92 results on '"Logeat F"'
Search Results
2. Control of Notch Activity by the Ubiquitin-Proteasome Pathway
- Author
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Gupta-Rossi, N., Le Bail, O., Brou, Ch., Logeat, F., Six, E., Israël, A., Christen, Yves, editor, Israël, Alain, editor, De Strooper, Bart, editor, and Checler, Frédéric, editor
- Published
- 2002
- Full Text
- View/download PDF
Catalog
3. Control of Notch Activity by the Ubiquitin-Proteasome Pathway
- Author
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Gupta-Rossi, N., primary, Le Bail, O., additional, Brou, Ch., additional, Logeat, F., additional, Six, E., additional, and Israël, A., additional
- Published
- 2002
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4. Structure, Function and Cellular Distribution of Mammalian Progesterone Receptors
- Author
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Bailly, A., Guiochon-Mantel, A., Misrahi, M., Loosfelt, H., Atger, M., Savouret, J. F., Perrot-Applanat, M., Vu Hai, M. T., Rauch, M., Lorenzo, F., Logeat, F., Milgrom, E., Carlstedt-Duke, Jan, editor, Eriksson, Håkan, editor, and Gustafsson, Jan-Åke, editor more...
- Published
- 1989
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5. Recent progess in the study of the mechanism of action of progesterone
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Logeat, F., Pamphile, R., Applanat, M., Vu Hai, M. T., Milgrom, E., Notelovitz, M., editor, and van Keep, P., editor
- Published
- 1986
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6. Complex Regulation of MHC Class I Expression: Constitutive and Modulated Patterns of Expression
- Author
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David-Watine, B., Kieran, M., Logeat, F., Israël, A., Kourilsky, P., Melchers, Fritz, editor, Albert, E. D., editor, von Boehmer, H., editor, Dierich, M. P., editor, Du Pasquier, L., editor, Eichmann, K., editor, Gemsa, D., editor, Götze, O., editor, Kalden, J. R., editor, Kaufmann, S. H. E., editor, Kirchner, H., editor, Resch, K., editor, Riethmüller, G., editor, Schimpl, A., editor, Sorg, C., editor, Steinmetz, M., editor, Wagner, H., editor, and Zachau, H. G., editor more...
- Published
- 1989
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7. The Two Phosphorylation Reactions of the Progesterone Receptor
- Author
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Logeat, F., le Cunff, M., Pamphile, R., Milgrom, E., Roy, Arun K., editor, and Clark, James H., editor
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- 1987
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8. LIST OF CONTRIBUTORS AND DISCUSSANTS
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Abramowitz, J., primary, Allan, E.H., additional, Andersen, R., additional, Atger, M., additional, Bailly, A., additional, Bardin, C.W., additional, Barton, M.C., additional, Bicsak, T.A., additional, Birnbaumer, L., additional, Birnbaumer, M., additional, Black, V.H., additional, Blume, J., additional, Boime, I., additional, Bouchard, P., additional, Bradlow, L.H., additional, Brown, A.M., additional, Callard, I., additional, Caple, I.W., additional, Care, A.D., additional, Carter, A., additional, Chan, B.L., additional, Chang, T.-C., additional, Chao, M.V., additional, Chretien, M., additional, Clark, J.H., additional, Codina, J., additional, Cook, K.S., additional, Czekala, N., additional, Dahl, K.D., additional, Danks, J.A., additional, Darnell, J.C., additional, Dickson, R.B., additional, Diefenbach-Jagger, H., additional, Dumont, J.E., additional, Ebeling, P.R., additional, Edgren, R., additional, Evans, R.M., additional, Fauser, B.C.J.M., additional, Finlay, T., additional, Flier, J.S., additional, Friesen, H., additional, Galway, A.B., additional, Geller, J., additional, Gillespie, M.T., additional, Gould, L., additional, Graf, R., additional, Guiochon-Mantel, A., additional, Hamm, H.E., additional, Hammonds, G., additional, Heath, J.A., additional, Hempstead, B.L., additional, Hsueh, A.J.W., additional, Hudson, P.J., additional, Imoto, Y., additional, Iyengar, R., additional, Jellinck, P., additional, Jia, X.-c., additional, Jolivet, A., additional, Keene, J., additional, Kelly, P.A., additional, Kemp, B.E., additional, Kubota, M., additional, Kukreja, S.C., additional, Leavitt, W., additional, Lew, D., additional, Liao, C.-F., additional, Lippman, M.E., additional, Logeat, F., additional, Loosfelt, H., additional, Lorenzo, F., additional, Lowell, B., additional, Martin, T.J., additional, Mattera, R., additional, McKearin, D.M., additional, McKnight, S., additional, Means, A.R., additional, Milgrom, E., additional, Misrahi, M., additional, Moseley, J.M., additional, Mundy, G.R., additional, Murakami, N., additional, Napolitano, A., additional, Ng, K.W., additional, Nielsen, D.A., additional, Nikaido, S.S., additional, Okabe, K., additional, Olate, J., additional, Orth, D., additional, Osterman, D.G., additional, Papkoff, H., additional, Pavlou, S.N., additional, Pearson-Murphy, B., additional, Perrot-Applanat, M., additional, Pichon, M.F., additional, Pratt, B.L., additional, Raisz, L.G., additional, Rall, J.E., additional, Rice, B.F., additional, Ringold, G., additional, Robertson, L.M., additional, Rodda, C.P., additional, Rosen, B., additional, Sakamoto, H., additional, Saltiel, A.R., additional, Samaan, N.A., additional, Sanford, J., additional, Savouret, J.F., additional, Schwartz, N.B., additional, Shapiro, D.J., additional, Simmons, H.A., additional, Simpson, E.R., additional, Sorbara-Cazan, L.R., additional, Spiegelman, B., additional, Stalvey, J., additional, Suki, W.N., additional, Suva, L.J., additional, Swaneck, G., additional, Takahashi, J.S., additional, Themmen, A.P.N., additional, Thorner, J., additional, Usher, P., additional, Vaitukaitis, J.L., additional, Vu Hai, M.T., additional, Waterman, M.R., additional, Wettenhall, R.E.H., additional, Winniker, R., additional, Wood, W.I., additional, Yatani, A., additional, and Zhou, Z., additional more...
- Published
- 1989
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9. STRUCTURE OF THE MAMMALIAN PROGESTERONE RECEPTOR
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MILGROM, E., primary, LOGEAT, F., additional, LOOSFELT, H., additional, ATGER, M., additional, and VU HAI, M.T., additional
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- 1987
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10. Molecular and Cellular Biology of Mammalian Progesterone Receptors
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SAVOURET, J.F., primary, MISRAHI, M., additional, LOOSFELT, H., additional, ATGER, M., additional, BAILLY, A., additional, PERROT-APPLANAT, M., additional, VU HAI, M.T., additional, GUIOCHON-MANTEL, A., additional, JOLIVET, A., additional, LORENZO, F., additional, LOGEAT, F., additional, PICHON, M.F., additional, MILGROM, E., additional, and BOUCHARD, P., additional more...
- Published
- 1989
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11. Role of Hairless and Suppressor of Hairless in the Notch signaling pathway in Drosophila
- Author
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Lecourtois, M., primary, Brou, C., additional, Logeat, F., additional, Israel, A., additional, and Schweisguth, F., additional
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- 1995
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12. The human J kappa recombination signal sequence binding protein (RBP-J kappa) targets the Epstein-Barr virus EBNA2 protein to its DNA responsive elements.
- Author
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Waltzer, L., primary, Logeat, F., additional, Brou, C., additional, Israel, A., additional, Sergeant, A., additional, and Manet, E., additional
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- 1994
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13. Inhibition of the DNA-binding activity of Drosophila suppressor of hairless and of its human homolog, KBF2/RBP-J kappa, by direct protein-protein interaction with Drosophila hairless.
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Brou, C, primary, Logeat, F, additional, Lecourtois, M, additional, Vandekerckhove, J, additional, Kourilsky, P, additional, Schweisguth, F, additional, and Israël, A, additional
- Published
- 1994
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14. Inhibition of transcription factors belonging to the rel/NF-kappa B family by a transdominant negative mutant.
- Author
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Logeat, F., primary, Israël, N., additional, Ten, R., additional, Blank, V., additional, Le Bail, O., additional, Kourilsky, P., additional, and Israël, A., additional
- Published
- 1991
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15. HORMONAL CONTROL OF PROGESTERONE RECEPTORS*.
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Hai, M. T. Vu, Logeat, F., Warembourg, M., and Milgrom, E.
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- 1977
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16. TNF stimulates expression of mouse MHC class I genes by inducing an NF kappa B‐like enhancer binding activity which displaces constitutive factors.
- Author
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Israël, A., Le Bail, O., Hatat, D., Piette, J., Kieran, M., Logeat, F., Wallach, D., Fellous, M., and Kourilsky, P.
- Abstract
We have dissected the mouse H‐2Kb gene promoter in order to define the sequences responsible for induction by tumour necrosis factor (TNF‐alpha). An enhancer element (‐187 to ‐158) composed of two imperfect direct palindromic repeats has been shown to be necessary and sufficient for TNF‐alpha induction of a heterologous promoter. A multimer of either repeat is also responsive, while a single copy is not: this is the situation in the beta 2‐microglobulin (beta 2‐m) promoter which contains a single palindrome and does not respond to TNF‐alpha. We had previously found that the two repeats can bind a factor named KBF1. We show here that in the uninduced state the transcription factor AP2 binds to the interpalindromic region, while in TNF‐treated cells an NF kappa B‐like activity is induced which displaces both KBF1 and AP2 and binds to the two palindromes. This strongly suggests that induction of an NF kappa B‐like activity is responsible for TNF‐alpha stimulation of mouse MHC class I genes. more...
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- 1989
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17. Antibodies to rabbit progesterone receptor: crossreaction with human receptor.
- Author
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Logeat, F, Hai, M T, and Milgrom, E
- Abstract
Progesterone receptor from rabbit uterine cytosol was purified to a specific activity of approximately 2 nmol of bound hormone per mg of protein. A goat was immunized with this preparation and, after two injections of 0.7-0.8 nmol, yielded antireceptor antibodies. The antiserum reacted with both cytosolic and nuclear rabbit progesterone receptor and also with progesterone receptor from other rabbit tissues (vagina and pituitary). A crossreaction was observed with progesterone receptors from other mammalian, especially human, tissues (cytosolic receptor from rat and guinea pig uterus, cytosolic receptor from human breast cancer, and nuclear receptor from human endometrium). On the contrary, there was no interaction with a nonmammalian receptor (chicken oviduct progesterone receptor). The antibodies did not crossreact with other rabbit steroid receptors (uterine estradiol receptor and liver glucocorticoid receptor) or with nonreceptor progesterone-binding proteins (transcortin from plasma and uteroglobin from uterine fluid). more...
- Published
- 1981
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18. The rabbit progesterone receptor. Evidence for a single steroid-binding subunit and characterization of receptor mRNA.
- Author
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Loosfelt, H, Logeat, F, Vu Hai, M T, and Milgrom, E
- Abstract
Monoclonal antibodies were used to study the structure and the biosynthesis of the rabbit progesterone receptor. Proteins in nonfractionated uterine cytosol were submitted to gel electrophoresis in denaturing conditions, transferred onto nitrocellulose, and reacted with monoclonal antireceptor antibodies and 125I-protein A. A single 110,000-dalton protein was observed when precautions were taken during homogenization of the uteri and protease inhibitors used. Smaller forms of receptor (essentially of 79,000 daltons but also of 72,000 and in some experiments of 64,000 daltons) were present when these precautions were not observed and thus probably arose from artifactual proteolysis of receptor. When poly(A)+ RNA from rabbit uterus was translated in a reticulocyte lysate and the radioactive proteins precipitated by the antireceptor monoclonal antibodies, a radioactive protein of 110,000 daltons was also observed. Further evidence that this protein was the product of the translation of progesterone receptor mRNA was obtained by precipitation and immunoaffinity purification with several antireceptor monoclonal and polyclonal antibodies, inhibition of immunoprecipitation by purified receptor and its absence in a receptor-poor tissue (liver). Estrogen treatment is known to increase the concentration of progesterone receptor. RNA translation experiments showed that this effect is due to an increase in the concentration of receptor mRNA. The size of this messenger RNA was studied by sucrose gradient ultracentrifugation, followed by mRNA translation, and specific immunoprecipitation: progesterone receptor mRNA was found by this method to sediment at 20 S. more...
- Published
- 1984
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19. PROGESTERONE RECEPTORS IN THE RAT UTERUS: VARIATIONS IN CYTOSOL AND NUCLEI DURING THE OESTROUS CYCLE AND PREGNANCY
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VU HAI, M. T., LOGEAT, F., and MILGROM, E.
- Abstract
The concentration of progesterone receptors in rat uterine cytosol and nuclei was measured during the oestrous cycle and pregnancy. The method used allowed the measurement of the total concentration of binding sites (unbound and hormone-bound).During the oestrous cycle, the concentration of receptors in the cytosol peaked at pro-oestrus, low concentrations were observed at oestrus and metoestrus, and an increase was seen at dioestrus. In the nuclei, maximum concentrations occurred at pro-oestrus and dioestrus. The number of receptors in the cytosol was very low during the first half of pregnancy, but the concentration increased progressively after day 15 to attain a very high level (about 26 000 binding sites/cell) on day 22.In the nuclei, the concentration of receptors was low at the beginning of pregnancy. On day 5 (day of implantation) there was a slight increase, which corresponded to a decrease in the number of cytosolic receptors and a small peak in the level of progesterone in the plasma. Maximum concentrations were attained during a 'plateau' period between days 9 and 15. Thereafter, there was a decrease in the concentration of nuclear receptors and on day 22, the mean value was very low; in some animals, probably on the verge of parturition, no receptors were detectable in the nuclei. more...
- Published
- 1978
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20. The rabbit uteroglobin gene. Structure and interaction with the progesterone receptor.
- Author
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Bailly, A, Atger, M, Atger, P, Cerbon, M A, Alizon, M, Vu Haï, M T, Logeat, F, and Milgrom, E
- Abstract
The study of the regulation of uteroglobin gene in the rabbit endometrium constitutes a model for analyzing the mechanism of action of progesterone in mammals. The gene has been cloned into lambda phage and sequenced. Comparison of the sequence of the gene with the amino acid sequence of preuteroglobin and the three-dimensional structure of uteroglobin established by crystal x-ray diffraction showed that the 3 exons correspond to different functional domains of the protein and that at least one of the splice junctions does not map at the surface of the protein. S1 mapping allowed us to define the RNA polymerase initiation site. No difference was observed when analyzing premessengers from the endometrium, where the gene is controlled by progesterone and estradiol, and from lung where the gene is constitutively expressed and not controlled by these hormones. In addition, S1 mapping revealed the existence of several minor transcription initiation sites. In the 5' flanking region between positions -33 and -24 there is the sequence AATACAAAAA which may correspond to a Goldberg-Hogness box. Two other A- and T-rich sequences were found further upstream from the gene, one of these preceding by about 30 nucleotides a minor start of transcription. No obvious feature, possibly related to steroid regulation, was observed in the nucleotide sequence. A fragment of the gene containing the “promoter” region (from nucleotide +10 to nucleotide -394) was preferentially retained on nitrocellulose filters after incubation with purified rabbit uterine receptor. A competitive binding assay was used to compare the affinity for the receptor of various DNA fragments. Labeled “promoter” region DNA was incubated with receptor and various concentrations of nonlabeled competing DNA, and the nitrocellulose-bound radioactivity was measured. This method showed the existence of several high affinity binding sites in the 5' part of the gene and in adjacent regions. However, no high affinity binding sites were observed in the 3' part of the gene. Also, within the “promoter” region there were at least two high affinity binding sites for the receptor. more...
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- 1983
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21. Monoclonal antibodies to rabbit progesterone receptor: crossreaction with other mammalian progesterone receptors.
- Author
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Logeat, F, Vu Hai, M T, Fournier, A, Legrain, P, Buttin, G, and Milgrom, E
- Abstract
A mouse was immunized with purified rabbit uterine cytosolic progesterone receptor (specific activity: 3 nmol of steroid bound per mg of protein). After fusion of its spleen cells with Sp2-OAg myeloma cells, supernatants of 11 hybrid cultures were found to react in both an immunoenzymatic test and a double-immunoprecipitation test with the progesterone receptor. Clones were obtained from the five hybrid cells that gave the strongest response in both tests. Antibodies from cell culture supernatants and ascitic fluids were characterized. Three are of the IgG1 and two of the IgG2a isotype. Their apparent affinity for the progesterone receptor was measured by immunoprecipitation in physiological salt conditions. The equilibrium dissociation constants were between 0.1 and 4 nM. All five monoclonal antibodies crossreacted with the rabbit nuclear receptor, the human cytosolic receptor, and other mammalian (rat, guinea pig) but not avian (chicken) cytosolic progesterone receptors. There was no interaction with the glucocorticoid receptor and corticosteroid binding globulin. more...
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- 1983
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22. Phosphorylation of p105 PEST sequence via a redox-insensitive pathway up-regulates processing of p50 NF-kappaB.
- Author
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MacKichan, M L, Logeat, F, and Israël, A
- Abstract
The p105 Rel protein has dual functions; it is the precursor of the p5O subunit of NF-kappaB, and it acts as an IkappaB-like inhibitor to retain other Rel subunits in the cytoplasm. We have investigated the posttranslational regulation of p105 following activation of Jurkat T cells and find that a rapid and sustained phosphorylation of p105 is induced. The inducible phosphorylation occurs on multiple serines in the C-terminal-most 150 amino acids of the molecule, a region rich in Pro, Glu, Ser, and Thr residues. Phosphorylation of p105 in Jurkat cells treated with phorbol 12-myristate 13-acetate/ionomycin or with okadaic acid, another activator of NF-kappaB, is correlated with an increase in proteolytic processing to p5O. Intact PEST sequences are required for the phorbol 12-myristate 13-acetate/ionomycin-induced p105 processing, as a 68-amino acid C-terminal deletion abolishes the response to stimulation. When compounds that block Ikappa B alpha phosphorylation and degradation were tested, the serine protease inhibitors L-1-tosylamido-2-phenylethyl chloromethyl ketone and 1-chloro-3-tosyl-amido-7-amino-2-heptanone blocked inducible p105 phosphorylation, but the antioxidants pyrrolidine dithiocarbamate and butylated hydroxyanisol did not. Thus, while regulation of the p105 IkappaB resembles that of lkappaBa, involving inducible serine phosphorylation and proteolysis of the inhibitory ankyrin repeat domain, it depends on a different, redox-insensitive, signaling pathway. more...
- Published
- 1996
23. Ultrastructural localization of the progesterone receptor by an immunogold method: effect of hormone administration.
- Author
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Perrot-Applanat, M, Groyer-Picard, M T, Logeat, F, and Milgrom, E
- Abstract
The progesterone receptor has been localized in the rabbit uterus by immunocytochemistry at the electron microscopic level, using monoclonal antibodies and the protein A-gold technique. The progesterone receptor in uterine stromal cells was mainly localized in the nucleus; however, a small fraction of antigen was present in the cytoplasm, where it was associated with the rough endoplasmic reticulum and with free ribosomes. The plasma membrane was not labeled. In the nucleus, the receptor was always associated with condensed chromatin or areas surrounding condensed chromatin, whereas the nuceolus was not labeled. In the chromatin, receptor distribution varied according to the hormonal state: in the absence of progesterone, the receptor was randomly scattered over the clumps of condensed chromatin; after administration of the progestin R5020, it was mainly detected in the border regions between condensed chromatin and nucleoplasm and, to a lesser extent, over dispersed chromatin in the nucleoplasm. These areas have been shown to be the most active sites of gene transcription. more...
- Published
- 1986
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24. Radioimmunoassay of progesterone receptor in human tissues: application to breast cancer
- Author
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Brailly, S., Lorenzo, F., Jolivet, A., Logeat, F., Pallud, C., and Milgrom, E.
- Abstract
A radioimmunoassay method to measure progesterone receptor in rabbit and human tissues was devised and applied to human breast cancer. A specific progesterone receptor antibody was prepared by purifying rabbit receptor by immunoaffinity chromatography, sodium dodecylsulphate-polyacrylamide gel electrophoresis and injection of the isolated 110 000 dalton receptor band into a goat. Immunoblot studies of progesterone target and non-target tissues showed the specificity of the antibody, which was used at a dilution of 1/45 000. The tracer consisted of 125I-labelled electroeluted 110 000 dalton receptor.The sensitivity of the method was 1 fmol/tube for the rabbit receptor and 3 fmol/tube for the human receptor. The intra-assay coefficient of variation was 11% for tumours positive for the progesterone receptor and 9·9% for those on the borderline (10–30 fmol receptor/mg protein). The interassay coefficients of variation were 20 and 19% respectively. The correlation between the radioimmunoassay and a steroid-binding assay was studied in 40 tumour biopsies. In 39 cases, very good correlation was found (r= 0·99); in a single case an immunoreactive protein was detected which apparently bound steroid poorly.One important feature of this method was that receptor immunoreactivity remained unchanged when either the tissue or the cytosol was exposed to a temperature of 20 °C for relatively long periods of time. Under the same conditions the steroid-binding capacity declined rapidly. This characteristic of the radioimmunoassay may prevent errors due to improper handling of tissue samples. Such stability was not observed for oestrogen receptors when measured by a sandwich immunoenzymatic method after incubation of tissue at 20 °C.J. Endocr.(1988) 116,427–434 more...
- Published
- 1988
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25. Cloning and sequence analysis of rabbit progesterone-receptor complementary DNA.
- Author
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Loosfelt, H, Atger, M, Misrahi, M, Guiochon-Mantel, A, Meriel, C, Logeat, F, Benarous, R, and Milgrom, E
- Abstract
Two lambda gt11 clones containing fragments of cDNA encoding the rabbit progesterone receptor were isolated with the aid of monoclonal and monospecific polyclonal antireceptor antibodies. RNA gel blot analysis showed that the corresponding mRNA was approximately equal to 5900 nucleotides in size and present in the uterus, where its concentration was increased by estrogen treatment, and in the vagina. This mRNA was not detected in liver, in spleen, in intestine, and in kidney where the receptor protein is known to be absent or present in very small concentration. Cross-hybridizing clones were isolated from a lambda 10 library. The DNA was sequenced, and the primary structure of the progesterone receptor was deduced. It consists of 930 amino acids and contains a basic, cysteine-rich region (residues 568-645) with extensive homology to the glucocorticoid and estrogen receptors and the v-erbA oncogene protein. This region is followed by a C-terminal domain that is similar in size to the corresponding domains of the other steroid receptors and v-erbA and shows striking amino acid homology with the glucocorticoid receptor and significant homology with the estrogen receptor. In contrast, the region extending from the cysteine-rich segment toward the N terminus differed in size and amino acid sequence from that of the other receptors and v-erbA. This region had a high proline content in the progesterone receptor. more...
- Published
- 1986
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26. Poly (A) Polymerase Activity in L Cells Following Encephalomyocarditis Virus Infection
- Author
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Giron, M.-L., primary, Logeat, F., additional, Fossar, N., additional, and Huppert, J., additional
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- 1978
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27. Immunocytochemical Study of Mammalian Progesterone Receptor Using Monoclonal Antibodies*
- Author
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PERROT-APPLANAT, M., primary, LOGEAT, F., additional, GROYER-PICARD, M. T., additional, and MILGROM, E., additional
- Published
- 1985
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28. REGULATION BY PROGESTERONE OF GENE EXPRESSION IN THE ENDOMETRIUM
- Author
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Loosfelt, H., primary, Atger, M., additional, Logeat, F., additional, Vu Hai, M. T., additional, and Milgrom, E., additional
- Published
- 1981
- Full Text
- View/download PDF
29. HORMONAL CONTROL OF PROGESTERONE RECEPTORS
- Author
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Hai, M. T. Vu, primary, Logeat, F., additional, Warembourg, M., additional, and Milgrom, E., additional
- Published
- 1977
- Full Text
- View/download PDF
30. Molecular and Cellular Biology of Mammalian Progesterone Receptors
- Author
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SAVOURET, J.F., MISRAHI, M., LOOSFELT, H., ATGER, M., BAILLY, A., PERROT-APPLANAT, M., VU HAI, M.T., GUIOCHON-MANTEL, A., JOLIVET, A., LORENZO, F., LOGEAT, F., PICHON, M.F., BOUCHARD, P., and MLLGROM, E. more...
- Published
- 1989
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31. Chapter 9 - STRUCTURE OF THE MAMMALIAN PROGESTERONE RECEPTOR
- Author
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MILGROM, E., LOGEAT, F., LOOSFELT, H., ATGER, M., and VU HAI, M.T.
- Published
- 1987
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32. A glycosphingolipid binding domain controls trafficking and activity of the mammalian notch ligand delta-like 1.
- Author
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Heuss SF, Tarantino N, Fantini J, Ndiaye-Lobry D, Moretti J, Israël A, and Logeat F
- Subjects
- Amino Acid Sequence, Animals, Cell Membrane chemistry, Cell Membrane metabolism, Gene Silencing, Glucosyltransferases genetics, Glycosphingolipids chemistry, Humans, Ligands, Membrane Lipids metabolism, Mice, Molecular Sequence Data, Protein Binding, Protein Stability, Protein Transport, RNA Interference, Signal Transduction, Glycosphingolipids metabolism, Intercellular Signaling Peptides and Proteins chemistry, Intercellular Signaling Peptides and Proteins metabolism, Protein Interaction Domains and Motifs, Receptors, Notch metabolism
- Abstract
The activity of Notch ligands is tightly regulated by trafficking events occurring both before and after ligand-receptor interaction. In particular endocytosis and recycling have been shown to be required for full signaling activity of the ligands before they encounter the Notch receptor. However little is known about the precise endocytic processes that contribute to ligand internalization. Here we demonstrate that endocytosis contributes to Dll1 signaling activity by preserving the ligand from shedding and degradation. We further show that the glycosphingolipid-binding motif originally identified in Drosophila Notch ligands is conserved in mammals and is necessary for Dll1 internalization. Mutation of its conserved tryptophan residue results in a Dll1 molecule which is rapidly inactivated by shedding and degradation, does not recycle to the cell surface and does not activate Notch signaling. Finally, silencing in the signal-sending cells of glucosylceramide synthase, the enzyme implicated in the initial phase of glycosphingolipid synthesis, down-regulates Notch activation. Our data indicate that glycosphingolipids, by interacting with Dll1, may act as functional co-factors to promote its biological activity. more...
- Published
- 2013
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33. The intracellular region of Notch ligands Dll1 and Dll3 regulates their trafficking and signaling activity.
- Author
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Heuss SF, Ndiaye-Lobry D, Six EM, Israël A, and Logeat F
- Subjects
- Animals, Calcium-Binding Proteins, Drosophila, Endocytosis physiology, HeLa Cells, Humans, Intercellular Signaling Peptides and Proteins genetics, Intracellular Signaling Peptides and Proteins genetics, Ligands, Membrane Microdomains genetics, Membrane Microdomains metabolism, Membrane Proteins genetics, Mice, Protein Transport physiology, Receptor, Notch1 genetics, Receptor, Notch1 metabolism, Recombinant Fusion Proteins genetics, Recombinant Fusion Proteins metabolism, Intercellular Signaling Peptides and Proteins metabolism, Intracellular Signaling Peptides and Proteins metabolism, Membrane Proteins metabolism, Signal Transduction physiology, Ubiquitination physiology
- Abstract
Genetic studies have shown that ubiquitination and endocytosis of the Drosophila ligand Delta in signal-sending cells are required for activation of Notch signaling, but how these events promote Notch activation remains poorly understood. Here, we show that an ubiquitination-defective mutant of the murine Delta-homologue Dll1 is endocytosed but, in contrast to the wild-type Dll1, is unable to subsequently recycle back to the cell surface or to bind Notch1 efficiently. These results demonstrate that ubiquitination, although not required for endocytosis, is essential for Dll1 recycling and that recycling is required to acquire affinity for the receptor. On the other hand, a chimeric molecule encompassing the extracellular domain of Dll1 and the transmembrane/intracellular domain of Dll3, which contains no lysine, is endocytosed, recycled, and interacts with Notch1 but is unable to induce transendocytosis of the extracellular region of Notch1 or to signal. These observations suggest that the chimera uses an ubiquitination-independent signal to recycle, allowing it to acquire affinity for Notch1. Our results support the idea that ligand recycling determines its competence to bind efficiently to the receptor but that this is insufficient to allow it to perform transendocytosis, an event required for activation of Notch signaling. Finally, the present study indicates that Dll1 partially localizes to lipid microdomains, whereas both ubiquitination-defective Dll1 and the Dll1-3 chimera are excluded from these compartments, suggesting that these microdomains provide the environment necessary for Dll1 to activate Notch signaling. more...
- Published
- 2008
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34. [Endocytosis and Notch signalling].
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Brou C and Logeat F
- Subjects
- Animals, Humans, Ligands, Mammals, Models, Biological, Signal Transduction, Endocytosis physiology, Receptors, Notch physiology
- Published
- 2006
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35. The notch ligand Delta1 recruits Dlg1 at cell-cell contacts and regulates cell migration.
- Author
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Six EM, Ndiaye D, Sauer G, Laâbi Y, Athman R, Cumano A, Brou C, Israël A, and Logeat F
- Subjects
- 3T3 Cells, Adaptor Proteins, Signal Transducing, Amino Acid Motifs, Amino Acid Sequence, Animals, Biotinylation, Cell Communication, Cell Differentiation, Cell Line, Cell Movement, Discs Large Homolog 1 Protein, Electrophoresis, Polyacrylamide Gel, Flow Cytometry, Green Fluorescent Proteins metabolism, Guanylate Kinases, HeLa Cells, Hematopoietic Stem Cells metabolism, Humans, Immunoblotting, Immunoprecipitation, Intracellular Signaling Peptides and Proteins, Ligands, Mass Spectrometry, Membrane Proteins chemistry, Membrane Proteins metabolism, Mice, Microscopy, Fluorescence, Molecular Sequence Data, Plasmids metabolism, Protein Binding, Protein Structure, Tertiary, Proteins chemistry, Receptors, Notch, Sequence Homology, Amino Acid, Transfection, Wound Healing, Membrane Proteins physiology, Proteins physiology
- Abstract
Delta1 acts as a membrane-bound ligand that interacts with the Notch receptor and plays a critical role in cell fate specification. By using peptide affinity chromatography followed by mass spectrometry, we have identified Dlg1 as a partner of the Delta1 C-terminal region. Dlg1 is a human homolog of the Drosophila Discs large tumor suppressor, a member of the membrane-associated guanylate kinase family of molecular scaffolds. We confirmed this interaction by co-immunoprecipitation experiments between endogenous Dlg1 and transduced Delta1 in a 3T3 cell line stably expressing Delta1. Moreover, we showed that deletion of a canonical C-terminal PDZ-binding motif (ATEV) in Delta1 abrogated this interaction. Delta4 also interacted with Dlg1, whereas Jagged1, another Notch ligand, did not. In HeLa cells, transfected Delta1 triggered the accumulation of endogenous Dlg1 at sites of cell-cell contact. Expression of Delta1 also reduced the motility of 3T3 cells. Finally, deletion of the ATEV motif totally abolished these effects but did not interfere with the ability of Delta1 to induce Notch signaling and T cell differentiation in co-culture experiments. These results point to a new, probably cell-autonomous function of Delta1, which is independent of its activity as a Notch ligand. more...
- Published
- 2004
- Full Text
- View/download PDF
36. Monoubiquitination and endocytosis direct gamma-secretase cleavage of activated Notch receptor.
- Author
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Gupta-Rossi N, Six E, LeBail O, Logeat F, Chastagner P, Olry A, Israël A, and Brou C
- Subjects
- Amino Acid Sequence, Amyloid Precursor Protein Secretases, Animals, Aspartic Acid Endopeptidases, Cell Line, HeLa Cells, Humans, Immunoblotting, Ligands, Lysine chemistry, Microscopy, Confocal, Microscopy, Fluorescence, Molecular Sequence Data, Precipitin Tests, Presenilin-1, Protein Binding, Protein Structure, Tertiary, Receptors, Notch, Sequence Homology, Amino Acid, Signal Transduction, Time Factors, Transfection, Ubiquitin chemistry, Endocytosis, Endopeptidases metabolism, Membrane Proteins metabolism, Ubiquitin metabolism
- Abstract
Activation of mammalian Notch receptor by its ligands induces TNFalpha-converting enzyme-dependent ectodomain shedding, followed by intramembrane proteolysis due to presenilin (PS)-dependent gamma-secretase activity. Here, we demonstrate that a new modification, a monoubiquitination, as well as clathrin-dependent endocytosis, is required for gamma-secretase processing of a constitutively active Notch derivative, DeltaE, which mimics the TNFalpha-converting enzyme-processing product. PS interacts with this modified form of DeltaE, DeltaEu. We identified the lysine residue targeted by the monoubiquitination event and confirmed its importance for activation of Notch receptor by its ligand, Delta-like 1. We propose a new model where monoubiquitination and endocytosis of Notch are a prerequisite for its PS-dependent cleavage, and discuss its relevance for other gamma-secretase substrates. more...
- Published
- 2004
- Full Text
- View/download PDF
37. The Notch ligand Delta1 is sequentially cleaved by an ADAM protease and gamma-secretase.
- Author
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Six E, Ndiaye D, Laabi Y, Brou C, Gupta-Rossi N, Israel A, and Logeat F
- Subjects
- Amino Acid Sequence, Amyloid Precursor Protein Secretases, Animals, Aspartic Acid Endopeptidases, Cell Line, Cell Nucleus metabolism, Cells, Cultured, Chromatography, Gel, Electrophoresis, Polyacrylamide Gel, Flow Cytometry, Genetic Vectors, Humans, Immunoblotting, Intracellular Signaling Peptides and Proteins, Membrane Proteins genetics, Mice, Microscopy, Fluorescence, Models, Genetic, Molecular Sequence Data, Mutation, Precipitin Tests, Presenilin-1, Protein Binding, Protein Structure, Tertiary, Sequence Homology, Amino Acid, Signal Transduction, Transfection, Endopeptidases metabolism, Membrane Proteins metabolism, Metalloendopeptidases metabolism
- Abstract
Notch signaling is involved in numerous cell fate decisions in invertebrates and vertebrates. The Notch receptor is a type I transmembrane (TM) protein that undergoes two proteolytic steps after ligand binding, first by an ADAM (a distintegrin and metalloprotease) in the extracellular region, followed by gamma-secretase-mediated cleavage inside the TM domain. We demonstrate here that the murine ligand Delta1 (Dll1) undergoes the same sequence of cleavages, in an apparently signal-independent manner. Identification of the ADAM-mediated shedding site localized 10 aa N-terminal to the TM domain has enabled us to generate a noncleavable mutant. Kuzbanian/ADAM10 is involved in this processing event, but other proteases can probably substitute for it. We then show that Dll1 is part of a high-molecular-weight complex containing presenilin1 and undergoes further cleavage by a gamma-secretase-like activity, therefore releasing the intracellular domain that localizes in part to the nucleus. Using the shedding-resistant mutant, we demonstrate that this gamma-secretase cleavage depends on prior ectodomain shedding. Therefore Dll1 is a substrate for regulated intramembrane proteolysis, and its intracellular region possibly fulfills a specific function in the nucleus. more...
- Published
- 2003
- Full Text
- View/download PDF
38. Functional interaction between SEL-10, an F-box protein, and the nuclear form of activated Notch1 receptor.
- Author
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Gupta-Rossi N, Le Bail O, Gonen H, Brou C, Logeat F, Six E, Ciechanover A, and Israël A
- Subjects
- Amino Acid Sequence, Animals, Cell Cycle Proteins genetics, Cell Line, Cysteine Endopeptidases physiology, Helminth Proteins genetics, Humans, Mice, Molecular Sequence Data, Multienzyme Complexes physiology, Phosphorylation, Proteasome Endopeptidase Complex, Receptor, Notch1, Transcriptional Activation, Ubiquitins metabolism, Caenorhabditis elegans Proteins, Cell Cycle Proteins physiology, Cell Nucleus metabolism, Helminth Proteins physiology, Membrane Proteins metabolism, Receptors, Cell Surface, Transcription Factors
- Abstract
The Notch signaling pathway is essential in many cell fate decisions in invertebrates as well as in vertebrates. After ligand binding, a two-step proteolytic cleavage releases the intracellular part of the receptor which translocates to the nucleus and acts as a transcriptional activator. Although Notch-induced transcription of genes has been reported extensively, its endogenous nuclear form has been seldom visualized. We report that the nuclear intracellular domain of Notch1 is stabilized by proteasome inhibitors and is a substrate for polyubiquitination in vitro. SEL-10, an F-box protein of the Cdc4 family, was isolated in a genetic screen for Lin12/Notch-negative regulators in Caenorhabditis elegans. We isolated human and murine counterparts of SEL-10 and investigated the role of a dominant-negative form of this protein, deleted of the F-box, on Notch1 stability and activity. This molecule could stabilize intracellular Notch1 and enhance its transcriptional activity but had no effect on inactive membrane-anchored forms of the receptor. We then demonstrated that SEL-10 specifically interacts with nuclear forms of Notch1 and that this interaction requires a phosphorylation event. Taken together, these data suggest that SEL-10 is involved in shutting off Notch signaling by ubiquitin-proteasome-mediated degradation of the active transcriptional factor after a nuclear phosphorylation event. more...
- Published
- 2001
- Full Text
- View/download PDF
39. A novel proteolytic cleavage involved in Notch signaling: the role of the disintegrin-metalloprotease TACE.
- Author
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Brou C, Logeat F, Gupta N, Bessia C, LeBail O, Doedens JR, Cumano A, Roux P, Black RA, and Israël A
- Subjects
- ADAM Proteins, ADAM17 Protein, Amino Acid Sequence, Animals, Bone Marrow Cells cytology, Bone Marrow Cells drug effects, Calcium-Binding Proteins, Cell Differentiation, Intercellular Signaling Peptides and Proteins, Mice, Molecular Sequence Data, Monocytes cytology, Monocytes drug effects, Protein Biosynthesis, Protein Processing, Post-Translational, Receptor, Notch1, Serrate-Jagged Proteins, Signal Transduction, Tetradecanoylphorbol Acetate pharmacology, Disintegrins metabolism, Membrane Proteins metabolism, Metalloendopeptidases metabolism, Proteins, Receptors, Cell Surface metabolism, Transcription Factors
- Abstract
The Notch1 receptor is presented at the cell membrane as a heterodimer after constitutive processing by a furin-like convertase. Ligand binding induces the proteolytic release of Notch intracellular domain by a gamma-secretase-like activity. This domain translocates to the nucleus and interacts with the DNA-binding protein CSL, resulting in transcriptional activation of target genes. Here we show that an additional processing event occurs in the extracellular part of the receptor, preceding cleavage by the gamma-secretase-like activity. Purification of the activity accounting for this cleavage in vitro shows that it is due to TACE (TNFalpha-converting enzyme), a member of the ADAM (a disintegrin and metalloprotease domain) family of metalloproteases. Furthermore, experiments carried out on TACE-/- bone marrow-derived monocytic precursor cells suggest that this metalloprotease plays a prominent role in the activation of the Notch pathway. more...
- Published
- 2000
- Full Text
- View/download PDF
40. Delta-1 activation of notch-1 signaling results in HES-1 transactivation.
- Author
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Jarriault S, Le Bail O, Hirsinger E, Pourquié O, Logeat F, Strong CF, Brou C, Seidah NG, and Isra l A
- Subjects
- Basic Helix-Loop-Helix Transcription Factors, Cell Differentiation genetics, DNA-Binding Proteins genetics, Disintegrins genetics, Fluorescent Antibody Technique, Gene Expression Regulation genetics, Genes, Reporter genetics, HeLa Cells, Humans, Intracellular Signaling Peptides and Proteins, Metalloendopeptidases genetics, Promoter Regions, Genetic genetics, Receptor, Notch1, Transcription Factor HES-1, Transcription Factors genetics, Transfection genetics, Drosophila Proteins, Homeodomain Proteins genetics, Membrane Proteins genetics, Receptors, Cell Surface, Signal Transduction genetics, Transcriptional Activation genetics
- Abstract
The Notch receptor is involved in many cell fate determination events in vertebrates and invertebrates. It has been shown in Drosophila melanogaster that Delta-dependent Notch signaling activates the transcription factor Suppressor of Hairless, leading to an increased expression of the Enhancer of Split genes. Genetic evidence has also implicated the kuzbanian gene, which encodes a disintegrin metalloprotease, in the Notch signaling pathway. By using a two-cell coculture assay, we show here that vertebrate Dl-1 activates the Notch-1 cascade. Consistent with previous data obtained with active forms of Notch-1 a HES-1-derived promoter construct is transactivated in cells expressing Notch-1 in response to Dl-1 stimulation. Impairing the proteolytic maturation of the full-length receptor leads to a decrease in HES-1 transactivation, further supporting the hypothesis that only mature processed Notch is expressed at the cell surface and activated by its ligand. Furthermore, we observed that Dl-1-induced HES-1 transactivation was dependent both on Kuzbanian and RBP-J activities, consistent with the involvement of these two proteins in Notch signaling in Drosophila. We also observed that exposure of Notch-1-expressing cells to Dl-1 results in an increased level of endogenous HES-1 mRNA. Finally, coculture of Dl-1-expressing cells with myogenic C2 cells suppresses differentiation of C2 cells into myotubes, as previously demonstrated for Jagged-1 and Jagged-2, and also leads to an increased level of endogenous HES-1 mRNA. Thus, Dl-1 behaves as a functional ligand for Notch-1 and has the same ability to suppress cell differentiation as the Jagged proteins do. more...
- Published
- 1998
- Full Text
- View/download PDF
41. The Notch1 receptor is cleaved constitutively by a furin-like convertase.
- Author
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Logeat F, Bessia C, Brou C, LeBail O, Jarriault S, Seidah NG, and Israël A
- Subjects
- Calcimycin pharmacology, Enzyme Inhibitors pharmacology, Furin, HeLa Cells, Humans, Ionophores pharmacology, Membrane Proteins genetics, Mutation, Receptor, Notch1, Subtilisins antagonists & inhibitors, Subtilisins genetics, Membrane Proteins metabolism, Receptors, Cell Surface, Signal Transduction drug effects, Subtilisins metabolism, Transcription Factors
- Abstract
The Notch receptor, which is involved in numerous cell fate decisions in invertebrates and vertebrates, is synthesized as a 300-kDa precursor molecule (p300). We show here that proteolytic processing of p300 is an essential step in the formation of the biologically active receptor because only the cleaved fragments are present at the cell surface. Our results confirm and extend recent reports indicating that the Notch receptor exists at the plasma membrane as a heterodimeric molecule, but disagree as to the nature of the protease that is responsible for the cleavage that takes place in the extracellular region. We report here that constitutive processing of murine Notch1 involves a furin-like convertase. We show that the calcium ionophore A23187 and the alpha1-antitrypsin variant, alpha 1-PDX, a known inhibitor of furin-like convertases, inhibit p300 processing. When expressed in the furin-deficient Lovo cell line, p300 is not processed. In vitro digestion of a recombinant Notch-derived substrate with purified furin allowed mapping of the processing site to the carboxyl side of the sequence RQRR (amino acids 1651-1654). Mutation of these four amino acids (and of two secondary dibasic furin sites located nearby) completely abolished processing of the Notch1 receptor. more...
- Published
- 1998
- Full Text
- View/download PDF
42. Signalling downstream of activated mammalian Notch.
- Author
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Jarriault S, Brou C, Logeat F, Schroeter EH, Kopan R, and Israel A
- Subjects
- Animals, Base Sequence, Basic Helix-Loop-Helix Transcription Factors, Cell Line, DNA-Binding Proteins metabolism, Drosophila, HeLa Cells, Homeodomain Proteins genetics, Humans, Immunoglobulin J Recombination Signal Sequence-Binding Protein, Mice, Molecular Sequence Data, Mutagenesis, Oligodeoxyribonucleotides, Promoter Regions, Genetic, Receptors, Notch, Repressor Proteins genetics, Transcription Factor HES-1, Transfection, Drosophila Proteins, Membrane Proteins metabolism, Nuclear Proteins, Transcription Factors metabolism, Transcriptional Activation
- Abstract
Notch belongs to a family of transmembrane proteins that are widely conserved from flies to vertebrates and are thought to be involved in cell-fate decisions. In Drosophila, the Suppressor of hairless (Su(H)) gene and genes of the Enhancer of split (E(Spl)) complex, which encode proteins of the basic helix-loop-helix type have been implicated in the Notch signalling pathway. Mammalian homologues of E(Spl), such as the mouse Hairy enhancer of split (HES-1), have been isolated. Both HES-1 and the intracellular domain of murine Notch (mNotch) are able to block MyoD-induced myogenesis. Here we show that activated forms of mNotch associate with the human analogue of Su(H), KBF2/RBP-J kappa (refs 8,9) and act as transcriptional activators through the KBF2-binding sites of the HES-1 promoter. more...
- Published
- 1995
- Full Text
- View/download PDF
43. Genomic structure and chromosomal localization of processed pseudogenes for human RBP-Jk.
- Author
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Zhang M, Tang X, Jin C, Logeat F, Alain I, Kondo S, Sun K, and Yokoyama K
- Subjects
- Base Sequence, Chromosomes, Human, Pair 9 chemistry, Cosmids genetics, DNA-Binding Proteins chemistry, Genes, Immunoglobulin genetics, Genomic Library, HeLa Cells, Humans, Immunoglobulin J Recombination Signal Sequence-Binding Protein, Molecular Sequence Data, DNA-Binding Proteins genetics, Nuclear Proteins, Pseudogenes genetics
- Abstract
The functional gene for human recombination signal sequence-binding protein (RBP-Jk) and corresponding processed psudogenes have been isolated from various species, such as Drosophila, Xenopus, mouse, and human. Here we report the isolation of another two genomic pseudogenes of human RBP-Jk, named K2 and K7, from a cosmid library of Hela cells. The nucleotide sequences of both genes exhibited more than 95% homology to the functional human gene for RBP-Jk. Moreover, they did not contain any intron sequences and were interrupted by several stop codons in all frames. In situ hybridization demonstrated that the pseudogenes, K2 and K7, were localized at chromosomes 9p13 and 9q13, respectively. Their physical maps differed from those of the true functional gene and of the pseudogenes reported previously by Amakawa et al. (1993). more...
- Published
- 1994
- Full Text
- View/download PDF
44. The DNA binding subunit of NF-kappa B is identical to factor KBF1 and homologous to the rel oncogene product.
- Author
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Kieran M, Blank V, Logeat F, Vandekerckhove J, Lottspeich F, Le Bail O, Urban MB, Kourilsky P, Baeuerle PA, and Israël A
- Subjects
- Amino Acid Sequence, Animals, Base Sequence, Binding Sites, Cloning, Molecular, DNA-Binding Proteins metabolism, Drosophila genetics, Enhancer Elements, Genetic, Female, Gene Library, Genes, MHC Class I, HeLa Cells metabolism, Humans, Macromolecular Substances, Molecular Sequence Data, NF-kappa B, NF-kappa B p50 Subunit, Oncogene Proteins v-rel, Plasmids, Polymerase Chain Reaction, Protein Biosynthesis, Protein-Tyrosine Kinases genetics, Sequence Homology, Nucleic Acid, Transcription Factors isolation & purification, Transcription Factors metabolism, Transcription, Genetic, DNA-Binding Proteins genetics, Oncogenes, Retroviridae Proteins, Oncogenic genetics, Transcription Factors genetics
- Abstract
The major determinant in the transcriptional control of class I genes of the major histocompatibility complex is an enhancer sequence located around -170 from the transcription start site, which binds a factor named KBF1. We have isolated a complementary cDNA coding for KBF1 and identified the DNA binding and dimerization domain of the protein. Because KBF1 and the transcription factor NF-kappa B bind to similar sequences, we investigated the relationship between these two molecules. It appeared that KBF1 is, by all criteria used, identical to the 50 kd DNA binding subunit of NF-kappa B. KBF1 (and therefore p50) also displays extensive amino acid sequence homology with the v-rel oncogene and the Drosophila maternal morphogen dorsal. In vitro experiments suggest functional homologies between KBF1 and v-rel. more...
- Published
- 1990
- Full Text
- View/download PDF
45. Regulatory elements involved in the liver-specific expression of the mouse MHC class I Q10 gene: characterization of a new TATA-binding factor.
- Author
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David-Watine B, Logeat F, Israel A, and Kourilsky P
- Subjects
- Animals, Base Sequence, DNA genetics, Enhancer Elements, Genetic, Genes, Regulator, H-2 Antigens genetics, Liver immunology, Mice, Molecular Sequence Data, Promoter Regions, Genetic, Sequence Homology, Nucleic Acid, TATA Box genetics, Carrier Proteins genetics, Genes, MHC Class I, Histocompatibility Antigens Class I genetics
- Abstract
The murine MHC genes code for the classical H-2K, D, and L transplantation antigens, and for other class I-like proteins called Qa and TIa molecules. Most of the latter have a restricted tissue distribution whereas classical transplantation antigens are virtually expressed by all somatic cells of the adult organism. Q10 is a Qa region gene, which was found to be expressed in liver and yolk sac, a regulatory pattern more evocative of the expression of a large set of serum proteins secreted by the liver than of a classical class I antigen. First, we have characterized several regions in the promoter of Q10 which bind factors present in liver nuclear extracts. Our most striking observation is that one of these factors, which we named TA-f, binds in the TATA box region of Q10 and Kb and displays tissue-specific expression, in that we found the activity only in liver and kidney. Secondly, we have performed a comparative analysis of the 5' upstream sequences of Q10 with those of H-2Kb, Ld, and other Qa genes. We have shown that most of the regulatory elements involved in the ubiquitous expression of H-2Kb are punctually altered and not functional in Q10. Similarly, most of the binding sequences for liver factors in the Q10 promoter, except the TA region, do not exist in the other H-2 class I genes which, however, have conserved most of the functional regions defined in H-2Kb and Ld. These results suggest that the tissue-specific expression of Q10 is associated with both alteration of the sequences conferring ubiquitous expression to other class I genes and/or creation of new sequences able to bind liver-specific regulatory factors. However, our observations also suggest that a unique sequence, the TATA box, may confer differential regulation in different tissues, since it binds a factor whose expression is restricted to the liver and kidney. more...
- Published
- 1990
- Full Text
- View/download PDF
46. Structure, function and immunolocalization of rabbit and human progesterone receptors.
- Author
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Misrahi M, Loosfelt H, Atger M, Bailly A, Perrot-Applanat M, Logeat F, Guiochon-Mantel A, Lorenzo F, and Milgrom E
- Subjects
- Animals, Antibodies, Monoclonal, Cloning, Molecular, DNA-Binding Proteins metabolism, Humans, Immunohistochemistry, Rabbits, Receptors, Progesterone genetics, Receptors, Progesterone metabolism
- Published
- 1990
47. [Physiology of progesterone receptors].
- Author
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Logeat F, Vu Hai MT, Atger M, and Milgrom E
- Subjects
- Animals, Cytosol physiology, Endometrium physiology, Estrus, Female, Guinea Pigs, Ovulation, Pregnancy, Uterus physiology, Pregnancy, Animal, Receptors, Progesterone physiology
- Published
- 1979
48. Estrogen receptors at implantation sites of rat endometrium.
- Author
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Logeat F, Sartor P, Hai MT, and Milgrom E
- Subjects
- Animals, Embryo Implantation, Female, Pregnancy, Rats, Endometrium metabolism, Receptors, Estrogen metabolism
- Published
- 1982
- Full Text
- View/download PDF
49. The nuclear-bound form of the progesterone receptor is generated through a hormone-dependent phosphorylation.
- Author
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Logeat F, Le Cunff M, Pamphile R, and Milgrom E
- Subjects
- Animals, Chromatography, Affinity, Cytosol metabolism, Electrophoresis, Polyacrylamide Gel, Female, Molecular Weight, Phosphorylation, Rabbits, Receptors, Progesterone drug effects, Cell Nucleus metabolism, Norpregnadienes pharmacology, Phosphoproteins metabolism, Promegestone pharmacology, Receptors, Progesterone metabolism, Uterus metabolism
- Abstract
The solubilized ("cytosolic") receptor present in the rabbit uterus in the absence of hormone and the chromatin-bound ("nuclear") receptor obtained after injection of a progestin were compared. Crude cellular extracts were analyzed by immunoblotting and receptors were purified by immunoaffinity chromatography. With both methods it was observed that the electrophoretic mobility of the "nuclear" receptor was slower than that of the "cytosolic" receptor. This difference in mobility appeared to be due to the existence of variably phosphorylated forms of receptor. The phosphorylation reaction was examined in uterine slices. In the absence of hormone the cytosolic receptor was phosphorylated. When hormone was added the phosphorylation of receptor was markedly enhanced and the electrophoretic mobility of the "nuclear" receptor was decreased. These experiments thus show that the receptor in its "cytosolic" form is a phosphoprotein. Under the effect of the hormone the receptor is further phosphorylated on some supplementary site(s). This polyphosphoprotein is the chromatin-bound, putatively active, form of the receptor. In this respect the intracellular progesterone receptor is similar to various membrane receptors for hormones and growth factors which are phosphorylated upon binding of their ligand. more...
- Published
- 1985
- Full Text
- View/download PDF
50. One-step immunoaffinity purification of active progesterone receptor. Further evidence in favor of the existence of a single steroid binding subunit.
- Author
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Logeat F, Pamphile R, Loosfelt H, Jolivet A, Fournier A, and Milgrom E
- Subjects
- Animals, Antibodies, Monoclonal, Chromatography, Affinity, Cytosol metabolism, Female, Kinetics, Macromolecular Substances, Molecular Weight, Peptide Fragments analysis, Promegestone metabolism, Rabbits, Receptors, Progesterone immunology, Receptors, Progesterone metabolism, Sepharose, Staphylococcal Protein A, Uterus metabolism, Receptors, Progesterone isolation & purification
- Abstract
A very high capacity immunoaffinity matrix for the purification of progesterone receptor was prepared by cross-linking a monoclonal antireceptor antibody to protein A-Sepharose through the Fc fragment. The monoclonal antibody was selected for its property of losing affinity for the receptor at pH 10.5, i.e., in conditions where the receptor remains stable for extensive periods of time. This made it possible to elute active receptor form the immunosorbent. From crude rabbit uterine cytosol the steroid-receptor complexes were purified in a single step. A 1-mL column (containing 7 mg of monoclonal antibody) bound 1600 pmol of steroid-receptor complexes of which 79.5% were eluted. The overall yield of purification was 49%. The specific activity of the purified steroid-receptor complexes was 6.71 +/- 0.79 nmol of bound steroid/mg of protein (mean +/- SE of four experiments). The purified receptor consisted of a mixture of 110 000- and 79 000-dalton forms. The latter appeared to be produced by proteolysis of the larger form during purification since immunoblot experiments showed that, at the start of purification, the 110 000-dalton form was present in overwhelming majority (80-95%) in the uterine cytosol and that the 79 000-dalton form only appeared during purification. This conclusion was also supported by the peptide analysis of both forms of receptor: the purified receptor was denatured and labeled with 125I; the 110 000- and 79 000-dalton forms were isolated by gel electrophoresis in denaturing conditions and electroelution and were then submitted to mild or extensive digestions by trypsin, chymotrypsin, and protease V8 from Staphylococcus aureus.(ABSTRACT TRUNCATED AT 250 WORDS) more...
- Published
- 1985
- Full Text
- View/download PDF
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