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1. Metabolic reprogramming involving glycolysis in the hibernating brown bear skeletal muscle

Author

Blandine Chazarin, Kenneth B. Storey, Anna Ziemianin, Stéphanie Chanon, Marine Plumel, Isabelle Chery, Christine Durand, Alina L. Evans, Jon M. Arnemo, Andreas Zedrosser, Jon E. Swenson, Guillemette Gauquelin-Koch, Chantal Simon, Stephane Blanc, Etienne Lefai, and Fabrice Bertile

Subjects
Hibernation, Brown bears, Skeletal muscle, Omics, Enzymology, Glycolysis, Zoology, QL1-991
Abstract

Abstract Background In mammals, the hibernating state is characterized by biochemical adjustments, which include metabolic rate depression and a shift in the primary fuel oxidized from carbohydrates to lipids. A number of studies of hibernating species report an upregulation of the levels and/or activity of lipid oxidizing enzymes in muscles during torpor, with a concomitant downregulation for glycolytic enzymes. However, other studies provide contrasting data about the regulation of fuel utilization in skeletal muscles during hibernation. Bears hibernate with only moderate hypothermia but with a drop in metabolic rate down to ~ 25% of basal metabolism. To gain insights into how fuel metabolism is regulated in hibernating bear skeletal muscles, we examined the vastus lateralis proteome and other changes elicited in brown bears during hibernation. Results We show that bear muscle metabolic reorganization is in line with a suppression of ATP turnover. Regulation of muscle enzyme expression and activity, as well as of circulating metabolite profiles, highlighted a preference for lipid substrates during hibernation, although the data suggested that muscular lipid oxidation levels decreased due to metabolic rate depression. Our data also supported maintenance of muscle glycolysis that could be fuelled from liver gluconeogenesis and mobilization of muscle glycogen stores. During hibernation, our data also suggest that carbohydrate metabolism in bear muscle, as well as protein sparing, could be controlled, in part, by actions of n-3 polyunsaturated fatty acids like docosahexaenoic acid. Conclusions Our work shows that molecular mechanisms in hibernating bear skeletal muscle, which appear consistent with a hypometabolic state, likely contribute to energy and protein savings. Maintenance of glycolysis could help to sustain muscle functionality for situations such as an unexpected exit from hibernation that would require a rapid increase in ATP production for muscle contraction. The molecular data we report here for skeletal muscles of bears hibernating at near normal body temperature represent a signature of muscle preservation despite atrophying conditions.

Published
2019
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2. Limited Oxidative Stress Favors Resistance to Skeletal Muscle Atrophy in Hibernating Brown Bears (Ursus Arctos)

Author

Blandine Chazarin, Anna Ziemianin, Alina L. Evans, Emmanuelle Meugnier, Emmanuelle Loizon, Isabelle Chery, Jon M. Arnemo, Jon E. Swenson, Guillemette Gauquelin-Koch, Chantal Simon, Stéphane Blanc, Etienne Lefai, and Fabrice Bertile

Subjects
hibernation, brown bears, skeletal muscle, cold response, oxidative stress, NRF2, Therapeutics. Pharmacology, RM1-950
Abstract

Oxidative stress, which is believed to promote muscle atrophy, has been reported to occur in a few hibernators. However, hibernating bears exhibit efficient energy savings and muscle protein sparing, despite long-term physical inactivity and fasting. We hypothesized that the regulation of the oxidant/antioxidant balance and oxidative stress could favor skeletal muscle maintenance in hibernating brown bears. We showed that increased expressions of cold-inducible proteins CIRBP and RBM3 could favor muscle mass maintenance and alleviate oxidative stress during hibernation. Downregulation of the subunits of the mitochondrial electron transfer chain complexes I, II, and III, and antioxidant enzymes, possibly due to the reduced mitochondrial content, indicated a possible reduction of the production of reactive oxygen species in the hibernating muscle. Concomitantly, the upregulation of cytosolic antioxidant systems, under the control of the transcription factor NRF2, and the maintenance of the GSH/GSSG ratio suggested that bear skeletal muscle is not under a significant oxidative insult during hibernation. Accordingly, lower levels of oxidative damage were recorded in hibernating bear skeletal muscles. These results identify mechanisms by which limited oxidative stress may underlie the resistance to skeletal muscle atrophy in hibernating brown bears. They may constitute therapeutic targets for the treatment of human muscle atrophy.

Published
2019
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3. Effectiveness of Resistive Vibration Exercise and Whey Protein Supplementation Plus Alkaline Salt on the Skeletal Muscle Proteome Following 21 Days of Bed Rest in Healthy Males

Author

Guillemette Gauquelin-Koch, Anna Ziemianin, Alexandre Zahariev, Helena Kenny, Martina Heer, Floriane Rudwill, Fabrice Bertile, Donal J. O’Gorman, Georg Tascher, Stéphane Blanc, Marie-Pierre Barielle, Isabelle Chery, Dublin City University [Dublin] (DCU), Département Sciences Analytiques et Interactions Ioniques et Biomoléculaires (DSA-IPHC), Institut Pluridisciplinaire Hubert Curien (IPHC), Université de Strasbourg (UNISTRA)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS), Département Ecologie, Physiologie et Ethologie (DEPE-IPHC), Centre National d’Études Spatiales [Paris] (CNES), Institut de Médecine et de Physiologie Spatiales (MEDES), Centre Hospitalier Universitaire d'Angers (CHU Angers), PRES Université Nantes Angers Le Mans (UNAM)-PRES Université Nantes Angers Le Mans (UNAM)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Université de Bordeaux (UB)-CHU Toulouse [Toulouse]-Université Jean Monnet [Saint-Étienne] (UJM)-Université de Tours-Université de Clermont-Ferrand-Centre National d'Études Spatiales [Toulouse] (CNES), University of Bonn, and Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Université de Bordeaux (UB)-CHU Toulouse [Toulouse]-Université Jean Monnet [Saint-Étienne] (UJM)-Université de Tours (UT)-Université de Clermont-Ferrand-Centre National d'Études Spatiales [Toulouse] (CNES)

Subjects
0301 basic medicine, Male, medicine.medical_specialty, mitochondrial metabolism, protein synthesis, Proteome, Vastus lateralis muscle, medicine.medical_treatment, Protein degradation, Bed rest, Biochemistry, Vibration, 03 medical and health sciences, Insulin resistance, Internal medicine, insulin resistance, [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], Whey, medicine, [SDV.MHEP.PHY]Life Sciences [q-bio]/Human health and pathology/Tissues and Organs [q-bio.TO], Humans, Muscle, Skeletal, Cross-Over Studies, 030102 biochemistry & molecular biology, exercise, Chemistry, VO2 max, Skeletal muscle, General Chemistry, medicine.disease, Muscle atrophy, 030104 developmental biology, medicine.anatomical_structure, Endocrinology, nutrition, Whey Proteins, Dietary Supplements, Lean body mass, protein degradation, medicine.symptom, [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition, Bed Rest
Abstract

International audience; Muscle atrophy is a deleterious consequence of physical inactivity and is associated with increased morbidity and mortality. The aim of this study was to decipher the mechanisms involved in disuse muscle atrophy in eight healthy men using a 21 day bed rest with a cross-over design (control, with resistive vibration exercise (RVE), or RVE combined with whey protein supplementation and an alkaline salt (NEX)). The main physiological findings show a significant reduction in whole-body fat-free mass (CON −4.1%, RVE −4.3%, NEX −2.7%, p < 0.05), maximal oxygen consumption (CON −20.5%, RVE −6.46%, NEX −7.9%, p < 0.05), and maximal voluntary contraction (CON −15%, RVE −12%, and NEX −9.5%, p < 0.05) and a reduction in mitochondrial enzyme activity (CON −30.7%, RVE −31.3%, NEX −17%, p < 0.05). The benefits of nutrition and exercise countermeasure were evident with an increase in leg lean mass (CON −1.7%, RVE +8.9%, NEX +15%, p < 0.05). Changes to the vastus lateralis muscle proteome were characterized using mass spectrometry-based label-free quantitative proteomics, the findings of which suggest alterations to cell metabolism, mitochondrial metabolism, protein synthesis, and degradation pathways during bed rest. The observed changes were partially mitigated during RVE, but there were no significant pathway changes during the NEX trial. The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium with the dataset identifier PXD006882. In conclusion, resistive vibration exercise, when combined with whey/alkalizing salt supplementation, could be an effective strategy to prevent skeletal muscle protein changes, muscle atrophy, and insulin sensitivity during medium duration bed rest.

Published
2020
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4. Metabolic reprogramming involving glycolysis in the hibernating brown bear skeletal muscle

Author

Marine Plumel, Stéphanie Chanon, Jon E. Swenson, Kenneth B. Storey, Stéphane Blanc, Guillemette Gauquelin-Koch, Etienne Lefai, Chantal Simon, Isabelle Chery, Fabrice Bertile, Blandine Chazarin, Anna Ziemianin, Jon M. Arnemo, Alina L. Evans, Andreas Zedrosser, Christine Durand, Sciences Analytiques et Interactions Ioniques et Biomoléculaires (DSA-IPHC), Institut Pluridisciplinaire Hubert Curien (IPHC), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS), Centre National d'Études Spatiales [Toulouse] (CNES), Carleton University, 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)-Hospices Civils de Lyon (HCL)-Institut National de la Santé et de la Recherche Médicale (INSERM), Département Ecologie, Physiologie et Ethologie (DEPE-IPHC), Inland Norway University of Applied Sciences - Høgskolen i Innlandet, Swedish University of Agricultural Sciences (SLU), University of Natural Resources and Applied Life Sciences (BOKU), Norwegian University of Life Sciences (NMBU), Régulations métaboliques, nutrition et diabètes (RMND), Département Sciences Analytiques et Interactions Ioniques et Biomoléculaires (DSA-IPHC), Université de Strasbourg (UNISTRA)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS), 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), Université de Lyon-Institut National de la Recherche Agronomique (INRA), University of Natural Resources and Life Sciences (BOKU), 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), and Bertile, F.

Subjects
0106 biological sciences, 0301 basic medicine, medicine.medical_specialty, Brown bears, Enzymology, Glycolysis, Hibernation, Lipid oxidation, Metabolism shift, Omics, Skeletal muscle, Biology, Carbohydrate metabolism, 010603 evolutionary biology, 01 natural sciences, 03 medical and health sciences, chemistry.chemical_compound, Internal medicine, lcsh:Zoology, Biologie animale, [SDV.BA.ZV]Life Sciences [q-bio]/Animal biology/Vertebrate Zoology, medicine, lcsh:QL1-991, Ecology, Evolution, Behavior and Systematics, Animal biology, Glycogen, Research, Torpor, 030104 developmental biology, medicine.anatomical_structure, Endocrinology, chemistry, Basal metabolic rate, Animal Science and Zoology, medicine.symptom, Muscle contraction
Abstract

Open Access This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. Background In mammals, the hibernating state is characterized by biochemical adjustments, which include metabolic rate depression and a shift in the primary fuel oxidized from carbohydrates to lipids. A number of studies of hibernating species report an upregulation of the levels and/or activity of lipid oxidizing enzymes in muscles during torpor, with a concomitant downregulation for glycolytic enzymes. However, other studies provide contrasting data about the regulation of fuel utilization in skeletal muscles during hibernation. Bears hibernate with only moderate hypothermia but with a drop in metabolic rate down to ~ 25% of basal metabolism. To gain insights into how fuel metabolism is regulated in hibernating bear skeletal muscles, we examined the vastus lateralis proteome and other changes elicited in brown bears during hibernation. Results We show that bear muscle metabolic reorganization is in line with a suppression of ATP turnover. Regulation of muscle enzyme expression and activity, as well as of circulating metabolite profiles, highlighted a preference for lipid substrates during hibernation, although the data suggested that muscular lipid oxidation levels decreased due to metabolic rate depression. Our data also supported maintenance of muscle glycolysis that could be fuelled from liver gluconeogenesis and mobilization of muscle glycogen stores. During hibernation, our data also suggest that carbohydrate metabolism in bear muscle, as well as protein sparing, could be controlled, in part, by actions of n-3 polyunsaturated fatty acids like docosahexaenoic acid. Conclusions Our work shows that molecular mechanisms in hibernating bear skeletal muscle, which appear consistent with a hypometabolic state, likely contribute to energy and protein savings. Maintenance of glycolysis could help to sustain muscle functionality for situations such as an unexpected exit from hibernation that would require a rapid increase in ATP production for muscle contraction. The molecular data we report here for skeletal muscles of bears hibernating at near normal body temperature represent a signature of muscle preservation despite atrophying conditions.

Published
2019
Full Text
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5. Limited oxidative stress favors resistance to skeletal muscle atrophy in hibernating brown bears (Ursus Arctos)

Author

Alina L. Evans, Blandine Chazarin, Anna Ziemianin, Stéphane Blanc, Guillemette Gauquelin-Koch, Jon M. Arnemo, Jon E. Swenson, Isabelle Chery, Emmanuelle Meugnier, Etienne Lefai, Chantal Simon, Emmanuelle Loizon, Fabrice Bertile, Bertile, F., Département Sciences Analytiques et Interactions Ioniques et Biomoléculaires (DSA-IPHC), Institut Pluridisciplinaire Hubert Curien (IPHC), Université de Strasbourg (UNISTRA)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS), Centre National d'Etudes Spatiales, Department of Forestry and Wildlife Management Inland Norway University of Applied Sciences, Cardiovasculaire, métabolisme, diabétologie et nutrition (CarMeN), 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), Université de Lyon-Institut National de la Recherche Agronomique (INRA), Département Ecologie, Physiologie et Ethologie (DEPE-IPHC), Department of Wildlife, Fish and Environmental Studies, Swedish University of Agricultural Sciences (SLU), Faculty of Environmental Sciences and Natural Resource Management, Unité de Nutrition Humaine (UNH), Institut National de la Recherche Agronomique (INRA)-Université Clermont Auvergne [2017-2020] (UCA [2017-2020]), Gaillard, Brigitte, 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)-Hospices Civils de Lyon (HCL)-Institut National de la Santé et de la Recherche Médicale (INSERM), Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Institut National de Physique Nucléaire et de Physique des Particules du CNRS (IN2P3)-Centre National de la Recherche Scientifique (CNRS), ANR-16-IDEX-0001,CAP 20-25,CAP 20-25(2016), Sciences Analytiques et Interactions Ioniques et Biomoléculaires (DSA-IPHC), Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS), 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), Unité de Nutrition Humaine - Clermont Auvergne (UNH), and Institut National de la Recherche Agronomique (INRA)-Université Clermont Auvergne (UCA)

Subjects
[SDE] Environmental Sciences, Hibernation, medicine.medical_specialty, Physiology, Clinical Biochemistry, brown bears, Oxidative phosphorylation, medicine.disease_cause, Biochemistry, CIRBP, NRF2, 03 medical and health sciences, 0302 clinical medicine, Atrophy, Internal medicine, medicine, oxidative stress, skeletal muscle, hibernation, Molecular Biology, 030304 developmental biology, chemistry.chemical_classification, 0303 health sciences, Reactive oxygen species, lcsh:RM1-950, Skeletal muscle, Cell Biology, medicine.disease, Muscle atrophy, lcsh:Therapeutics. Pharmacology, Endocrinology, medicine.anatomical_structure, chemistry, cold response, [SDE]Environmental Sciences, medicine.symptom, 030217 neurology & neurosurgery, Oxidative stress, Autre (Sciences du Vivant)
Abstract

Oxidative stress, which is believed to promote muscle atrophy, has been reported to occur in a few hibernators. However, hibernating bears exhibit efficient energy savings and muscle protein sparing, despite long-term physical inactivity and fasting. We hypothesized that the regulation of the oxidant/antioxidant balance and oxidative stress could favor skeletal muscle maintenance in hibernating brown bears. We showed that increased expressions of cold-inducible proteins CIRBP and RBM3 could favor muscle mass maintenance and alleviate oxidative stress during hibernation. Downregulation of the subunits of the mitochondrial electron transfer chain complexes I, II, and III, and antioxidant enzymes, possibly due to the reduced mitochondrial content, indicated a possible reduction of the production of reactive oxygen species in the hibernating muscle. Concomitantly, the upregulation of cytosolic antioxidant systems, under the control of the transcription factor NRF2, and the maintenance of the GSH/GSSG ratio suggested that bear skeletal muscle is not under a significant oxidative insult during hibernation. Accordingly, lower levels of oxidative damage were recorded in hibernating bear skeletal muscles. These results identify mechanisms by which limited oxidative stress may underlie the resistance to skeletal muscle atrophy in hibernating brown bears. They may constitute therapeutic targets for the treatment of human muscle atrophy.

Published
2019
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6. Screening of new huprines--inhibitors of acetylcholinesterases by electrospray ionization ion trap mass spectrometry

Author

Pierre-Yves Renard, Catherine Lange, Romain Dolé, Anna Ziemianin, Ludovic Jean, Cyril Ronco, Chimie Organique et Bioorganique : Réactivité et Analyse (COBRA), Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Normandie Université (NU)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Institut de Chimie du CNRS (INC)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie Organique Fine (IRCOF), Université de Rouen Normandie (UNIROUEN), and Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Spectrometry, Mass, Electrospray Ionization, Aché, Stereochemistry, Electrospray ionization, Clinical Biochemistry, Pharmaceutical Science, Substrate analog, Mass spectrometry, GPI-Linked Proteins, 01 natural sciences, Heterocyclic Compounds, 4 or More Rings, Models, Biological, Analytical Chemistry, Choline, 03 medical and health sciences, chemistry.chemical_compound, Structure-Activity Relationship, Drug Discovery, medicine, Animals, Humans, Spectroscopy, ComputingMilieux_MISCELLANEOUS, 030304 developmental biology, 0303 health sciences, Chromatography, Dose-Response Relationship, Drug, Molecular Structure, 010405 organic chemistry, [CHIM.ORGA]Chemical Sciences/Organic chemistry, Acetylcholinesterase, language.human_language, Acetylcholine, Recombinant Proteins, 0104 chemical sciences, 3. Good health, Kinetics, chemistry, Acetylthiocholine, Electrophorus, language, Aminoquinolines, Cholinesterase Inhibitors, medicine.drug
Abstract

Acetylcholinesterase inhibitors (AChEI) are one of the drugs families validated for clinical use in the treatment of Alzheimer's disease (AD). For this reason, finding new more potent and more selective AChEIs is always of interest. Since 1961, the inhibitory activity of AChEI is evaluated through the Ellman's method. Herein, we reported a MS-based evaluation of potential new AChEI with the determination of their inhibitory activity (IC 50 and K I ). Compared to the Ellman's method, that uses the substrate analog acetylthiocholine, the electrospray ionization ion trap mass spectrometry (ESI-IT-MS) consists in monitoring the conversion ratio of a low concentration of the natural substrate – acetylcholine to choline. We present here the inhibition activity of huprine X and six of its derivates (bearing different functional groups at position 9) towards the recombinant human ( rh AChE) and Electrophorus electricus acetylcholinesterase ( Eel AChE). Mechanisms of action of selected inhibitors were evaluated by means of Lineweaver–Burk plot analysis. The Michaelis–Menten constants ( K M ), inhibitory constants ( K I ) were examined as well as the IC 50 to allow classifying a series of huprine derivatives by inhibition potency by a comparison with a reference (huprine X). Our results demonstrate that these drugs are very potent AChE inhibitors, especially (±)-huprine 6 with an inhibitory activity on recombinant human AChE ( rh AChE) in the picomolar range. This study reveals the interest of huprine compounds in the treatment of AD.

Published
2012
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