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5 results on '"Morad Roudbaraki"'

1. Evolution of the human cold/menthol receptor, TRPM8

Author

Morad Roudbaraki, Samuel Blanquart, Martin Figeac, Natalia Prevarskaya, Philippe Delcourt, Christopher A. Emerling, Anne-Sophie Borowiec, Gabriel Bidaux, Andrea S. Meseguer, Plateforme de génomique fonctionnelle et structurelle [Lille], Institut pour la recherche sur le cancer de Lille [Lille] (IRCL)-Université de Lille, Droit et Santé, Cardiovasculaire, métabolisme, diabétologie et nutrition (CarMeN), Institut National de la Recherche Agronomique (INRA)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National des Sciences Appliquées de Lyon (INSA Lyon), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Hospices Civils de Lyon (HCL), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Hospices Civils de Lyon (HCL)-Institut National de la Santé et de la Recherche Médicale (INSERM), INSERM, Ministère de l'Education Nationale, Région Nord-Pas-de-Calais, Inria, Fondation pour la Recherche Médicale, Centre National de la Recherche Scientifique (CNRS), Dynamics, Logics and Inference for biological Systems and Sequences (Dyliss), Inria Rennes – Bretagne Atlantique, Institut National de Recherche en Informatique et en Automatique (Inria)-Institut National de Recherche en Informatique et en Automatique (Inria)-GESTION DES DONNÉES ET DE LA CONNAISSANCE (IRISA-D7), Institut de Recherche en Informatique et Systèmes Aléatoires (IRISA), Université de Rennes (UR)-Institut National des Sciences Appliquées - Rennes (INSA Rennes), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Université de Bretagne Sud (UBS)-École normale supérieure - Rennes (ENS Rennes)-Institut National de Recherche en Informatique et en Automatique (Inria)-CentraleSupélec-Centre National de la Recherche Scientifique (CNRS)-IMT Atlantique (IMT Atlantique), Institut Mines-Télécom [Paris] (IMT)-Institut Mines-Télécom [Paris] (IMT)-Université de Rennes (UR)-Institut National des Sciences Appliquées - Rennes (INSA Rennes), Institut Mines-Télécom [Paris] (IMT)-Institut Mines-Télécom [Paris] (IMT)-Institut de Recherche en Informatique et Systèmes Aléatoires (IRISA), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Université de Bretagne Sud (UBS)-École normale supérieure - Rennes (ENS Rennes)-CentraleSupélec-Centre National de la Recherche Scientifique (CNRS)-IMT Atlantique (IMT Atlantique), Institut Mines-Télécom [Paris] (IMT)-Institut Mines-Télécom [Paris] (IMT), Laboratoire de Physiologie Cellulaire : Canaux ioniques, inflammation et cancer - U 1003 (PHYCELL), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille, Institut des Sciences de l'Evolution de Montpellier (UMR ISEM), Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-École Pratique des Hautes Études (EPHE), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Université de Montpellier (UM)-Institut de recherche pour le développement [IRD] : UR226-Centre National de la Recherche Scientifique (CNRS), Rôle des canaux ioniques membranaires et du calcium intracellulaire dans la physiopathologie de la prostate, Université de Lille, Sciences et Technologies-Institut National de la Santé et de la Recherche Médicale (INSERM), Université de Bretagne Sud (UBS)-Institut National des Sciences Appliquées - Rennes (INSA Rennes), Institut National des Sciences Appliquées (INSA)-Université de Rennes (UNIV-RENNES)-Institut National des Sciences Appliquées (INSA)-Université de Rennes (UNIV-RENNES)-Institut National de Recherche en Informatique et en Automatique (Inria)-École normale supérieure - Rennes (ENS Rennes)-Centre National de la Recherche Scientifique (CNRS)-Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-CentraleSupélec-IMT Atlantique Bretagne-Pays de la Loire (IMT Atlantique), Institut Mines-Télécom [Paris] (IMT)-Institut Mines-Télécom [Paris] (IMT)-Université de Bretagne Sud (UBS)-Institut National des Sciences Appliquées - Rennes (INSA Rennes), Institut National des Sciences Appliquées (INSA)-Université de Rennes (UNIV-RENNES)-Institut National des Sciences Appliquées (INSA)-Université de Rennes (UNIV-RENNES)-École normale supérieure - Rennes (ENS Rennes)-Centre National de la Recherche Scientifique (CNRS)-Université de Rennes 1 (UR1), École pratique des hautes études (EPHE), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Université de Montpellier (UM)-Centre de Coopération Internationale en Recherche Agronomique pour le Développement (Cirad)-Centre National de la Recherche Scientifique (CNRS)-Institut de recherche pour le développement [IRD] : UR226, Hospices Civils de Lyon (HCL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut National des Sciences Appliquées de Lyon (INSA Lyon), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Université de Lyon-Institut National des Sciences Appliquées (INSA)-Université Claude Bernard Lyon 1 (UCBL), and Université de Lyon-Institut National de la Recherche Agronomique (INRA)

Subjects
0106 biological sciences, 0301 basic medicine, Gene isoform, Bioinformatics, Evolution, [SDV]Life Sciences [q-bio], TRPM Cation Channels, Biology, 010603 evolutionary biology, 01 natural sciences, Cold and menthol receptor, Evolution, Molecular, Mice, Open Reading Frames, 03 medical and health sciences, Exon, Transient receptor potential channel, Alternative transcription, Splice variants, Cell Line, Tumor, Genetics, TRPM8, Animals, Humans, Protein Isoforms, RNA, Messenger, Molecular Biology, Gene, Phylogeny, Ecology, Evolution, Behavior and Systematics, Comparative genomics, Alternative splicing, Genetic Variation, Exons, Phylogenetics, Cold Temperature, Alternative Splicing, Menthol, HEK293 Cells, 030104 developmental biology, Evolutionary biology, Human genome, [INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM], Isoforms
Abstract

International audience; Genes showing versatile functions or subjected to fast expansion and contraction during the adaptation of species to specific ecological conditions, like sensory receptors for odors, pheromones and tastes, are characterized by a great plasticity through evolution. One of the most fascinating sensory receptors in the family of TRP channels, the cold and menthol receptor TRPM8, has received significant attention in the literature. Recent studies have reported the existence of TRPM8 channel isoforms encoded by alternative mRNAs transcribed from alternative promoters and processed by alternative splicing. Since the first draft of the human genome was accomplished in 2000, alternative transcription, alternative splicing and alternative translation have appeared as major sources of gene product diversity and are thought to participate in the generation of complexity in higher organisms. In this study, we investigate whether alternative transcription has been a driving force in the evolution of the human forms of the cold receptor TRPM8. We identified 33 TRPM8 alternative mRNAs (24 new sequences) and their associated protein isoforms in human tissues. Using comparative genomics, we described the evolution of the human TRPM8 sequences in eight ancestors since the origin of Amniota, and estimated in which ancestors the new TRPM8 variants originated. In order to validate the estimated origins of this receptor, we performed experimental validations of predicted exons in mouse tissues. Our results suggest a first diversification event of the cold receptor in the Boreoeutheria ancestor, and a subsequent divergence at the origin of Simiiformes.

Published
2019

2. Redefining the Ca2 >Apoptosis Link Reveals a Widespread Vulnerability of Cancer Cells

Author

Gabriel Bidaux, Etienne Dewailly, Christian Slomianny, Natacha Prevarskaya, Gilbert Lepage, F. Vanden Abeele, Pascal Mariot, Artem Kondratskyi, Jean-Louis Bonnal, D. Tierny, Morad Roudbaraki, E. Vancauwendberghe, Philippe Delcourt, Charlotte Dubois, and Robert-Allain Toillon

Subjects
chemistry, Apoptosis, Autophagy, Cancer cell, Vulnerability, Cancer research, medicine, chemistry.chemical_element, Cancer, Calcium, Biology, medicine.disease
Published
2018

3. Store-operated Ca2+ Current in Prostate Cancer Epithelial Cells

Author

Yaroslav M. Shuba, Roman Skryma, Morad Roudbaraki, Fabien Vanden Abeele, and Natalia Prevarskaya

Subjects
medicine.medical_specialty, Endogeny, Stimulation, Transporter, Cell Biology, Biology, medicine.disease, Biochemistry, Cell biology, Transient receptor potential channel, Prostate cancer, Endocrinology, Cell surface receptor, Internal medicine, LNCaP, otorhinolaryngologic diseases, medicine, Patch clamp, Molecular Biology
Abstract

Ca(2+) influx via store-operated channels (SOCs) following stimulation of the plasma membrane receptors is the key event controlling numerous processes in nonexcitable cells. The human transient receptor potential vanilloid type 6 channel, originally termed Ca(2+) transporter type 1 (CaT1) protein, is one of the promising candidates for the role of endogenous SOC, although investigations of its functions have generated considerable controversy. In order to assess the role of CaT1 in generating endogenous store-operated Ca(2+) current (I(SOC)) in the lymph node carcinoma of the prostate (LNCaP) human prostate cancer epithelial cell line, we manipulated its endogenous levels by means of antisense hybrid depletion or pharmacological up-regulation (antiandrogen treatment) combined with functional evaluation of I(SOC). Antisense hybrid depletion of CaT1 decreased I(SOC) in LNCaP cells by approximately 50%, whereas enhancement of CaT1 levels by 60% in response to Casodex treatment potentiated I(SOC) by 30%. The functional characteristics of I(SOC) in LNCaP cells were similar in many respects to those reported for heterologously expressed CaT1, although 2-aminoethoxydiphenyl borate sensitivity and lack of constitutive current highlighted notable departures. Our results suggest that CaT1 is definitely involved in I(SOC), but it may constitute only a part of the endogenous SOC, which in general may be a heteromultimeric channel composed of homologous CaT1 and other transient receptor potential subunits.

Published
2003

4. Bcl-2-dependent modulation of Ca2+ homeostasis and store-operated channels in prostate cancer cells

Author

Christian Slomianny, Morad Roudbaraki, Brigitte Mauroy, Frank Wuytack, Fabien Vanden Abeele, Yaroslav M. Shuba, Natalia Prevarskaya, Fabien Van Coppenolle, and Roman Skryma

Subjects
Male, Cancer Research, Patch-Clamp Techniques, Blotting, Western, Apoptosis, Calcium-Transporting ATPases, Endoplasmic Reticulum, Sarcoplasmic Reticulum Calcium-Transporting ATPases, Downregulation and upregulation, Calcium-binding protein, LNCaP, Tumor Cells, Cultured, Homeostasis, Humans, Patch clamp, Voltage-dependent calcium channel, biology, Endoplasmic reticulum, Calcium-Binding Proteins, Electric Conductivity, Prostatic Neoplasms, Cell Biology, Cell biology, Electrophysiology, Proto-Oncogene Proteins c-bcl-2, Ribonucleoproteins, Oncology, biology.protein, Calcium, Calcium Channels, Calreticulin
Abstract

Antiapoptotic oncoprotein Bcl-2 has extramitochondrial actions due to its localization on the endoplasmic reticulum (ER); however, the specific mechanisms of such actions remain unclear. Here we show that Bcl-2 overexpression in LNCaP prostate cancer epithelial cells results in downregulation of store-operated Ca(2+) current by decreasing the number of functional channels and inhibiting ER Ca(2+) uptake through a reduction in the expression of calreticulin and SERCA2b, two key proteins controlling ER Ca(2+) content. Furthermore, we demonstrate that Ca(2+) store depletion by itself is not sufficient to induce apoptosis in Bcl-2 overexpressing cells, and that sustained Ca(2+) entry via activated store-operated channels (SOCs) is required as well. Our data therefore suggest the pivotal role of SOCs in apoptosis and cancer progression.

Published
2002

5. KV1.1 K+ Channels Identification in Human Breast Carcinoma Cells: Involvement in Cell Proliferation

Author

F. Chaussade, Christian Slomianny, Morad Roudbaraki, Philippe Delcourt, Etienne Dewailly, Halima Ouadid-Ahidouch, and Natalia Prevarskaya

Subjects
medicine.medical_specialty, Potassium Channels, Charybdotoxin, Biophysics, Breast Neoplasms, Biochemistry, chemistry.chemical_compound, Internal medicine, Tumor Cells, Cultured, medicine, Humans, Molecular Biology, Incubation, Elapid Venoms, biology, Reverse Transcriptase Polymerase Chain Reaction, Cell growth, Conductance, Cell Biology, Iberiotoxin, Immunohistochemistry, Molecular biology, Electrophysiology, Endocrinology, chemistry, Potassium Channels, Voltage-Gated, Cancer cell, biology.protein, Antibody, Kv1.1 Potassium Channel, Cell Division
Abstract

Electrophysiological, immunocytochemical, and RT-PCR methods were used to identify a K(+) conductance not yet described in MCF-7 human breast cancer cells. A voltage-dependent and TEA-sensitive K(+) current was the most commonly observed in these cells. The noninactivating K(+) current (I(K)) was insensitive to iberiotoxin (100 nM) and charybdotoxin (100 nM) but reduced by alpha-dendrotoxin (alpha-DTX). Perfusion of alpha-DTX reduced a fraction of I(K) amplitude in a dose-dependent manner (IC(50) = 0.6 +/- 0.3 nM). This DTX sensitive I(K) exhibited a voltage threshold at -20 mV and was not inactivated. The time constant of activation was 5.3 +/- 2.2 ms measured at +60 mV. The averaged half-activation potential and slope factor values were 14 +/- 1.6 mV and 10 +/- 1.4, respectively. Immunocytochemical analysis demonstrated that plasma membrane was labeled by anti-Kv1.1 but not by anti-Kv1.2 nor anti-Kv1.3 antibodies. Furthermore, only Kv1.1 mRNA was detected in MCF-7 cells. Incubation in 1 and 10 nM alpha-DTX reduced cell proliferation by 20 and 30%, respectively. These data provide the first evidence of Kv1.1 K(+) channels expression in MCF-7 cells and indicate that these channels are implicated in cell proliferation.

Published
2000

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