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2. Hepatocyte iron loading capacity is associated with differentiation and repression of motility in the HepaRG cell line

Author

Troadec, Marie-Bérengère, Glaise, Denise, Lamirault, Guillaume, Le Cunff, Martine, Guérin, Emilie, Le Meur, Nolwenn, Détivaud, Lénaïck, Zindy, Pierre, Leroyer, Patricia, Guisle, Isabelle, Duval, Hélène, Gripon, Philippe, Théret, Nathalie, Boudjema, Karim, Guguen-Guillouzo, Christiane, Brissot, Pierre, Léger, Jean J., and Loréal, Olivier

Published
2006
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5. Screening for Copy Number Variation in Genes Associated With the Long QT Syndrome

Author

Barc, Julien, primary, Briec, François, additional, Schmitt, Sébastien, additional, Kyndt, Florence, additional, Le Cunff, Martine, additional, Baron, Estelle, additional, Vieyres, Claude, additional, Sacher, Frédéric, additional, Redon, Richard, additional, Le Caignec, Cédric, additional, Le Marec, Hervé, additional, Probst, Vincent, additional, and Schott, Jean-Jacques, additional

Published
2011
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10. Characterization of a casein kinase which interacts with the rabbit progesterone receptor.

Author

Logeat, Frédérique, le Cunff, Martine, Rauch, Michel, Brailly, Sylvie, and Milgrom, Edwin

Subjects
*PHOSPHORYLATION, *CHEMICAL reactions, *MILK proteins, *NUCLEOTIDES, *ANTICOAGULANTS, *POLYSACCHARIDES
Abstract

Previous in vivo studies have shown that the rabbit progesterone receptor undergoes two phosphorylation reactions: one basal and a second one which is hormone-dependent. We report here on the presence and characteristics of a kinase activity found in receptor preparations highly purified by immunoaffinity chromatography. 1. This kinase activity is not due to the receptor molecule itself since the two proteins may be separated by several chromatographic and immunological methods. 2. The presence of the kinase in receptor preparations is not an artefact of the purification procedure. The kinase binds to the receptor as shown by coelution in immunoaffinity experiments and during various chromatographics. This interaction probably takes place in vivo and is not artefactually formed during solubilization of the receptor since the kinase also copurifies with receptors isolated from the uterine nuclei of progestina treated rabbits. 3. This enzyme may be classified as a casein kinase since it readily phosphorylates the latter substrate (Km ≈ 0.15 mg/mI) and is not regulated by cyclic nucleotides, Ca2+ and calmodulin or phospholipids. Its classifi- cation as a casein kinase I or II is difficult since on the one hand it is Inhibited by heparin, activated by polyamines and may use both ATP and GTP, but on the other hand it modifies only serine residues, and is not inhibited by heparin when the receptor itself is employed as a substrate. 4. The kinase which copurifies with the receptor does not mimic in vitro the effects of the hormone-dependent phosphorylation of the receptor observed in vivo: there is no enhancement of kinase activity by the hormone. and the phosphorylated receptor does not exhibit the characteristic "upshift" in its electrophoretic mobility. Thus either this kinase is not the enzyme responsible for the hormone-dependent receptor phosphorylation or, during purification, a factor has been lost which is necessary for retaining the hormone dependency of the reaction. [ABSTRACT FROM AUTHOR]

Published
1987
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11. Screening for Copy Number Variation in Genes Associated With the Long QT Syndrome Clinical Relevance

Author

Barc, Julien, Briec, François, Schmitt, Sébastien, Kyndt, Florence, Le Cunff, Martine, Baron, Estelle, Vieyres, Claude, Sacher, Frédéric, Redon, Richard, Le Caignec, Cédric, Le Marec, Hervé, Probst, Vincent, and Schott, Jean-Jacques

Subjects
congenital, hereditary, and neonatal diseases and abnormalities, CNV, long QT syndrome, sudden death, cardiovascular diseases, deletion, MLPA
Abstract

ObjectivesThe aim of this study was to investigate, in a set of 93 mutation-negative long QT syndrome (LQTS) probands, the frequency of copy number variants (CNVs) in LQTS genes.BackgroundLQTS is an inherited cardiac arrhythmia characterized by a prolonged heart rate–corrected QT (QTc) interval associated with sudden cardiac death. Recent studies suggested the involvement of duplications or deletions in the occurrence of LQTS. However, their frequency remains unknown in LQTS patients.MethodsPoint mutations in KCNQ1, KCNH2, and SCN5A genes were excluded by denaturing high-performance liquid chromatography or direct sequencing. We applied Multiplex Ligation-dependent Probe Amplification (MLPA) to detect CNVs in exons of these 3 genes. Abnormal exon copy numbers were confirmed by quantitative multiplex PCR of short fluorescent fragment (QMPSF). Array-based comparative genomic hybridization (array CGH) analysis was performed using Agilent Human Genome 244K Microarrays to further map the genomic rearrangements.ResultsWe identified 3 different deletions in 3 unrelated families: 1 in KCNQ1 and 2 involving KCNH2. We showed in the largest family that the deletion involving KCNH2 is fully penetrant and segregates with the long QT phenotype in 7 affected members.ConclusionsOur study demonstrates that CNVs in KCNQ1 and KCNH2 explain around 3% of LQTS in patients with no point mutation in these genes. This percentage is likely higher than the frequency of point mutations in ANKB, KCNE1, KCNE2, KCNJ2, CACNA1C, CAV3, SCN4B, AKAP9, and SNTA1 together. Thus, we propose that CNV screening in KCNQ1 and KCNH2 may be performed routinely in LQTS patients.

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