3 results match your criteria: "Universities of Montpellier 1 and Montpellier 2[Affiliation]"
Alternative RNA processing of LMNA pre-mRNA produces three main protein isoforms, that is, lamin A, progerin, and lamin C. De novo mutations that favor the expression of progerin over lamin A lead to Hutchinson-Gilford progeria syndrome (HGPS), providing support for the involvement of LMNA processing in pathological aging. Lamin C expression is mutually exclusive with the splicing of lamin A and progerin isoforms and occurs by alternative polyadenylation.
View Article and Find Full Text PDFMol Biol Cell
October 2013
Institut de Génétique Moléculaire de Montpellier, CNRS UMR 5535/IFR122, Universities of Montpellier 1 and Montpellier 2, 34293 Montpellier Cedex 5, France Département de Physiologie, Université de Lausanne, CH-1015 Lausanne, Switzerland INSERM U844, Institut des Neurosciences de Montpellier, Centre Hospitalier Universitaire Saint Eloi, Université Montpellier 1, 34295 Montpellier Cedex 5, France Service Immuno-Rhumatologie, Centre Hospitalier Universitaire Lapeyronie, 34093 Montpellier Cedex, France.
Cell invasion targets specific tissues in physiological placental implantation and pathological metastasis, which raises questions about how this process is controlled. We compare dermis and endometrium capacities to support trophoblast invasion, using matching sets of human primary fibroblasts in a coculture assay with human placental explants. Substituting endometrium, the natural trophoblast target, with dermis dramatically reduces trophoblast interstitial invasion.
View Article and Find Full Text PDFAnal Biochem
January 2011
Institut des Biomolécules Max Mousseron (IBMM), CNRS UMR 5247, Universities of Montpellier 1 and Montpellier 2, Faculty of Pharmacy, 15 avenue Charles Flahaut, BP 14491, 34093 Montpellier cedex 5, France.
The growth hormone secretagogue receptor type 1a (GHS-R1a) belongs to class A G-protein-coupled receptors (GPCR). This receptor mediates pleiotropic effects of ghrelin and represents a promising target for dysfunctions of growth hormone secretion and energy homeostasis including obesity. Identification of new compounds which bind GHS-R1a is traditionally achieved using radioactive binding assays.
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