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1. Eighth annual meeting of the European Association for the Study of Diabetes

Author

K. G. M. M. Alberti, J. Darley, Pauline M. Emerson, T. D. R. Hockaday, M. Amherdt, A. A. Like, B. Blondel, B. Marliss, C. Wollheim, L. Orci, O. Ortved Andersen, Arne Andersson, F. M. Antonini, C. Fumagalli, E. Petruzzi, G. Bertini, S. Mori, P. Tinti, S. J. H. Ashcroft, L. C. C. Weerasinghe, P. J. Randle, R. Assan, N. Slusher, B. Guy-Grand, F. Girard, E. Soufflet, J. R. Attali, G. Ballerio, J. Boillot, T. Atkins, A. J. Matty, C. J. Bailey, A. Aynsley-Green, S. R. Bloom, R. A. Bacchus, L. G. Meade, D. R. London, L. Balant, G. Zahnd, B. Petitpierre, J. Fabre, E. O. Balasse, M. A. Neef, L. Barta, G. Brooser, Maria Molnar, D. P. Bataille, P. Freychet, P. Kitabgi, G. E. Rosselin, Christian Berne, J. Beyer, U. Cordes, G. Sell, C. Rosak, K. Schöffling, B. Birkner, J. Henner, P. Wagner, F. Erhardt, P. Dieterle, N. J. A. Vaughan, A. V. Edwards, L. Boquist, I. Brand, H. D. Söling, D. Brandenburg, J. Gliemann, H. A. Ooms, W. Puls, A. Wollmer, R. A. Camerini-Davalos, J. M. B. Bloodworth, B. Limburg, W. Oppermann, A. K. Campbell, K. Siddle, J. M. Cañadell, J. Barraquer, A. Muiños, C. D. Heredia, J. Castillo-Olivares, J. Guijo, L. F. Pallardo, E. Cerasi, S. Efendić, R. Luft, J. Wahren, P. Felig, Niels Juel Christensen, A. H. Christiansen, A. Vølund, J. J. Connon, E. Trimble, G. Copinschi, R. Leclercq, O. D. Bruno, E. Haupt, C. Creutzfeldt, N. S. Track, G. S. Cuendet, C. B. Wollheim, D. P. Cameron, W. Stauffacher, E. B. Marliss, A. Czyzyk, B. Lao, W. Bartosiewicz, Z. Szczepanik, E. De Nobel, A. Van't Laar, R. A. P. Koene, Th. J. Benraad, G. Dietze, K. D. Hepp, M. Wickmayr, H. Mehnert, K. Dixon, P. D. Exon, H. R. Hughes, D. W. Jones, R. S. Elkeles, M. G. FitzGerald, J. M. Malins, A. Falorni, F. Massi-Benedetti, G. Gallo, S. Maffei, D. Fedele, A. Tiengo, M. Muggeo, P. Fabris, G. Crepaldi, K. Federlin, K. Helmke, M. Slijepčević, E. F. Pfeiffer, J. P. Felber, J. Oulès, Ch. Schindler, V. Chabot, A. Fernandez-Cruz, E. Catalán, M. Luque Otero, O. Garcia Hermida, J. P. Flatt, G. Blackburn, G. Randers, H. Förster, I Hoos, D. Lerche, I. Hoos, M. Matthäus, J. R. M. Franckson, H. Frerichs, H. Daweke, F. Gries, D. Grüneklee, J. Hessing, K. Jahnke, U. Keup, H. Miss, H. Otto, D. Schmidt, C. Zumfelde, H. v. Funcke, G. Löffler, O. Wieland, D. J. Galton, R. Guttman, G. C. Gazzola, R. Franchi, P. Ronchi, V. Saibene, G. G. Guidotti, V. Gligore, N. Hîncu, Rodica Tecuceanu, R. Goberna, F. Garcia-Albertos, J. Tamarit-Rodriguez, E. del Rio, R. Roca, José Gomez-Acebo, A. V. Creco, G. Fedeli, G. Ghirlanda, R. Fenici, M. Lucente, A. Gutman, G. Agam, N. Nahas, P. Cazalis, E. Gylfe, B. Hellman, D. R. Hadden, J. H. Connolly, D. A. D. Montgomery, J. A. Weaver, Claes Hellerström, Simon Howell, John Edwards, J. Sehlin, I. -B. Täljedal, W. Heptner, H. B. Neubauer, A. Herchuelz, D. G. Pipeleers, W. J. Malaisse, E. Herrera, Eladio Montoya, H. Hommel, IT. Fischer, B. Schmid, H. Fiedler, H. Bibergeil, J. Iversen, P. B. Iynedjian, G. Peters, C. Jacquemin, B. Lambert, B. Ch. J. Sutter, A. Jakob, J. Zapf, E. R. Froesch, F. K. Jansen, G. Freytag, L. Herberg, R. J. Jarrett, I. A. Baker, C. Jarrousse, F. Rancon, D. Job, G. Tchobroutsky, E. Eschwege, C. Guyot-Argenton, J. P. Aubry, M. Déret, H. Karman, P. Mialhe, A. Kissebah, B. Tulloch, Russell Fraser, N. Vydelingum, J. Kissing, S. Raptis, H. Dollinger, J. Faulhaber, G. Rothenbuchner, J. Kleineke, H. Sauer, J. Kloeze, Eva M. Kohner, Barbara A. Sutcliffe, M. Tudball, C. T. Dollery, W. Korp, J. Neubert, H. Bruneder, A. Lenhardt, R. E. Levett, T. Koschinsky, F. A. Gries, M. M. C. Landgraf-Leurs, R. Landgraf, R. Hörl, D. R. Langslow, H. Laube, R. Fussgänger, R. Mayer, H. Klör, E. Lázaro, V. Leclercq-Meyer, J. J. Marchand, W. Malaisse, Thomas Ledet, P. J. Lefébvre, A. S. Luyckx, Y. Le Marchand, F. Assimacopoulos, A. Singh, Ch. Rouiller, B. Jeanrenaud, G. Lenti, R. Frezzotti, G. Angotzi, A. M. Bardelli, G. Pagano, A. Basetti-Sani, M. Galli, Å. Lernmark, G. Fex, D. G. Lindsay, O. Loge, C. Lopez-Quijada, L. Chiva, M. Rodriguez-Lopez, E. G. Loten, A. L. Loubatières, M. M. Loubatières-Mariani, G. Ribes, J. Chapal, J. Lubetzki, J. Duprey, Cl. Sambourg, P. J. Lefebvre, V. Maier, M. Hinz, H. Schatz, C. Nierle, F. Malaisse-Lagae, M. Ravazzola, A. E. Renold, P. Manzano, E. Rojas-Hidalgo, J. Marco, D. Diaz-Fierros, C. Calle, D. Roman, M. L. Villanueva, I. Valverde, A. Like, A. L. Luycks, F. Fracassini, R. Menzel, D. Michaelis, I. Neumann, B. Schulz, W. Wilke, P. Wulfert, K. Krämer, G. Menzinger, F. Fallucca, F. Tamburrano, R. Carratu', D. Andreani, P. Metzger, P. Franken, R. Michael, W. Hildmann, E. Jutzi, J. Michl, S. Fankhauser, J. Schlichtkrull, J. Mirouze, A. Orsetti, Y. Vierne, N. Arnoux, L. Mølsted-Pederson, Inge Tygstrup, Åge L. Villumsen, Jørgen Pedersen, W. Montague, S. L. Howell, A. J. Moody, G. S. Agerbak, F. Sundby, A. Baritussio, Peter Naeser, R. Navalesi, A. Pilo, S. Lenzi, P. Cecchetti, G. Corsini, L. Donato, J. Nerup, G. Bendixen, J. Egeberg, J. E. Poulsen, J. Høiriis Nielsen, F. Mølgaard Hansen, A. Niki, H. Niki, T. Koide, B. J. Lin, R. E. Nikkels, J. Terpstra, A. Gay, R. H. Oakman, Norman R. Lazarus, C. Rouiller, J. Ostman, L. Backman, D. Hallberg, K. Ostrowski, U. Panten, J. Christians, H. -H. Parving, S. Munkgaard Rasmussen, M. Marichal, H. Platilovà, M. Dufek, E. Konopàsek, V. Pozuelo, J. Tamarit, A. Suner, C. Castell, E. D. R. Pruett, S. Maehlum, B. Grebe, M. Chrissiku, R. Müller, H. J. Hinze, H. Reinauer, E. R. Müller-Ruchholtz, X. Rietzler, P. Passa, J. Canivet, J. Otto, G. Behrens, T. Bücher, U. Schlumpf, B. Morell, A. Zingg, J. Schönborn, P. Westphal, G. D. Bloom, L. -A. Idahl, A. Lernmark, M. Söderberg, M. Serrano Rios, F. G. Hawkins, F. Escobar, J. M. Mato, L. Larrodera, M. de Oya, J. L. Rodriguez-Miñon, E. Shafrir, G. Sitbon, Z. Skrabalo, N. Panajatović, Z. Papić, J. Posinovec, A. Stavljenić, V. Lipovac, I. Aganović, N. G. Soler, M. A. Bennett, H. Peters, G. Janson, P. H. Sönksen, M. C. Srivastava, C. V. Tompkins, J. D. N. Nabarro, N. Schwartz Sørensen, K. Ladefoged, K. E. Wildenhoff, F. Sorge, H. -J. Diehl, H. Hoffmann, W. Schwartzkopff, E. Standl, H. Kolb, A. Standl, H. W. Sutherland, J. M. Stowers, J. C. G. Whetham, B. C. J. Sutter, B. Billaudel, M. T. Sutter-Dub, R. Jacquot, I. B. Täljedal, R. Gobema, Gy. Tamás, Éva Baranyi, A. Baranyi, A. Radvanyi, J. Tatoń, A. Hinek, A. Wiśniewska, R. B. Tattersall, D. A. Pyke, J. Bruins Slot, P. L. M. v. d. Sande, J. K. Radder, K. J. J. Waldeok, R. C. P. A. v. Muijden, W. Creutzfeldt, D. S. Turner, R. W. Baker, W. G. L. Gent, A. Shabaan, V. Marks, D. A. B. Young, Ph. Vague, H. Heim, C. Martin Laval, M. Vegezzi, C.Di Campo, G. Rahamandridona, D. Garron, B. Heyraud, J. Vague, I. Lozano, M. Diaz-Fierros, F. A. Van Assche, W. Gepts, E. Van Obberghen, G. Somers, G. Devis, G. D. Vaughan, J. Veleminsky, E. Spirova, W. Waldhäusl, H. Frisch, H. Haydl, L. Weiss, B. Willms, U. Deuticke, M. Zrůstová, and J. Roštlapil

Subjects
0303 health sciences, medicine.medical_specialty, business.industry, Endocrinology, Diabetes and Metabolism, Association (object-oriented programming), 030209 endocrinology & metabolism, Human physiology, medicine.disease, 03 medical and health sciences, 0302 clinical medicine, Diabetes mellitus, Family medicine, Internal Medicine, medicine, business, 030304 developmental biology
Published
1973

2. Altered circadian plasma cortisol and aldosterone group rhythms in Cushing's syndrome versus obesity and health

Author

A, Kreze, E, Spirova, S, Sánchez de la Peña, P, Cugini, M, Mikulecky, E, Halberg, and F, Halberg

Subjects
Male, Hydrocortisone, Humans, Female, Obesity, Aldosterone, Cushing Syndrome, Circadian Rhythm
Abstract

According to textbooks, Cushing's syndrome (CS) is associated with a loss of the circadian rhythmicity in circulating cortisol. Documented cases of a persisting rhythm in CS are regarded as an exception. Herein, we show that a circadian rhythmicity in plasma cortisol, albeit of much reduced amplitude and with altered timing, remains a group characteristic of patients with CS, characterized further by a circadian rhythm in circulating aldosterone. In Lubochna, Czechoslovakia, 28 patients with CS, 120 patients with obesity imitating CS, 70 subjects with simple obesity, and 19 nonobese controls were sampled at 0800, 1600, 2000, 0000, and again at 0800 on the following day. In Rome, five women and three men with CS and 27 women and 30 men in clinical health gave blood for aldosterone determinations at 0600, 0800, 1200, 1800, 2000, and 0000. Results were first analyzed by single cosinor and then summarized by population-mean cosinor. A group rhythm was demonstrated for all categories of subjects by the methods employed, although, compared to health and even to simple obesity or Cushing-imitating obesity, the amplitude of the rhythm in CS was much reduced. Subgrouping according to etiology and individualized assessment in practice are mandatory. The scope of this group rhythm assessment, however, is merely to document that as a general rule the circadian rhythms in circulating cortisol and aldosterone persist in CS documented by surgery or at autopsy.

Published
1987

3. Point Mutations of Nicotinic Receptor α1 Subunit Reveal New Molecular Features of G153S Slow-Channel Myasthenia.

Author

Kudryavtsev D, Isaeva A, Barkova D, Spirova E, Mukhutdinova R, Kasheverov I, and Tsetlin V

Subjects
Acetylcholine metabolism, Binding Sites genetics, Calcium metabolism, Humans, Kinetics, Myasthenic Syndromes, Congenital pathology, Patch-Clamp Techniques, Point Mutation genetics, Protein Binding genetics, Acetylcholine genetics, Amino Acid Sequence genetics, Myasthenic Syndromes, Congenital genetics, Receptors, Nicotinic genetics
Abstract

Slow-channel congenital myasthenic syndromes (SCCMSs) are rare genetic diseases caused by mutations in muscle nicotinic acetylcholine receptor (nAChR) subunits. Most of the known SCCMS-associated mutations localize at the transmembrane region near the ion pore. Only two SCCMS point mutations are at the extracellular domains near the acetylcholine binding site, α1(G153S) being one of them. In this work, a combination of molecular dynamics, targeted mutagenesis, fluorescent Ca 2+ imaging and patch-clamp electrophysiology has been applied to G153S mutant muscle nAChR to investigate the role of hydrogen bonds formed by Ser 153 with C-loop residues near the acetylcholine-binding site. Introduction of L199T mutation to the C-loop in the vicinity of Ser 153 changed hydrogen bonds distribution, decreased acetylcholine potency (EC 50 2607 vs. 146 nM) of the double mutant and decay kinetics of acetylcholine-evoked cytoplasmic Ca 2+ rise (τ 14.2 ± 0.3 vs. 34.0 ± 0.4 s). These results shed light on molecular mechanisms of nAChR activation-desensitization and on the involvement of such mechanisms in channelopathy genesis.

Published
2021
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4. New Rigid Nicotine Analogues, Carrying a Norbornane Moiety, Are Potent Agonists of α7 and α3* Nicotinic Receptors.

Author

Manetti D, Garifulina A, Bartolucci G, Bazzicalupi C, Bellucci C, Chiaramonte N, Dei S, Di Cesare Mannelli L, Ghelardini C, Gratteri P, Spirova E, Shelukhina I, Teodori E, Varani K, Tsetlin V, and Romanelli MN

Subjects
Amines chemical synthesis, Amines pharmacology, Animals, Cell Line, Tumor, Cerebral Cortex metabolism, Drug Design, Humans, Molecular Docking Simulation, Nicotinic Agonists chemical synthesis, Nicotinic Antagonists chemical synthesis, Nicotinic Antagonists pharmacology, Norbornanes chemical synthesis, Pyridines chemical synthesis, Rats, Nicotinic Agonists pharmacology, Norbornanes pharmacology, Pyridines pharmacology, Receptors, Nicotinic metabolism, alpha7 Nicotinic Acetylcholine Receptor metabolism
Abstract

A three-dimensional database search has been applied to design a series of endo- and exo-3-(pyridin-3-yl)bicyclo[2.2.1]heptan-2-amines as nicotinic receptor ligands. The synthesized compounds were tested in radioligand binding assay on rat cortex against [ 3 H]-cytisine and [ 3 H]-methyllycaconitine to measure their affinity for α4β2* and α7* nicotinic receptors. The new derivatives showed some preference for the α4β2* over the α7* subtype, with their affinity being dependent on the endo/exo isomerism and on the methylation degree of the basic nitrogen. The endo primary amines displayed the lowest K i values on both receptor subtypes. Selected compounds (1a, 2a, 3a, and 6a) were tested on heterologously expressed α4β2, α7, and α3β2 receptors and on SHSY-5Y cells. Compounds 1a and 2a showed α4β2 antagonistic properties while behaved as full agonists on recombinant α7 and on SHSY5Y cells. On the α3β2 subtype, only the chloro derivative 2a showed full agonist activity and submicromolar potency (EC 50 = 0.43 μM). The primary amines described here represent new chemotypes for the α7 and α3* receptor subtypes.

Published
2019
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5. Calcium imaging with genetically encoded sensor Case12: Facile analysis of α7/α9 nAChR mutants.

Author

Shelukhina I, Spirova E, Kudryavtsev D, Ojomoko L, Werner M, Methfessel C, Hollmann M, and Tsetlin V

Subjects
Animals, Cell Line, Tumor, Humans, Mutagenesis, Site-Directed, Rats, Calcium metabolism, Receptors, Nicotinic genetics, alpha7 Nicotinic Acetylcholine Receptor genetics
Abstract

Elucidation of the structural basis of pharmacological differences for highly homologous α7 and α9 nicotinic acetylcholine receptors (nAChRs) may shed light on their involvement in different physiological functions and diseases. Combination of site-directed mutagenesis and electrophysiology is a powerful tool to pinpoint the key amino-acid residues in the receptor ligand-binding site, but for α7 and α9 nAChRs it is complicated by their poor expression and fast desensitization. Here, we probed the ligand-binding properties of α7/α9 nAChR mutants by a proposed simple and fast calcium imaging method. The method is based on transient co-expression of α7/α9 nAChR mutants in neuroblastoma cells together with Ric-3 or NACHO chaperones and Case12 fluorescent calcium ion sensor followed by analysis of their pharmacology using a fluorescence microscope or a fluorometric imaging plate reader (FLIPR) with a GFP filter set. The results obtained were confirmed by electrophysiology and by calcium imaging with the conventional calcium indicator Fluo-4. The affinities for acetylcholine and epibatidine were determined for human and rat α7 nAChRs, and for their mutants with homologous residues of α9 nAChR incorporated at positions 117-119, 184, 185, 187, and 189, which are anticipated to be involved in ligand binding. The strongest decrease in the affinity was observed for mutations at positions 187 and 119. The L119D mutation of α7 nAChR, showing a larger effect for epibatidine than for acetylcholine, may implicate this position in pharmacological differences between α7 and α9 nAChRs.

Published
2017
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6. New quinoline derivatives as nicotinic receptor modulators.

Author

Manetti D, Bellucci C, Dei S, Teodori E, Varani K, Spirova E, Kudryavtsev D, Shelukhina I, Tsetlin V, and Romanelli MN

Subjects
Animals, Bridged Bicyclo Compounds chemical synthesis, Bridged Bicyclo Compounds chemistry, Bridged Bicyclo Compounds pharmacology, Calcium metabolism, Cell Line, Tumor, Humans, Mice, Molecular Docking Simulation, Nicotine analogs & derivatives, Nicotine chemical synthesis, Nicotine pharmacology, Nicotinic Agonists chemical synthesis, Nicotinic Agonists chemistry, Nicotinic Agonists pharmacology, Nicotinic Antagonists chemical synthesis, Nicotinic Antagonists chemistry, Nicotinic Antagonists pharmacology, Quinolines chemical synthesis, Rats, Xenopus, alpha7 Nicotinic Acetylcholine Receptor agonists, alpha7 Nicotinic Acetylcholine Receptor antagonists & inhibitors, Quinolines chemistry, Quinolines pharmacology, Receptors, Nicotinic metabolism, alpha7 Nicotinic Acetylcholine Receptor metabolism
Abstract

As a continuation of previous work on quinoline derivatives, which showed some preference (2-3 times) for the α7 with respect to α4β2 acetylcholine nicotinic receptors (nAChRs), we synthesized a series of novel azabicyclic or diazabicyclic compounds carrying a quinoline or isoquinoline ring, with the aim of searching for more selective α7 nAChR compounds. Radioligand binding studies on α7* and α4β2* nAChRs (rat brain homogenate) revealed one compound (7) with a 2-fold higher affinity for the α4β2*-subtype, and four compounds (11, 13, 14 and 16) with at least 3-fold higher affinity for α7* nAChR. The most promising was 11, showing Ki∼100 nM and over 10-fold selectivity for α7* nAChR. Compounds 7, 11, 13 and 16 at 50 μM suppressed ion currents induced in the rat α4β2 nAChR and the chimeric nAChR composed of the ligand-binding domain of the chick α7 and transmembrane domain of the α1 glycine receptor, expressed in Xenopus oocytes. Calcium imaging experiments on the human α7 nAChR expressed in the Neuro2a cells and potentiated by PNU-120596 confirmed the antagonistic activity for 7; on the contrary, 11, 13 and 16 were agonists with the EC50 values in the range of 1.0-1.6 μM. Thus, the introduced modifications allowed us to enhance the selectivity of quinolines towards α7 nAChR and to get novel compounds with agonistic activity., (Copyright © 2016 Elsevier Masson SAS. All rights reserved.)

Published
2016
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7. Altered circadian plasma cortisol and aldosterone group rhythms in Cushing's syndrome versus obesity and health.

Author

Kreze A, Spirova E, Sánchez de la Peña S, Cugini P, Mikulecky M, Halberg E, and Halberg F

Subjects
Female, Humans, Male, Obesity blood, Aldosterone blood, Circadian Rhythm, Cushing Syndrome blood, Hydrocortisone blood
Abstract

According to textbooks, Cushing's syndrome (CS) is associated with a loss of the circadian rhythmicity in circulating cortisol. Documented cases of a persisting rhythm in CS are regarded as an exception. Herein, we show that a circadian rhythmicity in plasma cortisol, albeit of much reduced amplitude and with altered timing, remains a group characteristic of patients with CS, characterized further by a circadian rhythm in circulating aldosterone. In Lubochna, Czechoslovakia, 28 patients with CS, 120 patients with obesity imitating CS, 70 subjects with simple obesity, and 19 nonobese controls were sampled at 0800, 1600, 2000, 0000, and again at 0800 on the following day. In Rome, five women and three men with CS and 27 women and 30 men in clinical health gave blood for aldosterone determinations at 0600, 0800, 1200, 1800, 2000, and 0000. Results were first analyzed by single cosinor and then summarized by population-mean cosinor. A group rhythm was demonstrated for all categories of subjects by the methods employed, although, compared to health and even to simple obesity or Cushing-imitating obesity, the amplitude of the rhythm in CS was much reduced. Subgrouping according to etiology and individualized assessment in practice are mandatory. The scope of this group rhythm assessment, however, is merely to document that as a general rule the circadian rhythms in circulating cortisol and aldosterone persist in CS documented by surgery or at autopsy.

Published
1987

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