Search Results - (Author, Cooperation:L. Pastorino)

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  1. 1
    C. Bertolotto ; F. Lesueur ; S. Giuliano ; T. Strub ; M. de Lichy ; K. Bille ; P. Dessen ; B. d'Hayer ; H. Mohamdi ; A. Remenieras ; E. Maubec ; A. de la Fouchardiere ; V. Molinie ; P. Vabres ; S. Dalle ; N. Poulalhon ; T. Martin-Denavit ; L. Thomas ; P. Andry-Benzaquen ; N. Dupin ; F. Boitier ; A. Rossi ; J. L. Perrot ; B. Labeille ; C. Robert ; B. Escudier ; O. Caron ; L. Brugieres ; S. Saule ; B. Gardie ; S. Gad ; S. Richard ; J. Couturier ; B. T. Teh ; P. Ghiorzo ; L. Pastorino ; S. Puig ; C. Badenas ; H. Olsson ; C. Ingvar ; E. Rouleau ; R. Lidereau ; P. Bahadoran ; P. Vielh ; E. Corda ; H. Blanche ; D. Zelenika ; P. Galan ; V. Chaudru ; G. M. Lenoir ; M. Lathrop ; I. Davidson ; M. F. Avril ; F. Demenais ; R. Ballotti ; B. Bressac-de Paillerets
    Nature Publishing Group (NPG)
    Published 2015
    Staff View
    Publication Date:
    2015-12-04
    Publisher:
    Nature Publishing Group (NPG)
    Print ISSN:
    0028-0836
    Electronic ISSN:
    1476-4687
    Topics:
    Biology
    Chemistry and Pharmacology
    Medicine
    Natural Sciences in General
    Physics
    Published by:
    http://www.nature.com/

    Latest Papers from Table of Contents or Articles in Press
  2. 2
    C. Bertolotto ; F. Lesueur ; S. Giuliano ; T. Strub ; M. de Lichy ; K. Bille ; P. Dessen ; B. d'Hayer ; H. Mohamdi ; A. Remenieras ; E. Maubec ; A. de la Fouchardiere ; V. Molinie ; P. Vabres ; S. Dalle ; N. Poulalhon ; T. Martin-Denavit ; L. Thomas ; P. Andry-Benzaquen ; N. Dupin ; F. Boitier ; A. Rossi ; J. L. Perrot ; B. Labeille ; C. Robert ; B. Escudier ; O. Caron ; L. Brugieres ; S. Saule ; B. Gardie ; S. Gad ; S. Richard ; J. Couturier ; B. T. Teh ; P. Ghiorzo ; L. Pastorino ; S. Puig ; C. Badenas ; H. Olsson ; C. Ingvar ; E. Rouleau ; R. Lidereau ; P. Bahadoran ; P. Vielh ; E. Corda ; H. Blanche ; D. Zelenika ; P. Galan ; F. Aubin ; B. Bachollet ; C. Becuwe ; P. Berthet ; Y. J. Bignon ; V. Bonadona ; J. L. Bonafe ; M. N. Bonnet-Dupeyron ; F. Cambazard ; J. Chevrant-Breton ; I. Coupier ; S. Dalac ; L. Demange ; M. d'Incan ; C. Dugast ; L. Faivre ; L. Vincent-Fetita ; M. Gauthier-Villars ; B. Gilbert ; F. Grange ; J. J. Grob ; P. Humbert ; N. Janin ; P. Joly ; D. Kerob ; C. Lasset ; D. Leroux ; J. Levang ; J. M. Limacher ; C. Livideanu ; M. Longy ; A. Lortholary ; D. Stoppa-Lyonnet ; S. Mansard ; L. Mansuy ; K. Marrou ; C. Mateus ; C. Maugard ; N. Meyer ; C. Nogues ; P. Souteyrand ; L. Venat-Bouvet ; H. Zattara ; V. Chaudru ; G. M. Lenoir ; M. Lathrop ; I. Davidson ; M. F. Avril ; F. Demenais ; R. Ballotti ; B. Bressac-de Paillerets
    Nature Publishing Group (NPG)
    Published 2011
    Staff View
    Publication Date:
    2011-10-21
    Publisher:
    Nature Publishing Group (NPG)
    Print ISSN:
    0028-0836
    Electronic ISSN:
    1476-4687
    Topics:
    Biology
    Chemistry and Pharmacology
    Medicine
    Natural Sciences in General
    Physics
    Keywords:
    Carcinoma, Renal Cell/*genetics ; Cell Movement/genetics ; Gene Frequency ; *Genetic Predisposition to Disease ; *Germ-Line Mutation ; Humans ; Melanoma/*genetics ; Microphthalmia-Associated Transcription Factor/*genetics ; Neoplasm Invasiveness/genetics ; Sumoylation
    Published by:
    http://www.nature.com/

    Latest Papers from Table of Contents or Articles in Press
  3. 3
    Caputi, A. ; Barindelli, S. ; Pastorino, L. ; Cimino, M. ; Buxbaum, J. D. ; Cattabeni, F. ; Di Luca, M.

    Oxford, UK : Blackwell Science Ltd
    Published 1997
    Staff View
    ISSN:
    1471-4159
    Source:
    Blackwell Publishing Journal Backfiles 1879-2005
    Topics:
    Medicine
    Notes:
    Abstract: Protein kinase C (PKC) activation stimulates release of secreted amyloid precursor protein (APPs) in several cell lines. To ascertain the role of PKC in regulating APP metabolism in vivo, we used an animal model (methylazoxymethanol-treated rats; MAM rats) in which PKC is permanently hyperactivated in selected brain areas, i.e., cortex and hippocampus. A significant decrease in membrane-bound APP concentration was found in synaptosomes derived from cortex and hippocampus of MAM rats, where PKC is up-regulated, with a concomitant increase in APPs production in soluble fractions of the same brain areas. In contrast, in a brain area not affected by MAM treatment (i.e., cerebellum), APP secretion is similar in control and MAM rats, indicating that altered metabolism of APP is restricted to only those areas in which the PKC system is up-regulated. In addition, phorbol esters or H-7 modulate APPs release in hippocampal slices from both control and MAM rats, further supporting an in vivo role for this enzyme in regulating metabolism of mature APP.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1046/j.1471-4159.1997.68062523.x

    Articles: DFG German National Licenses
  4. 4
    Gardoni, F. ; Caputi, A. ; Cimino, M. ; Pastorino, L. ; Cattabeni, F. ; Di Luca, M.

    Oxford, UK : Blackwell Science Ltd
    Published 1998
    Staff View
    ISSN:
    1471-4159
    Source:
    Blackwell Publishing Journal Backfiles 1879-2005
    Topics:
    Medicine
    Notes:
    Abstract: NMDA receptors and Ca2+/calmodulin-dependent kinase II (CaMKII) have been reported to be highly concentrated in the postsynaptic density (PSD). Although the possibility that CaMKII in PSD might be associated with specific proteins has been put forward, the protein or proteins determining the targeting of the kinase in PSD have not yet been identified. Here we report that CaMKII binds to NR2A and NR2B subunits of NMDA receptors in PSD isolated from cortex and hippocampus. The association of NMDA receptor subunits and CaMKII was assessed by immunoprecipitating PSD proteins with antibodies specific for NR2A/B and CaMKII: CaMKII coprecipitated with NR2A/B and NR1 but not with other glutamate ionotropic receptor subunits, such as GluR1 and GluR2-3. A direct association between CaMKII and NR2A/B subunits was further confirmed by overlay experiments using either 32P-autophosphorylated CaMKII or 32P-NR2A/B and by evaluating the formation of a CaMKII-NR2A/B complex by means of the cross-linker disuccimidyl suberate. These data demonstrate an association between the NMDA receptor complex and CaMKII in the postsynaptic compartment, suggesting that this colocalization may be relevant for synaptic plasticity.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1046/j.1471-4159.1998.71041733.x

    Articles: DFG German National Licenses
  5. 5
    Staff View
    ISSN:
    1365-2214
    Source:
    Blackwell Publishing Journal Backfiles 1879-2005
    Topics:
    Medicine
    Psychology
    Notes:
    Background  Diagnosis of Nevoid Basal Cell Carcinoma Syndrome (NBCCS) in infants may pose significant challenges to clinicians owing to its variable expressivity and age-related manifestations.Methods  We report two paediatric cases of NBCCS who presented initially with a non-specific phenotype.Results  In case 1, a diagnosis of NBCCS was possible only after the father was interviewed and found to present with two major criteria for the disease. Subsequent molecular testing confirmed the diagnosis. In case 2, molecular testing of the infant and his father had diagnostic value as neither satisfied fully the current diagnostic criteria for NBCCS.Conclusions  Presence of the few clinical manifestations of NBCCS that appear in infants, typically congenital malformations and skeletal abnormalities, should prompt clinicians to conduct in-person interviews with both parents. In general, paediatricians should refer both parents of infants who are suspected of having an inherited condition to clinical geneticists for expert examination, given the potential unreliability of reported medical history.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1111/j.1365-2214.2005.00514.x

    Articles: DFG German National Licenses
  6. 6
    Caputi, A. ; Gardoni, F. ; Cimino, M. ; Pastorino, L. ; Cattabeni, F. ; Di Luca, M.

    Oxford, UK : Blackwell Science Ltd
    Published 1999
    Staff View
    ISSN:
    1460-9568
    Source:
    Blackwell Publishing Journal Backfiles 1879-2005
    Topics:
    Medicine
    Notes:
    The calcium-calmodulin-dependent protein kinase II (CaMKII) subserves activity-dependent plasticity in central neurons. To examine in vivo the implication of CaMKII activity in synaptic plasticity, we used an animal model characterized by developmentally induced targeted neuronal ablation within the cortex and the hippocampus, and showing, at presynaptic level, molecular alterations leading to facilitation of glutamate release in hippocampal synapses (methylazoxymethanol-treated rats, MAM-rats). We report here that at the postsynaptic side, the activity of CaMKII is markedly decreased in MAM-rats when compared to controls, although the concentration of the enzyme in Post Synaptic Density (PSD) is not altered. This effect is confined to PSD-associated CaMKII, as enzyme activity tested in the soluble fraction is unchanged in MAM-rats. In addition, the decreased activity is not due to inhibition by autophosphorylation in specific sites within the calmodulin-binding domain, as preincubation with purified phosphatases 1 and 2A failed to restore CaMKII activity in PSD of MAM-rats. The CaMKII-dependent phosphorylation of NR2A/B subunits of NMDA receptor is lower in MAM-rats when compared to controls (51.77 ± 7.39% of controls level), as revealed in back-phosphorylation experiments. In addition, a treatment able to restore long-term potentiation (LTP) in hippocampal slices from MAM-rats, e.g. exposure to d-serine, is able to restore CaMKII activity to the control value.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1046/j.1460-9568.1999.00414.x

    Articles: DFG German National Licenses
  7. 7
    Staff View
    ISSN:
    1460-9568
    Source:
    Blackwell Publishing Journal Backfiles 1879-2005
    Topics:
    Medicine
    Notes:
    We have tested whether different agonists of metabotropic glutamate receptors could induce translocation of selective protein kinase C isozymes in nerve terminals. In rat cortical synaptosomes 1S,3R-1-aminocyclopentane-1,3-dicarboxylic acid (1S,3R-ACPD; 100 μm) induced an increase in translocation to 124.6 ± 5.7% of basal unstimulated conditions of the Ca++-independent protein kinase Cε, but not of the Ca++-dependent isozyme β. This effect was counteracted by 1-aminoindan-1,5-dicarboxylic acid (100 μm), an antagonist of metabotropic glutamate receptor 1. On the other hand, (+)-α-methyl-4-carboxyphenylglycine [(+)-MCPG], an antagonist of metabotropic glutamate receptors group I and II, did not antagonize the effect of 1S,3R-ACPD, and per se induced a translocation of protein kinase Cε of 164 ± 17.7% of basal unstimulated conditions. Because the (+)-MCPG induction of protein kinase Cε translocation was not antagonized by 1-aminoindan-1,5-dicarboxylic acid, it is suggested that 1S,3R-ACPD and (+)-MCPG activate this signal transduction pathway through distinct membrane receptors. Indeed (2-[2′′-carboxy-3′-phenylcyclopropyl]glycine)-13 (300 n m), a new compound known to antagonize metabotropic glutamate receptors coupled to phospholipase D, was able to antagonize protein kinase Cε translocation induced by (+)-MCPG. Moreover (+)-MCPG directly induced phospholipase D activity, measured as [3H]phosphoethanol production in cortical synaptosomes. These data suggest that in cortical nerve terminals (i) distinct metabotropic glutamate receptors, coupled to different signal transduction pathways, are present, (ii) (+)-MCPG is able to induce protein kinase Cε translocation, and that (iii) a metabotropic glutamate receptor associated to phospholipase D might influence translocation of protein kinase C in a calcium-independent manner.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1046/j.1460-9568.2000.00023.x

    Articles: DFG German National Licenses
  8. 8
    Pastorino, L. ; Sun, A. ; Lu, P.-J. ; Zhou, X. Z. ; Balastik, M. ; Finn, G. ; Wulf, G. ; Lim, J. ; Li, S.-H. ; Li, X. ; Xia, W. ; Nicholson, L. K. ; Lu, K. P.

    [s.l.] : Nature Publishing Group
    Published 2007
    Staff View
    ISSN:
    1476-4687
    Source:
    Nature Archives 1869 - 2009
    Topics:
    Biology
    Chemistry and Pharmacology
    Medicine
    Natural Sciences in General
    Physics
    Notes:
    [Auszug] Nature 440, 528–534 (2006) During editing to meet Nature’s limits on length, we removed a reference to an earlier paper1 reporting that the prolyl isomerase Pin1 promotes production of Alzheimer’s ...
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1038/nature05606

    Articles: DFG German National Licenses