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2. Neuroexocytosis

Author

Benfenati, F., Valtorta, F., Capron, A., editor, Compans, R. W., editor, Cooper, M., editor, Koprowski, H., editor, McConnel, I., editor, Melchers, F., editor, Oldstone, M., editor, Olsnes, S., editor, Potter, M., editor, Saedler, H., editor, Vogt, P. K., editor, Wagner, H., editor, Wilson, I., editor, and Montecucco, Cesare, editor

Published
1995
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6. P.353 Peripheral melatonin levels in bipolar disorder: preliminary results of a cross-sectional analysis

Author

Manchia, M., primary, Dall'Acqua, S., additional, Squassina, A., additional, Pisanu, C., additional, Congiu, D., additional, Garzilli, M., additional, Guiso, B., additional, Suprani, F., additional, Paribello, P., additional, Pulcinelli, V., additional, Iaselli, M.N., additional, Pinna, F., additional, Valtorta, F., additional, Carpiniello, B., additional, and Comai, S., additional

Published
2020
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9. Role of palmitoylethanolamide (PEA) in depression: Translational evidence: Special Section on 'Translational and Neuroscience Studies in Affective Disorders'. Section Editor, Maria Nobile MD, PhD. This Section of JAD focuses on the relevance of translational and neuroscience studies in providing a better understanding of the neural basis of affective disorders. The main aim is to briefly summaries relevant research findings in clinical neuroscience with particular regards to specific innovative topics in mood and anxiety disorders

Author

De Gregorio, D., Manchia, M., Carpiniello, B., Valtorta, F., Nobile, M., Gobbi, G., Comai, S., De Gregorio, Danilo, Manchia, Mirko, Carpiniello, Bernardo, Valtorta, Flavia, Nobile, Maria, Gobbi, Gabriella, and Comai, Stefano

Subjects
Peroxisome proliferator-activated receptor-alpha, Dietary supplement, Clinical Psychology, Depression, Psychiatry and Mental Health, Dietary supplements, Palmitoylethanolamide, Endocannabinoids, Endocannabinoid
Abstract

Background: Antidepressants have a low rate of response paired with a delayed onset of action. Translational studies are thus seeking for novel targets for antidepressant drug development. Preclinical evidence has demonstrated that the endocannabinoid system plays an important role in mood and stress response, even if drugs targeting this system have not yet become available for clinical use. The dietary supplement N-Palmitoylethanolamide (PEA) is a fatty acid amide belonging to the endocannabinoid system with potential antidepressant properties. Methods: We performed a bibliographic search to review current knowledge on the potential antidepressant effects of PEA and its underlying mechanism of action. Results: PEA targets not only the peroxisome proliferator-activated receptor-alpha (PPAR-α), but also the endocannabinoid system, binding the G-protein-coupled receptor 55, a non-CB1/CB2 cannabinoid receptor, and also the CB1/CB2 receptors, although with a weak affinity. Preclinical studies have shown antidepressant activity of PEA in animal paradigms of depression and of depression associated with neuropathic pain and traumatic brain injury. In a translational perspective, PEA is increased in stress conditions, and a randomized, double-blind study in depressed patients indicated a fast-antidepressant action of PEA when associated with citalopram. Limitations: There are still limited preclinical and clinical studies investigating the effect of PEA upon the endocannabinoid system and its potential as antidepressant. Conclusions: PEA has potential antidepressant effects alone or in combinations with other classes of antidepressants. Future studies in depressed patients are needed to confirm the mood-modulating properties of PEA and its role as a biomarker of depression.

Published
2019

10. Abstract

Author

Andries, L. J., Sys, S. U., Meulemans, A. L., Schuurkes, J. A. J., Vanheel, B., Van de Voorde, J., De Smet, P., Li, J., Van Driessche, W., Flamion, B., Foulon, S., Abramow, M., Calders, P., Eechaute, W., Lacroix, E., Weyne, I., Hoeben, D., Burvenich, C., Fransen, P., Andries, L. J., Van Bedaf, D., Demolder, M., Sys, S. U., Ouedraogo, R., Lebrun, P., Herchuelz, A., Antoine, M. -H., Vandenput, S., Votion, D., Anciaux, N., Duvivier, D. H., Art, T., Lekeux, P., Votion, D., Ghafir, Y., Vandenput, S., Art, T., Lekeux, P., Geurts, M., Hermans, E., Maloteaux, J. -M., Perrad, B., Noel, B., Lagache, F., Bister, J. L., Paquay, R., Bister, J. L., Derycke, G., Vandermeir, M. A., Paquay, R., de Brouwer, S., Porret, C. -A., Stergiopulos, N., Meister, J. -J., Verbeke, M., Van de Voorde, J., Lameire, N., De Clerck, N. M., De Schuytter, J., Tytgato, J., Buyse, G., Eggermont, J., Droogmans, G., Nilius, B., Daenens, P., Salomone, S., Feron, O., Dessy, C., Morel, N., Godfraind, T., Aloisi, A. M., Sacerdote, P., Lodi, L., Carli, G., Carobi, C., Garinei, G., Miniaci, U. C., Scotto, P., Sabatino, M., Sardo, P., Iurato, L., La Grutta, V., Bagni, M. A., Cecchi, G., Cecchini, E., Colomo, F., Garzella, P., Bottinelli, R., Harridge, S. D. H., Canepari, M., Reggiani, C., Reggiani, Saltin, Bambagioni, D., Fanò, G., Menchetti, G,, Danieli-Betto, P., Esposito, A., Betto, R., Megighian, A., Midrio, M., Betto, D. Danieli, Esposito, A., Megighian, A., Midrio, M., Orizio, C., Liberati, D., Locatelli, C., De Grandis, D., Veicsteinas, A., Angoli, D., Delia, D., Wanke, E., Bramucci, M., Miano, A., Quassinti, L., Maccari, E., Murri, O., Amici, D., Cibelli, G., Jüngling, S., Schoch, S., Gerdest, H. H., Thiel, G., Demori, I., Bottazzi, C., Voci, A., Fugassa, E., Barreca, A., Minuto, F., Gallo, G., Fulle, S., Belia, S., Menchetti, G., Cacchio, M., Fanò, G., Gastaldi, G., Laforenza, U., Ferrari, G., Rindi, G., Doni, M. G., Padoin, E., Residori, O., Cesaro, M., Toma, L., Rubini, A., Mutinelli, F, Paulesu, L., Romagnolie, R., Cintorino, M., Pippia, P., Meloni, M. A., Sciola, L., Spano, A., Cogoli-Greuter, M., Cogoli, A., Sardini, A., Mintenig, G. M., Valverde, M. A., Sepùlveda, F. V., Gill, D. R., Hyde, S. C., Higgins, C. F., McNaughton, P. A., Spena, A., Arcuri, M. T., Bonofiglio, S., Chimenti, R., Covello, C., De Cicco, T., Mazzulla, S., Martino, G., Tottene, A., Moretti, A., Pietrobon, D., Baccari, M. C., Calamai, F., Staderini, G., Cova, E., Marelli, R., Sommi, P., Ventura, U., Lombardi, A. M., Fabris, R., Pagano, C., Federspil, G., Vettor, R., Mancinelli, R., Tonali, P., Servidei, S., Romani, R., Tringali, A., Azzena, G. B., Mulè, F., Serio, R., Postorino, A., Pagano, C., Rizzato, M., Granzotto, M., Lombardi, A. M., Fabris, R., Vettor, R., Federspil, G., Sommi, P., Ricci, V., Romano, M., Ivey, K. J., Ventura, U., Vacca, G., Papillo, B., Mary, D. A. S. G., Battaglia, A., Grossini, E., Vacca, G., Papillo, B., Battaglia, A., Grossini, E., Accili, E. A., Redaelli, G., DiFrancesco, D., Antoniotti, S., Distasi, C., Lovisolo, D., Munaron, L., Bertaso, F., Assandri, R., Mazzanti, M., Bianchi, L., Arcangeli, A., Faravelli, L., Becchetti, A., Coronello, M., Mini, E., Francini, F., Olivotto, M., Wanke, E., Bigiani, A., Kim, D. -J., Roper, S. D., Carabelli, V., Lovallo, M., Magnelli, V., Zucker, H., Carbone, E., D’Angelo, E., Rossi, P., De Filippi, G., Taglietti, V., Faravelli, L., Bianchi, L., Arcangeli, A., Francini, F., Olivotto, M., Wanke, E., Francini, F., Bencini, C., Squecco, R., Guatteo, E., Bacci, A., Franceschetti, S., Avanzini, G., Wanke, E., Magnelli, V., Carbone, E., Mazzanti, M., Assandri, R., Ferroni, A., DiFrancesco, D., Navangione, A., Vellani, V., Rispoli, G., Peres, A., Centinaio, E., Giovannardi, S., Russo, G., Marcotti, W., Prigioni, I., Trequattrini, C., Harper, A. A., Petris, A., Franciolini, F., Zaza, A., Micheletti, M., Brioschi, A., Antonutto, G., Capelli, C., Girardis, M., Zamparo, P., di Prampero, P. E., Antonutto, G., Girardis, M., Tuniz, D., di Prampero, P. E., Filippi, G. M., Troiani, D., Grassi, B., Poole, D. C., Richardson, R. S., Knight, D. R., Erickson, B. K., Wagner, P. D., Aimi, B., Stilli, D., Gallo, P., Sgoifo, A., Lagrasta, C., Olivetti, G., Reali, N., Casti, A., Musso, E., Alloatti, G., Penna, C., Gallo, M. P., Levi, R. C., Fenoglio, I., Appendino, G., Gallo, P., Sgoifo, A., Medici, D., Aimi, B., Manghi, M., Stilli, D., Musso, E., Sgoifo, A., Pasini, E., Gallo, P., Aimi, B., Stilli, D., Ceconi, C., Musso, E., Baldissera, F., Cavallari, P., Locatelli, M., Bartesaghi, R., Gessi, T., Benfenati, F., Valtorta, F., Onofri, F., Poo, M., Greengard, P., Biagini, G., Sala, D., Viani§, P., Kozlov, A. V., Zini, I., Bravin, M., Tempia, F., Strata, P., Brescia, G., Di Benedetto, C., Corsi, P., Cangiano, G., Buttiglione, M., Ambrosini, M., Gennarini, G., Casadio, A., Levi, R. C., Montarolo, P. G., Cesare, P., Stoughton, R., McNaughton, P. A., D’Arcangelo, G., Dodt, H. U., Brancati, A., Zieglgänsberger, W., Errico, P., Ferraresi, A., Barmack, N. H., Pettorossi, V. E., Gasparini, S., D’Ambrosio, R., Janigro, D., DiFrancesco, D., Gritti, I., Marintti, M., Calcaterra, R., Freddi, R., Mancia, M., Imeri, I., Bianchi, S., Mancia, M., Lui, F., Gregory, K. M., Blanks, R. H. I., Giolli, R. A., Benassi, C., Corazza, R., Magherini, P. C., Bardoni, R., Belluzzi, O., Mancinelli, R., Manni, E., Azzena, G. B., Tringali, A., Romani, R., Diana, M., Fratta, W., Manzoni, D., Andre, P., Pompeiano, O., Mazzocchio, R., Rossi, A., Melis, F., Kitura, A., Caria, M. A., Asanuma, H., Melone, M, De Biasi, S, Minelli, A, Conti, F, Minelli, A, Karschin, C, DeBiasi, S, Brecha, N C, Conti, F, Monda, M., Amaro, S., Sullo, A., De Luca, B., Monda, M., Amaro, S., Sullo, A., De Luca, B., Pantò, M. R., Cicirata, F., Parenti, R., Serapide, M. F., Parenti, R., Wassef, M., Cicirata, F., Podda, M. V., Solinas, A., Chessa, G., Deriu, F., Mameli, O., Tolu, E., Pompeiano, O., Andre, P., Manzoni, D., Porro, C. A., Francescato, M. P., Cettolo, V., Diamond, M. E., Baraldi, P., Bazzocchi, M., Rivosecchi, R., Konnerth, A., Rossi, M. L., Martini, M., Pelucchi, B., Fesce, R., Santarelli, L., Schacher, S., Montarolo, P. G., Santarelli, R., Grassi, C., Valente, A., Nisticò, S., Bagetta, G., Azzena, G. B., Scuri, Rossana, Garcia-Gil, Mercedes, Mozzachiodi, Riccardo, Brunelli, Marcello, Stefani, G., Onofri, F., Vaccaro, P., Nielander, H. B., Benfenati, F., Tancredi, V., D’Antuono, M., Siniscalchi, A., Brancati, A., Avoli, M., Vellani, V., Navangione, A., Rispoli, G., Verzè, L., Buffo, A., Rossi, F., Oestreicher, A. B., Gispen, W. H., Strata, P., Zamboni, G., Amici, R., Jones, C. A., Perez, E., Domeniconi, R., Parmeggiani, P. L., Zoli, Michele, Le Novàre, Nicolas, Changeux, Jean -Pierre, Lafortuna, C. L., Reinach, E., Saibene, F., Scotto, P., Zocchi, L., Agostoni, E., and Cremaschi, D.

Published
1996
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13. Phosphorylation of synapsin I by cdk5 sets the ratio between the resting and recycling pools of synaptic vesicles at hippocampal synapses

Author

Fassio, A., Verstegen, A. J., Erica Tagliatti, Lignani, G., Marte, Antonella, Stolero, T., Orenbuch, A., Corradi, A., Valtorta, F., Gitler, D., Onofri, F., Benfenati, F., A. M. G., Verstegen, E., Tagliatti, G., Lignani, A., Marte, T., Stolero, A., Orenbuch, A., Corradi, Valtorta, Flavia, D., Gitler, F., Onofri, A., Fassio, and F., Benfenati

Subjects
synapse, phosphorylation, neuron
Abstract

Cyclin-dependent kinase-5 (Cdk5) was reported to downscale neurotransmission by sequestering synaptic vesicles (SVs) in the release-reluctant resting pool, but the molecular targets mediating this activity remain unknown. Synapsin I (SynI), a major SV phosphoprotein involved in the regulation of SV trafficking and neurotransmitter release, is one of the presynaptic substrates of Cdk5, which phosphorylates it in its C-terminal region at Ser549 (site 6) and Ser551 (site 7). Here we demonstrate that Cdk5 phosphorylation of SynI fine tunes the recruitment of SVs to the active recycling pool and contributes to the Cdk5-mediated homeostatic responses. Phosphorylation of SynI by Cdk5 is physiologically regulated and enhances its binding to F-actin. The effects of Cdk5 inhibition on the size and depletion kinetics of the recycling pool as well as on SV distribution within the nerve terminal were virtually abolished in SynI knockout (KO) neurons or in KO neurons expressing the dephosphomimetic SynI mutants at sites 6,7 or site 7 only. The observation that the single site-7 mutant phenocopies the effects of the deletion of SynI identifies this site as the central switch in mediating the synaptic effects of Cdk5 and demonstrates that SynI is necessary and sufficient for achieving the effects of the kinase on SV trafficking. The phosphorylation state of SynI by Cdk5 at site-7 was regulated during chronic modification of neuronal activity and was an essential downstream effector for the Cdk5-mediated homeostatic scaling.

Published
2014

15. Epidermal growth factor-mediated inhibition of neurotransmitter glutamate release from rat forebrain synaptosomes

Author

Barrie, A., Evelina Chieregatti, Miloso, M., Benfenati, F., Valtorta, F., A., Barrie, E., Chieregatti, M. R., Miloso, F., Benfenati, Valtorta, Flavia, Barrie, A, Chieregatti, E, Miloso, M, Benfenati, F, and Valtorta, F

Subjects
Male, Epidermal Growth Factor, Epidermal growth factor, glutamate, rat forebrain synaptosomes, Glutamic Acid, Receptor Protein-Tyrosine Kinases, Rats, Rats, Sprague-Dawley, Prosencephalon, Animals, Insulin, Calcium, 4-Aminopyridine, Insulin-Like Growth Factor I, Phosphorylation, Phosphotyrosine, Synaptosomes
Abstract

We investigated the possibility that receptor tyrosine kinases are involved in modulating neurotransmitter release from isolated nerve terminals. We examined the effects of epidermal growth factor on the release of neurotransmitter glutamate evoked from rat forebrain synaptosomes by KCI and 4-aminopyridine. We detected a significant inhibition of the Ca2+-dependent component of release. This effect appears to be mediated by a reduction in the depolarization-evoked increase in cytosolic free calcium levels, in the absence of significant effects on the plasma membrane potential. On depolarization, a Ca2+-dependent increase was observed in the phosphotyrosine content of bands at molecular masses of approximately 107 and approximately 40 kDa. The addition of epidermal growth factor before depolarization induced a significant phosphorylation of the growth factor receptor in the absence of detectable changes in the phosphotyrosine pattern of total synaptosomal proteins, suggesting that phosphorylation of a minor protein is responsible for the epidermal growth factor-mediated inhibition of glutamate release.

Published
1996

16. Synapsins and neuroexocytosis: recent views from functional studies on synapsin null mutant mice

Author

Baldelli, P., Anna Fassio, Corradi, A., Cremona, O., Valtorta, F., Benfenati, F., Baldelli, P, Fassio, A, Corradi, A, Cremona, Ottavio, Valtorta, Flavia, and Benfenati, F.

Subjects
Central Nervous System, Mice, Knockout, Neurotransmitter Agents, TRANSMISSION, Presynaptic Terminals, SQUID GIANT SYNAPSE, IMPAIRMENT, Synapsins, Synaptic Transmission, DEFICIENT MICE, Endocytosis, Exocytosis, VESICLES, RAB3 EFFECTOR PROTEIN, Mice, Protein Transport, PROTEIN-KINASE-II, NEUROTRANSMITTER RELEASE, NERVE-TERMINALS, PLASTICITY, Animals, Humans, Synaptic Vesicles
Abstract

This review will be focused on the functional studies which have outlined the role played by synapsins in the regulation of neurotransmitter release.

Published
2005

19. Phosphorylation of Synapsin I by Cyclin-Dependent Kinase-5 Sets the Ratio between the Resting and Recycling Pools of Synaptic Vesicles at Hippocampal Synapses

Author

Verstegen, A. M. J., primary, Tagliatti, E., additional, Lignani, G., additional, Marte, A., additional, Stolero, T., additional, Atias, M., additional, Corradi, A., additional, Valtorta, F., additional, Gitler, D., additional, Onofri, F., additional, Fassio, A., additional, and Benfenati, F., additional

Published
2014
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21. Functional morphology of the nerve terminal at the frog neuromuscular junction: recent insights using immunocytochemistry

Author

Torri Tarelli, F, Valtorta, F, VILLA, ANTONELLO, Meldolesi, J., Torri Tarelli, F, Valtorta, Flavia, Villa, A, Meldolesi, Jacopo, Sten-Magnus Aquilonius, Per-Göran Gillberg, Valtorta, F, and Meldolesi, J

Subjects
Nerve Ending, Microscopy, Electron, Ranidae, Animal, Nerve Tissue Protein, Neuromuscular Junction, Synapsins, Membrane Protein, Electric Stimulation
Abstract

This chapter describes the functional morphology of the nerve terminal in a frog neuromuscular junction by using immunocytochemistry. Acetylcholine (ACh) is secreted from motor nerve terminals by two means: by release of multimolecular packages or quanta and by molecular leakage across the presynaptic membrane. The spontaneous or neurally evoked release of quanta generates the discrete, transient miniature end-plate potentials and the endplate potentials that mediate neuromuscular transmission. As far as molecular leakage is concerned, this process can be the predominant way in which neurotransmitter is released under resting conditions. The identification within the nerve terminals of a rich population of synaptic vesicles filled with neurotransmitter lead to the interpretation that synaptic vesicles are the anatomical correlates of quanta. The most widely accepted hypothesis to explain the quantal nature of transmitter release holds that the molecular packets are preformed in the nerve terminal, each quantum being confined within one synaptic vesicle and released by exocytosis. The study of synapsin I and of the regulation of its state of phosphorylation at the neuromuscular junction may provide important information on its role in synaptic function

Published
1990

27. Neuroexocytosis

Author

Benfenati, Fabio and Valtorta, F.

Published
1995

38. The synapsins and the regulation of synaptic function

Author

Bähler, M, Benfenati, Fabio, Valtorta, F, Greengard, P., Bã¤hler, Martin, Benfenati, Fabio, Valtorta, Flavia, and Greengard, Paul

Subjects
Neuropeptide, Biochemistry, Genetics and Molecular Biology (all), Synaptic Vesicle, Animal, Phosphoprotein, Medicine (all), Models, Neurological, Nerve Tissue Protein, Synapse, Synapsin
Abstract

Synapsins I and II are a family of synaptic vesicle‐associated phosphoproteins involved in the short‐term regulation of neurotransmitter release. In this review, we discuss a working model for the molecular mechanisms by which the synapsins act. We propose that synapsin I links synaptic vesicles to actin filaments in the presynaptic nerve terminal and that these interactions are modulated by the reversible phosphorylation of synapsin I through various signal transduction pathways. The high degree of homology between the synapsins suggests that some of the functional properties of synapsin I are also shared by synapsin II. Copyright © 1990 Cambridge University Press

Published
1990

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