Author: "Artero R" - Searchworks@Jio Institute Digital Library Search Results

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145 results on '"Artero R"'

1. P-025 USE OF PREOPERATORY PNEUMOPERITONEUM FOR GIANT INGUINOESCROTAL HERNIA TREATMENT WITH LOSS OF DOMAIN. A GREAT RESOURSE

Author: Gómez Torres, I, primary, Menor, P D, additional, Alcobilla, E, additional, Llorca, S, additional, Artero, R, additional, Gómez, S, additional, Tamayo, A, additional, and Laguna, M, additional
Published: 2022
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2. Deciphering the Complex Molecular Pathogenesis of Myotonic Dystrophy Type 1 through Omics Studies

Author: Espinosa-Espinosa J, Gonzalez-Barriga A, Lopez-Castel A, and Artero R
Abstract: Omics studies are crucial to improve our understanding of myotonic dystrophy type 1 (DM1), the most common muscular dystrophy in adults. Employing tissue samples and cell lines derived from patients and animal models, omics approaches have revealed the myriad alterations in gene and microRNA expression, alternative splicing, 3' polyadenylation, CpG methylation, and proteins levels, among others, that contribute to this complex multisystem disease. In addition, omics characterization of drug candidate treatment experiments provides crucial insight into the degree of therapeutic rescue and off-target effects that can be achieved. Finally, several innovative technologies such as single-cell sequencing and artificial intelligence will have a significant impact on future DM1 research.
Published: 2022

3. Rapid Determination of MBNL1 Protein Levels by Quantitative Dot Blot for the Evaluation of Antisense Oligonucleotides in Myotonic Dystrophy Myoblasts

Author: Moreno N, González-Martínez I, Artero R, and Cerro-Herreros E
Subjects: DM1 myoblasts, Quantitative dot blot, DM1 myoblasts, Muscleblind-like protein 1, Myotonic dystrophy, Oligonucleotides, Quantitative dot blot, Oligonucleotides, Muscleblind-like protein 1, Myotonic dystrophy
Abstract: Western blot assays are not adequate for high-throughput screening of protein expression because it is an expensive and time-consuming technique. Here we demonstrate that quantitative dot blots in plate format are a better option to determine the absolute contents of a given protein in less than 48 h. The method was optimized for the detection of the Muscleblind-like 1 protein in patient-derived myoblasts treated with a collection of more than 100 experimental oligonucleotides.
Published: 2022

4. Moxifloxacin rescues SMA phenotypes in patient-derived cells and animal model

Author: Januel C, Menduti G, Mamchaoui K, Martinat C, Artero R, Konieczny P, and Boido M
Subjects: Motoneurons, Drug repurposing, Spinal muscular atrophy, SMA delta7 mice, SMN2 splicing
Abstract: Spinal muscular atrophy (SMA) is a genetic disease resulting in the loss of alpha-motoneurons followed by muscle atrophy. It is caused by knock-out mutations in the survival of motor neuron 1 (SMN1) gene, which has an unaffected, but due to preferential exon 7 skipping, only partially functional human-specific SMN2 copy. We previously described a Drosophila-based screening of FDA-approved drugs that led us to discover moxifloxacin. We showed its positive effect on the SMN2 exon 7 splicing in SMA patient-derived skin cells and its ability to increase the SMN protein level. Here, we focus on moxifloxacin's therapeutic potential in additional SMA cellular and animal models. We demonstrate that moxifloxacin rescues the SMA-related molecular and phenotypical defects in muscle cells and motoneurons by improving the SMN2 splicing. The consequent increase of SMN levels was higher than in case of risdiplam, a potent exon 7 splicing modifier, and exceeded the threshold necessary for a survival improvement. We also demonstrate that daily subcutaneous injections of moxifloxacin in a severe SMA murine model reduces its characteristic neuroinflammation and increases the SMN levels in various tissues, leading to improved motor skills and extended lifespan. We show that moxifloxacin, originally used as an antibiotic, can be potentially repositioned for the SMA treatment.
Published: 2022

5. Proof of concept of peptide-linked blockmiR-induced MBNL functional rescue in myotonic dystrophy type 1 mouse model

Author: Overby S, Cerro-Herreros E, Gonzalez-Martinez I, Varela M, Seoane-Miraz D, Jad Y, Raz R, Moller T, Perez-Alonso M, Wood M, Llamusi B, and Artero R
Abstract: Myotonic dystrophy type 1 is a debilitating neuromuscular disease causing muscle weakness, myotonia, and cardiac dysfunction. The phenotypes are caused by muscleblind-like (MBNL) protein sequestration by toxic RNA in the DM1 protein kinase (DMPK) gene. DM1 patients exhibit a pathogenic number of repetitions in DMPK, which leads to downstream symptoms. Another disease characteristic is altered microRNA (miRNA) expression. It was previously shown that miR-23b regulates the translation of MBNL1 into protein. Antisense oligonucleotide (AON) treatment targeting this miRNA can improve disease symptoms. Here, we present a refinement of this strategy targeting a miR-23b binding site on the MBNL1 3MODIFIER LETTER PRIME UTR in DM1 model cells and mice by using AONs called blockmiRs. BlockmiRs linked to novel cell-penetrating peptide chemistry showed an increase in MBNL1 protein in DM1 model cells and HSALR mice. They also showed an increase in muscle strength and significant rescue of downstream splicing and histological phenotypes in mice without disturbing the endogenous levels of other miR-23b target transcripts.
Published: 2022

6. Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)

Author: Klionsky, DJ, Abdel-Aziz, AK, Abdelfatah, S, Abdellatif, M, Abdoli, A, Abel, S, Abeliovich, H, Abildgaard, MH, Abudu, YP, Acevedo-Arozena, A, Adamopoulos, IE, Adeli, K, Adolph, TE, Adornetto, A, Aflaki, E, Agam, G, Agarwal, A, Aggarwal, BB, Agnello, M, Agostinis, P, Agrewala, JN, Agrotis, A, Aguilar, PV, Ahmad, ST, Ahmed, ZM, Ahumada-Castro, U, Aits, S, Aizawa, S, Akkoc, Y, Akoumianaki, T, Akpinar, HA, Al-Abd, AM, Al-Akra, L, Al-Gharaibeh, A, Alaoui-Jamali, MA, Alberti, S, Alcocer-Gómez, E, Alessandri, C, Ali, M, Alim Al-Bari, MA, Aliwaini, S, Alizadeh, J, Almacellas, E, Almasan, A, Alonso, A, Alonso, GD, Altan-Bonnet, N, Altieri, DC, Álvarez, ÉMC, Alves, S, Alves da Costa, C, Alzaharna, MM, Amadio, M, Amantini, C, Amaral, C, Ambrosio, S, Amer, AO, Ammanathan, V, An, Z, Andersen, SU, Andrabi, SA, Andrade-Silva, M, Andres, AM, Angelini, S, Ann, D, Anozie, UC, Ansari, MY, Antas, P, Antebi, A, Antón, Z, Anwar, T, Apetoh, L, Apostolova, N, Araki, T, Araki, Y, Arasaki, K, Araújo, WL, Araya, J, Arden, C, Arévalo, M-A, Arguelles, S, Arias, E, Arikkath, J, Arimoto, H, Ariosa, AR, Armstrong-James, D, Arnauné-Pelloquin, L, Aroca, A, Arroyo, DS, Arsov, I, Artero, R, Asaro, DML, Aschner, M, Ashrafizadeh, M, Ashur-Fabian, O, Atanasov, AG, Au, AK, Auberger, P, Auner, HW, Aurelian, L, Autelli, R, Avagliano, L, Ávalos, Y, Aveic, S, Aveleira, CA, Avin-Wittenberg, T, Aydin, Y, Ayton, S, Ayyadevara, S, Azzopardi, M, Baba, M, Backer, JM, Backues, SK, Bae, D-H, Bae, O-N, Bae, SH, Baehrecke, EH, Baek, A, Baek, S-H, Baek, SH, Bagetta, G, Bagniewska-Zadworna, A, Bai, H, Bai, J, Bai, X, Bai, Y, Bairagi, N, Baksi, S, Balbi, T, Baldari, CT, Balduini, W, Ballabio, A, Ballester, M, Balazadeh, S, Balzan, R, Bandopadhyay, R, Banerjee, S, Bánréti, Á, Bao, Y, Baptista, MS, Baracca, A, Barbati, C, Bargiela, A, Barilà, D, Barlow, PG, Barmada, SJ, Barreiro, E, Barreto, GE, Bartek, J, Bartel, B, Bartolome, A, Barve, GR, Basagoudanavar, SH, Bassham, DC, Bast, RC, Basu, A, Batoko, H, Batten, I, Baulieu, EE, Baumgarner, BL, Bayry, J, Beale, R, Beau, I, Beaumatin, F, Bechara, LRG, Beck, GR, Beers, MF, Begun, J, Behrends, C, Behrens, GMN, Bei, R, Bejarano, E, Bel, S, Behl, C, Belaid, A, Belgareh-Touzé, N, Bellarosa, C, Belleudi, F, Belló Pérez, M, Bello-Morales, R, Beltran, JSDO, Beltran, S, Benbrook, DM, Bendorius, M, Benitez, BA, Benito-Cuesta, I, Bensalem, J, Berchtold, MW, Berezowska, S, Bergamaschi, D, Bergami, M, Bergmann, A, Berliocchi, L, Berlioz-Torrent, C, Bernard, A, Berthoux, L, Besirli, CG, Besteiro, S, Betin, VM, Beyaert, R, Bezbradica, JS, Bhaskar, K, Bhatia-Kissova, I, Bhattacharya, R, Bhattacharya, S, Bhattacharyya, S, Bhuiyan, MS, Bhutia, SK, Bi, L, Bi, X, Biden, TJ, Bijian, K, Billes, VA, Binart, N, Bincoletto, C, Birgisdottir, AB, Bjorkoy, G, Blanco, G, Blas-Garcia, A, Blasiak, J, Blomgran, R, Blomgren, K, Blum, JS, Boada-Romero, E, Boban, M, Boesze-Battaglia, K, Boeuf, P, Boland, B, Bomont, P, Bonaldo, P, Bonam, SR, Bonfili, L, Bonifacino, JS, Boone, BA, Bootman, MD, Bordi, M, Borner, C, Bornhauser, BC, Borthakur, G, Bosch, J, Bose, S, Botana, LM, Botas, J, Boulanger, CM, Boulton, ME, Bourdenx, M, Bourgeois, B, Bourke, NM, Bousquet, G, Boya, P, Bozhkov, PV, Bozi, LHM, Bozkurt, TO, Brackney, DE, Brandts, CH, Braun, RJ, Braus, GH, Bravo-Sagua, R, Bravo-San Pedro, JM, Brest, P, Bringer, M-A, Briones-Herrera, A, Broaddus, VC, Brodersen, P, Brodsky, JL, Brody, SL, Bronson, PG, Bronstein, JM, Brown, CN, Brown, RE, Brum, PC, Brumell, JH, Brunetti-Pierri, N, Bruno, D, Bryson-Richardson, RJ, Bucci, C, Buchrieser, C, Bueno, M, Buitrago-Molina, LE, Buraschi, S, Buch, S, Buchan, JR, Buckingham, EM, Budak, H, Budini, M, Bultynck, G, Burada, F, Burgoyne, JR, Burón, MI, Bustos, V, Büttner, S, Butturini, E, Byrd, A, Cabas, I, Cabrera-Benitez, S, Cadwell, K, Cai, J, Cai, L, Cai, Q, Cairó, M, Calbet, JA, Caldwell, GA, Caldwell, KA, Call, JA, Calvani, R, Calvo, AC, Calvo-Rubio Barrera, M, Camara, NO, Camonis, JH, Camougrand, N, Campanella, M, Campbell, EM, Campbell-Valois, F-X, Campello, S, Campesi, I, Campos, JC, Camuzard, O, Cancino, J, Candido de Almeida, D, Canesi, L, Caniggia, I, Canonico, B, Cantí, C, Cao, B, Caraglia, M, Caramés, B, Carchman, EH, Cardenal-Muñoz, E, Cardenas, C, Cardenas, L, Cardoso, SM, Carew, JS, Carle, GF, Carleton, G, Carloni, S, Carmona-Gutierrez, D, Carneiro, LA, Carnevali, O, Carosi, JM, Carra, S, Carrier, A, Carrier, L, Carroll, B, Carter, AB, Carvalho, AN, Casanova, M, Casas, C, Casas, J, Cassioli, C, Castillo, EF, Castillo, K, Castillo-Lluva, S, Castoldi, F, Castori, M, Castro, AF, Castro-Caldas, M, Castro-Hernandez, J, Castro-Obregon, S, Catz, SD, Cavadas, C, Cavaliere, F, Cavallini, G, Cavinato, M, Cayuela, ML, Cebollada Rica, P, Cecarini, V, Cecconi, F, Cechowska-Pasko, M, Cenci, S, Ceperuelo-Mallafré, V, Cerqueira, JJ, Cerutti, JM, Cervia, D, Cetintas, VB, Cetrullo, S, Chae, H-J, Chagin, AS, Chai, C-Y, Chakrabarti, G, Chakrabarti, O, Chakraborty, T, Chami, M, Chamilos, G, Chan, DW, Chan, EYW, Chan, ED, Chan, HYE, Chan, HH, Chan, H, Chan, MTV, Chan, YS, Chandra, PK, Chang, C-P, Chang, C, Chang, H-C, Chang, K, Chao, J, Chapman, T, Charlet-Berguerand, N, Chatterjee, S, Chaube, SK, Chaudhary, A, Chauhan, S, Chaum, E, Checler, F, Cheetham, ME, Chen, C-S, Chen, G-C, Chen, J-F, Chen, LL, Chen, L, Chen, M, Chen, M-K, Chen, N, Chen, Q, Chen, R-H, Chen, S, Chen, W, Chen, X-M, Chen, X-W, Chen, X, Chen, Y, Chen, Y-G, Chen, Y-J, Chen, Y-Q, Chen, ZS, Chen, Z, Chen, Z-H, Chen, ZJ, Cheng, H, Cheng, J, Cheng, S-Y, Cheng, W, Cheng, X, Cheng, X-T, Cheng, Y, Cheng, Z, Cheong, H, Cheong, JK, Chernyak, BV, Cherry, S, Cheung, CFR, Cheung, CHA, Cheung, K-H, Chevet, E, Chi, RJ, Chiang, AKS, Chiaradonna, F, Chiarelli, R, Chiariello, M, Chica, N, Chiocca, S, Chiong, M, Chiou, S-H, Chiramel, AI, Chiurchiù, V, Cho, D-H, Choe, S-K, Choi, AMK, Choi, ME, Choudhury, KR, Chow, NS, Chu, CT, Chua, JP, Chua, JJE, Chung, H, Chung, KP, Chung, S, Chung, S-H, Chung, Y-L, Cianfanelli, V, Ciechomska, IA, Cifuentes, M, Cinque, L, Cirak, S, Cirone, M, Clague, MJ, Clarke, R, Clementi, E, Coccia, EM, Codogno, P, Cohen, E, Cohen, MM, Colasanti, T, Colasuonno, F, Colbert, RA, Colell, A, Čolić, M, Coll, NS, Collins, MO, Colombo, MI, Colón-Ramos, DA, Combaret, L, Comincini, S, Cominetti, MR, Consiglio, A, Conte, A, Conti, F, Contu, VR, Cookson, MR, Coombs, KM, Coppens, I, Corasaniti, MT, Corkery, DP, Cordes, N, Cortese, K, Costa, MDC, Costantino, S, Costelli, P, Coto-Montes, A, Crack, PJ, Crespo, JL, Criollo, A, Crippa, V, Cristofani, R, Csizmadia, T, Cuadrado, A, Cui, B, Cui, J, Cui, Y, Culetto, E, Cumino, AC, Cybulsky, AV, Czaja, MJ, Czuczwar, SJ, D'Adamo, S, D'Amelio, M, D'Arcangelo, D, D'Lugos, AC, D'Orazi, G, da Silva, JA, Dafsari, HS, Dagda, RK, Dagdas, Y, Daglia, M, Dai, X, Dai, Y, Dal Col, J, Dalhaimer, P, Dalla Valle, L, Dallenga, T, Dalmasso, G, Damme, M, Dando, I, Dantuma, NP, Darling, AL, Das, H, Dasarathy, S, Dasari, SK, Dash, S, Daumke, O, Dauphinee, AN, Davies, JS, Dávila, VA, Davis, RJ, Davis, T, Dayalan Naidu, S, De Amicis, F, De Bosscher, K, De Felice, F, De Franceschi, L, De Leonibus, C, de Mattos Barbosa, MG, De Meyer, GRY, De Milito, A, De Nunzio, C, De Palma, C, De Santi, M, De Virgilio, C, De Zio, D, Debnath, J, DeBosch, BJ, Decuypere, J-P, Deehan, MA, Deflorian, G, DeGregori, J, Dehay, B, Del Rio, G, Delaney, JR, Delbridge, LMD, Delorme-Axford, E, Delpino, MV, Demarchi, F, Dembitz, V, Demers, ND, Deng, H, Deng, Z, Dengjel, J, Dent, P, Denton, D, DePamphilis, ML, Der, CJ, Deretic, V, Descoteaux, A, Devis, L, Devkota, S, Devuyst, O, Dewson, G, Dharmasivam, M, Dhiman, R, di Bernardo, D, Di Cristina, M, Di Domenico, F, Di Fazio, P, Di Fonzo, A, Di Guardo, G, Di Guglielmo, GM, Di Leo, L, Di Malta, C, Di Nardo, A, Di Rienzo, M, Di Sano, F, Diallinas, G, Diao, J, Diaz-Araya, G, Díaz-Laviada, I, Dickinson, JM, Diederich, M, Dieudé, M, Dikic, I, Ding, S, Ding, W-X, Dini, L, Dinić, J, Dinic, M, Dinkova-Kostova, AT, Dionne, MS, Distler, JHW, Diwan, A, Dixon, IMC, Djavaheri-Mergny, M, Dobrinski, I, Dobrovinskaya, O, Dobrowolski, R, Dobson, RCJ, Đokić, J, Dokmeci Emre, S, Donadelli, M, Dong, B, Dong, X, Dong, Z, Dorn Ii, GW, Dotsch, V, Dou, H, Dou, J, Dowaidar, M, Dridi, S, Drucker, L, Du, A, Du, C, Du, G, Du, H-N, Du, L-L, du Toit, A, Duan, S-B, Duan, X, Duarte, SP, Dubrovska, A, Dunlop, EA, Dupont, N, Durán, RV, Dwarakanath, BS, Dyshlovoy, SA, Ebrahimi-Fakhari, D, Eckhart, L, Edelstein, CL, Efferth, T, Eftekharpour, E, Eichinger, L, Eid, N, Eisenberg, T, Eissa, NT, Eissa, S, Ejarque, M, El Andaloussi, A, El-Hage, N, El-Naggar, S, Eleuteri, AM, El-Shafey, ES, Elgendy, M, Eliopoulos, AG, Elizalde, MM, Elks, PM, Elsasser, H-P, Elsherbiny, ES, Emerling, BM, Emre, NCT, Eng, CH, Engedal, N, Engelbrecht, A-M, Engelsen, AST, Enserink, JM, Escalante, R, Esclatine, A, Escobar-Henriques, M, Eskelinen, E-L, Espert, L, Eusebio, M-O, Fabrias, G, Fabrizi, C, Facchiano, A, Facchiano, F, Fadeel, B, Fader, C, Faesen, AC, Fairlie, WD, Falcó, A, Falkenburger, BH, Fan, D, Fan, J, Fan, Y, Fang, EF, Fang, Y, Fanto, M, Farfel-Becker, T, Faure, M, Fazeli, G, Fedele, AO, Feldman, AM, Feng, D, Feng, J, Feng, L, Feng, Y, Feng, W, Fenz Araujo, T, Ferguson, TA, Fernández, ÁF, Fernandez-Checa, JC, Fernández-Veledo, S, Fernie, AR, Ferrante, AW, Ferraresi, A, Ferrari, MF, Ferreira, JCB, Ferro-Novick, S, Figueras, A, Filadi, R, Filigheddu, N, Filippi-Chiela, E, Filomeni, G, Fimia, GM, Fineschi, V, Finetti, F, Finkbeiner, S, Fisher, EA, Fisher, PB, Flamigni, F, Fliesler, SJ, Flo, TH, Florance, I, Florey, O, Florio, T, Fodor, E, Follo, C, Fon, EA, Forlino, A, Fornai, F, Fortini, P, Fracassi, A, Fraldi, A, Franco, B, Franco, R, Franconi, F, Frankel, LB, Friedman, SL, Fröhlich, LF, Frühbeck, G, Fuentes, JM, Fujiki, Y, Fujita, N, Fujiwara, Y, Fukuda, M, Fulda, S, Furic, L, Furuya, N, Fusco, C, Gack, MU, Gaffke, L, Galadari, S, Galasso, A, Galindo, MF, Gallolu Kankanamalage, S, Galluzzi, L, Galy, V, Gammoh, N, Gan, B, Ganley, IG, Gao, F, Gao, H, Gao, M, Gao, P, Gao, S-J, Gao, W, Gao, X, Garcera, A, Garcia, MN, Garcia, VE, García-Del Portillo, F, Garcia-Escudero, V, Garcia-Garcia, A, Garcia-Macia, M, García-Moreno, D, Garcia-Ruiz, C, García-Sanz, P, Garg, AD, Gargini, R, Garofalo, T, Garry, RF, Gassen, NC, Gatica, D, Ge, L, Ge, W, Geiss-Friedlander, R, Gelfi, C, Genschik, P, Gentle, IE, Gerbino, V, Gerhardt, C, Germain, K, Germain, M, Gewirtz, DA, Ghasemipour Afshar, E, Ghavami, S, Ghigo, A, Ghosh, M, Giamas, G, Giampietri, C, Giatromanolaki, A, Gibson, GE, Gibson, SB, Ginet, V, Giniger, E, Giorgi, C, Girao, H, Girardin, SE, Giridharan, M, Giuliano, S, Giulivi, C, Giuriato, S, Giustiniani, J, Gluschko, A, Goder, V, Goginashvili, A, Golab, J, Goldstone, DC, Golebiewska, A, Gomes, LR, Gomez, R, Gómez-Sánchez, R, Gomez-Puerto, MC, Gomez-Sintes, R, Gong, Q, Goni, FM, González-Gallego, J, Gonzalez-Hernandez, T, Gonzalez-Polo, RA, Gonzalez-Reyes, JA, González-Rodríguez, P, Goping, IS, Gorbatyuk, MS, Gorbunov, NV, Görgülü, K, Gorojod, RM, Gorski, SM, Goruppi, S, Gotor, C, Gottlieb, RA, Gozes, I, Gozuacik, D, Graef, M, Gräler, MH, Granatiero, V, Grasso, D, Gray, JP, Green, DR, Greenhough, A, Gregory, SL, Griffin, EF, Grinstaff, MW, Gros, F, Grose, C, Gross, AS, Gruber, F, Grumati, P, Grune, T, Gu, X, Guan, J-L, Guardia, CM, Guda, K, Guerra, F, Guerri, C, Guha, P, Guillén, C, Gujar, S, Gukovskaya, A, Gukovsky, I, Gunst, J, Günther, A, Guntur, AR, Guo, C, Guo, H, Guo, L-W, Guo, M, Gupta, P, Gupta, SK, Gupta, S, Gupta, VB, Gupta, V, Gustafsson, AB, Gutterman, DD, H B, R, Haapasalo, A, Haber, JE, Hać, A, Hadano, S, Hafrén, AJ, Haidar, M, Hall, BS, Halldén, G, Hamacher-Brady, A, Hamann, A, Hamasaki, M, Han, W, Hansen, M, Hanson, PI, Hao, Z, Harada, M, Harhaji-Trajkovic, L, Hariharan, N, Haroon, N, Harris, J, Hasegawa, T, Hasima Nagoor, N, Haspel, JA, Haucke, V, Hawkins, WD, Hay, BA, Haynes, CM, Hayrabedyan, SB, Hays, TS, He, C, He, Q, He, R-R, He, Y-W, He, Y-Y, Heakal, Y, Heberle, AM, Hejtmancik, JF, Helgason, GV, Henkel, V, Herb, M, Hergovich, A, Herman-Antosiewicz, A, Hernández, A, Hernandez, C, Hernandez-Diaz, S, Hernandez-Gea, V, Herpin, A, Herreros, J, Hervás, JH, Hesselson, D, Hetz, C, Heussler, VT, Higuchi, Y, Hilfiker, S, Hill, JA, Hlavacek, WS, Ho, EA, Ho, IHT, Ho, PW-L, Ho, S-L, Ho, WY, Hobbs, GA, Hochstrasser, M, Hoet, PHM, Hofius, D, Hofman, P, Höhn, A, Holmberg, CI, Hombrebueno, JR, Yi-Ren Hong, C-WH, Hooper, LV, Hoppe, T, Horos, R, Hoshida, Y, Hsin, I-L, Hsu, H-Y, Hu, B, Hu, D, Hu, L-F, Hu, MC, Hu, R, Hu, W, Hu, Y-C, Hu, Z-W, Hua, F, Hua, J, Hua, Y, Huan, C, Huang, C, Huang, H, Huang, K, Huang, MLH, Huang, R, Huang, S, Huang, T, Huang, X, Huang, YJ, Huber, TB, Hubert, V, Hubner, CA, Hughes, SM, Hughes, WE, Humbert, M, Hummer, G, Hurley, JH, Hussain, S, Hussey, PJ, Hutabarat, M, Hwang, H-Y, Hwang, S, Ieni, A, Ikeda, F, Imagawa, Y, Imai, Y, Imbriano, C, Imoto, M, Inman, DM, Inoki, K, Iovanna, J, Iozzo, RV, Ippolito, G, Irazoqui, JE, Iribarren, P, Ishaq, M, Ishikawa, M, Ishimwe, N, Isidoro, C, Ismail, N, Issazadeh-Navikas, S, Itakura, E, Ito, D, Ivankovic, D, Ivanova, S, Iyer, AKV, Izquierdo, JM, Izumi, M, Jäättelä, M, Jabir, MS, Jackson, WT, Jacobo-Herrera, N, Jacomin, A-C, Jacquin, E, Jadiya, P, Jaeschke, H, Jagannath, C, Jakobi, AJ, Jakobsson, J, Janji, B, Jansen-Dürr, P, Jansson, PJ, Jantsch, J, Januszewski, S, Jassey, A, Jean, S, Jeltsch-David, H, Jendelova, P, Jenny, A, Jensen, TE, Jessen, N, Jewell, JL, Ji, J, Jia, L, Jia, R, Jiang, L, Jiang, Q, Jiang, R, Jiang, T, Jiang, X, Jiang, Y, Jimenez-Sanchez, M, Jin, E-J, Jin, F, Jin, H, Jin, L, Jin, M, Jin, S, Jo, E-K, Joffre, C, Johansen, T, Johnson, GVW, Johnston, SA, Jokitalo, E, Jolly, MK, Joosten, LAB, Jordan, J, Joseph, B, Ju, D, Ju, J-S, Ju, J, Juárez, E, Judith, D, Juhász, G, Jun, Y, Jung, CH, Jung, S-C, Jung, YK, Jungbluth, H, Jungverdorben, J, Just, S, Kaarniranta, K, Kaasik, A, Kabuta, T, Kaganovich, D, Kahana, A, Kain, R, Kajimura, S, Kalamvoki, M, Kalia, M, Kalinowski, DS, Kaludercic, N, Kalvari, I, Kaminska, J, Kaminskyy, 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Yuan, S-SF, Yuan, Y, Yuan, Z, Yue, J, Yue, Z, Yun, J, Yung, RL, Zacks, DN, Zaffagnini, G, Zambelli, VO, Zanella, I, Zang, QS, Zanivan, S, Zappavigna, S, Zaragoza, P, Zarbalis, KS, Zarebkohan, A, Zarrouk, A, Zeitlin, SO, Zeng, J, Zeng, J-D, Žerovnik, E, Zhan, L, Zhang, B, Zhang, DD, Zhang, H, Zhang, H-L, Zhang, J, Zhang, J-P, Zhang, KYB, Zhang, LW, Zhang, L, Zhang, M, Zhang, P, Zhang, S, Zhang, W, Zhang, X, Zhang, X-W, Zhang, XD, Zhang, Y, Zhang, Y-D, Zhang, Y-Y, Zhang, Z, Zhao, H, Zhao, L, Zhao, S, Zhao, T, Zhao, X-F, Zhao, Y, Zheng, G, Zheng, K, Zheng, L, Zheng, S, Zheng, X-L, Zheng, Y, Zheng, Z-G, Zhivotovsky, B, Zhong, Q, Zhou, A, Zhou, B, Zhou, C, Zhou, G, Zhou, H, Zhou, J, Zhou, K, Zhou, R, Zhou, X-J, Zhou, Y, Zhou, Z-Y, Zhou, Z, Zhu, B, Zhu, C, Zhu, G-Q, Zhu, H, Zhu, W-G, Zhu, Y, Zhuang, H, Zhuang, X, Zientara-Rytter, K, Zimmermann, CM, Ziviani, E, Zoladek, T, Zong, W-X, Zorov, DB, Zorzano, A, Zou, W, Zou, Z, Zuryn, S, Zwerschke, W, Brand-Saberi, B, Dong, XC, Kenchappa, CS, Lin, Y, Oshima, S, Rong, Y, Sluimer, JC, Stallings, CL, and Tong, C-K
Abstract: In 2008, we published the first set of guidelines for standardizing research in autophagy. Since then, this topic has received increasing attention, and many scientists have entered the field. Our knowledge base and relevant new technologies have also been expanding. Thus, it is important to formulate on a regular basis updated guidelines for monitoring autophagy in different organisms. Despite numerous reviews, there continues to be confusion regarding acceptable methods to evaluate autophagy, especially in multicellular eukaryotes. Here, we present a set of guidelines for investigators to select and interpret methods to examine autophagy and related processes, and for reviewers to provide realistic and reasonable critiques of reports that are focused on these processes. These guidelines are not meant to be a dogmatic set of rules, because the appropriateness of any assay largely depends on the question being asked and the system being used. Moreover, no individual assay is perfect for every situation, calling for the use of multiple techniques to properly monitor autophagy in each experimental setting. Finally, several core components of the autophagy machinery have been implicated in distinct autophagic processes (canonical and noncanonical autophagy), implying that genetic approaches to block autophagy should rely on targeting two or more autophagy-related genes that ideally participate in distinct steps of the pathway. Along similar lines, because multiple proteins involved in autophagy also regulate other cellular pathways including apoptosis, not all of them can be used as a specific marker for bona fide autophagic responses. Here, we critically discuss current methods of assessing autophagy and the information they can, or cannot, provide. Our ultimate goal is to encourage intellectual and technical innovation in the field.
Published: 2021

7. Myotonic dystrophy type 1 drug development: A pipeline toward the market

Author: Pascual-Gilabert M, Lopez-Castel A, and Artero R
Subjects: Clinical trial, Gene therapy, Myotonic dystrophy, Drug development, Repurposing drug, Antisense oligonucleotide
Abstract: Myotonic dystrophy type 1 (DM1) is a multisystemic neuromuscular genetic disease with an estimated prevalence of approximately at least half a million individuals based on its vast ethnic variation. Building upon a well-known physiopathology and several proof-of-concept therapeutic approaches, herein we compile a comprehensive overview of the most recent drug development programs under preclinical and clinical evaluation. Specifically, close to two dozen drug developments, eight of which are already in clinical trials, explore a diversity of new chemical entities, drug repurposing, oligonucleotide, and gene therapy-based approaches. Of these, repurposing of tideglusib, mexiletine, or metformin appear to be therapies with the most potential to receive marketing authorization for DM1.
Published: 2021

8. Inhibition of autophagy rescues muscle atrophy in a LGMDD2 Drosophila model

Author: Blázquez-Bernal Á, Fernandez-Costa JM, Bargiela A, and Artero R
Subjects: chloroquine, muscle atrophy, autophagy, Drosophila melanogaster, Drosophila melanogaster , autophagy, chloroquine, limb-girdle muscular dystrophy D2, muscle atrophy, transportin 3, transportin 3, limb-girdle muscular dystrophy D2
Abstract: Limb-girdle muscular dystrophy D2 (LGMDD2) is an ultrarare autosomal dominant myopathy caused by mutation of the normal stop codon of the TNPO3 nuclear importin. The mutant protein carries a 15 amino acid C-terminal extension associated with pathogenicity. Here we report the first animal model of the disease by expressing the human mutant TNPO3 gene in Drosophila musculature or motor neurons and concomitantly silencing the endogenous expression of the fly protein ortholog. A similar genotype expressing wildtype TNPO3 served as a control. Phenotypes characterization revealed that mutant TNPO3 expression targeted at muscles or motor neurons caused LGMDD2-like phenotypes such as muscle degeneration and atrophy, and reduced locomotor ability. Notably, LGMDD2 mutation increase TNPO3 at the transcript and protein level in the Drosophila model Upregulated muscle autophagy observed in LGMDD2 patients was also confirmed in the fly model, in which the anti-autophagic drug chloroquine was able to rescue histologic and functional phenotypes. Overall, we provide a proof of concept of autophagy as a target to treat disease phenotypes and propose a neurogenic component to explain mutant TNPO3 pathogenicity in diseased muscles.
Published: 2021

9. Practicing logical reasoning through Drosophila segmentation gene mutants

Author: Bargiela A and Artero R
Subjects: education, mutant phenotype, larval cuticle, Drosophila, development, segmentation genes
Abstract: Laboratory practical sessions are critical to scientific training in biology but usually fail to promote logical and hypothesis-driven reasoning and rely heavily on the teacher's instructions. This paper describes a 2-day laboratory practicum in which students prepare and analyze larval cuticle preparations of Drosophila segmentation gene mutant strains. Embryonic segmentation involves three major classes of genes according to their loss-of-function phenotypes: the establishment of broad regions by gap genes, the specification of the segments by the pair-rule genes, and the compartments within segments by the segment polarity genes. Students are asked to sort undefined segmentation mutants into gap, pair-rule, or segment polarity categories based on their knowledge of the Drosophila segmentation process and the microscopic anatomical traits they are capable of finding in the sample preparations. This technically simple practicum prompts students to pay attention to detailed observation to detect anatomic markers of intrasegmental compartments and thorax versus abdomen cuticle, and promote their logical reasoning in hypothesizing to which segmentation type a given mutant fits best.
Published: 2021

10. Neuroprotective properties of queen bee acid by autophagy induction

Author: Martínez-Chacón G, Paredes-Barquero M, Yakhine-Diop SMS, Uribe-Carretero E, Bargiela A, Sabater-Arcis M, Morales-García J, Alarcón-Gil J, Alegre-Cortés E, Canales-Cortés S, Rodríguez-Arribas M, Camello PJ, Pedro JMB, Perez-Castillo A, Artero R, Gonzalez-Polo RA, Fuentes JM, and Niso-Santano M
Subjects: SIRT1, QBA, Longevity, Autophagy, Parkinson’s disease, Neurodegeneration, Autophagy, Longevity, Neurodegeneration, Parkinson’s disease, QBA, SIRT1
Abstract: Autophagy is a conserved intracellular catabolic pathway that removes cytoplasmic components to contribute to neuronal homeostasis. Accumulating evidence has increasingly shown that the induction of autophagy improves neuronal health and extends longevity in several animal models. Therefore, there is a great interest in the identification of effective autophagy enhancers with potential nutraceutical or pharmaceutical properties to ameliorate age-related diseases, such as neurodegenerative disorders, and/or promote longevity. Queen bee acid (QBA, 10-hydroxy-2-decenoic acid) is the major fatty acid component of, and is found exclusively in, royal jelly, which has beneficial properties for human health. It is reported that QBA has antitumor, anti-inflammatory, and antibacterial activities and promotes neurogenesis and neuronal health; however, the mechanism by which QBA exerts these effects has not been fully elucidated. The present study investigated the role of the autophagic process in the protective effect of QBA. We found that QBA is a novel autophagy inducer that triggers autophagy in various neuronal cell lines and mouse and fly models. The beclin-1 (BECN1) and mTOR pathways participate in the regulation of QBA-induced autophagy. Moreover, our results showed that QBA stimulates sirtuin 1 (SIRT1), which promotes autophagy by the deacetylation of critical ATG proteins. Finally, QBA-mediated autophagy promotes neuroprotection in Parkinson's disease in vitro and in a mouse model and extends the lifespan of Drosophila melanogaster. This study provides detailed evidences showing that autophagy induction plays a critical role in the beneficial health effects of QBA.
Published: 2021

11. Rabphilin silencing causes dilated cardiomyopathy in a Drosophila model of nephrocyte damage

Author: Selma-Soriano E, Casillas-Serra C, Artero R, Llamusi B, Navarro J, and Redon J
Subjects: fungi
Abstract: Heart failure (HF) and the development of chronic kidney disease (CKD) have a direct association. Both can be cause and consequence of the other. Many factors are known, such as diabetes or hypertension, which can lead to the appearance and/or development of these two conditions. However, it is suspected that other factors, namely genetic ones, may explain the differences in the manifestation and progression of HF and CKD among patients. One candidate factor is Rph, a gene expressed in the nervous and excretory system in mammals and Drosophila, encoding a Rab small GTPase family effector protein implicated in vesicular trafficking. We found that Rph is expressed in the Drosophila heart, and the silencing of Rph gene expression in this organ had a strong impact in the organization of fibers and functional cardiac parameters. Specifically, we observed a significant increase in diastolic and systolic diameters of the heart tube, which is a phenotype that resembles dilated cardiomyopathy in humans. Importantly, we also show that silencing of Rabphilin (Rph) expression exclusively in the pericardial nephrocytes, which are part of the flies' excretory system, brings about a non-cell-autonomous effect on the Drosophila cardiac system. In summary, in this work, we demonstrate the importance of Rph in the fly cardiac system and how silencing Rph expression in nephrocytes affects the Drosophila cardiac system.
Published: 2021

12. Musashi-2 contributes to myotonic dystrophy muscle dysfunction by promoting excessive autophagy through miR-7 biogenesis repression

Author: Sabater-Arcis M, Bargiela A, Moreno N, Poyatos-Garcia J, Vilchez J, and Artero R
Abstract: Skeletal muscle symptoms strongly contribute to mortality of myotonic dystrophy type 1 (DM1) patients. DM1 is a neuromuscular genetic disease caused by CTG repeat expansions that, upon transcription, sequester the Muscleblind-like family of proteins and dysregulate alternative splicing of hundreds of genes. However, mis-splicing does not satisfactorily explain muscle atrophy and wasting, and several other contributing factors have been suggested, including hyperactivated autophagy leading to excessive catabolism. MicroRNA (miR)-7 has been demonstrated to be necessary and sufficient to repress the autophagy pathway in cell models of the disease, but the origin of its low levels in DM1 was unknown. We have found that the RNA-binding protein Musashi-2 (MSI2) is upregulated in patient-derived myoblasts and biopsy samples. Because it has been previously reported that MSI2 controls miR-7 biogenesis, we tested the hypothesis that excessive MSI2 was repressing miR-7 maturation. Using gene-silencing strategies (small interfering RNAs [siRNAs] and gapmers) and the small molecule MSI2-inhibitor Ro 08-2750, we demonstrate that reducing MSI2 levels or activity boosts miR-7 expression, represses excessive autophagy, and downregulates atrophy related genes of the UPS system. We also detect a significant upregulation of MBNL1 upon MSI2 silencing. Taken together, we propose MSI2 as a new therapeutic target to treat muscle dysfunction in DM1.
Published: 2021

13. Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)(1)

Author: Klionsky, D.J., Abdel-Aziz, A.K., Abdelfatah, S., Abdellatif, M., Abdoli, A., Abel, S., Abeliovich, H., Abildgaard, M.H., Abudu, Y.P., Acevedo-Arozena, A., Adamopoulos, I.E., Adeli, K., Adolph, T.E., Adornetto, A., Aflaki, E., Agam, G., Agarwal, A., Aggarwal, B.B., Agnello, M., Agostinis, P., Agrewala, J.N., Agrotis, A., Aguilar, P.V., Ahmad, S.T., Ahmed, Z.M., Ahumada-Castro, U., Aits, S., Aizawa, S., Akkoc, Y., Akoumianaki, T., Akpinar, H.A., Al-Abd, A.M., Al-Akra, L., Al-Gharaibeh, A., Alaoui-Jamali, M.A., Alberti, S., Alcocer-Gómez, E., Alessandri, C., Ali, M, Al-Bari, M.A. Alim, Aliwaini, S., Alizadeh, J., Almacellas, E., Almasan, A., Alonso, A., Alonso, G.D., Altan-Bonnet, N., Altieri, D.C., É, M.C. Álvarez, Alves, S., Costa, C., Alzaharna, M.M., Amadio, M., Amantini, C., Amaral, C., Ambrosio, S., Amer, A.O., Ammanathan, V., An, Z., Andersen, S.U., Andrabi, S.A., Andrade-Silva, M., Andres, A.M., Angelini, S., Ann, D., Anozie, U.C., Ansari, M.Y., Antas, P., Antebi, A., Antón, Z., Anwar, T., Apetoh, L., Apostolova, N., Araki, T., Araki, Y., Arasaki, K., Araújo, W.L., Araya, J., Arden, C., Arévalo, M.A., Arguelles, S., Arias, E., Arikkath, J., Arimoto, H., Ariosa, A.R., Armstrong-James, D., Arnauné-Pelloquin, L., Aroca, A., Arroyo, D.S., Arsov, I., Artero, R., Asaro, D.M.L., Aschner, M., Ashrafizadeh, M., Ashur-Fabian, O., Atanasov, A.G., Au, A.K., Auberger, P., Auner, H.W., Aurelian, L., Joosten, L.A.B., Netea, M.G., Plantinga, T.S., Stallings, C.L., Tong, C.K., Klionsky, D.J., Abdel-Aziz, A.K., Abdelfatah, S., Abdellatif, M., Abdoli, A., Abel, S., Abeliovich, H., Abildgaard, M.H., Abudu, Y.P., Acevedo-Arozena, A., Adamopoulos, I.E., Adeli, K., Adolph, T.E., Adornetto, A., Aflaki, E., Agam, G., Agarwal, A., Aggarwal, B.B., Agnello, M., Agostinis, P., Agrewala, J.N., Agrotis, A., Aguilar, P.V., Ahmad, S.T., Ahmed, Z.M., Ahumada-Castro, U., Aits, S., Aizawa, S., Akkoc, Y., Akoumianaki, T., Akpinar, H.A., Al-Abd, A.M., Al-Akra, L., Al-Gharaibeh, A., Alaoui-Jamali, M.A., Alberti, S., Alcocer-Gómez, E., Alessandri, C., Ali, M, Al-Bari, M.A. Alim, Aliwaini, S., Alizadeh, J., Almacellas, E., Almasan, A., Alonso, A., Alonso, G.D., Altan-Bonnet, N., Altieri, D.C., É, M.C. Álvarez, Alves, S., Costa, C., Alzaharna, M.M., Amadio, M., Amantini, C., Amaral, C., Ambrosio, S., Amer, A.O., Ammanathan, V., An, Z., Andersen, S.U., Andrabi, S.A., Andrade-Silva, M., Andres, A.M., Angelini, S., Ann, D., Anozie, U.C., Ansari, M.Y., Antas, P., Antebi, A., Antón, Z., Anwar, T., Apetoh, L., Apostolova, N., Araki, T., Araki, Y., Arasaki, K., Araújo, W.L., Araya, J., Arden, C., Arévalo, M.A., Arguelles, S., Arias, E., Arikkath, J., Arimoto, H., Ariosa, A.R., Armstrong-James, D., Arnauné-Pelloquin, L., Aroca, A., Arroyo, D.S., Arsov, I., Artero, R., Asaro, D.M.L., Aschner, M., Ashrafizadeh, M., Ashur-Fabian, O., Atanasov, A.G., Au, A.K., Auberger, P., Auner, H.W., Aurelian, L., Joosten, L.A.B., Netea, M.G., Plantinga, T.S., Stallings, C.L., and Tong, C.K.
Abstract: Contains fulltext : 232759.pdf (Publisher’s version ) (Closed access), In 2008, we published the first set of guidelines for standardizing research in autophagy. Since then, this topic has received increasing attention, and many scientists have entered the field. Our knowledge base and relevant new technologies have also been expanding. Thus, it is important to formulate on a regular basis updated guidelines for monitoring autophagy in different organisms. Despite numerous reviews, there continues to be confusion regarding acceptable methods to evaluate autophagy, especially in multicellular eukaryotes. Here, we present a set of guidelines for investigators to select and interpret methods to examine autophagy and related processes, and for reviewers to provide realistic and reasonable critiques of reports that are focused on these processes. These guidelines are not meant to be a dogmatic set of rules, because the appropriateness of any assay largely depends on the question being asked and the system being used. Moreover, no individual assay is perfect for every situation, calling for the use of multiple techniques to properly monitor autophagy in each experimental setting. Finally, several core components of the autophagy machinery have been implicated in distinct autophagic processes (canonical and noncanonical autophagy), implying that genetic approaches to block autophagy should rely on targeting two or more autophagy-related genes that ideally participate in distinct steps of the pathway. Along similar lines, because multiple proteins involved in autophagy also regulate other cellular pathways including apoptosis, not all of them can be used as a specific marker for bona fide autophagic responses. Here, we critically discuss current methods of assessing autophagy and the information they can, or cannot, provide. Our ultimate goal is to encourage intellectual and technical innovation in the field.
Published: 2021

14. Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition).

Author: Quadrilatero J., Walker D.W., Walker M.J., Walker S.A., Walter J., Wandosell F.G., Wang B., Wang C., Wang C.-Y., Wang D., Wang F., Wang G., Wang H., Wang H.-G., Wang J., Wang K., Wang L., Wang M.H., Wang M., Wang N., Wang P., Wang Q.J., Wang Q., Wang Q.K., Wang Q.A., Wang W.-T., Wang W., Wang X., Wang Y.-Y., Wang Y., Wang Z., Warnes G., Warnsmann V., Watada H., Watanabe E., Watchon M., Wawrzynska A., Weaver T.E., Wegrzyn G., Wehman A.M., Wei H., Wei L., Wei T., Wei Y., Weiergraber O.H., Weihl C.C., Weindl G., Weiskirchen R., Wells A., Wen R.H., Wen X., Werner A., Weykopf B., Wheatley S.P., W... [Ovid has truncated this field to avoid Excel character limitations], Klionsky D.J., Abdel-Aziz A.K., Abdelfatah S., Abdellatif M., Abdoli A., Abel S., Abeliovich H., Abildgaard M.H., Abudu Y.P., Acevedo-Arozena A., Adamopoulos I.E., Adeli K., Adolph T.E., Adornetto A., Aflaki E., Agam G., Agarwal A., Aggarwal B.B., Agnello M., Agostinis P., Agrewala J.N., Agrotis A., Aguilar P.V., Ahmad S.T., Ahmed Z.M., Ahumada-Castro U., Aits S., Aizawa S., Akkoc Y., Akoumianaki T., Akpinar H.A., Al-Abd A.M., Al-Akra L., Al-Gharaibeh A., Alaoui-Jamali M.A., Alberti S., Alcocer-Gomez E., Alessandri C., Ali M., Alim Al-Bari M.A., Aliwaini S., Alizadeh J., Almacellas E., Almasan A., Alonso A., Alonso G.D., Altan-Bonnet N., Altieri D.C., Alvarez E.M.C., Alves S., Alves da Costa C., Alzaharna M.M., Amadio M., Amantini C., Amaral C., Ambrosio S., Amer A.O., Ammanathan V., An Z., Andersen S.U., Andrabi S.A., Andrade-Silva M., Andres A.M., Angelini S., Ann D., Anozie U.C., Ansari M.Y., Antas P., Antebi A., 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Abstract: In 2008, we published the first set of guidelines for standardizing research in autophagy. Since then, this topic has received increasing attention, and many scientists have entered the field. Our knowledge base and relevant new technologies have also been expanding. Thus, it is important to formulate on a regular basis updated guidelines for monitoring autophagy in different organisms. Despite numerous reviews, there continues to be confusion regarding acceptable methods to evaluate autophagy, especially in multicellular eukaryotes. Here, we present a set of guidelines for investigators to select and interpret methods to examine autophagy and related processes, and for reviewers to provide realistic and reasonable critiques of reports that are focused on these processes. These guidelines are not meant to be a dogmatic set of rules, because the appropriateness of any assay largely depends on the question being asked and the system being used. Moreover, no individual assay is perfect for every situation, calling for the use of multiple techniques to properly monitor autophagy in each experimental setting. Finally, several core components of the autophagy machinery have been implicated in distinct autophagic processes (canonical and noncanonical autophagy), implying that genetic approaches to block autophagy should rely on targeting two or more autophagy-related genes that ideally participate in distinct steps of the pathway. Along similar lines, because multiple proteins involved in autophagy also regulate other cellular pathways including apoptosis, not all of them can be used as a specific marker for bona fide autophagic responses. Here, we critically discuss current methods of assessing autophagy and the information they can, or cannot, provide. Our ultimate goal is to encourage intellectual and technical innovation in the field.Copyright © 2020 Informa UK Limited, trading as Taylor & Francis Group.
Published: 2021

15. Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)1.

Author: Klionsky D.J., Abdel-Aziz A.K., Abdelfatah S., Abdellatif M., Abdoli A., Abel S., Abeliovich H., Abildgaard M.H., Abudu Y.P., Acevedo-Arozena A., Adamopoulos I.E., Adeli K., Adolph T.E., Adornetto A., Aflaki E., Agam G., Agarwal A., Aggarwal B.B., Agnello M., Agostinis P., Agrewala J.N., Agrotis A., Aguilar P.V., Ahmad S.T., Ahmed Z.M., Ahumada-Castro U., Aits S., Aizawa S., Akkoc Y., Akoumianaki T., Akpinar H.A., Al-Abd A.M., Al-Akra L., Al-Gharaibeh A., Alaoui-Jamali M.A., Alberti S., Alcocer-Gomez E., Alessandri C., Ali M., Alim Al-Bari M.A., Aliwaini S., Alizadeh J., Almacellas E., Almasan A., Alonso A., Alonso G.D., Altan-Bonnet N., Altieri D.C., Alvarez E.M.C., Alves S., Alves da Costa C., Alzaharna M.M., Amadio M., Amantini C., Amaral C., Ambrosio S., Amer A.O., Ammanathan V., An Z., Andersen S.U., Andrabi S.A., Andrade-Silva M., Andres A.M., Angelini S., Ann D., Anozie U.C., Ansari M.Y., Antas P., Antebi A., Anton Z., Anwar T., Apetoh L., Apostolova N., Araki T., Araki 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[Ovid has truncated this field to avoid Excel character limitations], Klionsky D.J., Abdel-Aziz A.K., Abdelfatah S., Abdellatif M., Abdoli A., Abel S., Abeliovich H., Abildgaard M.H., Abudu Y.P., Acevedo-Arozena A., Adamopoulos I.E., Adeli K., Adolph T.E., Adornetto A., Aflaki E., Agam G., Agarwal A., Aggarwal B.B., Agnello M., Agostinis P., Agrewala J.N., Agrotis A., Aguilar P.V., Ahmad S.T., Ahmed Z.M., Ahumada-Castro U., Aits S., Aizawa S., Akkoc Y., Akoumianaki T., Akpinar H.A., Al-Abd A.M., Al-Akra L., Al-Gharaibeh A., Alaoui-Jamali M.A., Alberti S., Alcocer-Gomez E., Alessandri C., Ali M., Alim Al-Bari M.A., Aliwaini S., Alizadeh J., Almacellas E., Almasan A., Alonso A., Alonso G.D., Altan-Bonnet N., Altieri D.C., Alvarez E.M.C., Alves S., Alves da Costa C., Alzaharna M.M., Amadio M., Amantini C., Amaral C., Ambrosio S., Amer A.O., Ammanathan V., An Z., Andersen S.U., Andrabi S.A., Andrade-Silva M., Andres A.M., Angelini S., Ann D., Anozie U.C., Ansari M.Y., Antas P., Antebi A., 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Onal G., Ondrej M., Ong S.-B., Ong S.-G., Onnis A., Orellana J.A., Orellana-Munoz S., Ortega-Villaizan M.D.M., Ortiz-Gonzalez X.R., Ortona E., Osiewacz H.D., Osman A.-H.K., Osta R., Otegui M.S., Otsu K., Ott C., Ottobrini L., Ou J.-H.J., Outeiro T.F., Oynebraten I., Ozturk M., Pages G., Pahari S., Pajares M., Pajvani U.B., Pal R., Paladino S., Pallet N., Palmieri M., Palmisano G., Palumbo C., Pampaloni F., Pan L., Pan Q., Pan W., Pan X., Panasyuk G., Pandey R., Pandey U.B., Pandya V., Paneni F., Pang S.Y., Panzarini E., Papademetrio D.L., Papaleo E., Papinski D., Papp D., Park E.C., Park H.T., Park J.-M., Park J.-I., Park J.T., Park J., Park S.C., Park S.-Y., Parola A.H., Parys J.B., Pasquier A., Pasquier B., Passos J.F., Pastore N., Patel H.H., Patschan D., Pattingre S., Pedraza-Alva G., Pedraza-Chaverri J., Pedrozo Z., Pei G., Pei J., Peled-Zehavi H., Pellegrini J.M., Pelletier J., Penalva M.A., Peng D., Peng Y., Penna F., Pennuto M., Pentimalli F., Pereira C.M.F., Pereira G.J.S., Pereira L.C., Pereira de Almeida L., Perera N.D., Perez-Lara A., Perez-Oliva A.B., Perez-Perez M.E., Periyasamy P., Perl A., Perrotta C., Perrotta I., Pestell R.G., Petersen M., Petrache I., Petrovski G., Pfirrmann T., Pfister A.S., Philips J.A., Pi H., Picca A., Pickrell A.M., Picot S., Pierantoni G.M., Pierdominici M., Pierre P., Pierrefite-Carle V., Pierzynowska K., Pietrocola F., Pietruczuk M., Pignata C., Pimentel-Muinos F.X., Pinar M., Pinheiro R.O., Pinkas-Kramarski R., Pinton P., Pircs K., Piya S., Pizzo P., Plantinga T.S., Platta H.W., Plaza-Zabala A., Plomann M., Plotnikov E.Y., Plun-Favreau H., Pluta R., Pocock R., Poggeler S., Pohl C., Poirot M., Poletti A., Ponpuak M., Popelka H., Popova B., Porta H., Porte Alcon S., Portilla-Fernandez E., Post M., Potts M.B., Poulton J., Powers T., Prahlad V., Prajsnar T.K., Pratico D., Prencipe R., Priault M., Proikas-Cezanne T., Promponas V.J., Proud C.G., Puertollano R., Puglielli L., Pulinilkunnil T., Puri D., Puri R., Puyal J., Qi X., Qi Y., Qian W., Qiang L., Qiu Y., Quadrilatero J., Quarleri J., Raben N., Rabinowich H., Ragona D., Ragusa M.J., Rahimi N., Rahmati M., Raia V., Raimundo N., Rajasekaran N.-S., Ramachandra Rao S., Rami A., Ramirez-Pardo I., Ramsden D.B., Randow F., Rangarajan P.N., Ranieri D., Rao H., Rao L., Rao R., Rathore S., Ratnayaka J.A., Ratovitski E.A., Ravanan P., Ravegnini G., Ray S.K., Razani B., Rebecca V., Reggiori F., Regnier-Vigouroux A., Reichert A.S., Reigada D., Reiling J.H., Rein T., Reipert S., Rekha R.S., Ren H., Ren J., Ren W., Renault T., Renga G., Reue K., Rewitz K., Ribeiro de Andrade Ramos B., Riazuddin S.A., Ribeiro-Rodrigues T.M., Ricci J.-E., Ricci R., Riccio V., Richardson D.R., Rikihisa Y., Risbud M.V., Risueno R.M., Ritis K., Rizza S., Rizzuto R., Roberts H.C., Roberts L.D., Robinson K.J., Roccheri M.C., Rocchi S., Rodney G.G., Rodrigues T., Rodrigues Silva V.R., Rodriguez A., Rodriguez-Barrueco R., Rodriguez-Henche N., Rodriguez-Rocha H., Roelofs J., Rogers R.S., Rogov V.V., Rojo A.I., Rolka K., Romanello V., Romani L., Romano A., Romano P.S., Romeo-Guitart D., Romero L.C., Romero M., Roney J.C., Rongo C., Roperto S., Rosenfeldt M.T., Rosenstiel P., Rosenwald A.G., Roth K.A., Roth L., Roth S., Rouschop K.M.A., Roussel B.D., Roux S., Rovere-Querini P., Roy A., Rozieres A., Ruano D., Rubinsztein D.C., Rubtsova M.P., Ruckdeschel K., Ruckenstuhl C., Rudolf E., Rudolf R., Ruggieri A., Ruparelia A.A., Rusmini P., Russell R.R., Russo G.L., Russo M., Russo R., Ryabaya O.O., Ryan K.M., Ryu K.-Y., Sabater-Arcis M., Sachdev U., Sacher M., Sachse C., Sadhu A., Sadoshima J., Safren N., Saftig P., Sagona A.P., Sahay G., Sahebkar A., Sahin M., Sahin O., Sahni S., Saito N., Saito S., Saito T., Sakai R., Sakai Y., Sakamaki J.-I., Saksela K., Salazar G., Salazar-Degracia A., Salekdeh G.H., Saluja A.K., Sampaio-Marques B., Sanchez M.C., Sanchez-Alcazar J.A., Sanchez-Vera V., Sancho-Shimizu V., Sanderson J.T., Sandri M., Santaguida S., Santambrogio L., Santana 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O., Vindis C., Viret C., Viscomi M.T., Visnjic D., Vitale I., Vocadlo D.J., Voitsekhovskaja O.V., Volonte C., Volta M., Vomero M., Von Haefen C., Vooijs M.A., Voos W., Vucicevic L., Wade-Martins R., Waguri S., Waite K.A., Wakatsuki S., Walker D.W., Walker M.J., Walker S.A., Walter J., Wandosell F.G., Wang B., Wang C., Wang C.-Y., Wang D., Wang F., Wang G., Wang H., Wang H.-G., Wang J., Wang K., Wang L., Wang M.H., Wang M., Wang N., Wang P., Wang Q.J., Wang Q., Wang Q.K., Wang Q.A., Wang W.-T., Wang W., Wang X., Wang Y.-Y., Wang Y., Wang Z., Warnes G., Warnsmann V., Watada H., Watanabe E., Watchon M., Wawrzynska A., Weaver T.E., Wegrzyn G., Wehman A.M., Wei H., Wei L., Wei T., Wei Y., Weiergraber O.H., Weihl C.C., Weindl G., Weiskirchen R., Wells A., Wen R.H., Wen X., Werner A., Weykopf B., Wheatley S.P., and W... [Ovid has truncated this field to avoid Excel character limitations]
Abstract: In 2008, we published the first set of guidelines for standardizing research in autophagy. Since then, this topic has received increasing attention, and many scientists have entered the field. Our knowledge base and relevant new technologies have also been expanding. Thus, it is important to formulate on a regular basis updated guidelines for monitoring autophagy in different organisms. Despite numerous reviews, there continues to be confusion regarding acceptable methods to evaluate autophagy, especially in multicellular eukaryotes. Here, we present a set of guidelines for investigators to select and interpret methods to examine autophagy and related processes, and for reviewers to provide realistic and reasonable critiques of reports that are focused on these processes. These guidelines are not meant to be a dogmatic set of rules, because the appropriateness of any assay largely depends on the question being asked and the system being used. Moreover, no individual assay is perfect for every situation, calling for the use of multiple techniques to properly monitor autophagy in each experimental setting. Finally, several core components of the autophagy machinery have been implicated in distinct autophagic processes (canonical and noncanonical autophagy), implying that genetic approaches to block autophagy should rely on targeting two or more autophagy-related genes that ideally participate in distinct steps of the pathway. Along similar lines, because multiple proteins involved in autophagy also regulate other cellular pathways including apoptosis, not all of them can be used as a specific marker for bona fide autophagic responses. Here, we critically discuss current methods of assessing autophagy and the information they can, or cannot, provide. Our ultimate goal is to encourage intellectual and technical innovation in the field.Copyright © 2020 Informa UK Limited, trading as Taylor & Francis Group.
Published: 2021

16. Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)

Author: Klionsky, D, Abdel-Aziz, A, Abdelfatah, S, Abdellatif, M, Abdoli, A, Abel, S, Abeliovich, H, Abildgaard, M, Abudu, Y, Acevedo-Arozena, A, Adamopoulos, I, Adeli, K, Adolph, T, Adornetto, A, Aflaki, E, Agam, G, Agarwal, A, Aggarwal, B, Agnello, M, Agostinis, P, Agrewala, J, Agrotis, A, Aguilar, P, Ahmad, S, Ahmed, Z, Ahumada-Castro, U, Aits, S, Aizawa, S, Akkoc, Y, Akoumianaki, T, Akpinar, H, Al-Abd, A, Al-Akra, L, Al-Gharaibeh, A, Alaoui-Jamali, M, Alberti, S, Alcocer-Gómez, E, Alessandri, C, Ali, M, Alim Al-Bari, M, Aliwaini, S, Alizadeh, J, Almacellas, E, Almasan, A, Alonso, A, Alonso, G, Altan-Bonnet, N, Altieri, D, Álvarez, É, Alves, S, Alves da Costa, C, Alzaharna, M, Amadio, M, Amantini, C, Amaral, C, Ambrosio, S, Amer, A, Ammanathan, V, An, Z, Andersen, S, Andrabi, S, Andrade-Silva, M, Andres, A, Angelini, S, Ann, D, Anozie, U, Ansari, M, Antas, P, Antebi, A, Antón, Z, Anwar, T, Apetoh, L, Apostolova, N, Araki, T, Araki, Y, Arasaki, K, Araújo, W, Araya, J, Arden, C, 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Abstract: In 2008, we published the first set of guidelines for standardizing research in autophagy. Since then, this topic has received increasing attention, and many scientists have entered the field. Our knowledge base and relevant new technologies have also been expanding. Thus, it is important to formulate on a regular basis updated guidelines for monitoring autophagy in different organisms. Despite numerous reviews, there continues to be confusion regarding acceptable methods to evaluate autophagy, especially in multicellular eukaryotes. Here, we present a set of guidelines for investigators to select and interpret methods to examine autophagy and related processes, and for reviewers to provide realistic and reasonable critiques of reports that are focused on these processes. These guidelines are not meant to be a dogmatic set of rules, because the appropriateness of any assay largely depends on the question being asked and the system being used. Moreover, no individual assay is perfect for every situation, calling for the use of multiple techniques to properly monitor autophagy in each experimental setting. Finally, several core components of the autophagy machinery have been implicated in distinct autophagic processes (canonical and noncanonical autophagy), implying that genetic approaches to block autophagy should rely on targeting two or more autophagy-related genes that ideally participate in distinct steps of the pathway. Along similar lines, because multiple proteins involved in autophagy also regulate other cellular pathways including apoptosis, not all of them can be used as a specific marker for bona fide autophagic responses. Here, we critically discuss current methods of assessing autophagy and the information they can, or cannot, provide. Our ultimate goal is to encourage intellectual and technical innovation in the field.
Published: 2021

17. Therapeutic Potential of AntagomiR-23b for Treating Myotonic Dystrophy

Author: Cerro-Herreros E, Gonzalez-Martinez I, Moreno-Cervera N, Overby S, Perez-Alonso M, Llamusi B, and Artero R
Subjects: musculoskeletal diseases, congenital, hereditary, and neonatal diseases and abnormalities
Abstract: Myotonic dystrophy type 1 (DM1) is a chronically debilitating, rare genetic disease that originates from an expansion of a noncoding CTG repeat in the dystrophia myotonica protein kinase (DMPK) gene. The expansion becomes pathogenic when DMPK transcripts contain 50 or more repetitions due to the sequestration of the muscleblind-like (MBNL) family of proteins. Depletion of MBNLs causes alterations in splicing patterns in transcripts that contribute to clinical symptoms such as myotonia and muscle weakness and wasting. We previously found that microRNA (miR)-23b directly regulates MBNL1 in DM1 myoblasts and mice and that antisense technology ("antagomiRs") blocking this microRNA (miRNA) boosts MBNL1 protein levels. Here, we show the therapeutic effect over time in response to administration of antagomiR-23b as a treatment in human skeletal actin long repeat (HSALR) mice. Subcutaneous administration of antagomiR-23b upregulated the expression of MBNL1 protein and rescued splicing alterations, grip strength, and myotonia in a dose-dependent manner with long-lasting effects. Additionally, the effects of the treatment on grip strength and myotonia were still slightly notable after 45days. The pharmacokinetic data obtained provide further evidence that miR-23b could be a valid therapeutic target for DM1. Copyright © 2020 The Authors. Published by Elsevier Inc. All rights reserved.
Published: 2020

18. miR-7 Restores Phenotypes in Myotonic Dystrophy Muscle Cells by Repressing Hyperactivated Autophagy

Author: Sabater-Arcis M, Bargiela A, Furling D, and Artero R
Subjects: musculoskeletal diseases, CTG expansions, Muscleblind, Myotonic Dystrophy, UPS system, autophagy, miR-7, miRNA, muscle atrophy, oligonucleotide, therapy
Abstract: Unstable CTG expansions in the 3' UTR of the DMPK gene are responsible for myotonic dystrophy type 1 (DM1) condition. Muscle dysfunction is one of the main contributors to DM1 mortality and morbidity. Pathways by which mutant DMPK trigger muscle defects, however, are not fully understood. We previously reported that miR-7 was downregulated in a DM1 Drosophila model and in biopsies from patients. Here, using DM1 and normal muscle cells, we investigated whether miR-7 contributes to the muscle phenotype by studying the consequences of replenishing or blocking miR-7, respectively. Restoration of miR-7 with agomiR-7 was sufficient to rescue DM1 myoblast fusion defects and myotube growth. Conversely, oligonucleotide-mediated blocking of miR-7 in normal myoblasts led to fusion and myotube growth defects. miR-7 was found to regulate autophagy and the ubiquitin-proteasome system in human muscle cells. Thus, low levels of miR-7 promoted both processes, and high levels of miR-7 repressed them. Furthermore, we uncovered that the mechanism by which miR-7 improves atrophy-related phenotypes is independent of MBNL1, thus suggesting that miR-7 acts downstream or in parallel to MBNL1. Collectively, these results highlight an unknown function for miR-7 in muscle dysfunction through autophagy- and atrophy-related pathways and support that restoration of miR-7 levels is a candidate therapeutic target for counteracting muscle dysfunction in DM1.
Published: 2020

19. Protective effects of mirtazapine in mice lacking the Mbnl2 gene in forebrain glutamatergic neurons: Relevance for myotonic dystrophy 1

Author: Ramon-Duaso C, Rodríguez-Morató J, Selma-Soriano E, Fernández-Avilés C, Artero R, de la Torre R, Pozo ÓJ, and Robledo P
Subjects: nervous system, Cognitive deficits, DM1, Dentate gyrus, Depression, Inflammation, Neuronal loss
Abstract: Myotonic dystrophy type 1 (DM1) is a multisystemic disorder characterized by muscle weakness and wasting and by important central nervous system-related symptoms including impairments in executive functions, spatial abilities and increased anxiety and depression. The Mbnl2 gene has been implicated in several phenotypes consistent with DM1 neuropathology. In this study, we developed a tissue-specific knockout mouse model lacking the Mbnl2 gene in forebrain glutamatergic neurons to examine its specific contribution to the neurobiological perturbations related to DM1. We found that these mice exhibit long-term cognitive deficits and a depressive-like state associated with neuronal loss, increased microglia and decreased neurogenesis, specifically in the dentate gyrus (DG). Chronic treatment with the atypical antidepressant mirtazapine (3 and 10mg/kg) for 21 days rescued these behavioral alterations, reduced inflammatory microglial overexpression, and reversed neuronal loss in the DG. We also show that mirtazapine re-established 5-HT1A and histaminergic H1 receptor gene expression in the hippocampus. Finally, metabolomics studies indicated that mirtazapine increased serotonin, noradrenaline, gamma-aminobutyric acid and adenosine production. These data suggest that loss of Mbnl2 gene in the glutamatergic neurons of hippocampus and cortex may underlie the most relevant DM1 neurobiological and behavioral features, and provide evidence that mirtazapine could be a novel potential candidate to alleviate these debilitating symptoms in DM1 patients. Copyright © 2020 Elsevier Ltd. All rights reserved.
Published: 2020

20. Drosophila SMN2 minigene reporter model identifies moxifloxacin as a candidate therapy for SMA

Author: Konieczny P and Artero R
Subjects: splicing, drug repurposing, SMA, SMA, SMN2, drug repurposing, splicing, SMN2, nervous system diseases
Abstract: Spinal muscular atrophy is a rare and fatal neuromuscular disorder caused by the loss of alpha motor neurons. The affected individuals have mutated the ubiquitously expressed SMN1 gene resulting in the loss or reduction in the survival motor neuron (SMN) protein levels. However, an almost identical paralog exists in humans: SMN2. Pharmacological activation of SMN2 exon 7 inclusion by small molecules or modified antisense oligonucleotides is a valid approach to treat SMA. Here we describe an in vivo SMN2 minigene reporter system in Drosophila motor neurons that serves as a cost-effective, feasible, and stringent primary screening model for identifying chemicals capable of crossing the conserved Drosophila blood-brain barrier and modulating exon 7 inclusion. The model was used for the screening of 1100 drugs from the Prestwick Chemical Library, resulting in 2.45% hit rate. The most promising candidate drugs were validated in patient-derived fibroblasts where they proved to increase SMN protein levels. Among them, moxifloxacin modulated SMN2 splicing by promoting exon 7 inclusion. The recovery of SMN protein levels was confirmed by increased colocalization of nuclear gems with Cajal Bodies. Thus, a Drosophila-based drug screen allowed the discovery of an FDA-approved small molecule with the potential to become a novel therapy for SMA.
Published: 2020

21. Electron Microscopic In Situ Hybridization of Digoxigenin-dUTP-labelled DNA Probes with Drosophila Melanogaster Polytene Chromosomes

Author: Semeshin, V. F., Artero, R., Perez-alonso, M., and Shloma, V. V.
Published: 1998
Full Text: View/download PDF

22. MicroRNA-Based Therapeutic Perspectives in Myotonic Dystrophy

Author: Lopez Castel A, Overby S, and Artero R
Published: 2019

23. Stage, tissue, and cell specific distribution of alternative Ultrabithorax mRNAs and protein isoforms in the Drosophila embryo

Author: López, A. J., Artero, R. D., and Pérez-Alonso, M.
Published: 1996
Full Text: View/download PDF

24. RNA-mediated therapies in myotonic dystrophy

Author: Overby SJ, Cerro-Herreros E, Llamusi B, and Artero R
Subjects: musculoskeletal diseases, congenital, hereditary, and neonatal diseases and abnormalities
Abstract: Myotonic dystrophy 1 (DM1) is a multisystemic neuromuscular disease caused by a dominantly inherited `CTG' repeat expansion in the gene encoding DM Protein Kinase (DMPK). The repeats are transcribed into mRNA, which forms hairpins and binds with high affinity to the Muscleblind-like (MBNL) family of proteins, sequestering them from their normal function. The loss of function of MBNL proteins causes numerous downstream effects, primarily the appearance of nuclear foci, mis-splicing, and ultimately myotonia and other clinical symptoms. Antisense and other RNA-mediated technologies have been applied to target toxic-repeat mRNA transcripts to restore MBNL protein function in DM1 models, such as cells and mice, and in humans. This technique has had promising results in DM1 therapeutics by alleviating pathogenic phenotypes.
Published: 2018

25. Optical Cross-Sectional Muscle Area Determination of Drosophila Melanogaster Adult Indirect Flight Muscles

Author: Selma-Soriano E, Artero R, and Llamusi B
Subjects: Muscle Atrophy, Issue 133, Indirect Flight Muscles, Drosophila Melanogaster, fungi, Muscle Degeneration, Neuromuscular Diseases, Muscle Area Determination, Biology
Abstract: Muscle mass wasting, known as muscle atrophy, is a common phenotype in Drosophila models of neuromuscular diseases. We have used the indirect flight muscles (IFMs) of flies, specifically the dorso-longitudinal muscles (DLM), as the experimental subject to measure the atrophic phenotype brought about by different genetic causes. In this protocol, we describe how to embed fly thorax muscles for semi thin sectioning, how to obtain a good contrast between muscle and the surrounding tissue, and how to process optical microscope images for semiautomatic acquisition of quantifiable data and analysis. We describe three specific applications of the methodological pipeline. First, we show how the method can be applied to quantify muscle degeneration in a myotonic dystrophy fly model; second, measurement of muscle cross-sectional area can help to identify genes that either promote or prevent muscle atrophy and/or muscle degeneration; third, this protocol can be applied to determine whether a candidate compound is able to significantly modify a given atrophic phenotype induced by a disease-causing mutation or by an environmental trigger.
Published: 2018

26. rbFOX1/MBNL1 competition for CCUG RNA repeats binding contributes to myotonic dystrophy type 1/type 2 differences

Author: Sellier C, Cerro-Herreros E, Blatter M, Freyermuth F, Gaucherot A, Ruffenach F, Sarkar P, Puymirat J, Udd B, Day JW, Meola G, Bassez G, Fujimura H, Takahashi MP, Schoser B, Furling D, Artero R, Allain FHT, Llamusi B, and Charlet-Berguerand N
Published: 2018

27. Daunorubicin reduces MBNL1 sequestration caused by CUG-repeat expansion and rescues cardiac dysfunctions in a Drosophila model of myotonic dystrophy

Author: Chakraborty M, Sellier C, Ney M, Pascal V, Charlet-Berguerand N, Artero R, and Llamusi B
Subjects: congenital, hereditary, and neonatal diseases and abnormalities, Trinucleotide repeat disorder, Daunorubicin, Myotonic dystrophy, Drosophila, Muscleblind
Abstract: Myotonic dystrophy (DM) is a dominantly inherited neuromuscular disorder caused by expression of mutant myotonin- protein kinase (DMPK) transcripts containing expanded CUG repeats. Pathogenic DMPK RNA sequesters the muscleblind-like (MBNL) proteins, causing alterations in metabolism of various RNAs. Cardiac dysfunction represents the second most common cause of death in DM type 1 (DM1) patients. However, the contribution of MBNL sequestration in DM1 cardiac dysfunction is unclear. We overexpressed Muscleblind (Mbl), the Drosophila MBNL orthologue, in cardiomyocytes of DM1 model flies and observed a rescue of heart dysfunctions, which are characteristic of these model flies and resemble cardiac defects observed in patients. We also identified a drug - daunorubicin hydrochloride - that directly binds to CUG repeats and alleviates Mbl sequestration in Drosophila DM1 cardiomyocytes, resulting in missplicing rescue and cardiac function recovery. These results demonstrate the relevance of Mbl sequestration caused by expanded-CUG-repeat RNA in cardiac dysfunctions in DM1, and highlight the potential of strategies aimed at inhibiting this protein-RNA interaction to recover normal cardiac function.
Published: 2018

28. miR-23b and miR-218 silencing increase Muscleblind-like expression and alleviate myotonic dystrophy phenotypes in mammalian models

Author: Cerro-Herreros E, Sabater-Arcis M, Fernandez-Costa J, Moreno N, Perez-Alonso M, Llamusi B, and Artero R
Subjects: musculoskeletal diseases, congenital, hereditary, and neonatal diseases and abnormalities
Abstract: Functional depletion of the alternative splicing factors Muscleblind-like (MBNL 1 and 2) is at the basis of the neuromuscular disease myotonic dystrophy type 1 (DM1). We previously showed the efficacy of miRNA downregulation in Drosophila DM1 model. Here, we screen for miRNAs that regulate MBNL1 and MBNL2 in HeLa cells. We thus identify miR-23b and miR218, and confirm that they downregulate MBNL proteins in this cell line. Antagonists of miR23b and miR-218 miRNAs enhance MBNL protein levels and rescue pathogenic missplicing events in DM1 myoblasts. Systemic delivery of these "antagomiRs" similarly boost MBNL expression and improve DM1-like phenotypes, including splicing alterations, histopathology, and myotonia in the HSA(LR) DM1 model mice. These mammalian data provide evidence for therapeutic blocking of the miRNAs that control Muscleblind-like protein expression in myotonic dystrophy.
Published: 2018

29. Modeling of Myotonic Dystrophy Cardiac Phenotypes in Drosophila

Author: Chakraborty M, Llamusi B, and Artero R
Subjects: myotonic dystrophy, cardiac dysfunction, CTG expansion, CCTG expansion, Drosophila disease model, Muscleblind, drugs
Abstract: After respiratory distress, cardiac dysfunction is the second most common cause of fatality associated with the myotonic dystrophy (DM) disease. Despite the prevalance of heart failure in DM, physiopathological studies on heart symptoms have been relatively scarce because few murine models faithfully reproduce the cardiac disease. Consequently, only a small number of candidate compounds have been evaluated in this specific phenotype. To help cover this gap Drosophila combines the amenability of its invertebrate genetics with the possibility of quickly acquiring physiological parameters suitable for meaningful comparisons with vertebrate animal models and humans. Here we review available descriptions of cardiac disease in DM type 1 and type 2, and three recent papers reporting the cardiac toxicity of non-coding CUG (DM1) and CCUG (DM2) repeat RNA in flies. Notably, flies expressing CUG or CCUG RNA in their hearts developed strong arrhythmias and had reduced fractional shortening, which correlates with similar phenotypes in DM patients. Overexpression of Muscleblind, which is abnormally sequestered by CUG and CCUG repeat RNA, managed to strongly suppress arrhythmias and fractional shortening, thus demonstrating that Muscleblind depletion causes cardiac phenotypes in flies. Importantly, small molecules pentamidine and daunorubicin were able to rescue cardiac phenotypes by releasing Muscleblind from sequestration. Taken together, fly heart models have the potential to make important contributions to the understanding of the molecular causes of cardiac dysfunction in DM and in the quick assessment of candidate therapeutics.
Published: 2018

30. The Drosophila junctophilin gene is functionally equivalent to its four mammalian counterparts and is a modifier of a Huntingtin poly-Q expansion and the Notch pathway

Author: Universitat Politècnica de València. Departamento de Biotecnología - Departament de Biotecnologia, Generalitat Valenciana, Instituto de Salud Carlos III, Centro de Investigación Príncipe Felipe, Association Française contre les Myopathies, International Rare Diseases Research Consortium, Calpena-Corpas, Eduardo, Lopez del Amo, V, Chakraborty M, Llamusi, B, Artero R, Espinos, Carmen, Galindo, Máximo Ibo, Universitat Politècnica de València. Departamento de Biotecnología - Departament de Biotecnologia, Generalitat Valenciana, Instituto de Salud Carlos III, Centro de Investigación Príncipe Felipe, Association Française contre les Myopathies, International Rare Diseases Research Consortium, Calpena-Corpas, Eduardo, Lopez del Amo, V, Chakraborty M, Llamusi, B, Artero R, Espinos, Carmen, and Galindo, Máximo Ibo
Abstract: [EN] Members of the Junctophilin (JPH) protein family have emerged as key actors in all excitable cells, with crucial implications for human pathophysiology. In mammals, this family consists of four members (JPH1-JPH4) that are differentially expressed throughout excitable cells. The analysis of knockout mice lacking JPH subtypes has demonstrated their essential contribution to physiological functions in skeletal and cardiac muscles and in neurons. Moreover, mutations in the human JPH2 gene are associated with hypertrophic and dilated cardiomyopathies; mutations in JPH3 are responsible for the neurodegenerative Huntington's disease-like-2 (HDL2), whereas JPH1 acts as a genetic modifier in Charcot-Marie-Tooth 2K peripheral neuropathy. Drosophila melanogaster has a single junctophilin (jp) gene, as is the case in all invertebrates, which might retain equivalent functions of the four homologous JPH genes present in mammalian genomes. Therefore, owing to the lack of putatively redundant genes, a jp Drosophila model could provide an excellent platform to model the Junctophilin-related diseases, to discover the ancestral functions of the JPH proteins and to reveal new pathways. By up-and downregulation of Jp in a tissue-specific manner in Drosophila, we show that altering its levels of expression produces a phenotypic spectrum characterized by muscular deficits, dilated cardiomyopathy and neuronal alterations. Importantly, our study has demonstrated that Jp modifies the neuronal degeneration in a Drosophila model of Huntington's disease, and it has allowed us to uncover an unsuspected functional relationship with the Notch pathway. Therefore, this Drosophila model has revealed new aspects of Junctophilin function that can be relevant for the disease mechanisms of their human counterparts.
Published: 2018

31. In silico discovery of substituted pyrido[2,3-d] pyrimidines and pentamidine-like compounds with biological activity in myotonic dystrophy models

Author: González ÀL, Konieczny P, Llamusi B, Delgado-Pinar E, Borrell JI, Teixidó J, García-España E, Pérez-Alonso M, Estrada-Tejedor R, and Artero R
Subjects: congenital, hereditary, and neonatal diseases and abnormalities
Abstract: Myotonic dystrophy type 1 (DM1) is a rare multisystemic disorder associated with an expansion of CUG repeats in mutant DMPK (dystrophia myotonica protein kinase) transcripts; the main effect of these expansions is the induction of pre-mRNA splicing defects by sequestering muscleblind-like family proteins (e.g. MBNL1). Disruption of the CUG repeats and the MBNL1 protein complex has been established as the best therapeutic approach for DM1, hence two main strategies have been proposed: targeted degradation of mutant DMPK transcripts and the development of CUG-binding molecules that prevent MBNL1 sequestration. Herein, suitable CUG-binding small molecules were selected using in silico approaches such as scaffold analysis, similarity searching, and druggability analysis. We used polarization assays to confirm the CUG repeat binding in vitro for a number of candidate compounds, and went on to evaluate the biological activity of the two with the strongest affinity for CUG repeats (which we refer to as compounds 1-2 and 2-5) in DM1 mutant cells and Drosophila DM1 models with an impaired locomotion phenotype. In particular, 1-2 and 2-5 enhanced the levels of free MBNL1 in patient-derived myoblasts in vitro and greatly improved DM1 fly locomotion in climbing assays. This work provides new computational approaches for rational large-scale virtual screens of molecules that selectively recognize CUG structures. Moreover, it contributes valuable knowledge regarding two compounds with desirable biological activity in DM1 models.
Published: 2017

32. Myotonic dystrophy: candidate small molecule therapeutics

Author: Konieczny P, Selma-Soriano E, Rapisarda AS, Fernandez-Costa JM, Perez-Alonso M, and Artero R
Subjects: musculoskeletal diseases, congenital, hereditary, and neonatal diseases and abnormalities
Abstract: Myotonic dystrophy type 1 (DM1) is a rare multisystemic neuromuscular disorder caused by expansion of CTG trinucleotide repeats in the noncoding region of the DMPK gene. Mutant DMPK transcripts are toxic and alter gene expression at several levels. Chiefly, the secondary structure formed by CUGs has a strong propensity to capture and retain proteins, like those of the muscleblind-like (MBNL) family. Sequestered MBNL proteins cannot then fulfill their normal functions. Many therapeutic approaches have been explored to reverse these pathological consequences. Here, we review the myriad of small molecules that have been proposed for DM1, including examples obtained from computational rational design, HTS, drug repurposing and therapeutic gene modulation.
Published: 2017

33. Expanded CCUG repeat RNA expression in Drosophila heart and muscle trigger Myotonic Dystrophy type 1-like phenotypes and activate autophagocytosis genes

Author: Cerro-Herreros E, Chakraborty M, Pérez-Alonso M, Artero R, and Llamusí B
Subjects: musculoskeletal diseases, congenital, hereditary, and neonatal diseases and abnormalities
Abstract: Myotonic dystrophies (DM1-2) are neuromuscular genetic disorders caused by the pathological expansion of untranslated microsatellites. DM1 and DM2, are caused by expanded CTG repeats in the 3' UTR of the DMPK gene and CCTG repeats in the first intron of the CNBP gene, respectively. Mutant RNAs containing expanded repeats are retained in the cell nucleus, where they sequester nuclear factors and cause alterations in RNA metabolism. However, for unknown reasons, DM1 is more severe than DM2. To study the differences and similarities in the pathogenesis of DM1 and DM2, we generated model flies by expressing pure expanded CUG ([250]x) or CCUG ([1100]x) repeats, respectively, and compared them with control flies expressing either 20 repeat units or GFP. We observed surprisingly severe muscle reduction and cardiac dysfunction in CCUG-expressing model flies. The muscle and cardiac tissue of both DM1 and DM2 model flies showed DM1-like phenotypes including overexpression of autophagy-related genes, RNA mis-splicing and repeat RNA aggregation in ribonuclear foci along with the Muscleblind protein. These data reveal, for the first time, that expanded non-coding CCUG repeat-RNA has similar in vivo toxicity potential as expanded CUG RNA in muscle and heart tissues and suggests that specific, as yet unknown factors, quench CCUG-repeat toxicity in DM2 patients.
Published: 2017

34. In silico discovery of substituted pyrido[2,3-d]pyrimidines and pentamidine-like compounds with biological activity in myotonic dystrophy models

Author: González ÀL, Konieczny P, Llamusi B, Delgado-Pinar E, Borrell JI, Teixidó J, García-España E, Pérez-Alonso M, Estrada-Tejedor R, and Artero R
Published: 2017

35. Muscleblind-like 1 regulates epithelial to mesenchymal transition markers in triple-negative breast cancer

Author: Adam Artigues, A., primary, Tormo, E., additional, Cerro-Herreros, E., additional, Sabater, M., additional, Garrido-Cano, I., additional, Pineda Merlo, B., additional, Pattanayak, B., additional, Cabello, P., additional, Artero, R., additional, and Eroles, P., additional
Published: 2018
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36. NMR solution structure of the TSL2 RNA hairpin

Author: Garcia-Lopez, A., primary, Wacker, A., additional, Tessaro, F., additional, Jonker, H.R.A., additional, Richter, C., additional, Comte, A., additional, Berntenis, N., additional, Schmucki, R., additional, Hatje, K., additional, Sciarra, D., additional, Konieczny, P., additional, Fournet, G., additional, Faustino, I., additional, Orozco, M., additional, Artero, R., additional, Goekjian, P., additional, Metzger, F., additional, Ebeling, M., additional, Joseph, B., additional, Schwalbe, H., additional, and Scapozza, L., additional
Published: 2018
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37. Daunorubicin reduces MBNL1 titration by expanded CUG repeat RNA and rescues cardiac dysfunctions in a Drosophila model of myotonic dystrophy

Author: Chakraborty, M., primary, Sellier, Chantal, additional, Ney, Michel, additional, Villa, Pascal, additional, Charlet-Berguerand, Nicolas, additional, Artero, R., additional, and Llamusi, B., additional
Published: 2018
Full Text: View/download PDF

38. Derepressing muscleblind expression by miRNA sponges ameliorates myotonic dystrophy-like phenotypes in Drosophila

Author: Cerro-Herreros E, Fernandez-Costa J, Sabater-Arcis M, Llamusi B, and Artero R
Published: 2016

39. Six Serum miRNAs Fail to Validate as Myotonic Dystrophy Type 1 Biomarkers

Author: Fernandez-Costa J, Llamusi B, Bargiela A, Zulaica M, Alvarez-Abril M, Perez-Alonso M, de Munain A, Lopez-Castel A, and Artero R
Published: 2016

40. Dificultades y errores en matemáticas en la prueba de ingreso al cuerpo de maestros

Author: Nortes-Martínez-Artero, R. and Nortes-Checa, A.
Subjects: Dificultades, Matemáticas, Didáctica de la Matemática, Grado de Maestro de Primaria, Errores
Published: 2015

41. Difficulties and errors in Mathematics in the public exam to become Primary Teachers

Author: Nortes-Martínez-Artero, R. and Nortes-Checa, A.
Subjects: Dificultades, Matemáticas, Didáctica de la Matemática, Grado de Maestro de Primaria, Errores
Published: 2015

42. Increased autophagy and apoptosis contribute to muscle atrophy in a myotonic dystrophy type 1 Drosophila model

Author: Bargiela A, Cerro-Herreros E, Fernandez-Costa JM, Vilchez JJ, Llamusi B, and Artero R
Subjects: congenital, hereditary, and neonatal diseases and abnormalities, CTG repeat expansion, Autophagy, Apoptosis, Muscle atrophy, Dystrophy, Muscleblind
Abstract: Muscle mass wasting is one of the most debilitating symptoms of myotonic dystrophy type 1 (DM1) disease, ultimately leading to immobility, respiratory defects, dysarthria, dysphagia and death in advanced stages of the disease. In order to study the molecular mechanisms leading to the degenerative loss of adult muscle tissue in DM1, we generated an inducible Drosophila model of expanded CTG trinucleotide repeat toxicity that resembles an adult-onset form of the disease. Heat-shock induced expression of 480 CUG repeats in adult flies resulted in a reduction in the area of the indirect flight muscles. In these model flies, reduction of muscle area was concomitant with increased apoptosis and autophagy. Inhibition of apoptosis or autophagy mediated by the overexpression of DIAP1, mTOR (also known as Tor) or muscleblind, or by RNA interference (RNAi)-mediated silencing of autophagy regulatory genes, achieved a rescue of the muscle-loss phenotype. In fact, mTOR overexpression rescued muscle size to a size comparable to that in control flies. These results were validated in skeletal muscle biopsies from DM1 patients in which we found downregulated autophagy and apoptosis repressor genes, and also in DM1 myoblasts where we found increased autophagy. These findings provide new insights into the signaling pathways involved in DM1 disease pathogenesis.
Published: 2015

43. 102P - Muscleblind-like 1 regulates epithelial to mesenchymal transition markers in triple-negative breast cancer

Author: Adam Artigues, A., Tormo, E., Cerro-Herreros, E., Sabater, M., Garrido-Cano, I., Pineda Merlo, B., Pattanayak, B., Cabello, P., Artero, R., and Eroles, P.
Published: 2018
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44. A practical approach to FRET-based PNA fluorescence in situ hybridization

Author: Blanco AM and Artero R
Subjects: biological sciences
Abstract: Given the demand for improved methods for detecting and characterizing RNA variants in situ, we developed a quantitative method for detecting RNA alternative splicing variants that combines in situ hybridization of fluorescently labeled peptide nucleic acid (PNA) probes with confocal microscopy Förster resonance energy transfer (FRET). The use of PNA probes complementary to sequences flanking a given splice junction allows to specifically quantify, within the cell, the RNA isoform generating such splice junction as FRET efficiency measure. The FRET-based PNA fluorescence in situ hybridization (FP-FISH) method offers a conceptually new approach for characterizing at the subcellular level not only splice variant isoform structure, location, and dynamics but also potentially a wide variety of close range RNA-RNA interactions. In this paper, we explain the FP-FISH technique workflow for reliable and reproducible results.
Published: 2010

45. A FRET-based assay for characterization of alternative splicing events using peptide nucleic acid fluorescence in situ hybridization

Author: Blanco AM, Rausell L, Aguado B, Perez-Alonso M, and Artero R
Abstract: We describe a quantitative method for detecting RNA alternative splicing variants that combines in situ hybridization of fluorescently labeled peptide nucleic acid (PNA) probes with confocal microscopy Förster resonance energy transfer (FRET). The use of PNA probes complementary to sequences flanking a given splice junction allows to specifically quantify, within the cell, the RNA isoform generating such splice junction by FRET measure. As a proof of concept we analyzed two alternative splicing events originating from lymphocyte antigen 6 (LY6) complex, locus G5B (LY6G5B) pre-mRNA. These are characterized by the removal of the first intron (Fully Spliced Isoform, FSI) or by retention of such intron (Intron-Retained Isoform, IRI). The use of PNA probe pairs labeled with donor (Cy3) and acceptor (Cy5) fluorophores, suitable to FRET, flanking FSI and IRI specific splice junctions specifically detected both mRNA isoforms in HeLa cells. We have observed that the method works efficiently with probes 5-11 nt apart. The data supports that this FRET-based PNA fluorescence in situ hybridization (FP-FISH) method offers a conceptually new approach for characterizing at the subcellular level not only splice variant isoform structure, location and dynamics but also potentially a wide variety of close range RNA-RNA interactions.
Published: 2009

46. Mutations in the EPHA2 Gene Are a Major Contributor to Inherited Cataracts in South-Eastern Australia

Author: Artero, R, Dave, A, Laurie, K, Staffieri, SE, Taranath, D, Mackey, DA, Mitchell, P, Wang, JJ, Craig, JE, Burdon, KP, Sharma, S, Artero, R, Dave, A, Laurie, K, Staffieri, SE, Taranath, D, Mackey, DA, Mitchell, P, Wang, JJ, Craig, JE, Burdon, KP, and Sharma, S
Abstract: Congenital cataract is the most common cause of treatable visual impairment in children worldwide. Mutations in many different genes lead to congenital cataract. Recently, mutations in the receptor tyrosine kinase gene, EPHA2, have been found to cause congenital cataract in six different families. Although these findings have established EPHA2 as a causative gene, the total contribution of mutations in this gene to congenital cataract is unknown. In this study, for the first time, a population-based approach was used to investigate the frequency of disease causing mutations in the EPHA2 gene in inherited cataract cases in South-Eastern Australia. A cohort of 84 familial congenital or juvenile cataract index cases was screened for mutations in the EPHA2 gene by direct sequencing. Novel changes were assessed for segregation with the disease within the family and in unrelated controls. Microsatellite marker analysis was performed to establish any relationship between families carrying the same mutation. We report a novel congenital cataract causing mutation c.1751C>T in the EPHA2 gene and the previously reported splice mutation c.2826-9G>A in two new families. Additionally, we report a rare variant rs139787163 potentially associated with increased susceptibility to cataract. Thus mutations in EPHA2 account for 4.7% of inherited cataract cases in South-Eastern Australia. Interestingly, the identified rare variant provides a link between congenital and age-related cataract.
Published: 2013

47. muscleblind, a gene required for photoreceptor differentiation in Drosophila, encodes novel nuclear Cys3His-type zinc-finger-containing proteins

Author: Begemann, G., primary, Paricio, N., additional, Artero, R., additional, Kiss, I., additional, Perez-Alonso, M., additional, and Mlodzik, M., additional
Published: 1997
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48. Stage, tissue, and cell specific distribution of alternative Ultrabithorax mRNAs and protein isoforms in the Drosophila embryo

Author: L�pez, A. J., primary, Artero, R. D., additional, and P�rez-Alonso, M., additional
Published: 1996
Full Text: View/download PDF

49. Poly(dC) segments and cloning artifacts in databases.

Author: Paricio, N, primary, Terol, J, additional, Artero, R D, additional, and Pérez-Alonso, M, additional
Published: 1995
Full Text: View/download PDF

50. The immunoglobulin-like protein Hibris functions as a dose-dependent regulator of myoblast fusion and is differentially controlled by Ras and Notch signaling.

Author: Artero, R D, Castanon, I, and Baylies, M K
Abstract: Hibris (Hbs) is a transmembrane immunoglobulin-like protein that shows extensive homology to Drosophila Sticks and stones (Sns) and human kidney protein Nephrin. Hbs is expressed in embryonic visceral, somatic and pharyngeal mesoderm among other tissues. In the somatic mesoderm, Hbs is restricted to fusion competent myoblasts and is regulated by Notch and Ras signaling pathways. Embryos that lack or overexpress hbs show a partial block of myoblast fusion, followed by abnormal muscle morphogenesis. Abnormalities in visceral mesoderm are also observed. In vivo mapping of functional domains suggests that the intracellular domain mediates Hbs activity. Hbs and its paralog, Sns, co-localize at the cell membrane of fusion-competent myoblasts. The two proteins act antagonistically: loss of sns dominantly suppresses the hbs myoblast fusion and visceral mesoderm phenotypes, and enhances Hbs overexpression phenotypes. Data from a P-homed enhancer reporter into hbs and co-localization studies with Sns suggest that hbs is not continuously expressed in all fusion-competent myoblasts during the fusion process. We propose that the temporal pattern of hbs expression within fusion-competent myoblasts may reflect previously undescribed functional differences within this myoblast population.
Published: 2001

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