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Darren Edward Richard
Professeur titulaire

Contribution à la recherche
Thématiques de recherche de la Faculté de médecine
- Oncologie
- Santé cardiovasculaire, respiratoire et métabolisme
Projets de recherche en cours
- Hydrochlorothiazide and accelerated CKD-related vascular calcification - Fondation canadienne du rein - Subventions de recherche en santé des reins, co-chercheur - 2023-07-01 au 2025-06-30
Financements des 2 dernières années
- Novel Interactions and Functions for Hypoxia-Inducible Factor-1 (HIF-1) during Vascular Responses - Fondation de l'Université Laval, chercheur principal - 2016-04-01 au 2022-03-31
Publications
- Hypoxia-inducible factor-1 activation in nonhypoxic conditions: The essential role of mitochondrial-derived reactive oxygen species, Richard, D.E., Giaccia, A.J., Chan, D.A., Robitaille, G.A., Lafleur, V.N., Patten, D.A., Molecular Biology of the Cell, 2010, 10.1091/mbc.E10-01-0025
- The organization of the suprachiasmatic circadian pacemaker of the rat and its regulation by neurotransmitters and modulators., Tcheng, T.K., Richard, D., Medanic, M., McArthur, A.J., Liu, C., Faiman, L.E., Gallman, E.A., Ding, J.M., DeMarco, S.J., Gillette, M.U., 1993
- The tyrosine within the NPXnY motif of the human angiotensin II type 1 receptor is involved in mediating signal transduction but is not essential for internalization, Servant, G., Richard, D.E., Leduc, R., Laporte, S.A., Guillemette, G., Escher, E., Molecular Pharmacology, 1996
- HIF-1 inhibition decreases systemic vascular remodelling diseases by promoting apoptosis through a hexokinase 2-dependent mechanism, Bonnet, S., Richard, D.E., Robitaille, G.A., Roy, M., Lambert, C.M., Continuing Education in Anaesthesia, Critical Care and Pain, 2010
- Arrest-defective-1 protein, an acetyltransferase, does not alter stability of hypoxia-inducible factor (HIF)-1α and is not induced by hypoxia or HIF, Brahimi-Horn, M.C., Pouysségur, J., Richard, D.E., Déry, M.-A., Hattab, M., Trottier, E., Mazure, N., Bilton, R., Journal of Biological Chemistry, 2005, 10.1074/jbc.M504482200
- Angiogenesis and G-protein-coupled receptors: Signals that bridge the gap, Pouysségur, J., Vouret-Craviari, V., Richard, D.E., Oncogene, 2001, 10.1038/sj.onc.1204193
- Identification of alternative spliced variants of human hypoxia- inducible factor-1α, Pouysségur, J., Pagès, G., Berra, E., Richard, D.E., Gothié, E., Journal of Biological Chemistry, 2000, 10.1074/jbc.275.10.6922
- Signaling angiogenesis via p42/p44 MAP kinase cascade, Viñals, F., Richard, D.E., Pouysségur, J., Pagès, G., Milanini, J., Gothié, E., Berra, E., Annals of the New York Academy of Sciences, 2000
- Endothelin type A receptor blockade reduces vascular calcification and inflammation in rats with chronic kidney disease, Agharazii, M., Richard, D.E., Mac-Way, F., St-Hilaire, J., Ung, R.-V., Gauthier-Bastien, A., Lariviere, R., Journal of Hypertension, 2017, 10.1097/HJH.0000000000001161
- Desensitization of AT1 receptor-mediated cellular responses requires long term receptor down-regulation in bovine adrenal glomerulosa cells, Richard, D.E., Leduc, R., Laporte, S.A., Guillemette, G., Bernier, S.G., Endocrinology, 1997, 10.1210/en.138.9.3828
- The high affinity state of inositol 1,4,5-trisphosphate receptor is a functional state, Servant, M., Richard, D.E., Poitras, M., Guillemette, G., Boulay, G., Bernier, S., Journal of Biological Chemistry, 1993
- Selective HIF-1 regulation under nonhypoxic conditions by the p42/p44 MAP kinase inhibitor PD184161, Richard, D.E., Lamalice, L., Turgeon, C.A., Mokas, S., Jalouli, M., Molecular Pharmacology, 2017, 10.1124/mol.117.108654
- Stimulation of the angiotensin II type I receptor on bovine adrenal glomerulosa cells activates a temperature-sensitive internalization-recycling pathway, Guillemette, G., Caron, M., Chrétien, L., Richard, D.E., Molecular and Cellular Endocrinology, 1997, 10.1016/S0303-7207(97)00065-8
- HIF-1-dependent transcriptional activity is required for oxygen-mediated HIF-1α degradation, Pouysségur, J., Gothié, E., Richard, D.E., Berra, E., FEBS Letters, 2001, 10.1016/S0014-5793(01)02159-7
- Hypoxia-inducible factor 1: Regulation by hypoxic and non-hypoxic activators, Richard, D.E., Michaud, M.D., Déry, M.-A.C., International Journal of Biochemistry and Cell Biology, 2005, 10.1016/j.biocel.2004.08.012
- Angiogenesis: How a tumor adapts to hypoxia, Pouysségur, J., Berra, E., Richard, D.E., Biochemical and Biophysical Research Communications, 1999, 10.1006/bbrc.1999.1889
- TGFβ-induced GRK2 expression attenuates AngII-regulated vascular smooth muscle cell proliferation and migration, Lebrun, J.-J., Richard, D.E., Laporte, S.A., Mancini, J., Sontag, T., Ho, J., Chen, H., Guo, J., Cellular Signalling, 2009, 10.1016/j.cellsig.2009.01.037
- Effects of TGF-β1 on endothelial factors, Lebel, M., Larivire, R., Richard, D.E., Robitaille, G.A., Midaoui, A.E., Cellier, E., Archives of Physiology and Biochemistry, 2010, 10.3109/13813451003610862
- p42/p44 mitogen-activated protein kinases phosphorylate hypoxia- reducible factor (HIF-1α) and enhance the transcriptional activity of HIF-1, Pouysségur, J., Roux, D., Gothié, E., Berra, E., Richard, D.E., Journal of Biological Chemistry, 1999, 10.1074/jbc.274.46.32631
- Effect of uncoupling agents on AT1 receptor affinity for antagonist analogs of angiotensin II, Sidibé, A., Richard, D.E., Poitras, M., Guillemette, G., Chrétien, L., Receptors and Channels, 1998
- Short-term desensitization of the angiotensin II receptor of bovine adrenal glomerulosa cells corresponds to a shift from a high to a low affinity state, Richard, D.E., Guillemette, G., Chrétien, L., Boulay, G., Endocrinology, 1994, 10.1210/en.135.5.2130
- Adenoviral protein E4orf4 interacts with the polarity protein Par3 to induce nuclear rupture and tumor cell death, Josée N. Lavoie, Marc-Étienne Huot, François Bordeleau, Darren E. Richard, Patrick Laprise, Herman Lambert, Margit Fuchs, Jonathan Bergeman, Marie-Chloé Boulanger, Kévin Jacquet, Alexia Caillier, Marc-Antoine Rodrigue, Claire Dziengelewski, Journal of Cell Biology, 2020, 10.1083/jcb.201805122
- A role for hypoxia-inducible factor-1 (HIF-1) in phosphate-induced vascular smooth muscle cell calcification, , Kidney International (In Press), 2016
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Bovine adrenal glomerulosa cells express such a low level of functional B
2 receptors that bradykinin does not significantly increase their aldosterone production, Guillemette, G., Paitras, M., Poirier, S.N., Richard, D.E., Chrétien, L., Journal of Endocrinology, 1998, 10.1677/joe.0.1560449 - Desensitization of AT1 receptor-mediated cellular responses requires long term receptor down-regulation in bovine adrenal glomerulosa cells., Guillemette, G., Leduc, R., Bernier, S.G., Laporte, S.A., Richard, D.E., Endocrinology, 1997
- Nonhypoxic pathway mediates the induction of hypoxia-inducible factor 1α in vascular smooth muscle cells, Pouyssegur, J., Berra, E., Richard, D.E., Journal of Biological Chemistry, 2000, 10.1074/jbc.M003325200
- HIF-1 inhibition decreases systemic vascular remodelling diseases by promoting apoptosis through a hexokinase 2-dependent mechanism, Bonnet, S., Richard, D.E., Robitaille, G.A., Roy, M., Lambert, C.M., Cardiovascular Research, 2010, 10.1093/cvr/cvq152
- Induction of hypoxia-inducible factor-1α by transcriptional and translational mechanisms, Richard, D.E., Pouysségur, J., Robitaille, G.A., Pagé, E.L., Journal of Biological Chemistry, 2002, 10.1074/jbc.M209114200
- Short-term desensitization of the angiotensin II receptor of bovine adrenal glomerulosa cells corresponds to a shift from a high to a low affinity state, Guillemettes, G., Richard, D.E., Chrétien, L., Boulay, G., Endocrinology, 1994, 10.1210/endo.135.5.7956936
- Conserved molecular interactions within the HBO1 acetyltransferase complexes regulate cell proliferation, Côté, J., Kutateladze, T.G., Yang, X.-J., Richard, D.E., Robitaille, G.A., Cayrou, C., Doyon, Y., Landry, A.-J., Glass, K.C., Paquet, E., Saksouk, N., Lalonde, M.-E., Avvakumov, N., Molecular and Cellular Biology, 2012, 10.1128/MCB.06455-11
- The prolyl isomerase Pin1 regulates hypoxia-inducible transcription factor (HIF) activity, Richard, D.E., Lamalice, L., Zhou, X.Z., Lu, K.P., Lafleur, V.N., Déry, M.A.C., Jalouli, M., 2014, 10.1016/j.cellsig.2014.04.005
- Hypoxia-inducible factor-1α stabilization in nonhypoxic conditions: Role of oxidation and intracellular ascorbate depletion, Richard, D.E., Levine, M., Giaccia, A.J., Chan, D.A., Page, E.L., Molecular Biology of the Cell, 2008, 10.1091/mbc.E07-06-0612
- Erratum: Arrest-defective-1 protein, an acetyltransferase, does not alter stability of hypoxia-inducible factor (HIF)-1α and is not induced by hypoxia or HIF (Journal of Biological Chemistry (2005) 280 (31132-31140)), Trottier, E., Richard, D.E., Pouysségur, J., Mazure, N., Hattab, M., Déry, M.-A., Bilton, R., Brahimi-Horn, M.C., Journal of Biological Chemistry, 2006
- Hypoxic gene activation by lipopolysaccharide in macrophages: Implication of hypoxia-inducible factor 1α, Richard, D.E., Soucy, G.M., Pagé, E.L., Blouin, C.C., Blood, 2004, 10.1182/blood-2003-07-2427
- Targeting Axl favors an antitumorigenic microenvironment that enhances immunotherapy responses by decreasing Hif-1α levels, Jean-François Côté, Jean-Philippe Gratton, Morag Park, Darren E. Richard, William J. Muller, Carla V. Rothlin, Hellen Kuasne, Chloé Apcher, Islam E. Elkholi, Marie-Anne Goyette, Proceedings of the National Academy of Sciences, 2021, 10.1073/pnas.2023868118
- Transforming growth factor β1 induces hypoxia-inducible factor-1 stabilization through selective inhibition of PHD2 expression, Dubois, C.M., Richard, D.E., Grandmont, S., Charbonneau, M., McMahon, S., Journal of Biological Chemistry, 2006, 10.1074/jbc.M604507200
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Desensitization of AT
1 receptor-mediated cellular responses requires long term receptor down-regulation in bovine adrenal glomerulosa cells, Guillemette, G., Leduc, R., Bernier, S.G., Laporte, S.A., Richard, D.E., Endocrinology, 1997, 10.1210/endo.138.9.5409 - Novel cyclic analogs of angiotensin II with cyclization between positions 5 and 7: Conformational and biological implications, Marshall, G.R., Escher, E., Richard, D.E., Pérodin, J., Nikiforovich, G.V., Zhang, W.-J., Journal of Medicinal Chemistry, 1996, 10.1021/jm9507744
- Inflammatory cytokines and reactive oxygen species as mediators of chronic kidney disease-related vascular calcification, Richard, D.E., Larivière, R., Mokas, S., Ung, R.-V., Gautier-Bastien, A., St-Louis, R., Agharazii, M., American Journal of Hypertension, 2015, 10.1093/ajh/hpu225
- Differential regulation of hypoxia-inducible factor-1 through receptor tyrosine kinase transactivation in vascular smooth muscle cells, Richard, D.E., Michaud, M.D., Pagé, E.L., Lauzier, M.-C., Endocrinology, 2007, 10.1210/en.2007-0285
- Selective interaction of chemical dyes with inositol 1,4,5-trisphosphate recognition sites, Richard, D.E., Guillemette, G., Boulay, G., Bernier, S., Canadian Journal of Physiology and Pharmacology, 1994
- Hypoxia-enhanced expression of the proprotein convertase furin is mediated by hypoxia-inducible factor-1: Impact on the bioactivation of proproteins, Dubois, C.M., Richard, D.E., McDonald, P.P., Grondin, F., McMahon, S., Journal of Biological Chemistry, 2005, 10.1074/jbc.M413248200
- The Werner syndrome gene product (WRN): A repressor of hypoxia-inducible factor-1 activity, Richard, D.E., Lebel, M., Lamalice, L., Garand, C., Robitaille, G.A., Patten, D.A., Lafleur, V.N., Labbé, A., Experimental Cell Research, 2012, 10.1016/j.yexcr.2012.04.010
- Signaling angiogenesis via p42/p44 MAP kinase and hypoxia, Pouysségur, J., Pagès, G., Roux, D., Gothié, E., Viñals, F., Le Gall, M., Richard, D.E., Milanini, J., Berra, E., Biochemical Pharmacology, 2000, 10.1016/S0006-2952(00)00423-8
- Hypoxia-inducible factor-1 plays a role in phosphate-induced vascular smooth muscle cell calcification, Richard, D.E., Agharazii, M., Cornfield, D.N., Gobeil, S., Lamalice, L., Larivière, R., Mokas, S., Kidney International, 2016, 10.1016/j.kint.2016.05.020
- Transcriptional repression of hypoxia-inducible factor-1 (HIF-1) by the protein arginine methyltransferase PRMT1, Richard, D.E., Richard, S., Lafleur, V.N., Molecular Biology of the Cell, 2014, 10.1091/mbc.E13-07-0423
- Sphingosine-1-phosphate: A novel nonhypoxic activator of hypoxia-inducible factor-1 in vascular cells, Gratton, J.-P., Richard, D.E., Robitaille, G.A., Michaud, M.D., Arteriosclerosis, Thrombosis, and Vascular Biology, 2009, 10.1161/ATVBAHA.109.185280
- The adenoviral protein E4orf4: a probing tool to decipher mechanical stress-induced nuclear envelope remodeling in tumor cells, Josée N. Lavoie, Darren E. Richard, Marc-Antoine Rodrigue, Kévin Jacquet, Cell Cycle, 2020, 10.1080/15384101.2020.1836441
- Tumor necrosis factor inhibitors as novel therapeutic tools for vascular remodeling diseases, Bonnet, S., Richard, D.E., Agharazii, M., Robitaille, G.A., Meloche, J., Roy, M., Lambert, C.M., American Journal of Physiology - Heart and Circulatory Physiology, 2010, 10.1152/ajpheart.00562.2010
- (2R)-[(4-Biphenylylsulfonyl)amino]-N-hydroxy-3-phenylpropionamide (BiPS), a matrix metalloprotease inhibitor, is a novel and potent activator of hypoxia-inducible factors, Richard, D.E., Giaccia, A.J., Chan, D.A., Robitaille, G.A., Lauzier, M.-C., Molecular Pharmacology, 2008, 10.1124/mol.108.045690
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Hypoxia-inducible factor-1α (HIF-1 escapes O
2 -driven proteasomal degradation irrespective of its subcellular localization: Nucleus or cytoplasm, Pouysségur, J., Richard, D.E., Roux, D., Berra, E., EMBO Reports, 2001, 10.1093/embo-reports/kve130 - HIF-1 activation during tumor progression: Implications and consequences | Activation de HIF1 dans le cancer: Implications et conséquences, Richard, D.E., Michaud, M.D., Lauzier, M.-C., Déry, M.-A.C., Bulletin du Cancer, 2006
Contribution à l'enseignement aux cycles supérieurs
Étudiant(e)s dirigé(e)s*
Depuis 2020/06- Arianne Gervais - Maîtrise avec mémoire - En cours
- Arielle Beaudoin - Maîtrise avec mémoire - En cours
- Rémi Riga - Maîtrise avec mémoire - En cours
- Hadrien Benk-Fortin - Maîtrise avec mémoire - 2022/05
Encadrement d'étudiant(e)s
Direction de recherche dans les domaines suivants :
- Biologie cellulaire et moléculaire
- Sciences cliniques et biomédicales
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