H Vaudry

Université de Rouen, Mont-Saint-Aignan, Upper Normandy, France

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Publications (717)2167.76 Total impact

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    ABSTRACT: The neuropeptide 26RFa and its cognate receptor GPR103 are involved in the control of food intake and bone mineralization. The aim of the present study was to experimentally characterize predicted ligand-receptor interactions by site-directed mutagenesis of GPR103 and to design point-substituted 26RFa analogs.
    British Journal of Pharmacology 06/2014; · 5.07 Impact Factor
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    ABSTRACT: The hypothalamus senses hormones and nutrients in order to regulate energy balance. In particular, detection of hypothalamic glucose levels has been shown to regulate both feeding behavior and peripheral glucose homeostasis, and impairment of this regulatory system is believed to be involved in the development of obesity and diabetes. Several data clearly demonstrate that glial cells are key elements in the perception of glucose, constituting with neurons a "glucose-sensing unit". Characterization of this interplay between glia and neurons represents an exciting challenge, and will undoubtedly contribute to identify new candidates for therapeutic intervention. The purpose of this review is to summarize the current data that stress the importance of glia in central glucose-sensing. The nature of the glia-to-neuron signaling is discussed, with a special focus on the endozepine ODN, a potent anorexigenic peptide that is highly expressed in hypothalamic glia.
    Hormone and Metabolic Research 09/2013; · 2.15 Impact Factor
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    ABSTRACT: Pituitary adenylate cyclase-activating polypeptide (PACAP), a hypophysiotropic neurohormone, participates in the regulation of pleiotropic functions. The recent discovery of intracellular PACAP receptors in the brain and the testis as well as the physico-chemical characteristics of PACAP, i.e. extended α-helix containing basic residues, prompted us to evaluate the propensity of PACAP to cross the plasma membrane in a receptor-independent manner. Using confocal microscopy and flow cytometry, we demonstrated the ability of FITC-conjugated PACAP to efficiently penetrate into the internal cell compartment by direct translocation and endocytosis through clathrin-coated pits and macropinocytosis. Our study also revealed that, once inside the cells, PACAP38 is not entirely degraded by intracellular enzymes and that a significant amount of intact PACAP38 is also able to exit cells. Moreover, using binding assay on rat nuclear fractions from various tissues we identified nuclear receptors for PACAP. We also found that PACAP stimulates calcium release in rat testis nuclei. Interestingly, PACAP27 and PACAP38 but not VIP were able to upregulate de novo DNA synthesis in testis nuclei and that this effect was abolished by PACAP(6-38). These results support the presence of PAC1 receptors at the nuclear membrane and raise questions about their role in the biological activity of the peptide. These findings contribute to the characterization of PACAP as an intracrine factor and extend the scope of PACAP derivatives to decipher the mechanisms of action of PACAP and to develop therapeutic treatments.
    Biochimica et Biophysica Acta 01/2012; · 4.66 Impact Factor
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    ABSTRACT: Identification of novel molecules that can induce neuronal differentiation of embryonic stem (ES) cells is essential for deciphering the molecular mechanisms of early development and for exploring cell therapy approaches. Pituitary adenylate cyclase-activating polypeptide (PACAP) and vasoactive intestinal polypeptide (VIP) are known to be implicated early during ontogenesis in cell proliferation and neuronal differentiation. The aim of the present study was to determine the effects of VIP and PACAP on functional differentiation of ES cells. Quantitative-reverse transcription-polymerase chain reaction analysis showed an inversion of the expression pattern of PAC1 and VPAC1 receptors with time. ES cells expressed genes encoding extracellular signal-regulated kinase 1 and 2 and c-jun amino terminal kinase1. ES cells also expressed T-type α1I and α1G, L-type α1C and α1D, and N-type α1B calcium channel subunit mRNAs. Both peptides modified the shape of undifferentiated ES cells into bipolar cells expressing the neuronal marker neuron-specific enolase (NSE). Immunostaining indicated that PACAP intensified T-type α1I subunit immunoreactivity, whereas VIP increased L-types α1C and α1D, as well as N-type α1B subunit. Electrophysiological recording showed that VIP and PACAP enhanced transient calcium current. Moreover, VIP generated sustained calcium current. These findings demonstrate that PACAP and VIP induce morphological and functional differentiation of ES cells into a neuronal phenotype. Both peptides promote functional maturation of calcium channel subunits, suggesting that they can facilitate the genesis of cellular excitability.
    Neuroscience 12/2011; 199:103-15. · 3.12 Impact Factor
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    ABSTRACT: The kisspeptin system has emerged as one of the main puberty gatekeepers among vertebrates. The European eel (Anguilla anguilla) is a remarkable model due to its phylogenetical position at the basis of teleosts, and its unique life cycle with a blockade of puberty before reproductive migration. We cloned the full-length coding sequence of a kisspeptin receptor (Kissr) in the eel. Comparison of Kissr sequences assigned the eel Kissr to a basal position in a clade including most of the known teleost Kissr, in agreement with the eel phylogenetical position. Eel Kissr tissue distribution was analyzed by quantitative real-time PCR. Eel Kissr was highly expressed in the brain, especially in the telencephalon and di-/mes-encephalon, while a very low or undetectable expression was observed in various peripheral organs. A high expression of Kissr was also found in the pituitary indicating a possible direct pituitary role of kisspeptin. Primary cultures of eel pituitary cells were performed to investigate the direct effects of kisspeptin on pituitary hormone expression. Human/lamprey kisspeptin exerted a time- and dose-dependent inhibitory effect on LHβ expression. All other tested kisspeptins had a similar inhibitory effect on LHβ expression. The inhibitory effect of kisspeptins was exerted specifically on LHβ as no change was induced on the expression of other glycoprotein hormone subunits (GPα, FSHβ and TSHβ) nor of growth hormone. These data provide the first evidence for the existence, in the European eel, of a kisspeptin system, which may play a direct inhibitory role on pituitary LHβ expression.
    General and Comparative Endocrinology 06/2011; 173(1):216-25. · 2.82 Impact Factor
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    ABSTRACT: I.c.v. administration of the octadecaneuropeptide (ODN), a peptide derived from diazepam-binding inhibitor (DBI), induces anorexigenic and anxiogenic-like actions in rodents. We have recently shown that, in goldfish, i.c.v. injection of ODN also reduces food consumption via the metabotropic endozepine receptor. However, there is little information regarding the structure of DBI and the psychophysiological roles of endozepines in fish. Therefore, in the present study, we isolated and cloned a cDNA encoding goldfish DBI. The deduced sequence exhibits high similarity with non-mammalian DBIs, and we investigated the effect of homologous ODN on psychomotor activity in goldfish. i.c.v. injection of synthetic goldfish ODN at 10 pmol/g body weight (BW) stimulated locomotor activity. Since intact goldfish placed in a tank with both black and white background areas prefers the black compartment, we developed a method for measuring the time taken for fish to move from the black to the white area. I.c.v. administration of diazepam (35 and 350 pmol/g BW) decreased, whereas i.c.v. administration of ODN (10 pmol/g BW) or the central-type benzodiazepine receptor inverse agonist FG-7142 (9 pmol/g BW) increased the time taken to move from the black to the white background area. The anxiogenic-like effect of ODN was blocked by the central-type benzodiazepine receptor antagonist flumazenil (100 pmol/g BW), but was not affected by the metabotropic endozepine receptor antagonist cyclo1-8[d-Leu(5)]octapeptide (100 pmol/g BW). These data indicate that ODN can potently affect locomotor and psychomotor activities in goldfish and that this action is mediated via the central-type benzodiazepine receptor-signaling pathway.
    Neuroscience 03/2011; 181:100-8. · 3.12 Impact Factor
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    Canadian Journal of Physiology and Pharmacology 02/2011; 61(1):23-28. · 1.56 Impact Factor
  • . Current Pharmaceutical Design. 01/2011; 17:1002.
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    ABSTRACT: Before kisspeptins became new players in the field of reproductive biology, GnRH was acknowledged in all vertebrates as the major initiator of the hormonal cascade modulating the reproductive axis. Originally identified as a metastasis suppressor in mammals [1], the KISS1 gene produces several peptides named kisspeptins (kisspeptin -54, 14, 13, 10), which activate the KISS1 receptor (GPR54 or KISSR) previously known as an orphan receptor [2]. Recent phylogenetical analysesprovided evidence that the number of kiss genes andkiss receptors varies from one class of vertebrate to the other. According to these studies [3] modern mammals have only one KISS gene, monotrems have two, birds would have none, reptiles have one, amphibians have three and fishes have two KISS genes. Similarly, the number of genes encoding GPR54 receptors (or Kissr) also varies from one class to the other. With the aim to enlarge our knowledge on organization and potential functions of Kiss systems in relation to GPR54 receptors in non-mammalian species, so far very poorly investigated,we have focused our interest on the elucidation of these systems in zebrafish, taken as model of study. Zebrafish have two kiss genes, kiss1 and kiss2 and two kiss receptors (GPR54), kiss1r and kiss2r.
    Indian Journal of Science and Technology. 01/2011; 4:52-53.
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    ABSTRACT: In neurological insults, such as cerebral ischemia and traumatic brain injury, complex molecular mechanisms involving inflammation and apoptosis are known to cause severe neuronal cell loss, emphasizing the necessity of developing therapeutic strategies targeting simultaneously these two processes. Over the last decade, numerous in vitro and in vivo studies have demonstrated the unique therapeutical potential of pituitary adenylate cyclase-activating polypeptide (PACAP) for the treatment of neuronal disorders involving apoptotic cell death and neuroinflammation. The neuroprotective activity of PACAP is based on its capacity to reduce the production of deleterious cytokines from activated microglia, to stimulate the release of neuroprotective agents from astrocytes and to inhibit pro-apoptotic intracellular pathways. However, the use of PACAP as a clinically applicable drug is hindered by its peptidic nature. As most natural peptides, native PACAP shows poor metabolic stability, low bioavailability, inadequate distribution and rapid blood clearance. Moreover, injection of PACAP to human can induce peripheral adverse side effects. Therefore, targeted chemical modifications and/or conjugation of PACAP to different macromolecules are required to improve the pharmacokinetic and pharmacological properties of PACAP. This review presents the chemical, biochemical and pharmacological strategies that are currently under development to convert PACAP from a hypophysiotropic neurohormone into a clinically relevant neuroprotective drug.
    Current pharmaceutical design 01/2011; 17(10):1002-24. · 4.41 Impact Factor
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    ABSTRACT: Accumulating evidence indicate that the neuropeptide urotensin II and urotensin II receptors are expressed in subsets of mammal spinal motoneurons. In fact, a role for the peptide in the regulation of motoneuron function at neuromuscular junction has been suggested, while roles for urotensin II at central synapses in spinal cord have never been addressed. We found that urotensin II receptors were closely associated with cholinergic terminals apposed to a subset of motoneuron and non-motoneuron cell bodies in the ventral horn of the adult mouse cervical spinal cord; urotensin II receptor was also expressed on non-cholinergic nerve terminals. In particular, urotensin II receptor appeared associated with both large cholinergic C-boutons and standard cholinergic terminals contacting some motoneuron perikarya. Cholinergic nerve terminals from mouse cervical spinal cord were equipped with functional presynaptic urotensin II receptors linked to excitation of acetylcholine release. In fact, functional experiments conducted on cervical spinal synaptosomes demonstrated a urotensin II evoked calcium-dependent increase in [(3)H]acetylcholine release pharmacologically verified as consistent with activation of urotensin II receptors. In spinal cord these actions would facilitate cholinergic transmission. These data indicate that, in addition to its role at the neuromuscular junction, urotensin II may control motor function through the modulation of motoneuron activity within the spinal cord.
    Neuroscience 09/2010; 170(1):67-77. · 3.12 Impact Factor
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    ABSTRACT: Gonadotrophin-releasing hormone (GnRH) is the primary hypothalamic factor responsible for the control of gonadotrophin secretion in vertebrates. However, within the last decade, two other hypothalamic neuropeptides have been found to play key roles in the control of reproductive functions: gonadotrophin-inhibitory hormone (GnIH) and kisspeptin. In 2000, we discovered GnIH in the quail hypothalamus. GnIH inhibits gonadotrophin synthesis and release in birds through actions on GnRH neurones and gonadotrophs, mediated via GPR147. Subsequently, GnIH orthologues were identified in other vertebrate species from fish to humans. As in birds, mammalian and fish GnIH orthologues inhibit gonadotrophin release, indicating a conserved role for this neuropeptide in the control of the hypothalamic-pituitary-gonadal axis across species. Subsequent to the discovery of GnIH, kisspeptin, encoded by the KiSS-1 gene, was discovered in mammals. By contrast to GnIH, kisspeptin has a direct stimulatory effect on GnRH neurones via GPR54. GPR54 is also expressed in pituitary cells, but whether gonadotrophs are targets for kisspeptin remains unresolved. The KiSS-1 gene is also highly conserved and has been identified in mammals, amphibians and fish. We have recently found a second isoform of KiSS-1, designated KiSS-2, in several vertebrates, but not birds, rodents or primates. In this review, we highlight the discovery, mechanisms of action, and functional significance of these two chief regulators of the reproductive axis.
    Journal of Neuroendocrinology 05/2010; 22(7):716-27. · 3.51 Impact Factor
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    ABSTRACT: In the central nervous system of mammals, the gene encoding diazepam-binding inhibitor (DBI) is exclusively expressed in glial cells. Previous studies have shown that central administration of a DBI processing product, the octadecaneuropeptide ODN, causes a marked inhibition of food consumption in rodents. Paradoxically, however, the effect of food restriction on DBI gene expression has never been investigated. Here, we show that in mice, acute fasting dramatically reduces DBI mRNA levels in the hypothalamus and the ependyma bordering the third and lateral ventricles. I.p. injection of insulin, but not of leptin, selectively stimulated DBI expression in the lateral ventricle area. These data support the notion that glial cells, through the production of endozepines, may relay peripheral signals to neurons involved in the central regulation of energy homeostasis.
    Journal of Molecular Endocrinology 03/2010; 44(5):295-9. · 3.58 Impact Factor
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    ABSTRACT: Prolyl endopeptidase (PEP) is a serine protease that cleaves small peptides at the carboxyl side of L-proline. PEP has been reported to have important functions in the brain being implicated in learning and memory processes, psychological disorders and neurodegenerative diseases. Several PEP substrates have been shown to play a role during brain development and this observation led us to investigate the expression of PEP mRNA in the rat brain and spinal cord, from embryo to adult stages. In situ hybridization revealed that PEP mRNA is expressed early, from embryonic day 15, notably in germinative areas including the neocortical, hippocampal, pallidal, thalamic, anterior hypothalamic, tectal, cerebellar, pontine and medullary neuroepithelia. PEP mRNA was also found in the differentiating fields of the olfactory bulb, the orbital and cingulate cortex, the hippocampal formation, the cortical plate and the subventricular zone of the cortex. Quantitative RT-PCR analysis in various brain areas and the spinal cord showed that PEP mRNA levels are more abundant during the perinatal stages, coinciding with a period of neuronal migration and differentiation. From then on, PEP mRNA expression decreased, reaching its lowest levels at adulthood. Overall, the present data support the possibility that PEP exerts specific functions related to neurodevelopment besides those proposed to date.
    Journal of chemical neuroanatomy 03/2010; 40(1):53-62. · 1.75 Impact Factor
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    ABSTRACT: Apelin is a bioactive peptide isolated from bovine stomach extracts and identified as the endogenous ligand of the human orphan G protein-coupled receptor (GPCR), APJ. We characterized this receptor pharmacologically and demonstrated that apelin and its receptor were expressed together with vasopressin (AVP) in magnocellular hypothalamic neurons. We showed that the central injection of apelin in lactating rats decreased the activity of these neurons and the secretion of AVP into the bloodstream, resulting in aqueous diuresis. Apelin is thus a natural inhibitor of the anti-diuretic effects of AVP. Moreover, in rats and humans, plasma apelin levels were regulated by osmotic stimuli in the opposite direction to AVP, suggesting that apelin, like AVP, may be crucial to the maintenance of body fluid homeostasis. To explore further upstream the role played by apelin, non-peptidic agonists and antagonists of the apelin receptor are required. To identify such compounds which do not exist to date, we used an original FRET-based assay to screen a GPCR-focused library of fluorescent compounds on the human EGFP-tagged apelin receptor. This led to isolate E339-3D6 that displayed a 90 nM affinity, behaved as a partial agonist with regard to cAMP production and as a full agonist with regard to apelin receptor internalization. Finally, E339-3D6 induced vasorelaxation of rat aorta and potently inhibited systemic AVP release in water-deprived mice when centrally injected. This compound represents the first non-peptidic agonist of the apelin receptor, the optimization of which will allow to develop a new generation of vasodilator and aquaretic agents.
    Regulatory Peptides. 01/2010; 164(1):26.
  • Regulatory Peptides - REGUL PEPTIDES. 01/2010; 164(1):21-22.
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    ABSTRACT: Pituitary adenylate cyclase-activating polypeptide (PACAP) is a 38-amino acid peptide that was initially isolated from hypothalamus extracts on the basis of its ability to stimulate the production of cAMP in cultured pituitary cells. Recent studies have shown that PACAP exerts potent neuroprotective effects not only in vitro but also in in vivo models of Parkinson's disease, Huntington's disease, traumatic brain injury and stroke. The protective effects of PACAP are based on its capacity to prevent neuronal apoptosis by acting directly on neurons or indirectly through the release of neuroprotective factors by astrocytes. These biological activities are mainly mediated through activation of the PAC1 receptor which is currently considered as a potential target for the treatment of neurodegenerative diseases. However, the use of native PACAP, the endogenous ligand of PAC1, as an efficient neuroprotective drug is actually limited by its rapid degradation. Moreover, injection of PACAP to human induces peripheral side effects which are mainly mediated through VPAC1 and VPAC2 receptors. Strategies to overcome these compromising conditions include the development of metabolically stable analogs of PACAP acting as selective agonists of the PAC1 receptor. This review presents an overview of the structure-activity relationships of PACAP and summarizes the molecular and conformational requirements for activation of PAC1 receptor. The applicability of PACAP analogs as therapeutic agents for treatment of neurodegenerative diseases is also discussed.
    Current Medicinal Chemistry 10/2009; 16(33):4462-80. · 3.72 Impact Factor
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    ABSTRACT: Summary— Neuropeptide Y (NPY) is a 36-amino acid peptide first isolated and characterized from porcine brain extracts. A number of immunocytochemical investigations have been conducted to determine the localization of NPY-containing neurons in various animal species including both vertebrates and invertebrates. These studies have established the widespread distribution of NPY in the brain and in sympathetic neurons. In the rat brain, a high density of immunoreactive cell bodies and fibers is observed in the cortex, caudate putamen and hippocampus. In the diencephalon, NPY-containing perikarya are mainly located in the arcuate nucleus of the hypothalamus; numerous fibers innervate the paraventricular and suprachiasmatic nuclei of the hypothalamus, as well as the paraventricular nucleus of the thalamus and the periaqueductal gray. At the electron microscope level, using the pre- and post-embedding immunoperoxidase techniques, NPY-like immunoreactivity has been observed in neuronal cell body dendrites and axonal processes. In nerve terminals of the hypothalamus, the product of the immunoreaction is associated with large dense core vesicles. In lower vertebrates, including amphibians and fish, neurons originating from the diencephalic (or telencephalic) region innervate the intermediate lobe of the pituitary where a dense network of immunoreactive fibers has been detected. At the ultrastructural level, positive endings have been observed in direct contact with pituitary melanotrophs of frog and dogfish. These anatomical data suggest that NPY can act both as a neurotransmitter (or neuromodulator) and as a hypophysiotropic neurohormone.In the rat a few NPY-containing fibers are found in the internal zone of the median eminence and high concentrations of NPY-like immunoreactivity are detected in the hypothalamo-hypophyseal portal blood, suggesting that NPY may affect anterior pituitary hormone secretion. Intrajugular injection of NPY causes a marked inhibition of LH release but does not significantly affect other pituitary hormones. Passive immunoneutralization of endogenous NPY by specific NPY antibodies induces stimulation of LH release in female rats, suggesting that NPY could affect LH secretion at the pituitary level. However, NPY has no effect on LH release from cultured pituitary cells or hemipituitaries. In addition, autoradiographic studies show that sites for 125I-labeled Bolton-Hunter NPY or 125I-labeled PYY (2 specific ligands of NPY receptors) are not present in the adenohypophysis, while moderate concentrations of these binding sites are found in the neural lobe of the pituitary. It thus appears that the inhibitory effect of NPY on LH secretion must be mediated at the hypothalamic level. This hypothesis is supported by the following observations: i), intracerebroventricular injection of NPY causes a reduction in plasma LH; ii), NPY fibers have been observed in contact with LHRH neurons in the preoptic region; iii), the organum vasculosum of the lamina terminalis, where LHRH neurons are located, lacks a blood-brain barrier (NPY injected peripherally can thus reach LHRH neurons in this area). The fact that intracerebroventricular injection of NPY in 5,7-dihydroxytryptamine treated rats causes stimulation of LH release (instead of an inhibition in control animals) also suggests that the effect of NPY may in part be mediated via serotoninergic neurons.In amphibians, the existence of a NPY-neuronal system originating from the hypothalamus and terminating in the pars intermedia suggest that NPY may play a role in the control of pituitary melanotrophs. In vitro data show that NPY induces a marked inhibition of α-melanotropin (α-MSH) release in frog and toad. The biologically active determinant of NPY is located in the C-terminal region of the molecule. Experiments conducted with acutely dispersed pituitary cells and electrophysiological data using the patch-clamp technique indicate that NPY exerts a direct effect on pituitary melanotrophs. Administration of NPY in black background-adapted toads causes aggregation of dermal melanophores. Taken together, these data indicated that in amphibians NPY can be considered as a melanotropin-release inhibiting factor (MIF).From these studies, it is concluded that NPY was: i), a neurotransmitter which mediates a number of processes in the brain and in sympathetic nerves; and ii), a hypophysiotropic neurohormone which regulates the secretion of various pituitary hormones such as LH in mammals and α-MSH in amphibians.
    Fundamental and Clinical Pharmacology 08/2009; 4(3):307 - 340. · 1.99 Impact Factor
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    ABSTRACT: The distribution and density of pituitary adenylate cyclase–activating polypeptide (PACAP) binding sites have been investigated in the brain of the primates Jacchus callithrix (marmoset) and Macaca fascicularis (macaque) using [125I]-PACAP27 as a radioligand. PACAP binding sites were widely expressed in the brain of these two species with particularly high densities in the septum, hypothalamus and habenula. A moderate density of recognition sites was seen in all subdivisions of the cerebral cortex with a heterogenous distribution, the highest concentrations occurring in layers I and VI while the underlying white matter was almost devoid of binding sites. Reverse transcriptase–polymerase chain reaction (RT-PCR) analysis revealed intense expression of the mRNAs encoding the short and hop-1 variants of pituitary adenylate cyclase–activating polypeptide–specific receptor (PAC1-R) in the cortex of both marmoset and macaque, whereas vasoactive intestinal polypeptide/pituitary adenylate cyclase–activating polypeptide mutual receptor, subtype 1 (VPAC1-R) and vasoactive intestinal polypeptide/pituitary adenylate cyclase–activating polypeptide mutual receptor, subtype 2 (VPAC2-R) mRNAs were expressed at a much lower level. In situ hybridization histochemistry showed intense expression of PAC1-R and weak expression of VPAC1-R mRNAs in layer IV of the cerebral cortex. Incubation of cortical tissue slices with PACAP induced a dose-dependent stimulation of cyclic AMP formation, indicating that PACAP binding sites correspond to functional receptors. Moreover, treatment of primate cortical slices with 100 nM PACAP significantly reduced the activity of caspase-3, a key enzyme of the apoptotic cascade. The present results indicate that PACAP should exert the same neuroprotective effect in the brain of primates as in rodents and suggest that PAC1-R agonists may have a therapeutic value to prevent neuronal cell death after stroke or in specific neurodegenerative diseases.
    Neuroscience 03/2009; · 3.12 Impact Factor
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    ABSTRACT: This pilot train study compares the biofouling potential of two river waters that had been subjected to different pretreatment schemes conducting to equivalent microbial cells contents but different total and biodegradable organic carbon concentrations. Permeability and pressure drop of nanofiltration (NF) membranes were continuously monitored during the experiments. After a twenty week period of filtration, the membrane modules were autopsied, the composition and organization of membrane foulants were characterized by attenuated total reflection Fourier transform infrared (ATR-FTIR) spectroscopy and confocal laser scanning microscopy (CLSM). The ATR-FTIR spectra and CLSM observations of the fouled membranes revealed the presence of a biofilm at the membranes surface for the two feed waters. A positive correlation was observed between the biodegradable organic carbon concentration (BDOC) of feed water and the biofouling extent at the membrane surface: the BDOC concentration of feed water increase induced higher biofilm development. A longitudinal pressure drop increase was observed only with the water containing the higher concentration of BDOC whereas permeability decreases were equivalent with both feed waters. In conclusion, BDOC control through efficient pretreatments of raw water is a critical point for prevention of biofouling and maintenance of performances of NF membranes used in river water treatment.
    Desalination. 01/2009; 242(1):228-235.

Publication Stats

11k Citations
2,167.76 Total Impact Points

Institutions

  • 1979–2014
    • Université de Rouen
      • Microbiology Signals and Microenvironment Lab (LMSM) (EA 4312)
      Mont-Saint-Aignan, Upper Normandy, France
  • 2011
    • Institut national de la recherche scientifique
      Québec, Quebec, Canada
  • 2008–2011
    • University of Toyama
      Тояма, Toyama, Japan
    • Université de Cergy-Pontoise
      95001 CEDEX, Ile-de-France, France
    • Robert Wood Johnson University Hospital
      New Brunswick, New Jersey, United States
  • 2010
    • Waseda University
      • Department of Education (Faculty of Education and Integrated Arts and Sciences)
      Edo, Tōkyō, Japan
  • 2006
    • Université de Lomé
      Lomé, Maritime, Togo
  • 1999–2005
    • Université du Québec
      Québec, Quebec, Canada
  • 1998–2005
    • University of Camerino
      • Dipartimento Scienze Morfologiche e Biochimiche Comparate
      Camerino, The Marches, Italy
  • 1994–2005
    • French Institute of Health and Medical Research
      • Unit of Neuronal and Neuroendocrine Differentiation and Communication
      Lutetia Parisorum, Île-de-France, France
  • 1992–2005
    • University of Cordoba (Spain)
      • Departamento de Biología Celular, Fisiología e Inmunología
      Córdoba, Andalusia, Spain
    • University of Lille Nord de France
      Lille, Nord-Pas-de-Calais, France
    • University of New South Wales
      Kensington, New South Wales, Australia
  • 1998–2004
    • Fudan University
      • • School of Life Sciences
      • • Department of Physiology and Biophysics
      Shanghai, Shanghai Shi, China
  • 1988–2002
    • Laval University
      Québec, Quebec, Canada
    • University of Michigan
      • Department of Psychiatry
      Ann Arbor, MI, United States
    • University Hospital Brussels
      Bruxelles, Brussels Capital Region, Belgium
  • 1983–2002
    • French National Centre for Scientific Research
      Lutetia Parisorum, Île-de-France, France
  • 2001
    • Centre Hospitalier Universitaire Rouen
      Rouen, Upper Normandy, France
  • 1990–2001
    • Radboud University Nijmegen
      • • Department of Cellular Animal Physiology
      • • Department of Organismal Animal Physiology
      Nijmegen, Provincie Gelderland, Netherlands
    • Ecole Pratique des Hautes Etudes
      Lutetia Parisorum, Île-de-France, France
  • 1986–2001
    • Unité Inserm U1077
      Caen, Lower Normandy, France
    • Concordia University–Ann Arbor
      Ann Arbor, Michigan, United States
    • Lille Catholic University
      Lille, Nord-Pas-de-Calais, France
  • 2000
    • University of Denver
      • Department of Biological Sciences
      Denver, CO, United States
  • 1993–2000
    • European Space Agency
      Lutetia Parisorum, Île-de-France, France
  • 1991–2000
    • Creighton University
      • Department of Biomedical Sciences
      Omaha, NE, United States
    • Université de Montréal
      Montréal, Quebec, Canada
  • 1986–2000
    • Université de Sherbrooke
      • • Department of Medicine
      • • Department of Biochemistry
      Sherbrooke, Quebec, Canada
  • 1993–1999
    • Université de Bretagne Occidentale
      • Faculté de Médecine et des Sciences de la Santé
      Brest, Brittany, France
  • 1988–1999
    • Università degli Studi di Genova
      Genova, Liguria, Italy
  • 1994–1998
    • Università degli Studi di Torino
      Torino, Piedmont, Italy
  • 1989–1998
    • KU Leuven
      • Department of Biology
      Leuven, VLG, Belgium
    • University of Strasbourg
      • Faculty of Medicine
      Strasbourg, Alsace, France
  • 1997
    • Institut des Systèmes Complexes, Paris Île-de-France
      Lutetia Parisorum, Île-de-France, France
  • 1996
    • Second Military Medical University, Shanghai
      Shanghai, Shanghai Shi, China
  • 1995
    • Institut de Génétique et de Biologie Moléculaire et Cellulaire
      Strasburg, Alsace, France
  • 1988–1994
    • Institut Jacques Monod
      Lutetia Parisorum, Île-de-France, France
  • 1988–1992
    • Ecole Normale Supérieure de Paris
      Lutetia Parisorum, Île-de-France, France
  • 1989–1990
    • University of Ottawa
      • Faculty of Medicine
      Ottawa, Ontario, Canada
  • 1986–1988
    • Centre hospitalier de l'Université de Montréal (CHUM)
      Montréal, Quebec, Canada
  • 1975–1988
    • Observatoire des Sciences et des Techniques
      Lutetia Parisorum, Île-de-France, France
  • 1987
    • University of Gdansk
      • Department of Bioorganic Chemistry
      Danzig, Pomeranian Voivodeship, Poland
    • Salk Institute
      • Laboratories for Neuroendocrinology
      La Jolla, California, United States
  • 1986–1987
    • Université Libre de Bruxelles
      • Faculty of Sciences
      Bruxelles, Brussels Capital Region, Belgium
  • 1984
    • Tulane University
      New Orleans, Louisiana, United States