Marie V. St-Pierre
University of Zurich
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Publication
Featured researches published by Marie V. St-Pierre.
Molecular Pharmacology | 2006
Emanuel Hanggi; Anne Freimoser Grundschober; Simone Leuthold; Peter J. Meier; Marie V. St-Pierre
Organic anion transporting polypeptide (OATP) superfamily member 2B1 (OATP2B1) mediates the uptake of steroid hormone precursors and selected drugs in the placenta, liver, mammary gland, brain, and intestine. This action is modulated by sulfhydryl reagents. Common to all OATPs is a large extracellular loop between transmembrane domains IX and X with 10 conserved cysteines. To elucidate the structure-function relationship of this cysteine rich ectodomain, a truncated OATP2B1 lacking 10 extracellular cysteines (OATP2B1Δ489-557) and 10 OATP2B1 mutants containing individual Cys-to-Ala substitutions were generated and expressed in CHO-K1 cells. The immunolocalization, cell-surface expression, transport activity, and free cysteine labeling with N-biotinoylaminoethylmethane-thiosulfonate of mutant proteins and wild-type OATP2B1 were compared. OATP2B1Δ489-557 accumulated intracellularly. Nine Cys-to-Ala substitutions, C489A, C495A, C504A, C516A, C520A, C539A, C541A, C553A, and C557A, were misprocessed, appearing predominantly as core-glycosylated, 60-kDa proteins and as 180-kDa complexes. Only C493A was a fully glycosylated 75-kDa protein expressed at the cell surface. Thapsigargin partially corrected the misprocessing of mutants. Compared with OATP2B1, C493A and C557A transported estrone-3-sulfate and dehydroepiandrosterone sulfate less efficiently, whereas all other mutants were functionally impaired. MTSEA labeled free cysteines in all Cys-to-Ala mutants but not in OATP2B1, suggesting that all 10 extracellular cysteines are normally disulfide-bonded. Our findings show that the trafficking and function of OATP2B1 is vulnerable to changes in the cysteine residues of extracellular loop IX-X.
Pharmaceutical Research | 2016
Anand A. Joshi; Soniya Vaidya; Marie V. St-Pierre; Andrei M. Mikheev; Kelly E. Desino; Abner N. Nyandege; Kenneth L. Audus; Jashvant D. Unadkat; Phillip M. Gerk
The human placenta fulfills a variety of essential functions during prenatal life. Several ABC transporters are expressed in the human placenta, where they play a role in the transport of endogenous compounds and may protect the fetus from exogenous compounds such as therapeutic agents, drugs of abuse, and other xenobiotics. To date, considerable progress has been made toward understanding ABC transporters in the placenta. Recent studies on the expression and functional activities are discussed. This review discusses the placental expression and functional roles of several members of ABC transporter subfamilies B, C, and G including MDR1/P-glycoprotein, the MRPs, and BCRP, respectively. Since placental ABC transporters modulate fetal exposure to various compounds, an understanding of their functional and regulatory mechanisms will lead to more optimal medication use when necessary in pregnancy.
Archive | 2005
Christiane Pauli-Magnus; Marie V. St-Pierre; Peter J. Meier
Pharmacogenomics is a rapidly growing field that involves the systematic identification of all human genes, gene products and their genetic variants, and includes the study of changes in their expression over time in health and diseases [14]. Pharmacogenomic strategies have been designed with the aim of refining the classification of disease processes [33], of increasing the number and specificity of drug targets [48], and ultimately of predicting individual risks of acquiring a particular disease and of responding to a specific therapy. The better understanding of disease processes and the implementation of pharmacogenomic strategies in drug development promises to revolutionize medicine through an individual approach to a patient’s disease risk, diagnosis and drug therapy.
American Journal of Physiology-regulatory Integrative and Comparative Physiology | 2000
Marie V. St-Pierre; Maria A. Serrano; Rocio I.R. Macias; U. Dubs; M. Hoechli; U. Lauper; Peter J. Meier; Jose J.G. Marin
Hepatology | 2001
Johannes Noe; Bruno Hagenbuch; Peter J. Meier; Marie V. St-Pierre
Hepatology | 2002
Keiji Hirata; Jean-François Dufour; Kazunori Shibao; Roy G. Knickelbein; Allison F. O'Neill; Hans Peter Bode; Doris Cassio; Marie V. St-Pierre; Nicholas F. LaRusso; M. Fatima Leite; Michael H. Nathanson
American Journal of Physiology-regulatory Integrative and Comparative Physiology | 2004
Marie V. St-Pierre; T. Stallmach; A. Freimoser Grundschober; J.-F. Dufour; M. A. Serrano; J. J. G. Marin; Yuichi Sugiyama; Peter J. Meier
Hepatology | 2002
Hans-Peter Bode; LiFu Wang; Doris Cassio; M. Fatima Leite; Marie V. St-Pierre; Keiji Hirata; Keisuke Okazaki; Marvin Sears; Paolo Meda; Michael H. Nathanson; Jean-François Dufour
Journal of Pharmacology and Experimental Therapeutics | 2003
Maria A. Serrano; Rocio I.R. Macias; Marta Vallejo; Oscar Briz; Ana Bravo; Maria J. Pascual; Marie V. St-Pierre; Bruno Stieger; Peter J. Meier; Jose J.G. Marin
Gastroenterology | 2006
Juliette Martin; Fabrice Magnino; Karin Schmidt; Anne Christine Piguet; Ju Seog Lee; David Semela; Marie V. St-Pierre; Andrew Ziemiecki; Doris Cassio; Charles Brenner; Snorri S. Thorgeirsson; Jean-François Dufour