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4. Strategies for preventing group B streptococcal infections in newborns: A nation-wide survey of Italian policies

Author

Tzialla, C, berardi, A, farina, C, clerici, P, borghesi, A, viora, E, scollo, P, stronati, M, Task Force for group B streptococcal infections for the Italian Society of Neonatology including Stival, G, barbaglia, Ma, guala, A, giunta, E, parola, L, grossignani, Mr, perri, P, tubaldi, L, alletto, G, daidone, S, flacco, V, dani, C, sterpa, A, rapisardi, G, elicio, Mr, faldella, G, capretti, Mg, messner, H, bandiera, M, achille, C, azzali, A, montrasio, G, mariani, S, galvagno, G, giacosa, E, de Angelis, F, spandrio, M, serra, A, garofalo, F, perona, A, porcelli, F, ferrero, F, De Franco, S, paollilo, P, picone, S, besana, R, varisco, T, farina, M, memo, L, nicolini, G, lietti, D, Di Chiara, G, rottoli, A, Bonabitacola, T, Cortis, E, Neri, E, Martinelli, S, Ilardi, L, Rondanini, Gf, Calzi, P, Gatta, A, Quntadamo, Pa, Ivaldi, M, Terenzani, L, Di Lascio, N, Travaglio, Md, Vetrano, G, Furcolo, G, Vitacco, V, Intini, C, Frigerio, M, Stroppiana, P, Policicchio, G, Mesirca, P, Gianino, P, Audenio, E, Paludetto, R, Raimondi, F, Pugliese, A, Valentino, L, Nosari, N, Marchesano, G, Chirico, G, Bellù, R, Menchini, M, Poletti, A, E T, Vacchiano, Pinto, L, E D, Perri, Coppola, R, Perini, R, Vetrella, A, De Luca, G, Lista, G, Cavigioli, F, Bettinelli, A, Massironi, E, Franco, C, Bernardo, L, Poli, S, Palladini, M, Tota, V, Spadavecchia, F, Zuccotti, Gv, Pogliani, L, Bracaglia, G, Mancini, Al, Zocco, F, Iozzia, G, Auriemma, A, Teani, M, Mangilli, G, Tempra, Am, Di Terlizi, L, Bottino, R, Salvi, C, Fortunato, V, Musaico, R, Gargantini, G, Carrera, G, Magaldi, R, Taurino, L, D'Onofrio, Am, Buffone, E, Tempera, A, Agosti, M, Garzia, P, Mosca, F, Pugni, L, Tagliabue, P, Colombo, C, Demi, M, Picco, G, Carlucci, A, Zorzi, G, Padula, D, Cardone, Ml, Buonocore, G, Muraca, Mc, Boldrini, A, Ciantelli, M, Lanari, M, Serra, L, Felici, L, Banderalli, G, Brambilla, C, Dall'Agnola, A, Viviani, E, Zonca, Mc, Licardi, G, Chiara, A, Ancora, G, Papa, I, Gancia, P, Pomero, G, Deloglu, A, Villani, P, Mussini, P, Canidio, E, Migliavacca, D, Di Fabio, S, Cipollone, I, Biasucci, G, Rubbi, P, Piepoli, M, Guastaferro, N, Infriccioli, F, Bertino, E, Perathoner, C, Parmigiani, S, Suriano, G, Ianniello, C, Biasini, A, Azzalli, M, Timpani, G, Barresi, S, Caoci, G, Ciccotti, R, De Curtis, M, Natale, F, Finocchi, M, Haass, C, Milillo, F, Lucieri, S, Guercio, E, Canepa, Sa, Scozia, G, Antonucci, R, Limongelli, O, Macciò, S, Mongelli, F, Colonna, F, Dragovic, D, Calipa, Mt, Cohen, A, Moresco, L, Italian Society of Obstetricians and Gynecologists including La Spina, R, Ruggeri, R, Luehwink, A, Brattoli, M, Fedi, A, Lacchi, L, Ettore, G, Pappalardo, E, Conoscenti, G, Zeni, B, Spellecchia, D, Favretti, L, Spagna, L, Zaglio, S, Bresciani, D, Bandini, A, Mancini, R, Mustoni, P, Dodero, D, Grimaldi, M, Di Mario, M, Migliorini, P, Kemeny, A, Anastasio, Ps, Riccardi, T, Maggino, T, Cerri, G, Puggina, P, Marconi, Am, Morgia, S, Bellia, G, D'Anna, Mr, Catania, M, Bacchi Modena, A, Franchi, L, Calonaci, N, Schettini, S, Paradiso, R, Saccucci, P, Ioppi, M, Zorzi, M, Stellin, G, Patacchiola, F, Carrata, L, Bassini, D, San Marco, L, Todros, T, Tibadi, C, Liborio, M, Italian Association of Clinical Microbiologists including Laricchia, R, Tauro, L, Ferrara, F, Nuara, C, Ghiraldi, E, Molinari, F, Comessatti, A, Rocchetti, A, Di Matteo, L, Miconi, V, Calvi, P, Pernigotti, A, Fabozzi, F, Micca, G, Monticone, G, Sarti, M, Da Rin, G, Zoppelletto, M, Modolo, E, Landini, Mp, Furlini, G, Galluppi, E, Pagani, E, Aschbacher, R, Innocenti, P, Bresolin, N, Raggi, Me, Bonfanti, C, De Francesco, M, Santer, P, Griessmaier, A, De Francesco, D, Pirali, A, Prasciolu, C, Usai, F, Cuzzone, G, Scutellà, M, Tramacere, P, Fossati, D, Piaserico, G, Bordignon, G, Sciacca, A, Di Vincenzo, F, Imbriani, A, Melotti, D, Catanoso, G, Rivetti, I, Neri, G, Bruno, R, Bacelle, L, Sartore, P, Giana, G, Sala, E, Giraldi, C, Cavalcanti, P, Perugini, M, Perugini, A, Ginardi, C, Maritano, D, Ferrini, A, Bonettini, A, Avanzini, A, Gasperoni, S, Pieretti, B, Montanari, E, Carillo, C, Rossi, Mr, Laureti, A, Baldoni, Ml, Serra, D, Melioli, G, Bandettini, R, Oneto, F, Colla, R, Storchi Incerti, S, Lanzini, F, Pauri, P, Tili, E, Leone, Ra, Verdastro, G, Megha, M, Luzzaro, F, Conti, A, Busulini, L, Mirri, P, Diodati, R, Vettori, C, Pittalis, S, Anesi, A, Fiore, A, Goglia, L, Vitullo, E, Sinno, A, Platzgummer, S, Spitaler, C, Trabucchi, Mc, Besozzi, M, Cesana, E, Inghilleri, G, Grosso, S, D'Angelo, R, Fogato, E, Lavarda, F, Ortisi, G, Clementi, M, Cichero, P, Rumpianesi, F, Venturelli, C, Mortillaro, F, Daffara, S, Catania, Mr, Iula, D, Andreoni, S, Politi, A, Agostinelli, C, Paparella, C, Capozzi, D, Notaris, P, Bistoni, F, Mencacci, A, Valentini, M, Filippetti, A, Confalonieri, M, Novarese, O, Bonini, F, Salamone, D, Camporese, A, De Rosa, R, Casprini, P, Degl'Innocenti, R, Giordano, R, Allù, Mt, Zanella, D, Malandrino, M, Tronci, M, Valmarin, M, Leonetti, G, Falco, S, Meledandri, M, Ballardini, M, Spanò, A, Cava, Mc, Mascellino, Mt, Schinella, M, Gualdi, P, Casari, E, Scattolo, N, Motta, C, Perfetti, C, Bassano, M, Cera, G, Iafisco, P, Mura, I, Palmieri, A, Migliardi, M, Ferlini, M, Grandi, G, Giardini, F, Albano, F, Latino, M, Ferrero, Mp, Bellizia, L, Russolo, M, Russolo, S, Pesenti, A, Fasano, Ma, Previato, S, Radillo, O, Busetti, M, Ferrari, P, Siderini, V, Puzzolante, L, Scarparo, C, Arzese, A, Cappuccia, N, Lodolo, L, Delledonne, L, Gramoni, A, Maiolo, V, Gheller, A, Spadaro, S, Balzaretti, M, Tzialla, C., Berardi, A., Farina, C., Clerici, P., Borghesi, A., Viora, E., Scollo, P., Stronati, M., Stival, G., Barbaglia, M. A., Guala, A., Giunta, E., Parola, L., Grossignani, M. R., Perri, P., Tubaldi, L., Alletto, G., Daidone, S., Flacco, V., Dani, C., Sterpa, A., Rapisardi, G., Elicio, M. R., Faldella, G., Capretti, M. G., Messner, H., Bandiera, M., Achille, C., Azzali, A., Montrasio, G., Mariani, S., Galvagno, G., Giacosa, E., de Angelis, F., Spandrio, M., Serra, A., Garofalo, F., Perona, A., Porcelli, F., Ferrero, F., De Franco, S., Paollilo, P., Picone, S., Besana, R., Varisco, T., Farina, M., Memo, L., Nicolini, G., Lietti, D., Di Chiara, G., Rottoli, A., Bonabitacola, T., Cortis, E., Neri, E., Martinelli, S., Ilardi, L., Rondanini, G. F., Calzi, P., Gatta, A., Quntadamo, P. A., Ivaldi, M., Terenzani, L., Di Lascio, N., Travaglio, M. D., Vetrano, G., Furcolo, G., Vitacco, V., Intini, C., Frigerio, M., Stroppiana, P., Policicchio, G., Mesirca, P., Gianino, P., Audenio, E., Paludetto, R., Raimondi, F., Pugliese, A., Valentino, L., Nosari, N., Marchesano, G., Chirico, G., Bell(`u), R., Menchini, M., Poletti, A., Vacchiano, T., Pinto, L., Perri, D., Coppola, R., Perini, R., Vetrella, A., De Luca, G., Lista, G., Cavigioli, F., Bettinelli, A., Massironi, E., Franco, C., Bernardo, L., Poli, S., Palladini, M., Tota, V., Spadavecchia, F., Zuccotti, G. V., Pogliani, L., Bracaglia, G., Mancini, A. L., Zocco, F., Iozzia, G., Auriemma, A., Teani, M., Mangilli, G., Tempra, A. M., Di Terlizi, L., Bottino, R., Salvi, C., Fortunato, V., Musaico, R., Gargantini, G., Carrera, G., Magaldi, R., Taurino, L., D?onofrio, A. M., Buffone, E., Tempera, A., Agosti, M., Garzia, P., Mosca, F., Pugni, L., Tagliabue, P., Colombo, C., Demi, M., Picco, G., Carlucci, A., Zorzi, G., Padula, D., Cardone, M. L., Buonocore, G., Muraca, M. C., Boldrini, A., Ciantelli, M., Lanari, M., Serra, L., Felici, L., Banderalli, G., Brambilla, C., Dall?agnola, A., Viviani, E., Zonca, M. C., Licardi, G., Chiara, A., Ancora, G., Papa, I., Gancia, P., Pomero, G., Deloglu, A., Villani, P., Mussini, P., Canidio, E., Migliavacca, D., Di Fabio, S., Cipollone, I., Biasucci, G., Rubbi, P., Piepoli, M., Guastaferro, N., Infriccioli, F., Bertino, E., Perathoner, C., Parmigiani, S., Suriano, G., Ianniello, C., Biasini, A., Azzalli, M., Timpani, G., Barresi, S., Caoci, G., Ciccotti, R., De Curtis, M., Natale, F., Finocchi, M., Haass, C., Milillo, F., Lucieri, S., Guercio, E., Canepa, S. A., Scozia, G., Antonucci, R., Limongelli, O., Macci(`o), S., Mongelli, F., Colonna, F., Dragovic, D., Calipa, M. T., Cohen, A., Moresco, L., La Spina, R., Ruggeri, R., Luehwink, A., Brattoli, M., Fedi, A., Lacchi, L., Ettore, G., Pappalardo, E., Conoscenti, G., Zeni, B., Spellecchia, D., Favretti, L., Spagna, L., Zaglio, S., Bresciani, D., Bandini, A., Mancini, R., Mustoni, P., Dodero, D., Grimaldi, M., Di Mario, M., Migliorini, P., Kemeny, A., Anastasio, P. S., Riccardi, T., Maggino, T., Cerri, G., Puggina, P., Marconi, A. M., Morgia, S., Bellia, G., D?anna, M. R., Catania, M., Bacchi Modena, A., Franchi, L., Calonaci, N., Schettini, S., Paradiso, R., Saccucci, P., Ioppi, M., Zorzi, M., Stellin, G., Patacchiola, F., Carrata, L., Bassini, D., San Marco, L., Todros, T., Tibadi, C., Liborio, M., Laricchia, R., Tauro, L., Ferrara, F., Nuara, C., Ghiraldi, E., Molinari, F., Comessatti, A., Rocchetti, A., Di Matteo, L., Miconi, V., Calvi, P., Pernigotti, A., Fabozzi, F., Micca, G., Monticone, G., Sarti, M., Da Rin, G., Zoppelletto, M., Modolo, E., Landini, M. P., Furlini, G., Galluppi, E., Pagani, E., Aschbacher, R., Innocenti, P., Bresolin, N., Raggi, M. E., Bonfanti, C., De Francesco, M., Santer, P., Griessmaier, A., De Francesco, D., Pirali, A., Prasciolu, C., Usai, F., Cuzzone, G., Scutell(`a), M., Tramacere, P., Fossati, D., Piaserico, G., Bordignon, G., Sciacca, A., Di Vincenzo, F., Imbriani, A., Melotti, D., Catanoso, G., Rivetti, I., Neri, G., Bruno, R., Bacelle, L., Sartore, P., Giana, G., Sala, E., Giraldi, C., Cavalcanti, P., Perugini, M., Perugini, A., Ginardi, C., Maritano, D., Ferrini, A., Bonettini, A., Avanzini, A., Gasperoni, S., Pieretti, B., Montanari, E., Carillo, C., Rossi, M. R., Laureti, A., Baldoni, M. L., Serra, D., Melioli, G., Bandettini, R., Oneto, F., Colla, R., Storchi Incerti, S., Lanzini, F., Pauri, P., Tili, E., Leone, R. A., Verdastro, G., Megha, M., Luzzaro, F., Conti, A., Busulini, L., Mirri, P., Diodati, R., Vettori, C., Pittalis, S., Anesi, A., Fiore, A., Goglia, L., Vitullo, E., Sinno, A., Platzgummer, S., Spitaler, C., Trabucchi, M. C., Besozzi, M., Cesana, E., Inghilleri, G., Grosso, S., D?angelo, R., Fogato, E., Lavarda, F., Ortisi, G., Clementi, M., Cichero, P., Rumpianesi, F., Venturelli, C., Mortillaro, F., Daffara, S., Catania, M. R., Iula, D., Andreoni, S., Politi, A., Agostinelli, C., Paparella, C., Capozzi, D., Notaris, P., Bistoni, F., Mencacci, A., Valentini, M., Filippetti, A., Confalonieri, M., Novarese, O., Bonini, F., Salamone, D., Camporese, A., De Rosa, R., Casprini, P., Degl?innocenti, R., Giordano, R., All(`u), M. T., Zanella, D., Malandrino, M., Tronci, M., Valmarin, M., Leonetti, G., Falco, S., Meledandri, M., Ballardini, M., Span(`o), A., Cava, M. C., Mascellino, M. T., Schinella, M., Gualdi, P., Casari, E., Scattolo, N., Motta, C., Perfetti, C., Bassano, M., Cera, G., Iafisco, P., Mura, I., Palmieri, A., Migliardi, M., Ferlini, M., Grandi, G., Giardini, F., Albano, F., Latino, M., Ferrero, M. P., Bellizia, L., Russolo, M., Russolo, S., Pesenti, A., Fasano, M. A., Previato, S., Radillo, O., Busetti, M., Ferrari, P., Siderini, V., Puzzolante, L., Scarparo, C., Arzese, A., Cappuccia, N., Lodolo, L., Delledonne, L., Gramoni, A., Maiolo, V., Gheller, A., Spadaro, S., Balzaretti, M., Tzialla, Chryssoula, Berardi, Alberto, Farina, Claudio, Clerici, Pierangelo, Borghesi, Alessandro, Viora, Elsa, Scollo, Paolo, Stronati, Mauro, [.., Lanari, Marcello, Faldella, Giacomo, and ]

Subjects
Male, Pediatrics, Group B, 0302 clinical medicine, Neonate, Pregnancy, Surveys and Questionnaires, Prevalence, Mass Screening, Blood culture, 030212 general & internal medicine, Antibiotic prophylaxis, Survey, GBS, Group B streptococcus, Infection, Newborn infant, Adult, Antibiotic Prophylaxis, Female, Health Surveys, Humans, Infant, Newborn, Italy, Neonatal Screening, Pregnancy Complications, Infectious, Prenatal Care, Primary Prevention, Risk Assessment, Streptococcal Infections, Streptococcus agalactiae, reproductive and urinary physiology, Group B streptococcu, medicine.diagnostic_test, lcsh:RJ1-570, Infectious, Perinatology and Child Health, Pediatrics, Perinatology and Child Health, medicine.medical_specialty, Antibiotic sensitivity, Group B Streptococcal Infection, Prenatal care, 03 medical and health sciences, 030225 pediatrics, medicine, Intensive care medicine, Mass screening, business.industry, Public health, Infant, lcsh:Pediatrics, Newborn, Pregnancy Complications, business
Abstract

Background There are no Italian data regarding the strategies for preventing neonatal group B streptococcal (GBS) infection. We conducted a national survey in order to explore obstetrical, neonatal and microbiological practices for the GBS prevention. Methods Three distinct questionnaires were sent to obstetricians, neonatologists and microbiologists. Questionnaires included data on prenatal GBS screening, maternal risk factors, intrapartum antibiotic prophylaxis, microbiological information concerning specimen processing and GBS antimicrobial susceptibility. Results All respondent obstetrical units used the culture-based screening approach to identify women who should receive intrapartum antibiotic prophylaxis, and more than half of the microbiological laboratories (58%) reported using specimen processing consistent with CDC guidelines. Most neonatal units (89 out of 107, 82%) reported using protocols for preventing GBS early-onset sepsis consistent with CDC guidelines. Conclusions The screening-based strategy is largely prevalent in Italy, and most protocols for preventing GBS early-onset sepsis are consistent with CDC guidelines. However, we found discrepancies in practices among centers that may reflect the lack of Italian guidelines issued by public health organizations.

Published
2017

11. Comparative actions of progesterone, medroxyprogesterone acetate, drospirenone and nestorone on breast cancer cell migration and invasion.

Author

Fu XD, Giretti MS, Goglia L, Flamini MI, Sanchez AM, Baldacci C, Garibaldi S, Sitruk-Ware R, Genazzani AR, Simoncini T, Fu, Xiao-Dong, Giretti, Maria Silvia, Goglia, Lorenzo, Flamini, Marina Ines, Sanchez, Angel Matias, Baldacci, Chiara, Garibaldi, Silvia, Sitruk-Ware, Regine, Genazzani, Andrea Riccardo, and Simoncini, Tommaso

Abstract

Background: Limited information is available on the effects of progestins on breast cancer progression and metastasis. Cell migration and invasion are central for these processes, and require dynamic cytoskeletal and cell membrane rearrangements for cell motility to be enacted.Methods: We investigated the effects of progesterone (P), medroxyprogesterone acetate (MPA), drospirenone (DRSP) and nestorone (NES) alone or with 17beta-estradiol (E2) on T47-D breast cancer cell migration and invasion and we linked some of these actions to the regulation of the actin-regulatory protein, moesin and to cytoskeletal remodeling.Results: Breast cancer cell horizontal migration and invasion of three-dimensional matrices are enhanced by all the progestins, but differences are found in terms of potency, with MPA being the most effective and DRSP being the least. This is related to the differential ability of the progestins to activate the actin-binding protein moesin, leading to distinct effects on actin cytoskeleton remodeling and on the formation of cell membrane structures that mediate cell movement. E2 also induces actin remodeling through moesin activation. However, the addition of some progestins partially offsets the action of estradiol on cell migration and invasion of breast cancer cells.Conclusion: These results imply that P, MPA, DRSP and NES alone or in combination with E2 enhance the ability of breast cancer cells to move in the surrounding environment. However, these progestins show different potencies and to some extent use distinct intracellular intermediates to drive moesin activation and actin remodeling. These findings support the concept that each progestin acts differently on breast cancer cells, which may have relevant clinical implications. [ABSTRACT FROM AUTHOR]

Published
2008
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13. I cattolici italiani tra pace e guerra: dall’inizio del secolo al Concilio Vaticano II

Author

MORO, Renato, GOGLIA L., MORO R., NUTI L., and Moro, Renato

Subjects
Cattolici italiani, Italian Catholicism, Peace, War, Pace, Guerra
Abstract

Il saggio esamina le posizioni dei cattolici italiani sul problema della guerra e della pace dal principio del Novecento al Concilio Vaticano I, analizzando riviste, giornali e libri. Risultato principale della ricerca è quello della rilevante influenza delle ideologie di nassa (quelle democratiche, internazionaliste e pacifiste come quelle nazionaliste e militariste) sul sistema di valori e di principi cattolico e lo iato tra impostazione dottrinale e scelte politiche. The essay examines the reactions of Italian Catholics to the problem of peace and war from the beginning of the 20th century to the Vatican Council through a wide analysis of journals, magazines and books. The main result of the research is the influence of mass ideologies (democratic, internationalist and pacifist ones as well as nationalist and militarist ones) on the Catholic system of values and principles, as well as the hiatus between doctrine and politics.

Published
2006

15. La guerra degli ascari

Author

VOLTERRA, ALESSANDRO, GOGLIA L., MORO R., NUTI L., and Volterra, Alessandro

Published
2006

17. Discovery and binding mode of small molecule inhibitors of the apo form of human TDO2.

Author

Lotz-Jenne C, Lange R, Cren S, Bourquin G, Goglia L, Kimmerlin T, Wicki M, Müller M, Artico N, Ackerknecht S, Pfaff P, Joesch C, and Mac Sweeney A

Subjects
Humans, Crystallography, X-Ray, Heme metabolism, Heme chemistry, Binding Sites, Catalytic Domain, Small Molecule Libraries chemistry, Small Molecule Libraries pharmacology, Models, Molecular, Drug Discovery, Indoleamine-Pyrrole 2,3,-Dioxygenase antagonists & inhibitors, Indoleamine-Pyrrole 2,3,-Dioxygenase chemistry, Indoleamine-Pyrrole 2,3,-Dioxygenase metabolism, Tryptophan Oxygenase antagonists & inhibitors, Tryptophan Oxygenase metabolism, Tryptophan Oxygenase chemistry, Enzyme Inhibitors chemistry, Enzyme Inhibitors pharmacology, Protein Binding
Abstract

Tryptophan-2,3-dioxygenase (TDO2) and indoleamine-2,3-dioxygenase (IDO1) are structurally distinct heme enzymes that catalyze the conversion of L-tryptophan to N-formyl-kynurenine, and play important roles in metabolism, inflammation, and tumor immune surveillance. The enzymes can adopt an inactive, heme-free (apo) state or an active, heme-containing (holo) state, with the balance between them varying dynamically according to biological conditions. Inhibitors of holo-TDO2 are known but, despite several advantages of the heme-free state as a drug target, no inhibitors of apo-TDO2 have been reported. We describe the discovery of the first apo-TDO2 binding inhibitors, to our knowledge, and their inhibition of cellular TDO2 activity at low nanomolar concentrations. The crystal structure of a potent, small molecule inhibitor bound to apo-TDO2 reveals its detailed binding interactions within the large, hydrophobic heme binding pocket of the active site., Competing Interests: Declarations Competing interests The authors declare no competing interests., (© 2024. The Author(s).)

Published
2024
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18. Vasodilatory effects of the selective GPER agonist G-1 is maximal in arteries of postmenopausal women.

Author

Arefin S, Simoncini T, Wieland R, Hammarqvist F, Spina S, Goglia L, and Kublickiene K

Subjects
Aged, Arteries metabolism, Endothelium, Vascular drug effects, Enzyme Inhibitors pharmacology, Female, Human Umbilical Vein Endothelial Cells drug effects, Human Umbilical Vein Endothelial Cells metabolism, Humans, In Vitro Techniques, Male, Middle Aged, Muscle, Smooth, Vascular drug effects, NG-Nitroarginine Methyl Ester pharmacology, Nitric Oxide metabolism, Norepinephrine, Phosphorylation, Pregnancy metabolism, Receptors, Estrogen metabolism, Receptors, G-Protein-Coupled metabolism, Signal Transduction, Vasoconstriction drug effects, Arteries drug effects, Estrogens metabolism, Nitric Oxide Synthase Type III metabolism, Postmenopause metabolism, Receptors, Estrogen antagonists & inhibitors, Receptors, G-Protein-Coupled antagonists & inhibitors, Selective Estrogen Receptor Modulators pharmacology, Vasodilation drug effects
Abstract

G-protein-coupled estrogen receptors (GPERs) have been proposed to mediate estrogen-mediated vasodilation. The presence of GPER-dependent vasodilation in human resistance-sized arteries (HRAs) or its signal transduction pathways have not been investigated. HRAs in subcutaneous fat tissues (biopsies from postmenopausal women (PMW), age-matched men (M) and pregnant women (PGW)) were mounted for in vitro isometric force recording. Vasodilation induced by G-1 (selective GPER-agonist, 3 μM) from HRAs pre-contracted with norepinephrine amounted to 40±5% in PMW, significantly larger than those obtained from M (20±5%) or PGW (20±5%). L-NAME (nitric oxide (NO) synthase inhibitor) abolished these relaxations in PGW, attenuated them in PMW and had no effect in M. Immunohistochemical analysis confirmed the presence of GPER in both smooth muscle and endothelial cells of HRA with maximum expression in PGW. In cultured human umbilical vein endothelial cells (HUVECs), G-1 increased NO-synthesis concentration-dependently through higher expressions of endothelial NO-synthase (eNOS) and through enhanced phosphorylation of eNOS on Ser(1177). In conclusion, GPER vasodilates human resistance arteries through various activating mechanisms of the eNOS-signaling pathway., (Copyright © 2014 Elsevier Ireland Ltd. All rights reserved.)

Published
2014
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19. Estrogen receptor-alpha promotes breast cancer cell motility and invasion via focal adhesion kinase and N-WASP.

Author

Sanchez AM, Flamini MI, Baldacci C, Goglia L, Genazzani AR, and Simoncini T

Subjects
Actin-Related Protein 2-3 Complex metabolism, Cell Line, Tumor, Cytoskeleton drug effects, Cytoskeleton enzymology, Enzyme Activation drug effects, Estrogens pharmacology, Female, Focal Adhesions drug effects, Focal Adhesions enzymology, GTP-Binding Protein alpha Subunits, Gi-Go metabolism, GTP-Binding Protein beta Subunits metabolism, Humans, Neoplasm Invasiveness, Phosphatidylinositol 3-Kinases metabolism, Phosphorylation drug effects, Signal Transduction drug effects, cdc42 GTP-Binding Protein metabolism, src-Family Kinases metabolism, Breast Neoplasms enzymology, Breast Neoplasms pathology, Cell Movement drug effects, Estrogen Receptor alpha metabolism, Focal Adhesion Kinase 1 metabolism, Wiskott-Aldrich Syndrome Protein, Neuronal metabolism
Abstract

The ability of cancer cells to move and invade the surrounding environment is the basis of local and distant metastasis. Cancer cell movement requires dynamic remodeling of the cytoskeleton and cell membrane and is controlled by multiprotein complexes including focal adhesion kinase (FAK) or the Neural Wiskott-Aldrich Syndrome Protein (N-WASP). We show that 17β-estradiol induces phosphorylation of FAK and its translocation toward membrane sites where focal adhesion complexes are assembled. This process is triggered via a Gα/Gβ protein-dependent, rapid extranuclear signaling of estrogen receptor α interacts in a multiprotein complex with c-Src, phosphatidylinositol 3-OH kinase, and FAK. Within this complex FAK autophosphorylation ensues, and activated FAK recruits the small GTPase cdc42, which, in turn, triggers N-WASP phosphorylation. This results in the translocation of Arp2/3 complexes at sites where membrane structures related to cell movement are formed. Recruitment of FAK and N-WASP is necessary for cell migration and invasion induced by 17β-estradiol in breast cancer cells. Our findings identify an original mechanism through which estrogen promotes breast cancer cell motility and invasion. This information helps to understand the effects of estrogen on breast cancer metastasis and may provide new targets for therapeutic interventions.

Published
2010
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20. Progesterone receptor enhances breast cancer cell motility and invasion via extranuclear activation of focal adhesion kinase.

Author

Fu XD, Goglia L, Sanchez AM, Flamini M, Giretti MS, Tosi V, Genazzani AR, and Simoncini T

Subjects
Analysis of Variance, Blotting, Western, Cell Adhesion drug effects, Cell Line, Tumor, Cell Movement drug effects, Cell Proliferation drug effects, Cells, Cultured, Cytoskeleton drug effects, Cytoskeleton metabolism, Dose-Response Relationship, Drug, Female, Fluorescent Antibody Technique, Humans, Phosphorylation drug effects, Phosphorylation physiology, Progesterone pharmacology, Proto-Oncogene Proteins c-akt metabolism, Signal Transduction drug effects, Signal Transduction physiology, Time Factors, Breast metabolism, Cell Adhesion physiology, Cell Movement physiology, Focal Adhesion Protein-Tyrosine Kinases metabolism, Receptors, Progesterone metabolism
Abstract

While progesterone plays multiple roles in the process of breast development and differentiation, its role in breast cancer is less understood. We have shown previously that progestins stimulate breast cancer cell migration and invasion because of the activation of rapid signaling cascades leading to modifications in the actin cytoskeleton and cell membrane that are required for cell movement. In this study, we have investigated the effects of progesterone on the formation of focal adhesion (FA) complexes, which provide anchoring sites for cell attachment to the extracellular matrix during cell movement and invasion. In T47-D breast cancer cells, progesterone rapidly enhances FA kinase (FAK) phosphorylation at Tyr(397) in a time- and concentration-dependent manner. As a result, exposure to progesterone leads to increased formation of FA complexes within specialized cell membrane protrusions. The cascade of events required for this phenomenon involves progesterone receptor interaction with the tyrosine kinase c-Src, which activates the phosphatidylinositol-3-kinase/Akt pathway and the small GTPase RhoA/Rho-associated kinase complex. In the presence of progesterone, T47-D breast cancer cells display enhanced horizontal migration and invasion of three-dimensional matrices, which is reversed by small interfering RNAs abrogating FAK. In conclusion, progesterone promotes breast cancer cell movement and invasion by facilitating the formation of FA complexes via the rapid regulation of FAK. These results provide novel mechanistic views on the effects of progesterone on breast cancer progression, and may in the future be helpful to develop new strategies for the treatment of endocrine-sensitive breast cancers.

Published
2010
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21. Effects of raloxifene on breast cancer cell migration and invasion through the actin cytoskeleton.

Author

Flamini MI, Fu XD, Sanchez AM, Giretti MS, Garibaldi S, Goglia L, Pisaneschi S, Tosi V, Genazzani AR, and Simoncini T

Subjects
Breast Neoplasms metabolism, Cell Line, Tumor, Female, Humans, Actins metabolism, Breast Neoplasms pathology, Cytoskeleton metabolism, Neoplasm Invasiveness prevention & control, Neoplasm Metastasis prevention & control, Raloxifene Hydrochloride pharmacology
Abstract

Raloxifene (RAL) is a selective oestrogen receptor modulator (SERM) approved for the prevention and treatment of osteoporosis and for the prevention of breast cancer in postmenopausal women. However, little is known on the effects of this SERM on breast cancer cell metastasis, which is the main cause of morbidity and death. Cell movement is critical for local progression and distant metastasis of cancer cells. These processes rely on the dynamic control of the actin cytoskeleton and of cell membrane morphology. The aim of the present study was to characterize the effects of RAL or of 17beta-estradiol (E2) plus RAL on oestrogen receptor (ER) positive T47-D breast cancer cell cytoskeletal remodelling, migration and invasion. Our findings show that, when given alone, RAL induces a weak actin cytoskeleton remodelling in breast cancer cells, with the formation of specialized cell membrane structures implicated in cell motility. However, in the presence of physiological amounts of estradiol, which potently drives breast cancer cell cytoskeletal remodelling and motility, RAL displays a powerful inhibitory effect on oestrogen-promoted cell migration and invasion. These actions are plaid through an interference of RAL with an extra-nuclear signalling cascade involving G proteins and the RhoA-associated kinase, ROCK-2, linked to the recruitment of the cytoskeletal controller, moesin. Hence, in the presence of estradiol, RAL acts as an ER antagonist. These results highlight a novel mechanism of action of the SERM raloxifene that might be important for the interference of breast cancer progression or metastasis induced by oestrogens in postmenopausal women.

Published
2009
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22. Rapid signaling of estrogen to WAVE1 and moesin controls neuronal spine formation via the actin cytoskeleton.

Author

Sanchez AM, Flamini MI, Fu XD, Mannella P, Giretti MS, Goglia L, Genazzani AR, and Simoncini T

Subjects
Animals, Brain embryology, Cyclin-Dependent Kinase 5 metabolism, Dendritic Spines metabolism, Estrogen Receptor alpha metabolism, Gene Expression Regulation, Developmental, Phosphorylation, Proto-Oncogene Proteins pp60(c-src) metabolism, Rats, Serine chemistry, Signal Transduction, Actins metabolism, Cytoskeleton metabolism, Estrogens metabolism, Microfilament Proteins metabolism, Neurons metabolism, Wiskott-Aldrich Syndrome Protein Family metabolism
Abstract

Estrogens are important regulators of neuronal cell morphology, and this is thought to be critical for gender-specific differences in brain function and dysfunction. Dendritic spine formation is dependent on actin remodeling by the WASP-family verprolin homologous (WAVE1) protein, which controls actin polymerization through the actin-related protein (Arp)-2/3 complex. Emerging evidence indicates that estrogens are effective regulators of the actin cytoskeleton in various cell types via rapid, extranuclear signaling mechanisms. We here show that 17beta-estradiol (E2) administration to rat cortical neurons leads to phosphorylation of WAVE1 on the serine residues 310, 397, and 441 and to WAVE1 redistribution toward the cell membrane at sites of dendritic spine formation. WAVE1 phosphorylation is found to be triggered by a Galpha(i)/Gbeta protein-dependent, rapid extranuclear signaling of estrogen receptor alpha to c-Src and to the small GTPase Rac1. Rac1 recruits the cyclin-dependent kinase (Cdk5) that directly phosphorylates WAVE1 on the three serine residues. After WAVE1 phosphorylation by E2, the Arp-2/3 complex concentrates at sites of spine formation, where it triggers the local reorganization of actin fibers. In parallel, E2 recruits a Galpha(13)-dependent pathway to RhoA and ROCK-2, leading to activation of actin remodeling via the actin-binding protein, moesin. Silencing of WAVE1 or of moesin abrogates the increase in dendritic spines induced by E2 in cortical neurons. In conclusion, our findings indicate that the control of actin polymerization and branching via moesin or WAVE1 is a key function of estrogen receptor alpha in neurons, which may be particularly relevant for the regulation of dendritic spines.

Published
2009
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