of leukocytes in the pathogenesis of coronary arterial disease has become a focus for clinical research. The aim of this study was to determine whether neutrophil accumulation would participate in the development of intimal hyperplasia after endothelial injury in mice, and whether d-myo-inositol hexakisphosphate (phytic acid) which inhibits the binding of L- and P-selectin to sialyl Lewis(X) could inhibit the development of intimal hyperplasia. Endothelial injury was inflicted in one femoral artery via the photochemical reaction between systemically injected rose bengal and transillumination with green light (wavelength: 540 nm). Scanning electron microscopic observation at 3 days after the injury showed an increase in the number of leukocytes adhering to the injury site. Histological observation at 21 days showed that in the neutropenia group administered anti-neutrophil antibody and in the phytic acid-treated group the progression of intimal hyperplasia was significantly attenuated by comparison with the corresponding control groups. These results suggest that neutrophil accumulation contributes to the initiation and/or development of intimal hyperplasia and L- and/or P-selectin may participate in their mechanisms.

Animals↗
PubMed2006

The effects of oral Cardax (disodium disuccinate astaxanthin) on multiple independent oxidative stress markers in a mouse peritoneal inflammation model: influence on 5-lipoxygenase in vitro and in vivo.

Disodium disuccinate astaxanthin ('rac'-dAST; Cardax) is a water-dispersible C40 carotenoid derivative under development for oral and parenteral administration for cardioprotection of the at-risk ischemic cardiovascular patient. In experimental infarction models in animals (rats, rabbits, and dogs), significant myocardial salvage has been obtained, up to 100% at the appropriate dose in dogs. The documented mechanism of action in vitro includes direct scavenging of biologically produced superoxide anion; in vivo in rabbits, modulation of the complement activity of serum has also been shown. A direct correlation between administration of the test compound in animals and reductions of multiple, independent markers of oxidative stress in serum was recently obtained in a rat experimental infarction model. For the current study, it was hypothesized that oral Cardax administration would inhibit oxidative damage of multiple relevant biological targets in a representative, well-characterized murine peritoneal inflammation model. A previously developed mass spectrometry-based (LC/ESI/MS/MS) approach was used to interrogate multiple distinct pathways of oxidation in a black mouse (C57/BL6) model system. In vivo markers of oxidant stress from peritoneal lavage samples (supernatants) were evaluated in mice on day eight (8) after treatment with either Cardax or vehicle (lipophilic emulsion without drug) orally by gavage at 500 mg/kg once per day for seven (7) days at five (5) time points: (1) baseline prior to treatment (t=0); (2) 16 h following intraperitoneal (i.p.) injection with thioglycollate to elicit a neutrophilic infiltrate; (3) 4 h following i.p. injection of yeast cell wall (zymosan; t=16 h/4 h thioglycollate+zymosan); (4) 72 h following i.p. injection with thioglycollate to elicit monocyte/macrophage infiltration; and (5) 72 h/4 h thioglycollate+zymosan. A statistically significant sparing effect on the arachidonic acid (AA) and linoleic acid (LA) substrates was observed at time points two and five. When normalized to the concentration of the oxidative substrates, statistically significant reductions of 8-isoprostane-F(2alpha) (8-iso-F(2alpha)) at time point three (maximal neutrophil recruitment/activation), and 5-HETE, 5-oxo-EET, 11-HETE, 9-HODE, and PGF(2alpha) at time point five (maximal monocyte/macrophage recruitment/activation) were observed. Subsequently, the direct interaction of the optically inactive stereoisomer of Cardax (meso-dAST) with human 5-lipoxygenase (5-LOX) was evaluated in vitro with circular dichroism (CD) and electronic absorption (UV/Vis) spectroscopy, and subsequent molecular docking calculations were made using mammalian 15-LOX as a surrogate (for which XRC data has been reported). The results suggested that the meso-compound was capable of interaction with, and binding to, the solvent-exposed surface of the enzyme. These preliminary studies provide the foundation for more detailed evaluation of the therapeutic effects of this compound on the 5-LOX enzyme, important in chronic diseases such as atherosclerosis, asthma, and prostate cancer in humans.

Animals↗
PubMed1972

Two benzaldehyde dehydrogenases in bacterium N.C.I.B. 8250. Distinguishing properties and regulation.

Evidence is presented for the existence in bacterium N.C.I.B. 8250 of two inducible NAD(+)-linked benzaldehyde dehydrogenases. They may be distinguished in crude extracts by their different thermal stabilities at high pH values, benzaldehyde dehydrogenase I being much more heat-stable than benzaldehyde dehydrogenase II. Only benzaldehyde dehydrogenase I is activated by K(+) and certain other univalent cations. Gel-filtration experiments indicate that both enzymes have molecular weights of about 180000. Both enzymes are induced by growth on l-mandelate or phenylglyoxylate; only benzaldehyde dehydrogenase I is gratuitously induced by thiophenoxyacetate and only benzaldehyde dehydrogenase II is induced by benzyl alcohol, by benzaldehyde, and by a number of heterocyclic compounds which do not support growth. Mutants have been isolated that lack either benzaldehyde dehydrogenase II or benzyl alcohol dehydrogenase, or both of the enzymes. Results obtained in induction experiments with the wild-type bacterium N.C.I.B. 8250 and with the mutants show that benzaldehyde dehydrogenase II and benzyl alcohol dehydrogenase are co-ordinately regulated. Overall, the results suggest that benzaldehyde dehydrogenase I is associated with the metabolism of l-mandelate whereas benzaldehyde dehydrogenase II is associated with the metabolism of benzyl alcohol.

Alcaligenes↗
PubMed2001

Protein tyrosine nitration in mouse peritoneal macrophages activated in vitro and in vivo: evidence against an essential role of peroxynitrite.

Tyrosine nitration is considered a key reaction of peroxynitrite-triggered tissue injury in inflammatory diseases. We investigated the potential involvement of peroxynitrite in protein tyrosine nitration in isolated murine peritoneal macrophages activated either in vitro with interferon-gamma/lipopolysaccharide or in vivo by priming mice with Corynebacterium parvum (10 mgxkg-1). Both protocols led to release of NO and accumulation of nitrite accompanied by formation of protein-bound 3-nitrotyrosine. Oxidation of dihydrorhodamine 123, a measure of peroxynitrite release, remained close to basal levels upon in vitro activation of the macrophages but was increased approximately twofold in vivo. Tyrosine nitration in macrophages activated in vitro was inhibited by catalase and the time course of nitration correlated with nitrite accumulation, whereas superoxide (O2*-) and H2O2 release occurred at much earlier times. To address the contribution of O2*- and peroxynitrite to in vivo nitration, a O2*- scavenger (MnTBAP; 1 mgxkg-1) was given to C. parvum-primed mice. MnTBAP led to almost complete inhibition of C. parvum-triggered O2*- and peroxynitrite release, whereas nitrite accumulation and formation of 3-nitrotyrosine were less affected ( approximately 50% of controls). These results argue against an essential role of peroxynitrite in protein tyrosine nitration in vivo.

Animals↗