Schneider M

References (9)

Title : ADX71441, a novel, potent and selective positive allosteric modulator of the GABA(B) receptor, shows efficacy in rodent models of overactive bladder - Kalinichev_2014_Br.J.Pharmacol_171_995
Author(s) : Kalinichev M , Palea S , Haddouk H , Royer-Urios I , Guilloteau V , Lluel P , Schneider M , Saporito M , Poli S
Ref : British Journal of Pharmacology , 171 :995 , 2014
Abstract : BACKGROUND AND PURPOSE: The GABAB receptor agonist baclofen reduces urethral resistance and detrusor overactivity in patients with spasticity. However, baclofen's side effects limit its use for the treatment of overactive bladder (OAB). Here, we tested a novel GABAB positive allosteric modulator (PAM) ADX71441 in models of OAB in mice and guinea pigs. EXPERIMENTAL APPROACH: Mice were left untreated or given (p.o.) vehicle (1% CMC), ADX71441 (1, 3, 10 mg kg(-1) ) or oxybutynin (100 mg kg(-1) ; Experiment 1) or vehicle (1% CMC), baclofen (1, 3, 6 mg kg(-1) ) or oxybutynin (Experiment 2). Treated mice were then overhydrated with water, challenged with furosemide, before being placed into micturition chambers and monitored for urinary parameters. In anaesthetized guinea pigs, intravesical infusion of acetic acid was used to induce OAB and the effects of ADX71441 (1, 3 mg kg(-1) ) or baclofen (1 mg kg(-1) ), administered i.v., on cystometric parameters were monitored. KEY
RESULTS: In mice, 10 mg kg(-1) ADX71441 increased urinary latencies, reduced the number of urinary events and the total and average urinary volumes. In guinea pigs, ADX71441 (1 and 3 mg kg(-1) ) increased the intercontraction interval (ICI) and bladder capacity (BC), and reduced micturition frequency (MF) compared to vehicle. At 3 mg kg(-1) ADX71441 completely inhibited the micturition reflex and induced overflow incontinence in five out of 10 animals. Baclofen slightly increased ICI and BC and reduced MF. CONCLUSION AND IMPLICATIONS: Our findings demonstrate, for the first time, that a GABAB PAM has potential as a novel approach for the treatment of OAB.
ESTHER : Kalinichev_2014_Br.J.Pharmacol_171_995
PubMedSearch : Kalinichev_2014_Br.J.Pharmacol_171_995
PubMedID: 24224799

Title : Functional and evolutionary insights from the genomes of three parasitoid Nasonia species - Werren_2010_Science_327_343
Author(s) : Werren JH , Richards S , Desjardins CA , Niehuis O , Gadau J , Colbourne JK , Beukeboom LW , Desplan C , Elsik CG , Grimmelikhuijzen CJ , Kitts P , Lynch JA , Murphy T , Oliveira DC , Smith CD , van de Zande L , Worley KC , Zdobnov EM , Aerts M , Albert S , Anaya VH , Anzola JM , Barchuk AR , Behura SK , Bera AN , Berenbaum MR , Bertossa RC , Bitondi MM , Bordenstein SR , Bork P , Bornberg-Bauer E , Brunain M , Cazzamali G , Chaboub L , Chacko J , Chavez D , Childers CP , Choi JH , Clark ME , Claudianos C , Clinton RA , Cree AG , Cristino AS , Dang PM , Darby AC , de Graaf DC , Devreese B , Dinh HH , Edwards R , Elango N , Elhaik E , Ermolaeva O , Evans JD , Foret S , Fowler GR , Gerlach D , Gibson JD , Gilbert DG , Graur D , Grunder S , Hagen DE , Han Y , Hauser F , Hultmark D , Hunter HCt , Hurst GD , Jhangian SN , Jiang H , Johnson RM , Jones AK , Junier T , Kadowaki T , Kamping A , Kapustin Y , Kechavarzi B , Kim J , Kiryutin B , Koevoets T , Kovar CL , Kriventseva EV , Kucharski R , Lee H , Lee SL , Lees K , Lewis LR , Loehlin DW , Logsdon JM, Jr. , Lopez JA , Lozado RJ , Maglott D , Maleszka R , Mayampurath A , Mazur DJ , McClure MA , Moore AD , Morgan MB , Muller J , Munoz-Torres MC , Muzny DM , Nazareth LV , Neupert S , Nguyen NB , Nunes FM , Oakeshott JG , Okwuonu GO , Pannebakker BA , Pejaver VR , Peng Z , Pratt SC , Predel R , Pu LL , Ranson H , Raychoudhury R , Rechtsteiner A , Reese JT , Reid JG , Riddle M , Robertson HM , Romero-Severson J , Rosenberg M , Sackton TB , Sattelle DB , Schluns H , Schmitt T , Schneider M , Schuler A , Schurko AM , Shuker DM , Simoes ZL , Sinha S , Smith Z , Solovyev V , Souvorov A , Springauf A , Stafflinger E , Stage DE , Stanke M , Tanaka Y , Telschow A , Trent C , Vattathil S , Verhulst EC , Viljakainen L , Wanner KW , Waterhouse RM , Whitfield JB , Wilkes TE , Williamson MS , Willis JH , Wolschin F , Wyder S , Yamada T , Yi SV , Zecher CN , Zhang L , Gibbs RA , Williamson M
Ref : Science , 327 :343 , 2010
Abstract : We report here genome sequences and comparative analyses of three closely related parasitoid wasps: Nasonia vitripennis, N. giraulti, and N. longicornis. Parasitoids are important regulators of arthropod populations, including major agricultural pests and disease vectors, and Nasonia is an emerging genetic model, particularly for evolutionary and developmental genetics. Key findings include the identification of a functional DNA methylation tool kit; hymenopteran-specific genes including diverse venoms; lateral gene transfers among Pox viruses, Wolbachia, and Nasonia; and the rapid evolution of genes involved in nuclear-mitochondrial interactions that are implicated in speciation. Newly developed genome resources advance Nasonia for genetic research, accelerate mapping and cloning of quantitative trait loci, and will ultimately provide tools and knowledge for further increasing the utility of parasitoids as pest insect-control agents.
ESTHER : Werren_2010_Science_327_343
PubMedSearch : Werren_2010_Science_327_343
PubMedID: 20075255
Gene_locus related to this paper: nasvi-ACHE1 , nasvi-ACHE2 , nasvi-k7in31 , nasvi-k7iwl9 , nasvi-k7iyk8 , nasvi-k7jlv1 , nasvi-k7in32 , nasvi-k7ind2 , nasvi-k7inh0 , nasvi-k7inh1 , nasvi-k7inh2 , nasvi-k7inp9 , nasvi-k7iun7 , nasvi-k7iv21 , nasvi-k7ivn5 , nasvi-k7ivn6 , nasvi-k7iw29 , nasvi-k7iwk5 , nasvi-k7iwl8 , nasvi-k7iz24 , nasvi-k7izb4 , nasvi-k7j5u6 , nasvi-k7j6y1 , nasvi-k7j6y2 , nasvi-k7j6y4 , nasvi-k7j718 , nasvi-k7j755 , nasvi-k7j756 , nasvi-k7j757 , nasvi-k7j7k5 , nasvi-k7j7n7 , nasvi-k7j7r8 , nasvi-k7j7s8 , nasvi-k7j7s9 , nasvi-k7j811 , nasvi-k7iny8 , nasvi-k7izf2 , nasvi-k7iwe2 , nasvi-k7j6w4 , nasvi-k7izl9 , nasvi-k7jf39 , nasvi-k7izl8 , nasvi-k7irf1 , nasvi-k7j7l1

Title : Identification of a new functional domain in angiopoietin-like 3 (ANGPTL3) and angiopoietin-like 4 (ANGPTL4) involved in binding and inhibition of lipoprotein lipase (LPL) - Lee_2009_J.Biol.Chem_284_13735
Author(s) : Lee EC , Desai U , Gololobov G , Hong S , Feng X , Yu XC , Gay J , Wilganowski N , Gao C , Du LL , Chen J , Hu Y , Zhao S , Kirkpatrick L , Schneider M , Zambrowicz BP , Landes G , Powell DR , Sonnenburg WK
Ref : Journal of Biological Chemistry , 284 :13735 , 2009
Abstract : Angiopoietin-like 3 (ANGPTL3) and angiopoietin-like 4 (ANGPTL4) are secreted proteins that regulate triglyceride (TG) metabolism in part by inhibiting lipoprotein lipase (LPL). Recently, we showed that treatment of wild-type mice with monoclonal antibody (mAb) 14D12, specific for ANGPTL4, recapitulated the Angptl4 knock-out (-/-) mouse phenotype of reduced serum TG levels. In the present study, we mapped the region of mouse ANGPTL4 recognized by mAb 14D12 to amino acids Gln(29)-His(53), which we designate as specific epitope 1 (SE1). The 14D12 mAb prevented binding of ANGPTL4 with LPL, consistent with its ability to neutralize the LPL-inhibitory activity of ANGPTL4. Alignment of all angiopoietin family members revealed that a sequence similar to ANGPTL4 SE1 was present only in ANGPTL3, corresponding to amino acids Glu(32)-His(55). We produced a mouse mAb against this SE1-like region in ANGPTL3. This mAb, designated 5.50.3, inhibited the binding of ANGPTL3 to LPL and neutralized ANGPTL3-mediated inhibition of LPL activity in vitro. Treatment of wild-type as well as hyperlipidemic mice with mAb 5.50.3 resulted in reduced serum TG levels, recapitulating the lipid phenotype found in Angptl3(-/-) mice. These results show that the SE1 region of ANGPTL3 and ANGPTL4 functions as a domain important for binding LPL and inhibiting its activity in vitro and in vivo. Moreover, these results demonstrate that therapeutic antibodies that neutralize ANGPTL4 and ANGPTL3 may be useful for treatment of some forms of hyperlipidemia.
ESTHER : Lee_2009_J.Biol.Chem_284_13735
PubMedSearch : Lee_2009_J.Biol.Chem_284_13735
PubMedID: 19318355
Gene_locus related to this paper: human-LPL

Title : 1,3-Dichloropropene epoxides: intermediates in bioactivation of the promutagen 1,3-dichloropropene - Schneider_1998_Chem.Res.Toxicol_11_1137
Author(s) : Schneider M , Quistad GB , Casida JE
Ref : Chemical Research in Toxicology , 11 :1137 , 1998
Abstract : 1,3-Dichloropropene (1,3-D), a major soil fumigant nematicide, is genotoxic in many types of assays, leading to its classification as possibly carcinogenic in humans. This study tests in three steps the hypothesis that 1,3-D is a promutagen activated by epoxidation and further reaction of the 1,3-D-epoxides. Stereospecific epoxidation of 1,3-D (examined as the cis/trans mixture and as individual isomers) to the corresponding cis- and trans-1,3-D-epoxides is demonstrated here for the first time, both in vitro in a mouse liver microsome-NADPH system and in vivo in the liver of ip-treated mice, using GC/MS for product identification and quantitation. The cis epoxide is observed in higher yield than the trans epoxide, both in vitro and in vivo, and the cis isomer also reacts slower than the trans isomer with GSH alone or catalyzed by GSH S-transferase. cis- and trans-1,3-D-Epoxides are stable in acetone or chloroform but degrade completely in Me2SO exclusively to 2-chloroacrolein (30 min at 40 degrees C). Epoxide decomposition is slower in pH 7.4 phosphate buffer (t1/2 = 116 and 64 min for cis and trans, respectively, at 41 degrees C) with a >99% yield of 3-chloro-2-hydroxypropanal (and its dimer) and <0.5% formation of 2-chloroacrolein (for which the t1/2 is 248 min at 41 degrees C). Mutagenicity assays in Salmonella typhimurium TA100 (standard plate incorporation) establish high potencies of 37, 17, and 150 revertants/nmol for cis- and trans-1, 3-D-epoxides and 2-chloroacrolein, respectively. The mutagenicity of the epoxides is due either to their direct action or to a degradation product formed at physiological pH, i.e., 3-chloro-2-hydroxypropanal or its dehydrochlorination products. The candidate mutagens methylglyoxal and glycidaldehyde are not detected as breakdown products of 3-chloro-2-hydroxypropanal at pH 7.4 and also have low mutagenic activity in TA100. It is therefore proposed that the penultimate and ultimate mutagens of 1,3-D metabolism are the corresponding epoxides and their direct hydrolysis product 3-chloro-2-hydroxypropanal, respectively.
ESTHER : Schneider_1998_Chem.Res.Toxicol_11_1137
PubMedSearch : Schneider_1998_Chem.Res.Toxicol_11_1137
PubMedID: 9778309

Title : Biochemical characterization of two nicotinic receptors from the optic lobe of the chick - Schneider_1985_J.Biol.Chem_260_14505
Author(s) : Schneider M , Adee C , Betz H , Schmidt J
Ref : Journal of Biological Chemistry , 260 :14505 , 1985
Abstract : We have studied putative nicotinic acetylcholine receptors in the optic lobe of the newborn chick, using 125I-labeled alpha-bungarotoxin, a specific blocker of acetylcholine receptors in the neuromuscular junction, and [3H]acetylcholine, a ligand which in the presence of atropine selectively labels binding sites of nicotinic character in rat brain cortex (Schwartz et al., 1982). [3H]Acetylcholine binds reversibly to a single class of high affinity binding sites (KD = 2.2 X 10(-8) M) which occur at a tissue concentration of 5.7 pmol/g. A large fraction (approximately 60%) of these binding sites is solubilized by Triton X-100, sodium cholate, or the zwitterionic detergent 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate. Solubilization increases the affinity for acetylcholine and several nicotinic drugs from 1.5- to 7-fold. The acetylcholine-binding macromolecule resembles the receptor for alpha-bungarotoxin present in the same tissue with respect to subcellular distribution, hydrodynamic properties, lectin binding, and agonist affinity rank order. It differs from the toxin receptor in affinity for nicotinic antagonists, sensitivity to thermal inactivation, and regional distribution. The solubilized [3H]acetylcholine binding activity is separated from the toxin receptor by incubation with agarose-linked acetylcholine, by affinity chromatography on immobilized Naja naja siamensis alpha-toxin, and by precipitation with a monoclonal antibody to chick optic lobe toxin receptor.
ESTHER : Schneider_1985_J.Biol.Chem_260_14505
PubMedSearch : Schneider_1985_J.Biol.Chem_260_14505
PubMedID: 4055785

Title : Trifluoperazine stimulates acetylcholine receptor synthesis in cultured chick myotubes - Schneider_1984_J.Neurochem_42_1395
Author(s) : Schneider M , Shieh BH , Pezzementi L , Schmidt J
Ref : Journal of Neurochemistry , 42 :1395 , 1984
Abstract : Acetylcholine receptor appearance rate in the presence of the phenothiazines trifluoperazine and chlorpromazine was measured in cultured embryonic chick myotubes by means of 125I-alpha-bungarotoxin. At drug concentrations of 5 to 10 X 10(-6) M, receptor appearance rate was significantly enhanced while receptor half-life, cellular protein, net protein synthesis rate, and acetylcholinesterase levels were not similarly affected. The sulfoxide derivatives were without effect. At concentrations of 3 X 10(-5) M and above, both trifluoperazine and chlorpromazine caused myotube contracture and cell loss. Drug combination experiments revealed that receptor stimulation caused by phenothiazines is overcome by low concentrations of veratridine and ryanodine, but not by membrane depolarization with 20 mM KCl. These results lend support to the role of calcium as an intracellular messenger in acetylcholine receptor synthesis regulation, but are difficult to reconcile with the notion that cytosolic calmodulin serves as the calcium receptor in this signaling pathway. Since the trifluoperazine effect resembles that caused by the calcium antagonist D-600, phenothiazines may stimulate receptor synthesis by blocking a voltage-gated calcium channel.
ESTHER : Schneider_1984_J.Neurochem_42_1395
PubMedSearch : Schneider_1984_J.Neurochem_42_1395
PubMedID: 6142923

Title : Monoclonal antibodies to the thyrotropin receptor: the identification of blocking and stimulating antibodies - Valente_1982_J.Endocrinol.Invest_5_293
Author(s) : Valente WA , Yavin Z , Yavin E , Grollman EF , Schneider M , Rotella CM , Zonefrati R , Toccafondi RS , Kohn LD
Ref : J Endocrinol Invest , 5 :293 , 1982
Abstract : Monoclonal antibodies to the thyrotropin (TSH) receptor have been obtained from fusions of mouse myeloma cells with spleen cells immunized with solubilized thyroid membrane preparations. Two monoclonal antibodies which inhibit 125I-TSH binding and are reactive with the glycoprotein component of the bovine TSH receptor (11E8 and 13D11), are shown to inhibit basal and TSH stimulated adenylate cyclase activity in bovine thyroid membranes and human thyroid cells. Both antibodies also inhibit 125I-TSH binding in vitro, whether binding is measured at pH 6.0 in low salts and at 0-4 C or at pH 7.4 in 50 mM NaCl and at 37 C. The glycoprotein component is thus a portion of the physiologic TSH receptor in vivo and 125I-TSH binding studies apparently measure the high affinity glycoprotein component under nonphysiologic conditions and conditions more representative of the physiologic milieu. A third monoclonal antibody whose interaction with thyroid membranes is prevented by TSH is shown to stimulate adenylate cyclase activity in bovine thyroid membranes and human thyroid cells. This stimulating antibody only weakly inhibits 125I-TSH binding to thyroid membranes or to the glycoprotein component of the TSH receptor. The 22A6 antibody does, however, immunoprecipitate mixed brain gangliosides, in distinct contrast to the monoclonal antibodies to the glycoprotein receptor component, i.e., 11E8 and 13D11. The results support the speculation that autoimmune antibodies which inhibit TSH binding to thyroid membranes are not necessarily identical to antibodies which stimulate function; that antibodies directed at the high affinity initial site of TSH interaction with a cell can behave as blocking rather than stimulating antibodies and that a possible relationship exists between stimulating antibodies and the low affinity TSH binding sites (gangliosides) on thyroid membranes.
ESTHER : Valente_1982_J.Endocrinol.Invest_5_293
PubMedSearch : Valente_1982_J.Endocrinol.Invest_5_293
PubMedID: 6296219

Title : [Effect of insecticides on larvae of Musca domestica in swine manure], - Schneider_1976_Angew.Parasitol_17_128
Author(s) : Schneider M , Groth U
Ref : Angew Parasitol , 17 :128 , 1976
Abstract : The effectiveness of four inorganic compounds and six preparations of insecticides was examined on larvae of Musca domestica in pig manure. The activity of sodiumfluoride and chlorinated hydrocarbons was low. Carbaryl indicated better effect. Good to very good results showed trichlofon and bromophos and the inorganic compounds sodium hexafluorsilicate, sodium tetraborate and calcium cyanamid. The influence of calcium cyanamid and sodium tetraborate led to considerable morphological deformations of pupae. With the latter compound and with fluorides a distinct prolongation of period of development was established in comparison with control. The effect of trichlorfon and bromophos decomposes rapily in pig manure. With trichlorfon an indirect ovicide effect was observed.
ESTHER : Schneider_1976_Angew.Parasitol_17_128
PubMedSearch : Schneider_1976_Angew.Parasitol_17_128
PubMedID: 824979

Title : Acetylcholine-induced excitation on bilayers -
Author(s) : Leuzinger W , Schneider M
Ref : Experientia , 28 :256 , 1972
PubMedID: