Garcia Alvaro Baeza, Pierce Raymond J, Gourbal Benjamin, Werkmeister Elisabeth, Colinet Dominique, Reichhart Jean-Marc, Dissous Colette, Coustau Christine
Involvement of the cytokine MIF in the snail host immune response to the parasite Schistosoma mansoni Article de journal
Dans: PLoS Pathog., vol. 6, no. 9, p. e1001115, 2010, ISSN: 1553-7374.
Résumé | Liens | BibTeX | Étiquettes: Amino Acid, Animals, Apoptosis, Biomphalaria, Blotting, Cell Proliferation, Cells, Cricetinae, Cultured, Hemocytes, Host-Parasite Interactions, Humans, Liver, M3i, Macrophage Migration-Inhibitory Factors, messenger, Oocysts, Recombinant Proteins, reichhart, Reverse Transcriptase Polymerase Chain Reaction, RNA, Schistosoma mansoni, Schistosomiasis mansoni, Sequence Homology, Small Interfering, Western
@article{baeza_garcia_involvement_2010,
title = {Involvement of the cytokine MIF in the snail host immune response to the parasite Schistosoma mansoni},
author = {Alvaro Baeza Garcia and Raymond J Pierce and Benjamin Gourbal and Elisabeth Werkmeister and Dominique Colinet and Jean-Marc Reichhart and Colette Dissous and Christine Coustau},
doi = {10.1371/journal.ppat.1001115},
issn = {1553-7374},
year = {2010},
date = {2010-01-01},
journal = {PLoS Pathog.},
volume = {6},
number = {9},
pages = {e1001115},
abstract = {We have identified and characterized a Macrophage Migration Inhibitory Factor (MIF) family member in the Lophotrochozoan invertebrate, Biomphalaria glabrata, the snail intermediate host of the human blood fluke Schistosoma mansoni. In mammals, MIF is a widely expressed pleiotropic cytokine with potent pro-inflammatory properties that controls cell functions such as gene expression, proliferation or apoptosis. Here we show that the MIF protein from B. glabrata (BgMIF) is expressed in circulating immune defense cells (hemocytes) of the snail as well as in the B. glabrata embryonic (Bge) cell line that has hemocyte-like features. Recombinant BgMIF (rBgMIF) induced cell proliferation and inhibited NO-dependent p53-mediated apoptosis in Bge cells. Moreover, knock-down of BgMIF expression in Bge cells interfered with the in vitro encapsulation of S. mansoni sporocysts. Furthermore, the in vivo knock-down of BgMIF prevented the changes in circulating hemocyte populations that occur in response to an infection by S. mansoni miracidia and led to a significant increase in the parasite burden of the snails. These results provide the first functional evidence that a MIF ortholog is involved in an invertebrate immune response towards a parasitic infection and highlight the importance of cytokines in invertebrate-parasite interactions.},
keywords = {Amino Acid, Animals, Apoptosis, Biomphalaria, Blotting, Cell Proliferation, Cells, Cricetinae, Cultured, Hemocytes, Host-Parasite Interactions, Humans, Liver, M3i, Macrophage Migration-Inhibitory Factors, messenger, Oocysts, Recombinant Proteins, reichhart, Reverse Transcriptase Polymerase Chain Reaction, RNA, Schistosoma mansoni, Schistosomiasis mansoni, Sequence Homology, Small Interfering, Western},
pubstate = {published},
tppubtype = {article}
}
Costa A., de Barros J. P. Pais, Keith G., Baranowski W., Desgres J.
Determination of queuosine derivatives by reverse-phase liquid chromatography for the hypomodification study of Q-bearing tRNAs from various mammal liver cells Article de journal
Dans: J Chromatogr B Analyt Technol Biomed Life Sci, vol. 801, no. 2, p. 237-47, 2004, (1570-0232 Journal Article).
Résumé | BibTeX | Étiquettes: *Chromatography, &, Acyl/chemistry, Amino, Animals, Asn/chemistry, Cells, Chickens, Cultured, derivatives/*analysis, Experimental, Gov't, Hepatocytes/chemistry, high, KEITH, liquid, Liver, Liver/*chemistry, Neoplasms, Non-U.S., Nucleoside, Pressure, purification, Q/*analogs, Rats, RNA, Support, Transfer, Transfer/*chemistry/isolation, tumor
@article{,
title = {Determination of queuosine derivatives by reverse-phase liquid chromatography for the hypomodification study of Q-bearing tRNAs from various mammal liver cells},
author = { A. Costa and J. P. Pais de Barros and G. Keith and W. Baranowski and J. Desgres},
year = {2004},
date = {2004-01-01},
journal = {J Chromatogr B Analyt Technol Biomed Life Sci},
volume = {801},
number = {2},
pages = {237-47},
abstract = {Three queuosine derivatives (Q-derivatives) have been found at position 34 of four mammalian so-called Q-tRNAs: queuosine (Q) in tRNA(Asn) and tRNA(His), mannosyl-queuosine (manQ) in tRNA(Asp), and galactosyl-queuosine (galQ) in tRNA(Tyr). An analytical procedure based on the combined means of purified tRNA isolation from liver cells and ribonucleoside analysis by reverse-phase high performance liquid chromatography coupled with real-time UV-spectrometry (RPLC-UV) was developed for the quantitative analysis of the three Q-derivatives present in total tRNA from liver tissues and liver cell cultures. Using this analytical procedure, the rates of Q-tRNA modification were studied in total tRNAs from various mammalian hepatic cells. Our results show that the four Q-tRNAs are fully modified in liver tissues from adult mammals, regardless of the mammal species. However, a lack in the Q-modification level was observed in Q-tRNAs from newborn rat liver, as well in Q-tRNAs from normal rat liver cell cultures growing in a low queuine content medium, and from a rat hepatoma cell line. It is noteworthy that in all cases of Q-tRNA hypomodification, our analytical procedure showed that tRNA(Asp) is always the least affected by the hypomodification. The biological significance of this phenomenon is discussed.},
note = {1570-0232
Journal Article},
keywords = {*Chromatography, &, Acyl/chemistry, Amino, Animals, Asn/chemistry, Cells, Chickens, Cultured, derivatives/*analysis, Experimental, Gov't, Hepatocytes/chemistry, high, KEITH, liquid, Liver, Liver/*chemistry, Neoplasms, Non-U.S., Nucleoside, Pressure, purification, Q/*analogs, Rats, RNA, Support, Transfer, Transfer/*chemistry/isolation, tumor},
pubstate = {published},
tppubtype = {article}
}
Koolman J, Hoffmann Jules A, Karlson P
Sulphage esters as inactivation products of ecdysone in Locusta migratoria Article de journal
Dans: Hoppe-Seyler's Z. Physiol. Chem., vol. 354, no. 9, p. 1043–1048, 1973, ISSN: 0018-4888.
BibTeX | Étiquettes: Animals, Biological, Cattle, Chromatography, Ecdysone, Electrophoresis, Esterases, Glucosidases, Glucuronidase, Grasshoppers, hoffmann, Hydrogen-Ion Concentration, Hydrolysis, Ion Exchange, Isotope Labeling, Kinetics, Larva, Liver, M3i, Metamorphosis, Paper, Plants, Saccharomyces cerevisiae, Snails, Sulfatases, Sulfur Radioisotopes, Sulfuric Acids, Swine, Thin Layer, Time Factors, Tritium
@article{koolman_sulphage_1973,
title = {Sulphage esters as inactivation products of ecdysone in Locusta migratoria},
author = {J Koolman and Jules A Hoffmann and P Karlson},
issn = {0018-4888},
year = {1973},
date = {1973-09-01},
journal = {Hoppe-Seyler's Z. Physiol. Chem.},
volume = {354},
number = {9},
pages = {1043--1048},
keywords = {Animals, Biological, Cattle, Chromatography, Ecdysone, Electrophoresis, Esterases, Glucosidases, Glucuronidase, Grasshoppers, hoffmann, Hydrogen-Ion Concentration, Hydrolysis, Ion Exchange, Isotope Labeling, Kinetics, Larva, Liver, M3i, Metamorphosis, Paper, Plants, Saccharomyces cerevisiae, Snails, Sulfatases, Sulfur Radioisotopes, Sulfuric Acids, Swine, Thin Layer, Time Factors, Tritium},
pubstate = {published},
tppubtype = {article}
}