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At least 703 records · Page 39Linked to original sources
PubMed2001

Locobase repair cream following CO2 laser skin resurfacing reduces interstitial fluid oozing.

BACKGROUND: The cosmetic result after laser resurfacing depends not only on the type of laser and the technique used, but also on post-treatment care. The efficacy of Locobase Repair((R)) cream, which improves skin barrier function due to its content of natural skin analogue fats and cholesterol, was investigated. METHODS: A total of 18 Caucasian patients underwent resurfacing for acne scars. Laser treatment was performed with a Sharplan 1020 CO(2) laser and a Silk Touch scanner. Locobase Repair cream (a water-in-oil cream with 63% lipids including natural components of stratum corneum: cholesterol, ceramide and free fatty acids) was applied daily to one side of the face and petrolatum was applied to the other. In addition, both sides were treated with a 2% fusidic acid cream. RESULTS: There was a significant reduction of oozing during the first 2 days after CO(2) laser treatment on the sides treated with Locobase Repair cream (p < 0.05), CO(2) laser while from day 3 to day 7 no differences were demonstrated between the Locobase Repair cream and petrolatum. For the other parameters scored (scaling, oedema, erythema and pain), no significant differences between Locobase Repair cream and petrolatum were found. Furthermore, no significant differences were found between the two creams regarding the duration of wound healing and final cosmetic outcome. In all, 62% of the patients preferred to use Locobase Repair cream during the postoperative period, and 11% preferred petrolatum. The remaining 27% expressed no preferences. CONCLUSION: The use of Locobase Repair cream as a post laser resurfacing treatment reduces tissue fluid oozing during the first 2 postoperative days, indicating a quick restoration of skin barrier and hence possibly a reduction in the incidence of wound infections as well as enhancing patient compliance due to less fluid oozing.

Acne Vulgaris↗
PubMed1979

Antibiotics and suppression of lymphocyte function in vitro.

The effects on the mitogenic response of human T lymphocytes were studied for 20 different antibiotics. No apparent inhibitory effect could be detected for penicillins, cephalosporins, aminoglycosides, chloramphenicol, sulfamethoxazole, trimethoprim, nalidixic acid, and 5-fluorocytosine. There were effects at high concentrations with erythromycin, clindamycin, and rifampin, and these antibiotics could also be shown to depress the mitogenic response of B lymphocytes. With fusidic acid, nitrofurantoin, and doxycycline there was an inhibiting effect at low concentrations on the mitogenic responses of B and T lymphocytes and on in vitro antibody production. Protein synthesis in unstimulated lymphocytes was also inhibited. Some antibiotics thus may impair the function of human lymphocytes in vitro.

Anti-Bacterial Agents↗
PubMed1995

Properties of hybrid active sites in oligomeric proteins: kinetic and ligand binding studies with chloramphenicol acetyltransferase trimers.

Alteration of the charge of surface lysyl residues of chloramphenicol acetyltransferase (CAT) by site-directed mutagenesis was used to increase the charge difference between the subunits of two naturally occurring enzyme variants (CATI and CATIII). The introduced charge change greatly facilitates the purification of CATI/CATIII and CATIII/CATIII hybrid trimers by ion-exchange chromatography. Hybrids containing only one functional active site per trimer were generated in vitro by reversible denaturation of mixtures of "active" subunits (retention of a catalytic histidine at position 195) and "inactive" subunits (with alanine replacing histidine 195). Such hybrids were used (1) to demonstrate that the previously observed novel binding of a steroidal antibiotic (fusidic acid) by CATI involves amino acid residues at each subunit interface and (2) to identify specific residues contributing to such interactions. A pre-steady-state kinetic characterization of homotrimers containing the H195A substitution also revealed that fusidate binding to CATI may, like chloramphenicol binding, involve a hydrogen bond with the catalytic histidine residue. In addition, confirmation of the fact that His-195 interacts with chloramphenicol in CATI as well as in CATIII makes it likely that it is essential for the catalytic mechanism of all naturally occurring variants of CAT, as first suggested by structural evidence for the type III enzyme (Leslie, 1990).

Acetyl Coenzyme A↗
PubMed1991

Changes in sensitivity of in vitro rat brain protein synthesis to the acute action of ethanol and isopropanol as a consequence of the long-term ingestion of isopropanol.

Long-term treatment of rats with isopropanol in the drinking water results in a change or process of adaptation occurring in in vitro brain protein synthesis which increases the resistance of the ribosomal machinery to the acute effect of either ethanol or isopropanol. Such an increase was observed both in the system coded by endogenous messenger and in the system coded by polyuridylic acid. In both translation systems, the adaptation seems to affect the ribosomal step of polypeptide chain elongation. The increase in resistance to the alkanols apparently did not affect the inhibitory action of puromycin, fusidic acid and cycloheximide on the ribosome.

Adaptation, Physiological↗
PubMed1988

Sensitivity of clinical isolates from German hospitals to amoxicillin/clavulanic acid (Augmentin) compared with other antibiotics.

17,244 pathogens isolated from clinical specimens of 24 hospitals in the Moers area (North-Rhine Westphalia, FRG) were tested in regard to their susceptibility to Augmentin (amoxicillin and clavulanic acid). For this purpose, minimal inhibitory concentrations were determined by use of microbroth dilution technique. 80% of Gram-negative, 98% of Gram-positive and 97% of anaerobic isolates were susceptible to Augmentin (breakpoint 4 mg/l amoxicillin in the presence of 2.5 mg/l clavulanic acid). In a second part of the study the susceptibility to Augmentin of 4.137 Gram-negative and 10.958 Gram-positive pathogens was compared to their sensitivity against benzylpenicillin, flucloxacillin, mezlocillin, erythromycin, clindamycin, fusidic acid, ampicillin, cefaclor and doxycyclin.

Amoxicillin↗
PubMed2001

Natural antibiotic susceptibility of recently established coryneform bacteria.

The natural susceptibility of 20 strains each of Brevibacterium casei (formerly CDC coryneform groups B-1 and B-3), Dermabacter hominis (formerly CDC coryneform groups 3 and 5), and Turicella otitidis (formerly coryneform group ANF-1-like) isolated from clinical specimens to 71 antibiotics was investigated. Susceptibility testing was carried out with a microdilution procedure using H medium. All three species were naturally sensitive to tetracyclines, most aminoglycosides, carbapenems, macrolides, lincosamides, glycopeptides, and rifampin. Susceptibility patterns indicating natural resistance to pipemidic acid, sulfamethoxazole, and cotrimoxazole also were found for all three species. Species-dependent discrepancies in susceptibility leading to completely different categorizations (changing from sensitive to resistant or vice versa) were found for some penicillins (e.g., oxacillin and amoxicillin), a few cephalosporins (e.g., ceftibutene), aztreonam, tobramycin, norfloxacin, fleroxacin, trimethoprim, nitrofurantoin, fosfomycin, and fusidic acid. For the majority of antibiotics, Brevibacterium casei was the least susceptible species and Turicella otitidis the most susceptible taxon. The present study describes a database on the natural susceptibility of Brevibacterium casei, Dermabacter hominis, and Turicella otitidis to a wide range of antibiotics. This database can be applied for the validation of susceptibility testing results of these recently established coryneform bacteria.

Actinomycetales↗
PubMed1973

Messenger ribonucleic acid synthesis and degradation in Escherichia coli during inhibition of translation.

Various aspects of the coupling between the movement of ribosomes along messenger ribonucleic acids (mRNA) and the synthesis and degradation of mRNA have been investigated. Decreasing the rate of movement of ribosomes along an mRNA does not affect the rate of movement of some, and possibly most, of the RNA polymerases transcribing the gene coding for that mRNA. Inhibiting translation with antibiotics such as chloramphenicol, tetracycline, or fusidic acid protects extant mRNA from degradation, presumably by immobilizing ribosomes, whereas puromycin exposes mRNA to more rapid degradation than normal. The promoter distal (3') portion of mRNA, synthesized after ribosomes have been immobilized by chloramphenicol on the promoter proximal (5') portion of the mRNA, is subsequently degraded.

Carbon Radioisotopes↗
PubMed1999

Outer membrane permeability barrier in Escherichia coli mutants that are defective in the late acyltransferases of lipid A biosynthesis.

The tight packing of six fatty acids in the lipid A constituent of lipopolysaccharide (LPS) has been proposed to contribute to the unusually low permeability of the outer membrane of gram-negative enteric bacteria to hydrophobic antibiotics. Here it is shown that the Escherichia coli msbB mutant, which elaborates defective, penta-acylated lipid A, is practically as resistant to a representative set of hydrophobic solutes (rifampin, fusidic acid, erythromycin, clindamycin, and azithromycin) as the parent-type control strain. The susceptibility index, i.e., the approximate ratio between the MIC for the msbB mutant and that for the parent-type control, was maximally 2.7-fold. In comparison, the rfa mutant defective in the deep core oligosaccharide part of LPS displayed indices ranging from 20 to 64. The lpxA and lpxD lipid A mutants had indices higher than 512. Furthermore, the msbB mutant was resistant to glycopeptides (vancomycin, teicoplanin), whereas the rfa, lpxA, and lpxD mutants were susceptible. The msbB htrB double mutant, which elaborates even-more-defective, partially tetra-acylated lipid A, was still less susceptible than the rfa mutant. These findings indicate that hexa-acylated lipid A is not a prerequisite for the normal function of the outer membrane permeability barrier.

Acyltransferases↗
PubMed2003

First synthesis of racemic saphenamycin and its enantiomers. investigation of biological activity.

The natural antibiotic saphenamycin, 6-[1-(2-hydroxy-6-methyl-benzoyloxy)-ethyl]-phenazine-1-carboxylic acid, was synthesized from saphenic acid using temporary allyl protection of carboxy and phenoxy functionalities. Resolution of racemic saphenic acid was performed by crystallization of the corresponding (-)-brucine diastereomeric salts and the absolute configuration of (-)-brucinium (-)-saphenate was determined by X-ray crystallography to have R-configuration. This also proved to be the configuration of natural saphenic acid. Enantiomers of saphenamycin were obtained from resolved saphenic acid and screened against a range of skin flora and resistant Staphylococcus aureus strains. Biological activities of saphenamycin enantiomers were compared with that of the synthetic racemate as well as earlier reported activities of saphenamycin isolated from natural sources. No significant difference was observed in activity of the enantiomers of saphenamycin, which revealed that the chirality of saphenamycin has no consequences for the antibiotic activity. Saphenamycin proved to be a potent antibiotic against fusidic acid and rifampicin resistant S. aureus strains showing MIC of 0.1-0.2 microg/mL.

Anti-Bacterial Agents↗
PubMed1981

Role of peptide chain elongation factor G in guanosine 5'-diphosphate 3'-diphosphate synthesis.

In a wild-type strain (relA+) of Escherichia coli, starvation of amino acid led to an immediate cessation of the synthesis of stable ribonucleic acids, together with the accumulation of an unusual nucleotide, guanosine 5'-diphosphate 3'-diphosphate, commonly known as ppGpp. This compound also accumulated during heat shock. When temperature-sensitive protein synthesis elongation factor G (EF-G) was introduced into E. coli NF859, a relA+ strain, the synthesis of ppGpp was reduced to approximately one-half that of wild-type EF-G+ cells at a nonpermissive temperature of 40 degrees C. Furthermore, fusidic acid, an inhibitor of protein synthesis which specifically inactivates EF-G, prevented any accumulation of ppGpp during the heat shock. We suggest that a functional EF-G protein is necessary for ppGpp accumulation under temperature shift conditions, possibly by mediating changes in the function of another protein, the relA gene product. However, EF-G is probably not required for the synthesis of ppGpp during the stringent response, since its inactivation did not prevent ppGpp accumulation during amino acid starvation.

Amino Acids↗
PubMed1998

Elongation factor 2 as a novel target for selective inhibition of fungal protein synthesis.

Elongation factor 2 (EF2) is an essential protein catalyzing ribosomal translocation during protein synthesis and is highly conserved in all eukaryotes. It is largely interchangeable in translation systems reconstituted from such divergent organisms as human, wheat, and fungi. We have identified the sordarins as selective inhibitors of fungal protein synthesis acting via a specific interaction with EF2 despite the high degree of amino acid sequence homology exhibited by EF2s from various eukaryotes. In vitro reconstitution assays using purified components from human, yeast, and plant cells demonstrate that sordarin sensitivity is dependent on fungal EF2. Genetic analysis of sordarin-resistant mutants of Saccharomyces cerevisiae shows that resistance to the inhibitor is linked to the genes EFT1 and EFT2 that encode EF2. Sordarin blocks ribosomal translocation by stabilizing the fungal EF2-ribosome complex in a manner similar to that of fusidic acid. The fungal specificity of the sordarins, along with a detailed understanding of its mechanism of action, make EF2 an attractive antifungal target. These findings are of particular significance due to the need for new antifungal agents.

Antifungal Agents↗
PubMed1975

Chemical and physical studies on the structure of Escherichia coli elongation factor G.

Elongation Factor G (EF-G) from Escherichia coli was purified to homogenity by a previously published method (Rohrbach, M. S., Dempsey, M. E., and Bodley, J. W. (1974) J. Biol. Chem. 249, 5094). The protein is composed of a single polypeptide chain of molecular weight 74,000 under native conditions and 71,000 under denatured conditions as determined by high speed equilibrium centrifugation. An apparent molecular weight of 73,000 was found by sodium dodecyl sulfate gel electrophoresis. The protein has an apparent alpha helix content of 34% as determined from its circular dichroism spectrum. The extinction coefficient at 280 nm was found to be 62,200 M-1 cm-1. Lysine is the COOH-terminal residue and the sequence at the NH2 terminus is alanylarginine. No evidence of terminal heterogeneity was observed. The amino acid composition of EF-G revealed no unusual amino acids or prosthetic groups, but was notable in that the protein contains only 6 cysteine residues. The maintenance of at least one of these cysteines in the reduced form is essential for activity, since the protein is rapidly inactivated upon removal of protecting thiol. Under some conditions, activity can be partly restored by re-addition of a thiol. The per cent activity of the protein was examined by an active site titration, the formation of the EF-G-ribosome-GDP-fusidic acid complex. The formation of 1 mol of complex/mol of EF-G showed that the protein is 100% active.

Amino Acids↗
PubMed1993

Interaction between cholephilic anions and bile acid transport across basal membrane of human trophoblast.

The sensitivity of radiolabeled bile acid (BA) binding and transport by basal plasma membrane (BPM) vesicles of human trophoblast to cholephilic organic anions (COAs) was studied by a rapid filtration technique. Glycocholate (GC) efflux from preloaded (15 microM GC) vesicles was investigated in the presence of 300 microM COAs at the trans-side of the membrane. Bilirubin (BR) diglucuronide and rose bengal induced a very strong transstimulating effect, whereas phalloidin and phenol red showed a negligible effect. This effect was from strong to moderate for indocyanine green > bromosulfophthalein (BSP) > or = fusidic acid > or = phenolphthalein > or = BR ditaurate > or = rifamycin SV > or = rifampicin. BSP-induced transstimulation was not additive to the "velocity effect" previously reported for bicarbonate. At the cis-side, BSP reduced the saturable component of taurocholate (TC) binding to BPM vesicles. BSP also induced a partial and mixed type of inhibition both in TC uptake [inhibitor constant (Ki) 227 microM] and efflux (Ki 209 microM). Two binding sites with overlapping specificity for BAs and other COAs are proposed in this carrier, the site for non-BA COA presumably corresponding to that for bicarbonate. In summary, the results indicate that several COAs can act as potential substrates for the BA carrier located at the BPM of human trophoblast. This stresses the "biliary-like" role of the placenta and suggests the possibility of developing new functional tests for this organ on the basis of fetal-maternal transfer of nontoxic cholephilic dyes.

Anions↗
PubMed2005

Interfacial inhibitors of protein-nucleic acid interactions.

This essay develops the paradigm of "Interfacial Inhibitors" (Pommier and Cherfils, TiPS, 2005, 28: 136) for inhibitory drugs beside orthosteric (competitive or non-competitive) and allosteric inhibitors. Interfacial inhibitors bind with high selectivity to a binding site involving two or more macromolecules within macromolecular complexes undergoing conformational changes. Interfacial binding traps (generally reversibly) a transition state of the complex, resulting in kinetic inactivation. The exemplary case of interfacial inhibitor of protein-DNA interface is camptothecin and its clinical derivatives. We will also provide examples generalizing the interfacial inhibitor concept to inhibitors of topoisomerase II (anthracyclines, ellipticines, epipodophyllotoxins), gyrase (quinolones, ciprofloxacin, norfloxacin), RNA polymerases (alpha-amanitin and actinomycin D), and ribosomes (antibiotics such as streptomycin, hygromycin B, tetracycline, kirromycin, fusidic acid, thiostrepton, and possibly cycloheximide). We discuss the implications of the interfacial inhibitor concept for drug discovery.

Animals↗
PubMed2003

Curative effects of sodium fusidate on the development of dinitrobenzenesulfonic acid-induced colitis in rats.

Fusidic acid and sodium fusidate (fusidin) are antibiotics with low toxicity and powerful immunomodulatory activities in vitro and in vivo. In this study we have evaluated the effect of fusidin on the development of dinitrobenzenesulfonic acid (DNB)-induced colitis in rats that serves as a preclinical model of human inflammatory bowel disease (IBD). The data show that when administered orally at the dose of 80 (but not 40) mg/kg body wt under a "therapeutic" regimen soon after DNB application, fusidin significantly ameliorates clinical, histological, and seroimmunological signs of disease. These entailed a significant reduction in body weight loss, smaller increase in colon weights, milder macroscopic damage, and lower histological scores. In addition, when sacrificed at the end of the study, fusidin-treated rats had significantly lower blood levels of tumor necrosis factor alpha and interferon-gamma compared with untreated controls. The present findings concur with the beneficial actions of fusidin in a pilot study conducted in patients with Crohn's disease and warrant controlled studies in humans with IBD.

Administration, Oral↗
PubMed1994

Hepatic side-effects of antibiotics.

Although the liver is particularly exposed to drugs and their metabolites, hepatic side-effects of antibiotics are far less frequent than other adverse effects such as gastrointestinal disorders or cutaneous reactions. However, the potential severity of hepatic side-effects for some drugs is stressed. Antibiotic related liver injuries cover most of the clinical and pathological expressions of hepatic dysfunction, including cytotoxic hepatitis (isoniazid), intrahepatic cholestasis (macrolides, penicillins, clavulanic acid), mixed hepatitis (sulphonamides), chronic active hepatitis (nitrofurantoin), or microvesicular steatosis (tetracycline). In most cases, toxicity is idiosyncratic, reactions occurring only in some susceptible individuals. The mechanisms underlying toxicity may be primarily metabolite-dependent (isoniazid), hypersensitivity-mediated (beta-lactams), or result from both processes (sulphonamides, erythromycin derivatives). In some cases, the liver is not the primary target organ for toxicity but appears to mediate the clinical expression of some adverse effects induced by antibiotics. The most significant example of this is hypoprothrombinaemia due to the inhibition of hepatic gamma-carboxylation of vitamin K-dependent clotting factors by sulphydryl group-containing cephalosporins. Inhibition of bilirubin conjugation or transport by rifampicin or fusidic acid may also be viewed as hepatic side-effects of antibiotics. Ascertaining the casual relationship of a given drug to an hepatic adverse effect may prove particularly difficult, because of the potential contribution of host status and concurrent medications. Diagnosis is based mainly on circumstantial evidence, i.e. the temporal relationship between drug administration (or withdrawal) and the time-course of liver dysfunction. Improving morbidity related to drug hepatotoxicity relies on a free flow of information between manufacturers and practitioners in order to optimize detection of potentially serious liver damage, and advances in pharmacogenetics toward a better identification of those at particular risk for developing drug-related liver toxicity.

Animals↗
PubMed2005

Antibiotic susceptibility profiles of new probiotic Lactobacillus and Bifidobacterium strains.

The antimicrobial susceptibilities and presence of plasmids in four new probiotic lactic acid bacteria (LAB) strains, Lactobacillus rhamnosus HN001 (DR20) HN067, Lactobacillus acidophilus HN017 and Bifidobacterium lactis HN019 (DR10), were determined. Resistance to 18 commonly used antibiotics was assessed by disk diffusion. The three Lactobacillus strains had similar antibiotic susceptibility profiles to those of Lactobacillus plantarum strain HN045 and two commercial probiotic Lactobacillus strains, GG and LA-1. The B. lactis strain HN019 had a similar profile to three commercial probiotic B. lactis strains (Bb12, HN049 and HN098). All 10 strains were sensitive to the Gram-positive spectrum antibiotics erythromycin and novobiocin, the broad-spectrum antibiotics rifampicin, spectinomycin, tetracycline and chloramphenicol and the beta-lactam antibiotics penicillin, ampicillin and cephalothin. By contrast, most strains were resistant to the Gram-negative spectrum antibiotics fusidic acid, nalidixic acid and polymyxin B and the aminoglycosides neomycin, gentamicin, kanamycin and streptomycin. All three L. rhamnosus strains (HN001, HN067 and GG) were resistant to vancomycin and several strains were also resistant to cloxacillin. Of the four new probiotic strains, only L. rhamnosus HN001 contained plasmids; however, a plasmid-free derivative of HN001 had the same antibiotic susceptibility profile as the parent strain.

Anti-Bacterial Agents↗
PubMed2006

Characterization of a high-throughput screening assay for inhibitors of elongation factor p and ribosomal peptidyl transferase activity.

Elongation Factor P (EF-P) is an essential component of bacterial protein synthesis, enhancing the rate of translation by facilitating the addition of amino acids to the growing peptide chain. Using purified Staphylococcus aureus EF-P and a reconstituted Escherichia coli ribosomal system, an assay monitoring the addition of radiolabeled N-formyl methionine to biotinylated puromycin was developed. Reaction products were captured with streptavidin-coated scintillation proximity assay (SPA) beads and quantified by scintillation counting. Data from the assay were used to create a kinetic model of the reaction scheme. In this model, EF-P binding to the ribosome essentially doubled the rate of the ribosomal peptidyl transferase reaction. As described here, EF-P bound to the ribosomes with an apparent K(a) of 0.75 microM, and the substrates N-fMet-tRNA and biotinylated puromycin had apparent K(m)s of 19 microM and 0.5 microM, respectively. The assay was shown to be sensitive to a number of antibiotics known to target ribosomal peptide bond synthesis, such as chloramphenicol and puromycin, but not inhibitors that target other stages of protein synthesis, such as fusidic acid or thiostrepton.

Anti-Bacterial Agents↗