Renoir, Jack-Michel
- Etudes sur le métabolisme et la physiopathologie des hormones stéroïdes.
- Purification, caractérisation physicochimique et mesures des paramètres biologiques de la protéine de liaison plasmatique des hormones sexuelles testostérone et oestradiol (SBP: "Sex steroid Binding Plasma Protein).
- Etude phylogénique de la SBP.
- Mise au point d'un dosage radioimmunologique de la SBP.
03/09/1979 au 31/08/1980: Directeur de recherches au Centre International de Recherches Médicales de Franceville (GABON).
Formation de sept techniciens gabonais aux techniques:
- de biochimie classiques des protéines (Chromatographie, filtration, électrophorèse, électrofocalisation, immunoélectrophorèse, Western-Blot).
- enzymatiques.
- radioimmunologiques.
Mise au point des RIA de la testostérone, de l'oestradiol, de la progestérone, de la dihydrotestostérone, de la LH et de la FSH pour le service clinique de l'hôpital de Franceville.
01/09/1980 au 14/06/1982: INSERM U 33 - Etude du récepteur de la progestérone de l'oviducte de poulet: caractérisation biochimique et biologique, purification par chromatographie d'affinité des formes actives (liant l'ADN) et inactives (ne liant pas l'ADN) du récepteur, obtention d'anticorps polyclonaux anti-récepteur de la progestérone de poulet.
15/06/1982 au 30/11/1982: Salk Institute, San Diego C.A., USA; Laboratoire du Pr R.G. Guillemin. - Stage de formation aux techniques de microséquençage de protéines.
01/12/1982 au 30/05/1997: INSERM U 33 (Communications Hormonales)
- Etude de la structure du récepteur de la progestérone de l'oviducte de poulet et de l'utérus de lapin.
- Identification de la protéine de choc thermique hsp90 comme partenaire ubiquitaire des récepteurs stéroïdiens.
- Obtention d'anticorps monoclonaux anti-hsp90.
- Etude du mécanisme d'action d'antihormones, notamment de l'antiglucocorticostéroïde /antiprogestagènes RU486.
- Etude des interactions récepteurs-ligands avec l'ADN de gènes cibles. Empreinte à la DNAse I.
- Etude de la phosphorylation des récepteurs.
- Caractérisation des protéines associées aux récepteurs autres que la hsp90. Identification des immunophilines FKBP59 et CYP40 (cyclophiline 40).
- Etude de l'influence des immunosuppresseurs sur l'activité transcriptionnelle de gènes régulés par les stéroïdes.
- Mise en évidence de la participation des P-glycoprotéines dans le mécanisme de transduction du signal stéroïdien dans des fibroblastes de souris.
Depuis le 01/06/1997: CNRS UMR 8612 (Laboratoire de Physico-Chimie-Pharmacotechnie- Biopharmacie). Responsable du groupe Pharmacologie cellulaire et moléculaire.
Etude des effets des antihormones et des analogues inactifs d'immunosuppresseurs dans des cancers hormonodépendants. Vectorisation des molécules.
- Invité à délivrer le cours "Hormones and antihormones steroids", Course on Molecular Biology of Steroid Hormones, Milan, 1988.
- Membre de l'Endocrine Society depuis 1984.
- Membre de la société de Biologie cellulaire de France depuis 1992.
Renoir J.M., Mercier-Bodard C. & Baulieu E.E. (1980): Hormonal and immunological aspects of the phylogeny of sex binding plasma protein. Proc. Natl. Acad. Sci. USA 77, 4578-4582.
Renoir J.M., Mercier-Bodard C. & Baulieu E.E. (1980): Hormonal and immunological aspects of sex binding plasma protein of primates. J. Reprod. Fertil. suppl. 28, 113-119.
Schaison G., Renoir J.M., Lagoguey M. & Mowsovicz I. (1980): On the role of dihydrotestosterone in regulating luteinizing hormone secretion in man. J. Clin. Endocrinol. Metab. 51, 1133-1137.
Renoir J.M., Yang C.R., Formstecher P., Lustenberger P., Wolfson A., Redeuilh G., Mester Y., Richard-Foy H. & Baulieu E.E. (1982a): Chick oviduct progesterone receptor: purification of a molybdate-stabilized form and preliminary characterization. Eur. J. Biochem. 127, 71-79.
Renoir J.M., Radanyi C., Yang C.R. & Baulieu E.E. (1982b): Antibodies against chick oviduct progesterone receptor. Cross-reactivity with mammalian progesterone receptors. Eur. J. Biochem. 127, 81-86.
Yang C.R., Mester J., Wolfson A., Renoir J.M. & Baulieu E.E. (1982): Activation of the chick oviduct progesterone receptor by heparin in the presence or absence of hormone. Biochem. J. 208, 399-406.
Radanyi C., Joab I., Renoir J.M., Richard-Foy, H. & Baulieu E.E. (1983): Monoclonal antibody to chicken oviduct progesterone receptor. Proc. Natl. Acad. Sci. USA 80, 2854-2858.
Garcia T., Tuohimaa P., Mester J., Buchou T., Renoir J.M. & Baulieu E.E. (1983): Protein kinase activity of purified components of the chicken oviduct progesterone receptor. Biochem. Biophys. Res. Commun. 113, 960-966.
Buchou T., Mester J., Renoir J.M. & Baulieu,E.E. (1983): Effects of urea and molybdate on the chick oviduct progesterone receptor. Biochem. Biophys. Res. Commun. 114, 479-487.
Renoir J.M., Mester J., Buchou T., Catelli M.G., Tuohimaa P., Binart N., Joab I., Radanyi C. & Baulieu,E.E. (1984a): Purification by affinity chromatography and immunological characterization of a 110 kDa component of the chick oviduct progesterone receptor. Biochem. J. 217, 685-692.
Joab I., Radanyi C., Renoir J.M., Buchou T., Catelli M.G., Binart N., Mester J. & Baulieu E.E. (1984): Immunological evidence for a common non-hormone binding component in non-transformed chick oviduct receptors of four steroid hormones. Nature 308, 850-853.
Tuohimaa P., Renoir J.M., Radanyi C., Mester J., Joab I., Buchou T. & Baulieu E.E. (1984b): Antibodies against highly purified B-subunit of the chick oviduct progesterone receptor. Biochem. Biophys. Res. Commun. 119, 433-439.
Renoir J.M., Buchou T., Mester J., Radanyi C. & Baulieu E.E. (1984b): Oligomeric structure of the molybdate-stabilized, non-transformed "8S" progesterone receptor from chicken oviduct cytosol. Biochemistry 23, 6016-6023.
Gasc J.M., Renoir J.M., Radanyi, C., Joab I., Tuohimaa P. & Baulieu E.E. (1984): Progesterone receptor in the chick oviduct: an immunohistochemical study with antibodies to distinct receptor components. J. Cell Biol. 99, 1193-1201
Moudgil V.K., Eessalu T.E., Buchou T., Renoir J.M., Mester J. & Baulieu E.E. (1985): Transformation of chick oviduct progesterone receptor in vitro: effects of hormone, salt, heat and adenosine triphosphate. Endocrinology 116, 1267-1274.
Groyer A., Le Bouc Y., Joab I., Radanyi C., Renoir J.M., Robel P. & Baulieu E.E. (1985): Chick oviduct glucocorticosteroid receptor. Specific binding of RU486 and immunological studies with antibodies to chick oviduct progesterone receptor. Eur. J. Biochem. 149, 445-451.
Catelli M.G., Binart N., Jung-Testas I., Renoir J.M., Baulieu E.E., Feramisco J.R. & Welch W.J. (1985): The common 90-kDa protein component of non-transformed "8S" steroid receptors is a heat-shock protein. The EMBO J. 4, 3131-3135.
Von der Ahe D., Renoir J.M., Buchou T., Baulieu E.E. & Beato M. (1986): Receptors for glucocorticosteroid and progesterone recognize distinct features of a DNA regulatory element. Proc. Natl. Acad. Sci. USA 83, 2817-2821.
Renoir J.M., Buchou T. & Baulieu E.E. (1986): Involvement of a non-hormone-binding 90 kDa protein in the non-transformed 8S form of the rabbit uterus progesterone receptor. Biochemistry 25, 6405-6413.
Garcia T., Buchou,T., Renoir J.M., Mester J. & Baulieu E.E. (1986): A protein kinase copurified with chick oviduct progesterone receptor. Biochemistry 25, 7937-7942.
Aranyi P., Radanyi C., Renoir J.M., Devin J. & Baulieu E.E. (1988): Covalent stabilization of the non-transformed chick oviduct cytosol progesterone receptor by chemical cross-linking. Biochemistry 27, 1330-1336.
Renoir J.M., Radanyi C. & Baulieu E.E. (1989): The antiprogesterone RU486 stabilizes the heterooligomeric non-DNA-binding 8S-form of the rabbit uterus cytosol progesterone receptor. Steroids, 53, 1-20.
Radanyi C., Renoir J.M., Sabbah M. & Baulieu E.E. (1989): Chick heat-shock protein of Mr 90,000 (hsp90), free or released from progesterone receptor, is in a dimeric form. J. Biol. Chem. 264, 2568-2573.
Gasc J.M., Renoir J.M., Faber L.E. & Baulieu E.E. (1990): Nuclear localization of two steroid receptor-associated proteins, hsp90 and p59. Exp. Cell Res. 186, 362-367.
Renoir J.M., Radanyi C., Faber L. & Baulieu E.E. (1990a): The non-DNA binding heterooligomeric form of mammalian steroid hormone receptors contains a hsp90-bound 59 kDa protein. J. Biol. Chem. 265, 10740-10745.
Renoir J.M., Jung-Testas, I., Radanyi C., Faber L. & Baulieu E.E. (1990b): The non-activated progesterone receptor is a nuclear heterooligomer. J. Biol. Chem. 265, 14402-14406.
Jung-Testas I., Renoir J.M., Gasc J.M. & Baulieu E.E. (1991) Estrogen-inducible progesterone receptor in primary cultures of rat glial cells. Exp. Cell Res., 193, 12-19.
Lebeau M.C., Massol, N., Herrick, J., Faber, L.E., Renoir, J.M., Radanyi, C. & Baulieu, E.E. (1992): P59, an hsp90 binding protein; cloning and sequencing of its cDNA. Preparation of a peptide-directed polyclonal antibody. J. Biol. Chem., 267, 4281-4284.
Callebaut I., Renoir J.M., Lebeau M.C., Massol N., Burny A., Baulieu E.E. & Mornon J.P. (1992): An immunophilin that binds Mr 90,000 heat shock protein: main structural features of a mammalian p59 protein. Proc. Natl. Acad. Sci. USA, 89, 6270-6274.
Renoir J.M., Radanyi C. & Baulieu E.E. (1992): Un effet des immunosuppresseurs FK506 et rapamycine sur le fonctionnement du récepteur de la progestérone: la protéine "p59-HBI", un carrefour de l'immunologie et de l'endocrinologie? C.R. Acad. Sci. Paris, 315, 421-428.
Massol N., Lebeau M.C., Renoir J.M., Faber,L.E. & Baulieu E.E. (1992): Rabbit FKBP59-heat shock protein binding immunophilin (HBI) is a calmodulin binding protein. Biochem. Biophys. Res. Commun., 187, 1330-1335.
Le Bihan S., Renoir J.M., Radanyi C., Chambraud B., Joulin V., Catelli M.G. & Baulieu E.E. (1993): The mammalian heat shock protein binding immunophilin (p59/HBI) is an ATP and GTP binding protein. Biochem. Biophys. Res. Commun., 195, 600-607.
Renoir J.M., Le Bihan S., Mercier-Bodard C., Gold A., Arjomandi M., Radanyi C. & Baulieu E.E. (1994): Effects of immunosuppressants FK506 and rapamycin on the heterooligomeric form of the progesterone receptor. J. Steroid Biochem. Mol. Biol., 48, 101-110.
Perrot-Applanat M., Cibert C., Géraud G., Renoir J.M. & Baulieu E.E. (1995): The 59 kDa FK506-binding protein, a 90 kDa heat shock protein binding immunophilin (FKBP59-HBI), is associated with the nucleus, the cytoskeleton and mitotic apparatus. J. Cell Sci., 108, 2037-2051.
Czar M., Lyons R., Welsh M., Renoir M. & Pratt W. (1995): Evidence that the FK506-binding immunophilin heat shock protein 56 is required for trafficking of the glucocorticoid receptor from the cytoplasm to the nucleus. Molecular Endocrinology, 9, 1549-1560.
Renoir J.M., Mercier-Bodard C., Hoffmann,K., Le Bihan S., Ning Y.M., Sanchez E.R., Handschumacher R.E. & Baulieu E-E. (1995): Cyclosporin A potentiates the dexamethasone-induced mouse mammary tumor virus-chloramphenicol acetyltransferase activity in LMCAT cells: A possible role for different heat shock protein-binding immunophilins in glucocorticosteroid receptor-mediated gene expression. Proc. Natl. Acad.Sci. USA, 92, 4977-4981.
Doucet-Brutin S., Renoir M., Le Gallic L., Vincent S., Marty L. & Fort P. (1995): Growth-regulated expression of FKBP-59 immunophilin in normal and transformed fibroblastic cells. Experimental Cell Research, 220, 152-160.
Renoir J.M., Marsaud V., Mercier-Bodard C., Le Bihan S., Radanyi C. & Baulieu E.E. (1996) : Modulation of steroid-induced transcription by Cyclophilins and FKBPs. In Cyclophilin structure and function. Workshop Oct 10-12 1996, Lille, France, CNRS USTL eds, pp117-127.
Dayan G., Jault J.M., Baubichon-Cortay H., Renoir J-M, Baulieu E.E., Gros P & Di Pietro A. (1997): Binding of steroid modulators to recombinant cytosolic domain from mouse P-Glycoproteins: close proximity to tryptophan 696 and to ATP site. Biochemistry, 36, 15208-15215.
Miyata Y., Chambraud B., Radanyi C., Lebeau M-C., Renoir J-M., Leclerc J., Shirai R., Catelli M-G., Yahara I. & Baulieu E.E. (1997): Phosphorylation of immunosuppressant FK506 binding protein, FKBP52 by casein kinase II (CKII): regulation of hsp90-binding activity of FKBP-52. Proc. Natl. Acad. Sci. USA, 94, 14500-14505.
Marsaud V., Mercier-Bodard C., Fortin D., Le Bihan S. & Renoir J-M (1998a): Dexamethasone and triamcinolone acetonide accumulation in mouse fibroblasts is differently modulated by the immunosuppressants Cyclosporin A, FK506, Rapamycin and their analogues, as well as by other P-Glycoprotein ligands. J. Steroid. Biochem. Molec. Biol. 66, 11-25.
Le Bihan S., Marsaud V., Mercier-Bodard C., Baulieu E.E., Mader S., White J. & Renoir J-M (1998): Calcium/calmodulin kinases inhibitors and immunosuppressant macrolides rapamycin and FK506 inhibit stimulation of progestin/glucocorticosteroid responsive promoters in human breast cancer T47D cells. Mol. Endocrinol.12, 986-1001.
Marsaud V., Radanyi C. & Renoir J-M (1998b): Functional relationships between Steroid Receptors and Immunophilins. Current topics in steroid research 1 : 59-71.
Marsaud V., Radanyi C. & Renoir J-M (1999): Steroid receptors and immunophilins relationships in hormone-dependent cancers : use of long circulating anti-steroid hormone and/or immunosuppressants carriers as a promising therapeutic approach. STP Pharma, Sciences, 9 : 397-409.
Silverstein A.M., Galigniana M.D., Kanelakis K.C., Radanyi C., Renoir J-M. & Pratt W.B. (1999): Different regions of the immunophilin FKBP52 determine its association with the glucocorticosteroid receptor, hsp90 and cytoplasmic dynein J. Biol. Chem. 274 :36980-36986.
Brigger I., Desmaële D., d'Angelo J., Chaminade P., Gurny R., Renoir M. and Couvreur P.:Poly(MePegCyanoacrylate-co-Hexadecylcyanoacrylate) amphiphilic copolymer for stealth nanoparticle technology: further investigations of its macromolecular structure and nanoparticle characterization. accepted pharmaceutical research.
Stella B., Arpicco S. Perachia M-T., Desmae¨le D. Hoebecke J., Renoir J-M., d'Angelo J., Cattel L. & Couvreur P.: PEG-Coated biodegradable poly(cyanoacrylate) nanoparticles coupled to folic acid for tumoral intracellular targeting (submitted toJACS).
Membre de la société de Biologie cellulaire de France depuis 1992.
Vidéos
La vectorisation des médicaments.
La vectorisation des médicaments et le traitement des cancers oestrogéno-dépendants.
Les cancers de la femme.
Agir sur les récepteurs stéroidiens pour traiter les cancers de la femme.