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chloramphenicol |
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CHEBI:17698 |
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An organochlorine compound that is dichloro-substituted acetamide containing a nitrobenzene ring, an amide bond and two alcohol functions. |
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This entity has been manually annotated by the ChEBI Team.
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CHEBI:13965, CHEBI:47327, CHEBI:3603, CHEBI:23106, CHEBI:23108
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ChemicalBook:CB3364529, ChemicalBook:CB34796861, eMolecules:29538748, eMolecules:490388, Selleckchem:Chloramphenicol(Chloromycetin), ZINC000000113382 |
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Molfile
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SDF
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more structures >>
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Chloramphenicol is an antibiotic useful for the treatment of a number of bacterial infections. This includes use as an eye ointment to treat conjunctivitis. By mouth or by injection into a vein, it is used to treat meningitis, plague, cholera, and typhoid fever. Its use by mouth or by injection is only recommended when safer antibiotics cannot be used. Monitoring both blood levels of the medication and blood cell levels every two days is recommended during treatment.
Common side effects include bone marrow suppression, nausea, and diarrhea. The bone marrow suppression may result in death. To reduce the risk of side effects treatment duration should be as short as possible. People with liver or kidney problems may need lower doses. In young infants, a condition known as gray baby syndrome may occur which results in a swollen stomach and low blood pressure. Its use near the end of pregnancy and during breastfeeding is typically not recommended. Chloramphenicol is a broad-spectrum antibiotic that typically stops bacterial growth by stopping the production of proteins.
Chloramphenicol was discovered after being isolated from Streptomyces venezuelae in 1947. Its chemical structure was identified and it was first synthesized in 1949. It is on the World Health Organization's List of Essential Medicines. It is available as a generic medication. |
Read full article at Wikipedia
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InChI=1S/C11H12Cl2N2O5/c12- 10(13) 11(18) 14- 8(5- 16) 9(17) 6- 1- 3- 7(4- 2- 6) 15(19) 20/h1- 4,8- 10,16- 17H,5H2,(H,14,18) /t8- ,9- /m1/s1 |
WIIZWVCIJKGZOK-RKDXNWHRSA-N |
C1=C([C@H]([C@H](NC(C(Cl)Cl)=O)CO)O)C=CC(=C1)[N+]([O-])=O |
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Mycoplasma genitalium
(NCBI:txid2097)
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Binds L16 protein of the 50S ribosomal subunit and inhibits amino acid transfer to growing peptide chains
See:
PubMed
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Escherichia coli
(NCBI:txid562)
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See:
PubMed
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antimicrobial agent
A substance that kills or slows the growth of microorganisms, including bacteria, viruses, fungi and protozoans.
Escherichia coli metabolite
Any bacterial metabolite produced during a metabolic reaction in Escherichia coli.
protein synthesis inhibitor
A compound, usually an anti-bacterial agent or a toxin, which inhibits the synthesis of a protein.
antibacterial drug
A drug used to treat or prevent bacterial infections.
Mycoplasma genitalium metabolite
Any bacterial metabolite produced during a metabolic reaction in Mycoplasma genitalium.
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antibacterial drug
A drug used to treat or prevent bacterial infections.
geroprotector
Any compound that supports healthy aging, slows the biological aging process, or extends lifespan.
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View more via ChEBI Ontology
2,2- dichloro- N- [(1R,2R)- 2- hydroxy- 1- (hydroxymethyl)- 2- (4- nitrophenyl)ethyl]acetamide
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chloramphenicol
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WHO MedNet
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chloramphénicol
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WHO MedNet
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chloramphenicolum
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WHO MedNet
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cloramfenicol
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WHO MedNet
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(−)-chloramphenicol
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ChEBI
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Chloramphenicol
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KEGG COMPOUND
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CHLORAMPHENICOL
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PDBeChem
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chloramphenicol
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UniProt
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chlornitromycin
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ChEBI
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D- (−)- 2,2- dichloro- N- (β- hydroxy- α- (hydroxymethyl)- p- nitrophenylethyl)acetamide
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ChemIDplus
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D-(−)-threo-1-p-nitrophenyl-2-dichloroacetylamino-1,3-propanediol
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ChemIDplus
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laevomycetinum
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ChemIDplus
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levomicetina
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ChemIDplus
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levomycetin
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ChemIDplus
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Amphicol
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KEGG DRUG
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Chloramex
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ChemIDplus
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Chlorocid
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ChemIDplus
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Chlorocol
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ChemIDplus
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Chloromycetin
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ChemIDplus
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Econochlor
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KEGG DRUG
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Fenicol
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ChemIDplus
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Globenicol
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ChemIDplus
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Halomycetin
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ChemIDplus
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Oleomycetin
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ChemIDplus
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Sificetina
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ChemIDplus
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1835
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VSDB
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5744
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ChemSpider
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589
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DrugCentral
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C00918
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KEGG COMPOUND
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chloramphenicol
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Alan Wood's Pesticides
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Chloramphenicol
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Wikipedia
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CHLORAMPHENICOL
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MetaCyc
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CLM
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PDBeChem
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D00104
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KEGG DRUG
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DB00446
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DrugBank
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GB795131
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Patent
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GB796901
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Patent
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HMDB0014589
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HMDB
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LSM-5256
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LINCS
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US2483871
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Patent
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US2483884
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Patent
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US2483892
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Patent
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US2839577
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Patent
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View more database links |
2225532
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Beilstein Registry Number
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Beilstein
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56-75-7
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CAS Registry Number
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NIST Chemistry WebBook
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56-75-7
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CAS Registry Number
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ChemIDplus
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Berlina AN, Taranova NA, Zherdev AV, Vengerov YY, Dzantiev BB (2013) Quantum dot-based lateral flow immunoassay for detection of chloramphenicol in milk. Analytical and bioanalytical chemistry 405, 4997-5000 [PubMed:23494278] [show Abstract] A novel rapid (20 min) fluorescent lateral flow test for chloramphenicol (CAP) detection in milk was developed. The chosen format is a binding-inhibition assay. Water-soluble quantum dots with an emission peak at 625 nm were applied as a label. Milk samples were diluted by 20 % with phosphate buffer to eliminate the matrix effect. The result of the assay could be seen by eye under UV light excitation or registered by a portable power-dependent photometer. The limit of CAP detection by the second approach is 0.2 ng/mL, and the limit of quantitation is 0.3 ng/mL. | Livingston RJ, Butterworth JW, Belt P (2013) Reaction or infection: topical chloramphenicol treatment. Annals of the Royal College of Surgeons of England 95, e20-1 [PubMed:23317719] [show Abstract] Chloramphenicol is a topical treatment that is used widely, especially in wounds around the eyes. In our practice there have been a number of cases of delayed hypersensitivity to chloramphenicol that has been mismanaged initially as an infective cellulitis. We hope to share some of our experience of this uncommon reaction to highlight the delayed reaction that can occur with topical application of this drug. | Leston S, Nunes M, Viegas I, Ramos F, Pardal MÂ (2013) The effects of chloramphenicol on Ulva lactuca. Chemosphere 91, 552-557 [PubMed:23395526] [show Abstract] The administration of pharmacological substances in the food producing industry is a crucial and long established practice in ensuring animal welfare. However, a very high percentage of the drugs used will directly or indirectly be present in the various compartments of natural ecosystems therefore constituting a source of pollution. The reactions that these active compounds may impose on non-target organisms are still widely unknown and further research is essential. Also, new approaches on monitoring are necessary and in this sense, the present work aimed to assess the persistence of chloramphenicol (a banned but illegally used antibiotic) in seawater, together with its effects on the growth of the green macroalgae Ulva lactuca. Moreover, the potential use of this species as a bioindicator was assessed. Results showed CAP presented an exponential degradation pattern in seawater with concentrations decreasing faster than expected. As for the effects on U. lactuca it acted as a growth promoter also contradicting the initial assumptions. Regarding the role of this species in biomonitoring it successfully took up CAP in solution while reflecting the concentrations present conferring it good characteristics as a bioindicator. On the other hand, this ability points to a possibility of CAP being accumulated and transferred along the trophic web through the consumption of U. lactuca by organisms in higher levels. | Tao X, Jiang H, Yu X, Zhu J, Wang X, Wang Z, Niu L, Wu X, Shen J (2013) An ultrasensitive chemiluminescence immunoassay of chloramphenicol based on gold nanoparticles and magnetic beads. Drug testing and analysis 5, 346-352 [PubMed:23512826] [show Abstract] A competitive, direct, chemiluminescent immunoassay based on a magnetic beads (MBs) separation and gold nanoparticles (AuNPs) labelling technique to detect chloramphenicol (CAP) has been developed. Horseradish peroxidase (HRP)-labelled anti-CAP monoclonal antibody conjugated with AuNPs and antigen-immobilized MBs were prepared. After optimization parameters of immunocomplex MBs, the IC50 values of chemiluminescence magnetic nanoparticles immunoassay (CL-MBs-nano-immunoassay) were 0.017 µg L(-1) for extract method I and 0.17 µg L(-1) for extract method II. The immunoassay with two extract methods was applied to detect CAP in milk. Comparison of these two extract methods showed that extract method I was advantageous in better sensitivity, in which the sensitivity was 10 times compared to that of extract method II, while extract method II was superior in simple operation, suitable for high throughout screen. The recoveries were 86.7-98.0% (extract method I) and 80.0-103.0% (extract method II), and the coefficients of variation (CVs) were all <15%. The satisfactory recovery with both extract methods and high correlation with traditional ELISA kit in milk system confirmed that the immunomagnetic assay based on AuNPs exhibited promising potential in rapid field screening for trace CAP analysis. | Houtkooper RH, Mouchiroud L, Ryu D, Moullan N, Katsyuba E, Knott G, Williams RW, Auwerx J (2013) Mitonuclear protein imbalance as a conserved longevity mechanism. Nature 497, 451-457 [PubMed:23698443] [show Abstract] Longevity is regulated by a network of closely linked metabolic systems. We used a combination of mouse population genetics and RNA interference in Caenorhabditis elegans to identify mitochondrial ribosomal protein S5 (Mrps5) and other mitochondrial ribosomal proteins as metabolic and longevity regulators. MRP knockdown triggers mitonuclear protein imbalance, reducing mitochondrial respiration and activating the mitochondrial unfolded protein response. Specific antibiotics targeting mitochondrial translation and ethidium bromide (which impairs mitochondrial DNA transcription) pharmacologically mimic mrp knockdown and extend worm lifespan by inducing mitonuclear protein imbalance, a stoichiometric imbalance between nuclear and mitochondrially encoded proteins. This mechanism was also conserved in mammalian cells. In addition, resveratrol and rapamycin, longevity compounds acting on different molecular targets, similarly induced mitonuclear protein imbalance, the mitochondrial unfolded protein response and lifespan extension in C. elegans. Collectively these data demonstrate that MRPs represent an evolutionarily conserved protein family that ties the mitochondrial ribosome and mitonuclear protein imbalance to the mitochondrial unfolded protein response, an overarching longevity pathway across many species. | Adebusuyi A, Foght J (2013) Physico-chemical factors affect chloramphenicol efflux and EmhABC efflux pump expression in Pseudomonas fluorescens cLP6a. Research in microbiology 164, 172-180 [PubMed:23142491] [show Abstract] Protein synthesis inhibitors such as chloramphenicol and tetracycline may be inducers of efflux pumps such as MexY in Pseudomonas aeruginosa, complicating their use for the treatment of bacterial infections. We previously determined that chloramphenicol, a substrate of the EmhABC efflux pump in Pseudomonas fluorescens cLP6a, did not induce emhABC expression. In this study, we determined the effect of physico-chemical factors on chloramphenicol efflux by EmhABC, and the expression of emhABC. Efflux assays measuring accumulation of (14)C-chloramphenicol in cell pellets showed that chloramphenicol efflux is dependent on growth temperature, pH and concentration of Mg(2+). These physico-chemical factors modulated the efflux of chloramphenicol by 26 to >50%. All conditions tested that decreased the efflux of chloramphenicol unexpectedly induced transcription of emhABC efflux genes. EmhABC activity also effectively suppressed the deleterious effect of chloramphenicol on the cell membrane of strain cLP6a, which may explain why chloramphenicol is not an inducer of emhABC. Our results suggest that the detrimental effect of an antibiotic on cell membrane integrity and fatty acid composition may be the signal that induces emhABC expression, and that inducers of other bacterial efflux pumps may include environmental factors rather than their substrates per se. | Hafner V, Albermann N, Haefeli WE, Ebinger F (2008) Inhibition of voriconazole metabolism by chloramphenicol in an adolescent with central nervous system aspergillosis. Antimicrobial agents and chemotherapy 52, 4172-4174 [PubMed:18794387] [show Abstract] For an adolescent with bacterial meningitis and subsequent cerebral aspergillosis, intravenous voriconazole dose requirements substantially decreased during coadministration with intravenous chloramphenicol and considerably rose after discontinuation of the antibiotic. In agreement with in vitro evidence, these data suggest that chloramphenicol is a rather significant inhibitor of hepatic CYP3A4 and/or CYP2C19. | Yuan ZR, Shi Y (2008) Chloramphenicol induces abnormal differentiation and inhibits apoptosis in activated T cells. Cancer research 68, 4875-4881 [PubMed:18559535] [show Abstract] Chloramphenicol is a broad-spectrum antibiotic used for the treatment of many infectious diseases and has become one of the major seafood contaminants. Hematologic disorders such as aplastic anemia and leukemia induced by chloramphenicol are a major concern. However, the mechanism underlying chloramphenicol-induced leukemogenesis is not known. By investigating the effects of chloramphenicol on the activation of mouse T cells stimulated with anti-CD3 antibody or staphylococcal enterotoxin B, we found that chloramphenicol induces the differentiation of activated T cells into lymphoblastic leukemia-like cells, characterized by large cell size, multiploid nuclei, and expression of CD7, a maker for immature T cells and T-cell lymphocytic leukemia, thus phenotypically indicating differentiation toward leukemogenesis. High expression of cyclin B1, but not p53, c-myc, and CDC25A, was detected in chloramphenicol-treated activated T cells, which may relate to abnormal cell differentiation. Chloramphenicol inhibited the activation-induced cell death of mouse and human T-cell receptor-activated T cells by down-regulating the expression of Fas ligand. Our findings show that abnormal cell differentiation and inhibition of apoptosis may contribute to the development of leukemia associated with clinical applications of chloramphenicol. | Monari M, Foschi J, Cortesi P, Rosmini R, Cattani O, Serrazanetti GP (2008) Chloramphenicol influence on antioxidant enzymes with preliminary approach on microsomal CYP1A immunopositive-protein in Chamelea gallina. Chemosphere 73, 272-280 [PubMed:18657290] [show Abstract] Chloramphenicol (CA) is a largely used antibiotic and it is an inhibitor of protein synthesis that also induces ROS production. In this work there were investigated activities and expressions in the Adriatic bivalve Chamelea gallina of some antioxidant and detoxification proteins like superoxide dismutase (Mn-SOD, Cu/Zn-SOD), catalase (CAT) and Cytochrome P450 (CYP1A). Clams exposed to 5mgl(-1) of chloramphenicol were sampled 2, 4 and 8 days after treatment (CA2, CA4 and CA8). SODs, CAT, and CYP1A activity and/or expression were detected in pooled digestive glands by Western blotting and by spectrophotometrical analysis. Enzymes activities increase during the entire antibiotic exposure. With respect to the control Cu/Zn-SOD expression increases, while Mn-SOD expression decreases significantly after 4 days. Two CYP1A immunopositive-proteins (57.7 and 59.8kDa) were detected. The lower band significantly decreases in CA8, the upper one also in CA4 condition. High levels of Mn-SOD, CAT activity and Cu/Zn-SOD expression, indicate intense ROS production while Mn-SOD expression inhibition might be ascribable to mitochondrial alterations due to CA and indirectly to ROS. CYP1A1 action determines H2O2 production that would contribute to a CYP1A1 gene promoter down regulation, a response to oxidative stress with the antioxidant enzymes activation as a final result. This study highlights the close association, in C. gallina, in presence of chloramphenicol, between SOD/CAT and CYP system, and it appear particularly interesting to the lack of similar researches on mollusc species. | Chatzitakis A, Berberidou C, Paspaltsis I, Kyriakou G, Sklaviadis T, Poulios I (2008) Photocatalytic degradation and drug activity reduction of Chloramphenicol. Water research 42, 386-394 [PubMed:17692887] [show Abstract] The photocatalytic degradation of Chloramphenicol, an antibiotic drug, has been investigated in aqueous heterogeneous solutions containing n-type oxide semiconductors as photocatalysts. The disappearance of the organic molecule follows approximately a pseudo-first-order kinetics according to the Langmuir-Hinshelwood model. It was observed that, with TiO(2) P-25 as photocatalyst, quantitative degradation of the organic molecule occurs after 4h of illumination. During this time, the dechlorination of the substrate is complete, while the organic nitrogen was recovered in the form of nitrate and ammonium ions. The effect of temperature on the degradation rate of Chloramphenicol shows similar apparent activation energies for both TiO(2) P-25 and ZnO photocatalysts. The initial apparent photonic efficiency (zeta(0)) of the photo-oxidation and the mineralization under various experimental conditions have been calculated, while the Kirby-Bauer disc diffusion method showed a 100% reduction of the drug activity after 90 min of photocatalytic treatment. | Wesongah JO, Murilla GA, Guantai AN, Elliot C, Fodey T, Cannavan A (2007) A competitive enzyme-linked immunosorbent assay for determination of chloramphenicol. Journal of veterinary pharmacology and therapeutics 30, 68-73 [PubMed:17217404] [show Abstract] Chloramphenicol is a broad-spectrum antibiotic shown to have specific activity against a wide variety of organisms that are causative agents of several disease conditions in domestic animals. Chloramphenicol has been banned for use in food-producing animals for its serious adverse toxic effects in humans. Due to the harmful effects of chloramphenicol residues livestock products should be free of any traces of these residues. Several analytical methods are available for chloramphenicol analysis but sensitive methods are required in order to ensure that no traces of chloramphenicol residues are present in edible animal products. In order to prevent the illegal use of chloramphenicol, regulatory control of its residues in food of animal origin is essential. A competitive enzyme-linked immunosorbent assay for chloramphenicol has been locally developed and optimized for the detection of chloramphenicol in sheep serum. In the assay, chloramphenicol in the test samples and that in chloramphenicol-horseradish peroxidase conjugate compete for antibodies raised against the drug in camels and immobilized on a microtitre plate. Tetramethylbenzidine-hydrogen peroxide (TMB/H2O2) is used as chromogen-substrate system. The assay has a detection limit of 0.1 ng/mL of serum with a high specificity for chloramphenicol. Cross-reactivity with florfenicol, thiamphenicol, penicillin, tetracyclines and sulfamethazine was not observed. The assay was able to detect chloramphenicol concentrations in normal sheep serum for at least 1 week after intramuscular injection with the drug at a dose of 25 mg/kg body weight (b.w.). The assay can be used as a screening tool for chloramphenicol use in animals. | Eraso AJ, Albesa I (2007) Eriobotrya japonica counteracts reactive oxygen species and nitric oxide stimulated by chloramphenicol. The American journal of Chinese medicine 35, 875-885 [PubMed:17963326] [show Abstract] Chloramphenicol is a toxic antibiotic used for certain infections, though aplastic anaemia is one of its side-effects. The results of our experiments showed that blood cells suffered oxidative stress in the presence of chloramphenicol, with a significant increase in reactive oxygen species (ROS) detected by luminol-chemiluminescence (CL). The extract of fruits of Eriobotrya japonica markedly decreased ROS in leukocytes and erythrocytes, the oxidative stress caused by this antibiotic. Nitro Blue Tetrazolium (NBT) assay with purified leukocytes demonstrated that the antioxidant action of E. japonica caused an intracellular reduction in ROS, and that the extracts decreased these promoters of oxidative stress to normal levels in the cytoplasm. Determinations of nitric oxide (NO) generation indicated that E. japonica extracts also inhibited the stimuli of NO provoked by chloramphenicol. This study showed that the immediate antioxidant effect of E. japonica could be associated with the action of vitamin A. The protective action of this fruit was seen on mature leukocytes and erythrocytes, beneficial effect on blood cells suggest that its extract could be used as an antioxidant agent complementing the administration of chloramphenicol, as a modern-day extension to its traditional use in Chinese medicine. | Popadic S, Popadic D, Ramic Z, Mostarica Stojkovic M, Trajkovic V, Milinkovic M, Medenica L (2006) Chloramphenicol induces in vitro growth arrest and apoptosis of human keratinocytes. Cell biology and toxicology 22, 371-379 [PubMed:16897441] [show Abstract] Chloramphenicol (CAP) is a broad-spectrum antibacterial drug that is widely used for topical application in ophthalmology and dermatology. In the present study we investigated the influence of CAP on human keratinocyte proliferation and apoptosis in vitro. CAP significantly inhibited proliferation and induced apoptosis of cultivated human keratinocytes, as revealed by incorporation of radioactive thymidine and flow cytometry analysis of intracellular esterase activity in fluorescein diacetate-stained cells, respectively. CAP-induced keratinocyte apoptosis was associated with activation of caspases and increased production of reactive oxygen species. The pro-apoptotic action of CAP was antagonized by the antioxidant agent N-acetylcysteine, the protein synthesis inhibitor cycloheximide, and PD98059, a selective inhibitor of extracellular signal-regulated kinase (ERK) activation. Taken together, these data indicate that CAP inhibits keratinocyte proliferation through induction of oxidative stress and ERK-mediated caspase-dependent apoptosis. | Thompson J, O'Connor M, Mills JA, Dahlberg AE (2002) The protein synthesis inhibitors, oxazolidinones and chloramphenicol, cause extensive translational inaccuracy in vivo. Journal of molecular biology 322, 273-279 [PubMed:12217690] [show Abstract] The oxazolidinone family is a new class of synthetic antibiotics that bind to the bacterial 50S ribosomal subunit. Two members of the family, linezolid and XA043, were examined for their effects on translational fidelity using a lacZ reporter gene in vivo. Both promoted highly significant frameshifting and nonsense suppression. Chloramphenicol, a peptidyl transferase inhibitor, affected translational fidelity in a similar fashion. Neither the oxazolidinones nor chloramphenicol stimulated misincorporation of amino acid residues at position 461 in the lacZ gene. In contrast, the aminoglycosides gentamicin and paromomycin, which interact with the decoding region of the 30S subunit, caused significant misincorporation but only modest increases in frameshifting or stop codon readthrough of the lacZ gene. We conclude that effects on translational fidelity may play a significant role in the mechanism of action of the oxazolidinones. | Izard T (2001) Structural basis for chloramphenicol tolerance in Streptomyces venezuelae by chloramphenicol phosphotransferase activity. Protein science : a publication of the Protein Society 10, 1508-1513 [PubMed:11468347] [show Abstract] Streptomyces venezuelae synthesizes chloramphenicol (Cm), an inhibitor of ribosomal peptidyl transferase activity, thereby inhibiting bacterial growth. The producer escapes autoinhibition by its own secondary metabolite through phosphorylation of Cm by chloramphenicol phosphotransferase (CPT). In addition to active site binding, CPT binds its product 3-phosphoryl-Cm, in an alternate product binding site. To address the mechanisms of Cm tolerance of the producer, the crystal structures of CPT were determined in complex with either the nonchlorinated Cm (2-N-Ac-Cm) at 3.1 A resolution or the antibiotic's immediate precursor, the p-amino analog p-NH(2)-Cm, at 2.9 A resolution. Surprisingly, p-NH(2)-Cm binds CPT in a novel fashion. Additionally, neither 2-N-Ac-Cm nor p-NH(2)-Cm binds to the secondary product binding site. | Strick RA (1983) Lack of cross-reaction between DNCB and chloramphenicol. Contact dermatitis 9, 484-487 [PubMed:6653106] [show Abstract] Although one study has reported a cross-reactivity between DNCB and chloramphenicol in 40% of patients, other investigators have been unable to confirm the existence of any cross reaction. The purpose of this study is to determine whether sensitization of patients to DNCB poses a risk of cross reaction to chloramphenicol. In the present study, 100 consecutive patients who were sensitized to DNCB failed to show a single reaction to patch testing with chloramphenicol in a 1% ointment. The discrepancy between these results may be explained by a possible misinterpretation of a primary irritant reaction as an allergic contact reaction in the original report. | Powell DA, Nahata MC (1982) Chloramphenicol: new perspectives on an old drug. Drug intelligence & clinical pharmacy 16, 295-300 [PubMed:7040026] [show Abstract] Chloramphenicol is an old antibiotic being used with increasing frequency in serious childhood infections largely due to the emergence of ampicillin-resistant Hemophilus influenzae type b. Because of this renewed popularity and the recent availability of accurate analytical techniques for measurement of chloramphenicol, there have been many recent articles examining the pharmacokinetics of chloramphenicol and its two major prodrug esters, chloramphenicol succinate and chloramphenicol palmitate. New data from these studies include the incomplete bioavailability of chloramphenicol succinate, the possible superior bioavailability of chloramphenicol palmitate vs. chloramphenicol succinate, and the wide interpatient variability in chloramphenicol clearance. These observations, coupled with the known serious hematologic toxicity (reversible bone marrow suppression or irreversible aplastic anemia) and metabolic toxicity (gray baby syndrome) associated with chloramphenicol use, require that initial antibiotic doses be selected by age and be carefully individualized by measurement of peak serum chloramphenicol concentrations. | Eriksen K (1978) Cross allergy between paranitro compounds with special reference to DNCB and chloramphenicol. Contact dermatitis 4, 29-32 [PubMed:657786] [show Abstract] Cross allergy between paranitro compounds including DNCB and chloramphenicol, was studied in 42 patients. A total of 27 had been primarily sensitized to DNCB, and 15 patients with eczema exhibited a delayed-type reaction to chloramphenicol, showing a positive patch test. All 15 patients with chloramphenicol allergy cross reacted with chloramphenicol succinate and chloramphenicol palmitate. Three of them cross reacted with paranitrobenzoic acid, and two of these also with paradinitrobenzene. None of the 15 patients cross reacted with DNCB in acetone or DNCB in petrolatum, and none reacted to picric acid, paranitrophenol or dinitroorthocresol. The 27 patients primarily sensitized to DNCB did not cross react with any of the paranitro compounds studied, in particular not with chloramphenicol or its salts. Thus, the study confirms the specificity of the DNCB sensitivity. | Yang NS, Scandalios JG (1977) Effects of cycloheximide and chloramphenicol on the synthesis of polypeptides found in three subcellular fractions of maize scutellum. Plant physiology 59, 1067-1071 [PubMed:16659995] [show Abstract] The effects of two protein synthesis inhibitors, cycloheximide and chloramphenicol, on the synthesis of mitochondrial proteins in maize (Zea mays) have been studied. The results of these investigations suggest that while most of the mitochondrial proteins are synthesized in the cytoplasm and are subsequently associated with the mitochondrion, several proteins of the mitochondrial inner membrane are synthesized within the mitochondrion. These results are consistent with those observed in several other systems, but not previously reported for higher plants. |
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