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4. A nuclear matrix attachment site in the 4q35 locus has an enhancer-blocking activity in vivo: implications for the facio-scapulo-humeral dystrophy

Author

Petrov, Andrei, Allinne, Jeanne, Pirozhkova, Iryna, Laoudj, Dalila, Lipinski, Marc, and Vassetzky, Yegor S.

Subjects
Myotonic dystrophy -- Genetic aspects, Myotonic dystrophy -- Research, Quantitative trait loci -- Research, Nucleotide sequencing -- Analysis, Health
Abstract

The article discusses the existence and the significance of the nuclear matrix attachment site in the 4q35 locus, which is shown to exhibit an in vivo enhancer-blocking activity. The enhancer is found to be helpful in the treatment of facio-scapulo-humeral dystrophy (FSHD), a muscular hereditary disease.

Published
2008

8. Mutations in GJB6 cause hidrotic ectodermal dysplasia

Author

Lamartine, Jérôme, primary, Munhoz Essenfelder, Guilherme, additional, Kibar, Zoha, additional, Lanneluc, Isabelle, additional, Callouet, Edwige, additional, Laoudj, Dalila, additional, Lemaître, Gilles, additional, Hand, Colette, additional, Hayflick, Susan J., additional, Zonana, Jonathan, additional, Antonarakis, Stylianos, additional, Radhakrishna, Uppala, additional, Kelsell, David P., additional, Christianson, Arnold L., additional, Pitaval, Amandine, additional, Der Kaloustian, Vazken, additional, Fraser, Clarke, additional, Blanchet-Bardon, Claudine, additional, Rouleau, Guy A., additional, and Waksman, Gilles, additional

Published
2000
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10. EGTA induces the synthesis in <em>Escherichia coli</em> of three proteins that cross-react with calmodulin antibodies.

Author

Laoudj, Dalila, Andersen, Catherine L., Bras, Ana, Goldberg, Martin, Jacq, Annick, and Holland, I. Barry

Subjects
ESCHERICHIA coli, VERAPAMIL, ELECTROPHORESIS, PEPTIDE hormones, CELLS
Abstract

Escherichia coli mutants, (verA, dilA) specifically resistant to the Ca2+ channel inhibitors verapamil and diltiazem, respectively, are hypersensitive to EGTA and BAPTA. We have shown, using 1-D and 2-D gel electrophoresis, that the synthesis of at least 25 polypeptides in the mutants was enhanced by treatment with Ca2+ chelators and the synthesis of at least 11 polypeptides was repressed. This pattern of induction was not observed in heat- or SDS-treated cells and therefore does not appear to be a general stress response. The majority of the induced proteins are low molecular weight, extremely heat stable and acidic, characteristic properties of caimodulin. Moreover, of the major induced species, three with apparent molecular masses of 12, 18, and 34kDa all cross-reacted with polydonal and monoclonal anti-bodies to eukaryote calmodulins or calerythrin, a heat-resistant Ca2+-binding protein from Saccharo-polyspora erythraea. The verA, dilA mutants. In being hypersensitive to EGTA and to the Ca2+ ionophore A23187 + Ca2+, may be defective in the regulation of the level of free intracellular Ca2+. [ABSTRACT FROM AUTHOR]

Published
1994
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