321 results on '"Reue K"'
Search Results
2. Limiting Cholesterol Biosynthetic Flux Spontaneously Engages Type i IFN Signaling
- Author
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York, AG, Williams, KJ, Argus, JP, Zhou, QD, Brar, G, Vergnes, L, Gray, EE, Zhen, A, Wu, NC, Yamada, DH, Cunningham, CR, Tarling, EJ, Wilks, MQ, Casero, D, Gray, DH, Yu, AK, Wang, ES, Brooks, DG, Sun, R, Kitchen, SG, Wu, TT, Reue, K, Stetson, DB, and Bensinger, SJ
- Subjects
Biological Sciences ,Medical and Health Sciences ,Developmental Biology - Abstract
Cellular lipid requirements are achieved through a combination of biosynthesis and import programs. Using isotope tracer analysis, we show that type I interferon (IFN) signaling shifts the balance of these programs by decreasing synthesis and increasing import of cholesterol and long chain fatty acids. Genetically enforcing this metabolic shift in macrophages is sufficient to render mice resistant to viral challenge, demonstrating the importance of reprogramming the balance of these two metabolic pathways in vivo. Unexpectedly, mechanistic studies reveal that limiting flux through the cholesterol biosynthetic pathway spontaneously engages a type I IFN response in a STING-dependent manner. The upregulation of type I IFNs was traced to a decrease in the pool size of synthesized cholesterol and could be inhibited by replenishing cells with free cholesterol. Taken together, these studies delineate a metabolic-inflammatory circuit that links perturbations in cholesterol biosynthesis with activation of innate immunity.
- Published
- 2015
3. Sex-specific genetic regulation of adipose mitochondria and metabolic syndrome by Ndufv2
- Author
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K Chella Krishnan, Vergnes L, Acin-Perez R, Stiles L, Shum M, Ma L, Mouisel E, Pan C, Moore TM, Peterfy M, Romanoski CE, Reue K, Bjorkegren JLM, Laakso M, Liesa M, and Lusis AJ
- Subjects
General Economics, Econometrics and Finance - Published
- 2022
4. Proteome-wide systems genetics identifies UFMylation as a regulator of skeletal muscle function
- Author
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Molendijk, J, Blazev, R, Mills, RJ, Ng, Y-K, Watt, K, Chau, D, Gregorevic, P, Crouch, PJ, Hilton, JBW, Lisowski, L, Zhang, P, Reue, K, Lusis, AJ, Hudson, JE, James, DE, Seldin, MM, Parker, BL, Molendijk, J, Blazev, R, Mills, RJ, Ng, Y-K, Watt, K, Chau, D, Gregorevic, P, Crouch, PJ, Hilton, JBW, Lisowski, L, Zhang, P, Reue, K, Lusis, AJ, Hudson, JE, James, DE, Seldin, MM, and Parker, BL
- Abstract
Improving muscle function has great potential to improve the quality of life. To identify novel regulators of skeletal muscle metabolism and function, we performed a proteomic analysis of gastrocnemius muscle from 73 genetically distinct inbred mouse strains, and integrated the data with previously acquired genomics and >300 molecular/phenotypic traits via quantitative trait loci mapping and correlation network analysis. These data identified thousands of associations between protein abundance and phenotypes and can be accessed online (https://muscle.coffeeprot.com/) to identify regulators of muscle function. We used this resource to prioritize targets for a functional genomic screen in human bioengineered skeletal muscle. This identified several negative regulators of muscle function including UFC1, an E2 ligase for protein UFMylation. We show UFMylation is up-regulated in a mouse model of amyotrophic lateral sclerosis, a disease that involves muscle atrophy. Furthermore, in vivo knockdown of UFMylation increased contraction force, implicating its role as a negative regulator of skeletal muscle function.
- Published
- 2022
5. Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)
- Author
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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, 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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
6. Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition).
- Author
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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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C., Huang C., Huang H., Huang K., Huang M.L.H., Huang R., Huang S., Huang T., Huang X., Huang Y.J., Huber T.B., Hubert V., Hubner C.A., Hughes S.M., Hughes W.E., Humbert M., Hummer G., Hurley J.H., Hussain S., Hussey P.J., Hutabarat M., Hwang H.-Y., Hwang S., Ieni A., Ikeda F., Imagawa Y., Imai Y., Imbriano C., Imoto M., Inman D.M., Inoki K., Iovanna J., Iozzo R.V., Ippolito G., Irazoqui J.E., Iribarren P., Ishaq M., Ishikawa M., Ishimwe N., Isidoro C., Ismail N., Issazadeh-Navikas S., Itakura E., Ito D., Ivankovic D., Ivanova S., Iyer A.K.V., Izquierdo J.M., Izumi M., Jaattela M., Jabir M.S., Jackson W.T., Jacobo-Herrera N., Jacomin A.-C., Jacquin E., Jadiya P., Jaeschke H., Jagannath C., Jakobi A.J., Jakobsson J., Janji B., Jansen-Durr P., Jansson P.J., Jantsch J., Januszewski S., Jassey A., Jean S., Jeltsch-David H., Jendelova P., Jenny A., Jensen T.E., Jessen N., Jewell J.L., 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 G.V.W., Johnston S.A., Jokitalo E., Jolly M.K., Joosten L.A.B., Jordan J., Joseph B., Ju D., Ju J.-S., Ju J., Juarez E., Judith D., Juhasz G., Jun Y., Jung C.H., Jung S.-C., Jung Y.K., 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 D.S., Kaludercic N., Kalvari I., Kaminska J., Kaminskyy V.O., Kanamori H., Kanasaki K., Kang C., Kang R., Kang S.S., Kaniyappan S., Kanki T., Kanneganti T.-D., Kanthasamy A.G., Kanthasamy A., Kantorow M., Kapuy O., Karamouzis M.V., Karim M.R., Karmakar P., Katare R.G., Kato M., Kaufmann S.H.E., Kauppinen A., Kaushal G.P., Kaushik S., Kawasaki K., Kazan K., Ke P.-Y., Keating D.J., Keber U., Kehrl J.H., Keller K.E., Keller C.W., Kemper J.K., Kenific C.M., Kepp O., Kermorgant S., Kern A., Ketteler R., Keulers T.G., Khalfin B., Khalil H., Khambu B., Khan S.Y., Khandelwal V.K.M., Khandia R., Kho W., Khobrekar N.V., Khuansuwan S., Khundadze M., Killackey S.A., Kim D., Kim D.R., Kim D.-H., Kim D.-E., Kim E.Y., Kim E.-K., Kim H.-R., Kim H.-S., Hyung-Ryong Kim, Kim J.K., Kim J.-H., Kim J., Kim J.H., Kim K.I., Kim P.K., Kim S.-J., Kimball S.R., Kimchi A., Kimmelman A.C., Kimura T., King M.A., Kinghorn K.J., Kinsey C.G., Kirkin V., Kirshenbaum L.A., Kiselev S.L., Kishi S., Kitamoto K., Kitaoka Y., Kitazato K., Kitsis R.N., Kittler J.T., Kjaerulff O., Klein P.S., Klopstock T., Klucken J., Knaevelsrud H., Knorr R.L., Ko B.C.B., Ko F., Ko J.-L., Kobayashi H., Kobayashi S., Koch I., Koch J.C., Koenig U., Kogel D., Koh Y.H., Koike M., Kohlwein S.D., Kocaturk N.M., Komatsu M., Konig J., Kono T., Kopp B.T., Korcsmaros T., Korkmaz G., Korolchuk V.I., Korsnes M.S., Koskela A., Kota J., Kotake Y., Kotler M.L., Kou Y., Koukourakis M.I., Koustas E., Kovacs A.L., Kovacs T., Koya D., Kozako T., Kraft C., Krainc D., Kramer H., Krasnodembskaya A.D., Kretz-Remy C., 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Leitinger G., Lemus L., Leng S., Lenoir O., Lenz G., Lenz H.J., Lenzi P., Leon Y., Leopoldino A.M., Leschczyk C., Leskela S., Letellier E., Leung C.-T., Leung P.S., Leventhal J.S., Levine B., Lewis P.A., Ley K., Li B., Li D.-Q., Li J., Li K., Li L., Li M., Li P.-L., Li M.-Q., Li Q., Li S., Li T., Li W., Li X., Li Y.-P., Li Y., Lian J., Liang C., Liang Q., Liang W., Liang Y., Liao G., Liao L., Liao M., Liao Y.-F., Librizzi M., Lie P.P.Y., Lilly M.A., Lim H.J., Lima T.R.R., Limana F., Lin C., Lin C.-W., Lin D.-S., Lin F.-C., Lin J.D., Lin K.M., Lin K.-H., Lin L.-T., Lin P.-H., Lin Q., Lin S., Lin S.-J., Lin W., Lin X., Lin Y.-X., Lin Y.-S., Linden R., Lindner P., Ling S.-C., Lingor P., Linnemann A.K., Liou Y.-C., Lipinski M.M., Lipovsek S., Lira V.A., Lisiak N., Liton P.B., Liu C., Liu C.-H., Liu C.-F., Liu C.H., Liu F., Liu H.-S., Liu H.-F., Liu H., Liu J., Liu L., Liu M., Liu Q., Liu W., Liu X.-H., Liu X., Liu Y., Livingston J.A., Lizard G., Lizcano J.M., Ljubojevic-Holzer S., LLeonart 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Mallilankaraman K., Malorni W., Maloyan A., Mammadova N., Man G.C.W., Manai F., Mancias J.D., Mandelkow E.-M., Mandell M.A., Manfredi A.A., Manjili M.H., Manjithaya R., Manque P., Manshian B.B., Manzano R., Manzoni C., Mao K., Marchese C., Marchetti S., Marconi A.M., Marcucci F., Mardente S., Mareninova O.A., Margeta M., Mari M., Marinelli S., Marinelli O., Marino G., Mariotto S., Marshall R.S., Marten M.R., Martens S., Martin A.P.J., Martin K.R., Martin S., Martin-Segura A., Martin-Acebes M.A., Martin-Burriel I., Martin-Rincon M., Martin-Sanz P., Martina J.A., Martinet W., Martinez A., Martinez J., Martinez Velazquez M., Martinez-Lopez N., Martinez-Vicente M., Martins D.O., Martins J.O., Martins W.K., Martins-Marques T., Marzetti E., Masaldan S., Masclaux-Daubresse C., Mashek D.G., Massa V., Massieu L., Masson G.R., Masuelli L., Masyuk A.I., Masyuk T.V., Matarrese P., Matheu A., Matoba S., Matsuzaki S., Mattar P., Matte A., Mattoscio D., Mauriz J.L., Mauthe M., Mauvezin C., Maverakis 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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., 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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A., Franco B., Franco R., Franconi F., Frankel L.B., Friedman S.L., Frohlich L.F., Fruhbeck G., Fuentes J.M., Fujiki Y., Fujita N., Fujiwara Y., Fukuda M., Fulda S., Furic L., Furuya N., Fusco C., Gack M.U., Gaffke L., Galadari S., Galasso A., Galindo M.F., Gallolu Kankanamalage S., Galluzzi L., Galy V., Gammoh N., Gan B., Ganley I.G., Gao F., Gao H., Gao M., Gao P., Gao S.-J., Gao W., Gao X., Garcera A., Garcia M.N., Garcia V.E., Garcia-Del Portillo F., Garcia-Escudero V., Garcia-Garcia A., Garcia-Macia M., Garcia-Moreno D., Garcia-Ruiz C., Garcia-Sanz P., Garg A.D., Gargini R., Garofalo T., Garry R.F., Gassen N.C., Gatica D., Ge L., Ge W., Geiss-Friedlander R., Gelfi C., Genschik P., Gentle I.E., Gerbino V., Gerhardt C., Germain K., Germain M., Gewirtz D.A., Ghasemipour Afshar E., Ghavami S., Ghigo A., Ghosh M., Giamas G., Giampietri C., Giatromanolaki A., Gibson G.E., Gibson S.B., Ginet V., Giniger E., Giorgi C., Girao H., Girardin S.E., Giridharan M., Giuliano S., Giulivi C., Giuriato S., Giustiniani J., Gluschko A., Goder V., Goginashvili A., Golab J., Goldstone D.C., Golebiewska A., Gomes L.R., Gomez R., Gomez-Sanchez R., Gomez-Puerto M.C., Gomez-Sintes R., Gong Q., Goni F.M., Gonzalez-Gallego J., Gonzalez-Hernandez T., Gonzalez-Polo R.A., Gonzalez-Reyes J.A., Gonzalez-Rodriguez P., Goping I.S., Gorbatyuk M.S., Gorbunov N.V., Gorgulu K., Gorojod R.M., Gorski S.M., Goruppi S., Gotor C., Gottlieb R.A., Gozes I., Gozuacik D., Graef M., Graler M.H., Granatiero V., Grasso D., Gray J.P., Green D.R., Greenhough A., Gregory S.L., Griffin E.F., Grinstaff M.W., Gros F., Grose C., Gross A.S., Gruber F., Grumati P., Grune T., Gu X., Guan J.-L., Guardia C.M., Guda K., Guerra F., Guerri C., Guha P., Guillen C., Gujar S., Gukovskaya A., Gukovsky I., Gunst J., Gunther A., Guntur A.R., Guo C., Guo H., Guo L.-W., Guo M., Gupta P., Gupta S.K., Gupta S., Gupta V.B., Gupta V., Gustafsson A.B., Gutterman D.D., H.B R., Haapasalo A., Haber J.E., Hac A., Hadano S., Hafren A.J., 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C., Huang C., Huang H., Huang K., Huang M.L.H., Huang R., Huang S., Huang T., Huang X., Huang Y.J., Huber T.B., Hubert V., Hubner C.A., Hughes S.M., Hughes W.E., Humbert M., Hummer G., Hurley J.H., Hussain S., Hussey P.J., Hutabarat M., Hwang H.-Y., Hwang S., Ieni A., Ikeda F., Imagawa Y., Imai Y., Imbriano C., Imoto M., Inman D.M., Inoki K., Iovanna J., Iozzo R.V., Ippolito G., Irazoqui J.E., Iribarren P., Ishaq M., Ishikawa M., Ishimwe N., Isidoro C., Ismail N., Issazadeh-Navikas S., Itakura E., Ito D., Ivankovic D., Ivanova S., Iyer A.K.V., Izquierdo J.M., Izumi M., Jaattela M., Jabir M.S., Jackson W.T., Jacobo-Herrera N., Jacomin A.-C., Jacquin E., Jadiya P., Jaeschke H., Jagannath C., Jakobi A.J., Jakobsson J., Janji B., Jansen-Durr P., Jansson P.J., Jantsch J., Januszewski S., Jassey A., Jean S., Jeltsch-David H., Jendelova P., Jenny A., Jensen T.E., Jessen N., Jewell J.L., 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 G.V.W., Johnston S.A., Jokitalo E., Jolly M.K., Joosten L.A.B., Jordan J., Joseph B., Ju D., Ju J.-S., Ju J., Juarez E., Judith D., Juhasz G., Jun Y., Jung C.H., Jung S.-C., Jung Y.K., 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 D.S., Kaludercic N., Kalvari I., Kaminska J., Kaminskyy V.O., Kanamori H., Kanasaki K., Kang C., Kang R., Kang S.S., Kaniyappan S., Kanki T., Kanneganti T.-D., Kanthasamy A.G., Kanthasamy A., Kantorow M., Kapuy O., Karamouzis M.V., Karim M.R., Karmakar P., Katare R.G., Kato M., Kaufmann S.H.E., Kauppinen A., Kaushal G.P., Kaushik S., Kawasaki K., Kazan K., Ke P.-Y., Keating D.J., Keber U., Kehrl J.H., Keller K.E., Keller C.W., Kemper J.K., Kenific C.M., Kepp O., Kermorgant S., Kern A., Ketteler R., Keulers T.G., Khalfin B., Khalil H., Khambu B., Khan S.Y., Khandelwal V.K.M., Khandia R., Kho W., Khobrekar N.V., Khuansuwan S., Khundadze M., Killackey S.A., Kim D., Kim D.R., Kim D.-H., Kim D.-E., Kim E.Y., Kim E.-K., Kim H.-R., Kim H.-S., Hyung-Ryong Kim, Kim J.K., Kim J.-H., Kim J., Kim J.H., Kim K.I., Kim P.K., Kim S.-J., Kimball S.R., Kimchi A., Kimmelman A.C., Kimura T., King M.A., Kinghorn K.J., Kinsey C.G., Kirkin V., Kirshenbaum L.A., Kiselev S.L., Kishi S., Kitamoto K., Kitaoka Y., Kitazato K., Kitsis R.N., Kittler J.T., Kjaerulff O., Klein P.S., Klopstock T., Klucken J., Knaevelsrud H., Knorr R.L., Ko B.C.B., Ko F., Ko J.-L., Kobayashi H., Kobayashi S., Koch I., Koch J.C., Koenig U., Kogel D., Koh Y.H., Koike M., Kohlwein S.D., Kocaturk N.M., Komatsu M., Konig J., Kono T., Kopp B.T., Korcsmaros T., Korkmaz G., Korolchuk V.I., Korsnes M.S., Koskela A., Kota J., Kotake Y., Kotler M.L., Kou Y., Koukourakis M.I., Koustas E., Kovacs A.L., Kovacs T., Koya D., Kozako T., Kraft C., Krainc D., Kramer H., Krasnodembskaya A.D., Kretz-Remy C., Kroemer G., Ktistakis N.T., Kuchitsu K., Kuenen S., Kuerschner L., Kukar T., Kumar A., Kumar D., Kumar S., Kume S., Kumsta C., Kundu C.N., Kundu M., Kunnumakkara A.B., Kurgan L., Kutateladze T.G., Kutlu O., Kwak S., Kwon H.J., Kwon T.K., Kwon Y.T., Kyrmizi I., La Spada A., Labonte P., Ladoire S., Laface I., Lafont F., Lagace D.C., Lahiri V., Lai Z., Laird A.S., Lakkaraju A., Lamark T., Lan S.-H., Landajuela A., Lane D.J.R., Lane J.D., Lang C.H., Lange C., Langel U., Langer R., Lapaquette P., Laporte J., LaRusso N.F., Lastres-Becker I., Lau W.C.Y., Laurie G.W., Lavandero S., Law B.Y.K., Law H.K.-W., Layfield R., Le W., Le Stunff H., Leary A.Y., Lebrun J.-J., Leck L.Y.W., Leduc-Gaudet J.-P., Lee C., Lee C.-P., Lee D.-H., Lee E.B., Lee E.F., Lee G.M., Lee H.-J., Lee H.K., Lee J.M., Lee J.S., Lee J.-A., Lee J.-Y., Lee J.H., Lee M., Lee M.G., Lee M.J., Lee M.-S., Lee S.-J., Lee S.Y., Lee S.B., Lee W.H., Lee Y.-R., Lee Y.-H., Lee Y., Lefebvre C., Legouis R., Lei Y.L., Lei Y., Leikin S., Leitinger G., Lemus L., Leng S., Lenoir O., Lenz G., Lenz H.J., Lenzi P., Leon Y., Leopoldino A.M., Leschczyk C., Leskela S., Letellier E., Leung C.-T., Leung P.S., Leventhal J.S., Levine B., Lewis P.A., Ley K., Li B., Li D.-Q., Li J., Li K., Li L., Li M., Li P.-L., Li M.-Q., Li Q., Li S., Li T., Li W., Li X., Li Y.-P., Li Y., Lian J., Liang C., Liang Q., Liang W., Liang Y., Liao G., Liao L., Liao M., Liao Y.-F., Librizzi M., Lie P.P.Y., Lilly M.A., Lim H.J., Lima T.R.R., Limana F., Lin C., Lin C.-W., Lin D.-S., Lin F.-C., Lin J.D., Lin K.M., Lin K.-H., Lin L.-T., Lin P.-H., Lin Q., Lin S., Lin S.-J., Lin W., Lin X., Lin Y.-X., Lin Y.-S., Linden R., Lindner P., Ling S.-C., Lingor P., Linnemann A.K., Liou Y.-C., Lipinski M.M., Lipovsek S., Lira V.A., Lisiak N., Liton P.B., Liu C., Liu C.-H., Liu C.-F., Liu C.H., Liu F., Liu H.-S., Liu H.-F., Liu H., Liu J., Liu L., Liu M., Liu Q., Liu W., Liu X.-H., Liu X., Liu Y., Livingston J.A., Lizard G., Lizcano J.M., Ljubojevic-Holzer S., LLeonart 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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., and Wakatsuki S.
- 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
7. Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)1.
- Author
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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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Guglielmo G.M., Di Leo L., Di Malta C., Di Nardo A., Di Rienzo M., Di Sano F., Diallinas G., Diao J., Diaz-Araya G., Diaz-Laviada I., Dickinson J.M., Diederich M., Dieude M., Dikic I., Ding S., Ding W.-X., Dini L., Dinic J., Dinic M., Dinkova-Kostova A.T., Dionne M.S., Distler J.H.W., Diwan A., Dixon I.M.C., Djavaheri-Mergny M., Dobrinski I., Dobrovinskaya O., Dobrowolski R., Dobson R.C.J., Dokic J., Dokmeci Emre S., Donadelli M., Dong B., Dong X., Dong Z., Dorn II G.W., 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 S.P., Dubrovska A., Dunlop E.A., Dupont N., Duran R.V., Dwarakanath B.S., Dyshlovoy S.A., Ebrahimi-Fakhari D., Eckhart L., Edelstein C.L., Efferth T., Eftekharpour E., Eichinger L., Eid N., Eisenberg T., Eissa N.T., Eissa S., Ejarque M., El Andaloussi A., El-Hage N., El-Naggar S., Eleuteri A.M., El-Shafey E.S., Elgendy M., Eliopoulos A.G., Elizalde M.M., Elks P.M., Elsasser 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Haidar M., Hall B.S., Hallden G., Hamacher-Brady A., Hamann A., Hamasaki M., Han W., Hansen M., Hanson P.I., Hao Z., Harada M., Harhaji-Trajkovic L., Hariharan N., Haroon N., Harris J., Hasegawa T., Hasima Nagoor N., Haspel J.A., Haucke V., Hawkins W.D., Hay B.A., Haynes C.M., Hayrabedyan S.B., Hays T.S., He C., He Q., He R.-R., He Y.-W., He Y.-Y., Heakal Y., Heberle A.M., Hejtmancik J.F., Helgason G.V., Henkel V., Herb M., Hergovich A., Herman-Antosiewicz A., Hernandez A., Hernandez C., Hernandez-Diaz S., Hernandez-Gea V., Herpin A., Herreros J., Hervas J.H., Hesselson D., Hetz C., Heussler V.T., Higuchi Y., Hilfiker S., Hill J.A., Hlavacek W.S., Ho E.A., Ho I.H.T., Ho P.W.-L., Ho S.-L., Ho W.Y., Hobbs G.A., Hochstrasser M., Hoet P.H.M., Hofius D., Hofman P., Hohn A., Holmberg C.I., Hombrebueno J.R., Yi-Ren Hong C.-W.H., Hooper L.V., Hoppe T., Horos R., Hoshida Y., Hsin I.-L., Hsu H.-Y., Hu B., Hu D., Hu L.-F., Hu M.C., Hu R., Hu W., Hu Y.-C., Hu Z.-W., Hua F., Hua J., Hua Y., Huan 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E.-J., Jin F., Jin H., Jin L., Jin M., Jin S., Jo E.-K., Joffre C., Johansen T., Johnson G.V.W., Johnston S.A., Jokitalo E., Jolly M.K., Joosten L.A.B., Jordan J., Joseph B., Ju D., Ju J.-S., Ju J., Juarez E., Judith D., Juhasz G., Jun Y., Jung C.H., Jung S.-C., Jung Y.K., 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 D.S., Kaludercic N., Kalvari I., Kaminska J., Kaminskyy V.O., Kanamori H., Kanasaki K., Kang C., Kang R., Kang S.S., Kaniyappan S., Kanki T., Kanneganti T.-D., Kanthasamy A.G., Kanthasamy A., Kantorow M., Kapuy O., Karamouzis M.V., Karim M.R., Karmakar P., Katare R.G., Kato M., Kaufmann S.H.E., Kauppinen A., Kaushal G.P., Kaushik S., Kawasaki K., Kazan K., Ke P.-Y., Keating D.J., Keber U., Kehrl J.H., Keller K.E., Keller C.W., Kemper J.K., Kenific C.M., Kepp O., Kermorgant S., Kern A., Ketteler R., Keulers T.G., Khalfin B., Khalil H., Khambu B., Khan S.Y., Khandelwal V.K.M., Khandia R., Kho W., Khobrekar N.V., Khuansuwan S., Khundadze M., Killackey S.A., Kim D., Kim D.R., Kim D.-H., Kim D.-E., Kim E.Y., Kim E.-K., Kim H.-R., Kim H.-S., Hyung-Ryong Kim, Kim J.K., Kim J.-H., Kim J., Kim J.H., Kim K.I., Kim P.K., Kim S.-J., Kimball S.R., Kimchi A., Kimmelman A.C., Kimura T., King M.A., Kinghorn K.J., Kinsey C.G., Kirkin V., Kirshenbaum L.A., Kiselev S.L., Kishi S., Kitamoto K., Kitaoka Y., Kitazato K., Kitsis R.N., Kittler J.T., Kjaerulff O., Klein P.S., Klopstock T., Klucken J., Knaevelsrud H., Knorr R.L., Ko B.C.B., Ko F., Ko J.-L., Kobayashi H., Kobayashi S., Koch I., Koch J.C., Koenig U., Kogel D., Koh Y.H., Koike M., Kohlwein S.D., Kocaturk N.M., Komatsu M., Konig J., Kono T., Kopp B.T., Korcsmaros T., Korkmaz G., Korolchuk V.I., Korsnes M.S., Koskela A., Kota J., Kotake Y., Kotler M.L., Kou Y., Koukourakis M.I., Koustas E., Kovacs A.L., Kovacs T., Koya D., Kozako T., Kraft C., Krainc D., Kramer H., Krasnodembskaya A.D., Kretz-Remy C., Kroemer G., Ktistakis N.T., Kuchitsu K., Kuenen S., Kuerschner L., Kukar T., Kumar A., Kumar D., Kumar S., Kume S., Kumsta C., Kundu C.N., Kundu M., Kunnumakkara A.B., Kurgan L., Kutateladze T.G., Kutlu O., Kwak S., Kwon H.J., Kwon T.K., Kwon Y.T., Kyrmizi I., La Spada A., Labonte P., Ladoire S., Laface I., Lafont F., Lagace D.C., Lahiri V., Lai Z., Laird A.S., Lakkaraju A., Lamark T., Lan S.-H., Landajuela A., Lane D.J.R., Lane J.D., Lang C.H., Lange C., Langel U., Langer R., Lapaquette P., Laporte J., LaRusso N.F., Lastres-Becker I., Lau W.C.Y., Laurie G.W., Lavandero S., Law B.Y.K., Law H.K.-W., Layfield R., Le W., Le Stunff H., Leary A.Y., Lebrun J.-J., Leck L.Y.W., Leduc-Gaudet J.-P., Lee C., Lee C.-P., Lee D.-H., Lee E.B., Lee E.F., Lee G.M., Lee H.-J., Lee H.K., Lee J.M., Lee J.S., Lee J.-A., Lee J.-Y., Lee J.H., Lee M., Lee M.G., Lee M.J., Lee M.-S., Lee S.-J., Lee S.Y., Lee S.B., Lee W.H., Lee Y.-R., Lee Y.-H., Lee Y., Lefebvre C., Legouis R., Lei Y.L., Lei Y., Leikin S., Leitinger G., Lemus L., Leng S., Lenoir O., Lenz G., Lenz H.J., Lenzi P., Leon Y., Leopoldino A.M., Leschczyk C., Leskela S., Letellier E., Leung C.-T., Leung P.S., Leventhal J.S., Levine B., Lewis P.A., Ley K., Li B., Li D.-Q., Li J., Li K., Li L., Li M., Li P.-L., Li M.-Q., Li Q., Li S., Li T., Li W., Li X., Li Y.-P., Li Y., Lian J., Liang C., Liang Q., Liang W., Liang Y., Liao G., Liao L., Liao M., Liao Y.-F., Librizzi M., Lie P.P.Y., Lilly M.A., Lim H.J., Lima T.R.R., Limana F., Lin C., Lin C.-W., Lin D.-S., Lin F.-C., Lin J.D., Lin K.M., Lin K.-H., Lin L.-T., Lin P.-H., Lin Q., Lin S., Lin S.-J., Lin W., Lin X., Lin Y.-X., Lin Y.-S., Linden R., Lindner P., Ling S.-C., Lingor P., Linnemann A.K., Liou Y.-C., Lipinski M.M., Lipovsek S., Lira V.A., Lisiak N., Liton P.B., Liu C., Liu C.-H., Liu C.-F., Liu C.H., Liu F., Liu H.-S., Liu H.-F., Liu H., Liu J., Liu L., Liu M., Liu Q., Liu W., Liu X.-H., Liu X., Liu Y., Livingston J.A., Lizard G., Lizcano J.M., Ljubojevic-Holzer S., LLeonart 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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., 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[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
8. Lipin 1 modulates mRNA splicing during fasting adaptation in liver
- Author
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Wang, H, Chan, TW, Vashisht, AA, Drew, BG, Calkin, AC, Harris, TE, Wohlschlegel, JA, Xiao, X, Reue, K, Wang, H, Chan, TW, Vashisht, AA, Drew, BG, Calkin, AC, Harris, TE, Wohlschlegel, JA, Xiao, X, and Reue, K
- Abstract
Lipin 1 regulates cellular lipid homeostasis through roles in glycerolipid synthesis (through phosphatidic acid phosphatase activity) and transcriptional coactivation. Lipin 1-deficient individuals exhibit episodic disease symptoms that are triggered by metabolic stress, such as stress caused by prolonged fasting. We sought to identify critical lipin 1 activities during fasting. We determined that lipin 1 deficiency induces widespread alternative mRNA splicing in liver during fasting, much of which is normalized by refeeding. The role of lipin 1 in mRNA splicing was largely independent of its enzymatic function. We identified interactions between lipin 1 and spliceosome proteins, as well as a requirement for lipin 1 to maintain homeostatic levels of spliceosome small nuclear RNAs and specific RNA splicing factors. In fasted Lpin1-/- liver, we identified a correspondence between alternative splicing of phospholipid biosynthetic enzymes and dysregulated phospholipid levels; splicing patterns and phospholipid levels were partly normalized by feeding. Thus, lipin 1 influences hepatic lipid metabolism through mRNA splicing, as well as through enzymatic and transcriptional activities, and fasting exacerbates the deleterious effects of lipin 1 deficiency on metabolic homeostasis.
- Published
- 2021
9. Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)
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Zhonglin, Xilouri, Maria, Xu, Congfeng, Xu, En, Xu, Haoxing, Xu, Jing, Xu, JinRong, Xu, Liang, Xu, Wen Wen, Xu, Xiulong, Xue, Yu, Yakhine-Diop, Sokhna M S, Yamaguchi, Masamitsu, Yamaguchi, Osamu, Yamamoto, Ai, Yamashina, Shunhei, Yan, Shengmin, Yan, Shian-Jang, Yan, Zhen, Yanagi, Yasuo, Yang, Chuanbin, Yang, Dun-Sheng, Yang, Huan, Yang, Huang-Tian, Yang, Hui, Yang, Jin-Ming, Yang, Jing, Yang, Jingyu, Yang, Ling, Yang, Liu, Yang, Ming, Yang, Pei-Ming, Yang, Qian, Yang, Seungwon, Yang, Shu, Yang, Shun-Fa, Yang, Wannian, Yang, Wei Yuan, Yang, Xiaoyong, Yang, Xuesong, Yang, Yi, Yang, Ying, Yao, Honghong, Yao, Shenggen, Yao, Xiaoqiang, Yao, Yong-Gang, Yao, Yong-Ming, Yasui, Takahiro, Yazdankhah, Meysam, Yen, Paul M, Yi, Cong, Yin, Xiao-Ming, Yin, Yanhai, Yin, Zhangyuan, Yin, Ziyi, Ying, Meidan, Ying, Zheng, Yip, Calvin K, Yiu, Stephanie Pei Tung, Yoo, Young H, Yoshida, Kiyotsugu, Yoshii, Saori R, Yoshimori, Tamotsu, Yousefi, Bahman, Yu, Boxuan, Yu, Haiyang, Yu, Jun, Yu, Li, Yu, Ming-Lung, Yu, Seong-Woon, Yu, Victor C, Yu, W Haung, Yu, Zhengping, Yu, Zhou, Yuan, Junying, Yuan, Ling-Qing, Yuan, Shilin, Yuan, Shyng-Shiou F, Yuan, Yanggang, Yuan, Zengqiang, Yue, Jianbo, Yue, Zhenyu, Yun, Jeanho, Yung, Raymond L, Zacks, David N, Zaffagnini, Gabriele, Zambelli, Vanessa O, Zanella, Isabella, Zang, Qun S, Zanivan, Sara, Zappavigna, Silvia, Zaragoza, Pilar, Zarbalis, Konstantinos S, Zarebkohan, Amir, Zarrouk, Amira, Zeitlin, Scott O, Zeng, Jialiu, Zeng, Ju-Deng, Žerovnik, Eva, Zhan, Lixuan, Zhang, Bin, Zhang, Donna D, Zhang, Hanlin, Zhang, Hong, Zhang, Honghe, Zhang, Huafeng, Zhang, Huaye, Zhang, Hui, Zhang, Hui-Ling, Zhang, Jianbin, Zhang, Jianhua, Zhang, Jing-Pu, Zhang, Kalin Y B, Zhang, Leshuai W, Zhang, Lin, Zhang, Lisheng, Zhang, Lu, Zhang, Luoying, Zhang, Menghuan, Zhang, Peng, Zhang, Sheng, Zhang, Wei, Zhang, Xiangnan, Zhang, Xiao-Wei, Zhang, Xiaolei, Zhang, Xiaoyan, Zhang, Xin, Zhang, Xinxin, Zhang, Xu Dong, Zhang, Yang, Zhang, Yanjin, Zhang, Yi, Zhang, Ying-Dong, Zhang, Yingmei, Zhang, Yuan-Yuan, Zhang, Yuchen, Zhang, Zhe, Zhang, Zhengguang, Zhang, Zhibing, Zhang, Zhihai, Zhang, Zhiyong, Zhang, Zili, Zhao, Haobin, Zhao, Lei, Zhao, Shuang, Zhao, Tongbiao, Zhao, Xiao-Fan, Zhao, Ying, Zhao, Yongchao, Zhao, Yongliang, Zhao, Yuting, Zheng, Guoping, Zheng, Kai, Zheng, Ling, Zheng, Shizhong, Zheng, Xi-Long, Zheng, Yi, Zheng, Zu-Guo, Zhivotovsky, Boris, Zhong, Qing, Zhou, Ao, Zhou, Ben, Zhou, Cefan, Zhou, Gang, Zhou, Hao, Zhou, Hong, Zhou, Hongbo, Zhou, Jie, Zhou, Jing, Zhou, Jiyong, Zhou, Kailiang, Zhou, Rongjia, Zhou, Xu-Jie, Zhou, Yanshuang, Zhou, Yinghong, Zhou, Yubin, Zhou, Zheng-Yu, Zhou, Zhou, Zhu, Binglin, Zhu, Changlian, Zhu, Guo-Qing, Zhu, Haining, Zhu, Hongxin, Zhu, Hua, Zhu, Wei-Guo, Zhu, Yanping, Zhu, Yushan, Zhuang, Haixia, Zhuang, Xiaohong, Zientara-Rytter, Katarzyna, Zimmermann, Christine M, Ziviani, Elena, Zoladek, Teresa, Zong, Wei-Xing, Zorov, Dmitry B, Zorzano, Antonio, Zou, Weiping, Zou, Zhen, Zou, Zhengzhi, Zuryn, Steven, Zwerschke, Werner, Brand-Saberi, Beate, Dong, X Charlie, Kenchappa, Chandra Shekar, Li, Zuguo, Lin, Yong, Oshima, Shigeru, Rong, Yueguang, Sluimer, Judith C, Stallings, Christina L, and Tong, Chun-Kit
- 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.
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- 2021
10. Adipocyte fatty acid metabolism: T1:RS3.1
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Reue, K
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- 2010
11. Adipose tissue lipin expression levels distinguish HIV patients with and without lipodystrophy
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Lindegaard, B, Larsen, L F, Hansen, A-B E, Gerstoft, J, Pedersen, B K, and Reue, K
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- 2007
12. Animal models for genetic lipoprotein disorders
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Reue, K. L., Warden, C. H., and Lusis, A. J.
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- 1990
13. Acads gene deletion in BALB/cByJ mouse strain occurred after 1981 and is not present in BALB/cByJ-fld mutant mice
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Reue, K. and Cohen, R. D.
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- 1996
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14. Localization of mouse peroxisome proliferator-activated receptor δ (Ppard) on Chromosome 17 near colipase (Clps)
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Cohen, R. D., Welch, C., Xia, Y. -R., Lusis, A. J., and Reue, K.
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- 1996
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15. Localization of mouse peroxisome proliferator-activated receptor γ on Chromosome 6
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Reue, K., Xia, Y. -R., Shi, V. W., Cohen, R. D., Welch, C., and Lusis, A. J.
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- 1996
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16. The fatty liver dystrophy (fld) mutation: Developmentally related alterations in hepatic triglyceride metabolism and protein expression
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Reue, K., primary, Rehnmark, S., additional, Cohen, R.D., additional, Leete, T.H., additional, Doolittle, M.H., additional, Giometti, C.S., additional, Mishler, K., additional, and Slavin, B.G., additional
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- 1997
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17. Insulin Resistance and Altered Systemic Glucose Metabolism in Mice Lacking Nur77
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Chao, LC, Wroblewski, K, Zhang, Z, Pei, L, Vergnes, L, Ilkayeva, OR, Ding, SY, Reue, K, Watt, MJ, Newgard, CB, Pilch, PF, Hevener, AL, Tontonoz, P, Chao, LC, Wroblewski, K, Zhang, Z, Pei, L, Vergnes, L, Ilkayeva, OR, Ding, SY, Reue, K, Watt, MJ, Newgard, CB, Pilch, PF, Hevener, AL, and Tontonoz, P
- Abstract
OBJECTIVE: Nur77 is an orphan nuclear receptor with pleotropic functions. Previous studies have identified Nur77 as a transcriptional regulator of glucose utilization genes in skeletal muscle and gluconeogenesis in liver. However, the net functional impact of these pathways is unknown. To examine the consequence of Nur77 signaling for glucose metabolism in vivo, we challenged Nur77 null mice with high-fat feeding. RESEARCH DESIGN AND METHODS: Wild-type and Nur77 null mice were fed a high-fat diet (60% calories from fat) for 3 months. We determined glucose tolerance, tissue-specific insulin sensitivity, oxygen consumption, muscle and liver lipid content, muscle insulin signaling, and expression of glucose and lipid metabolism genes. RESULTS: Mice with genetic deletion of Nur77 exhibited increased susceptibility to diet-induced obesity and insulin resistance. Hyperinsulinemic-euglycemic clamp studies revealed greater high-fat diet-induced insulin resistance in both skeletal muscle and liver of Nur77 null mice compared with controls. Loss of Nur77 expression in skeletal muscle impaired insulin signaling and markedly reduced GLUT4 protein expression. Muscles lacking Nur77 also exhibited increased triglyceride content and accumulation of multiple even-chained acylcarnitine species. In the liver, Nur77 deletion led to hepatic steatosis and enhanced expression of lipogenic genes, likely reflecting the lipogenic effect of hyperinsulinemia. CONCLUSIONS: Collectively, these data demonstrate that loss of Nur77 influences systemic glucose metabolism and highlight the physiological contribution of muscle Nur77 to this regulatory pathway.
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- 2009
18. Zbtb16 has a role in brown adipocyte bioenergetics
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Plaisier, C L, primary, Bennett, B J, additional, He, A, additional, Guan, B, additional, Lusis, A J, additional, Reue, K, additional, and Vergnes, L, additional
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- 2012
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19. Adipose tissue lipin expression levels distinguish HIV patients with and without lipodystrophy
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Lindegaard, B, primary, Larsen, L F, additional, Hansen, A-B E, additional, Gerstoft, J, additional, Pedersen, B K, additional, and Reue, K, additional
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- 2006
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20. Lipin, a Lipodystrophy and Obesity Gene
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Phan, J., primary and Reue, K., additional
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- 2005
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21. Biphasic expression of lipin suggests dual roles in adipocyte development
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Phan, J., primary, Peterfy, M., additional, and Reue, K., additional
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- 2005
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22. 316 LIPIN, A LIPODYSTROPHY AND OBESITY GENE
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Phan, J., primary and Reue, K., additional
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- 2005
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23. LIPIN: A NOVEL MODULATOR OF ADIPOSITY.
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Phan, J., primary, Peterfy, M., additional, and Reue, K., additional
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- 2004
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24. 417 THE ROLE OF LIPIN IN DIABETES AND INSULIN RESISTANCE.
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Phan, J., primary and Reue, K, additional
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- 2004
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25. 328 LIPIN: A NOVEL MODULATOR OF ADIPOSITY.
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Phan, J., primary, Peterfy, M., additional, and Reue, K., additional
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- 2004
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26. THE ROLE OF LIPIN IN DIABETES AND INSULIN RESISTANCE.
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Phan, J., primary and Reue, K, additional
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- 2004
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27. Lipin: A Novel Modulator of Adiposity
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Phan, J., primary, Peterfy, M., additional, and Reue, K., additional
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- 2001
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28. The Role of Lipin in Diabetes and Insulin Resistance
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Phan, J., primary and Reue, K, additional
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- 2001
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29. A locus conferring resistance to diet-induced hypercholesterolemia and atherosclerosis on mouse chromosome 2
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Lusis, A.J., primary, Mouzeyan, A., additional, Choi, J., additional, Allayee, H., additional, Wang, X., additional, Sinsheimer, J., additional, Phan, J., additional, Castellani, L.W., additional, Reue, K., additional, and Davis, R.C., additional
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- 2000
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30. 3.P.151 Hormone-sensitive lipase overexpression increases cholesteryl-ester hydrolysis in macrophage foam cells
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Escary, J.-L., primary, Choy, H.A., additional, Reue, K., additional, and Schotz, M.C., additional
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- 1997
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31. Reduced aortic lesions and elevated high density lipoprotein levels in transgenic mice overexpressing mouse apolipoprotein A-IV.
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Cohen, R D, primary, Castellani, L W, additional, Qiao, J H, additional, Van Lenten, B J, additional, Lusis, A J, additional, and Reue, K, additional
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- 1997
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32. Complex genetic control of HDL levels in mice in response to an atherogenic diet. Coordinate regulation of HDL levels and bile acid metabolism.
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Machleder, D, primary, Ivandic, B, additional, Welch, C, additional, Castellani, L, additional, Reue, K, additional, and Lusis, A J, additional
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- 1997
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33. Naturally occurring mutations in mice affecting lipid transport and metabolism.
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Reue, K, primary and Doolittle, M H, additional
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- 1996
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34. Molecular characterization of human hepatic lipase deficiency. In vitro expression of two naturally occurring mutations.
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Durstenfeld, A, primary, Ben-Zeev, O, additional, Reue, K, additional, Stahnke, G, additional, and Doolittle, M H, additional
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- 1994
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35. Expression of hormone-sensitive lipase mRNA in macrophages.
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Khoo, JC, primary, Reue, K, additional, Steinberg, D, additional, and Schotz, MC, additional
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- 1993
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36. Genetic variation in mouse apolipoprotein A-IV expression is determined pre- and post-transcriptionally
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Reue, K, primary, Purcell-Huynh, DA, additional, Leete, TH, additional, Doolittle, MH, additional, Durstenfeld, A, additional, and Lusis, AJ, additional
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- 1993
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37. Genetic variation in mouse apolipoprotein A-IV due to insertion and deletion in a region of tandem repeats
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Reue, K., primary and Leete, T.H., additional
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- 1991
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38. cDNA cloning of carboxyl ester lipase from human pancreas reveals a unique proline-rich repeat unit.
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Reue, K, primary, Zambaux, J, additional, Wong, H, additional, Lee, G, additional, Leete, TH, additional, Ronk, M, additional, Shively, JE, additional, Sternby, B, additional, Borgström, B, additional, and Ameis, D, additional
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- 1991
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39. Lipin expression is attenuated in adipose tissue of insulin-resistant human subjects and increases with peroxisome proliferator-activated receptor gamma activation.
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Yao-Borengasser A, Rasouli N, Varma V, Miles LM, Phanavanh B, Starks TN, Phan J, Spencer HJ 3rd, McGehee RE Jr, Reue K, Kern PA, Yao-Borengasser, Aiwei, Rasouli, Neda, Varma, Vijayalakshmi, Miles, Leslie M, Phanavanh, Bounleut, Starks, Tasha N, Phan, Jack, Spencer, Horace J 3rd, and McGehee, Robert E Jr
- Subjects
PROTEIN metabolism ,ADIPOSE tissues ,INSULIN resistance ,OBESITY ,PROTEINS ,RESEARCH funding ,GLUCOSE intolerance ,SKELETAL muscle ,THIAZOLIDINEDIONES ,PHARMACODYNAMICS - Abstract
Lipin-alpha and -beta are the alternatively spliced gene products of the Lpin1 gene, whose product lipin is required for adipocyte differentiation. Lipin deficiency causes lipodystrophy, fatty liver, and insulin resistance in mice, whereas adipose tissue lipin overexpression results in increased adiposity but improved insulin sensitivity. To assess lipin expression and its relation to insulin resistance in humans, we examined lipin-alpha and -beta mRNA levels in subjects with normal or impaired glucose tolerance. We found higher expression levels of both lipin isoforms in lean, insulin-sensitive subjects. When compared with normal glucose-tolerant subjects, individuals with impaired glucose tolerance were more insulin resistant, demonstrated higher levels of intramyocellular lipids (IMCLs), and expressed approximately 50% lower levels of lipin-alpha and -beta. In addition, there was a strong inverse correlation between adipose tissue lipin expression and muscle IMCLs but no evidence for an increase in muscle lipid oxidation. After treatment of the impaired glucose-tolerant subjects with insulin sensitizers for 10 weeks, pioglitazone (but not metformin) resulted in a 60% increase in the insulin sensitivity index (Si) and a 32% decrease in IMCLs (both P < 0.01), along with an increase in lipin-beta (but not lipin-alpha) expression by 200% (P < 0.005). Lipin expression in skeletal muscle, however, was not related to obesity or insulin resistance. Hence, high adipose tissue lipin expression is found in insulin-sensitive subjects, and lipin-beta expression increases following treatment with pioglitazone. These results suggest that increased adipogenesis and/or lipogenesis in subcutaneous fat, mediated by the LPIN1 gene, may prevent lipotoxicity in muscle, leading to improved insulin sensitivity. [ABSTRACT FROM AUTHOR]
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- 2006
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40. Metabolic consequences of lipodystrophy in mouse models.
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Reue K and Phan J
- Abstract
PURPOSE OF REVIEW: Adipose tissue is a key player in metabolic homeostasis through its role as an energy depot and endocrine organ. The characterization of mouse models of lipodystrophy, in which adipose tissue development and function are impaired, has shed new light on the mechanisms by which adipose tissue dysregulation may contribute to conditions such as insulin resistance, fatty liver, and beta-cell toxicity. RECENT FINDINGS: Here we review recent findings from mouse models with genetic alterations leading to reduced adipose tissue mass. The metabolic consequences depend on the basis for the adipose tissue reduction, and we classify mouse models into three categories based on whether they confer (1) lipoatrophy accompanied by insulin resistance, (2) reduced adipose tissue storage associated with enhanced energy expenditure, or (3) both lipoatrophic and energetic effects. SUMMARY: Reductions in the capacity of adipose tissue to store triglycerides or to secrete adipokine hormones lead to altered lipid metabolism and insulin resistance. In contrast, depletion of fat stores by virtue of enhanced energy metabolism does not produce undesirable metabolic effects. However, enhanced energy metabolism cannot overcome the deleterious effects of impaired adipokine production, as revealed by studies of models with both lipoatrophic and energetic effects. [ABSTRACT FROM AUTHOR]
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- 2006
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41. Phenotypic characterization of the Ath-1 gene controlling high density lipoprotein levels and susceptibility to atherosclerosis.
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LeBoeuf, RC, primary, Doolittle, MH, additional, Montcalm, A, additional, Martin, DC, additional, Reue, K, additional, and Lusis, AJ, additional
- Published
- 1990
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42. mRNA quantitation techniques: considerations for experimental design and application.
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Reue, Karen and Reue, K
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- *
MESSENGER RNA , *RIBONUCLEASES , *RNA analysis , *ANIMAL experimentation , *COMPARATIVE studies , *ESTERASES , *IMMUNOBLOTTING , *RESEARCH methodology , *MEDICAL cooperation , *NUCLEOTIDE separation , *POLYMERASE chain reaction , *RESEARCH , *EVALUATION research , *REVERSE transcriptase polymerase chain reaction - Abstract
Discusses three messenger RNA (mRNA) quantitation techniques with focus on the applications and limitations of each. Northern blot analysis; Ribonuclease protection assay; Quantitative RT-PCR.
- Published
- 1998
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43. Adipose tissue deficiency, glucose intolerance, and increased atherosclerosis result from mutation in the mouse fatty liver dystrophy (fld) gene.
- Author
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Reue, K, Xu, P, Wang, X P, and Slavin, B G
- Abstract
The fatty liver dystrophy (fld) mutant mouse is characterized by neonatal fatty liver and hypertriglyceridemia that resolve at weaning, and neuropathy affecting peripheral nerve in adulthood. We now report additional significant manifestations of this single gene mutation, which include adipose tissue deficiency, glucose intolerance, and increased susceptibility to atherosclerosis. In adult fld/fld mice, both white and brown fat pads exhibit an 80% reduction in mass compared with wild-type controls, and consist of immature adipocytes as assessed by morphological and molecular criteria. The lack of lipid accumulation in fld/fld adipose tissue could be attributed, in part, to a failure to induce expression of lipoprotein lipase and enzymes involved in fatty acid synthesis, such as fatty acid synthase and acetyl-CoA carboxylase. Related to the deficiency of adipose tissue, fld/fld mice were also found to exhibit profound glucose intolerance, modest hyperinsulinemia, and reduced tissue response to insulin. As insulin resistance is a important risk factor in vascular disease, we examined susceptibility of fld/fld mice to diet-induced atherosclerosis. Mutant mice fed an atherogenic diet developed 2-fold greater aortic lesions than their wild-type counterparts, despite having a less atherogenic lipoprotein cholesterol profile. The fld adipose-deficient phenotype has both similarities to and distinctions from the group of rare human diseases known as lipodystrophies.
- Published
- 2000
44. A locus conferring resistance to diet-induced hypercholesterolemia and atherosclerosis on mouse chromosome 2.
- Author
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Mouzeyan, A, Choi, J, Allayee, H, Wang, X, Sinsheimer, J, Phan, J, Castellani, L W, Reue, K, Lusis, A J, and Davis, R C
- Abstract
Dietary cholesterol is known to raise total and low density lipoprotein cholesterol concentrations in humans and experimental animals, but the response among individuals varies greatly. Here we describe a mouse strain, C57BL/6ByJ (B6By), that is resistant to diet-induced hypercholesterolemia, in contrast to the phenotype seen in other common strains of mice including the closely related C57BL/6J (B6J) strain. Compared to B6J, B6By mice exhibit somewhat lower basal cholesterol levels on a chow diet, and show a relatively modest increase in absolute levels of total and LDL/VLDL cholesterol in response to an atherogenic diet containing 15% fat, 1.25% cholesterol, and 0.5% cholate. Correspondingly, B6By mice are also resistant to diet-induced aortic lesions, with less than 15% as many lesions as B6J. Food intake and cholesterol absorption are similar between B6By and B6J mice.To investigate the gene(s) underlying the resistant B6By phenotype, we performed genetic crosses with the unrelated mouse strain, A/J. A genome-wide scan revealed a locus, designated Diet1, on chromosome 2 near marker D2Mit117 showing highly significant linkage (lod = 9.6) between B6By alleles and hypo-response to diet. Examination of known genes in this region suggested that this locus represents a novel gene affecting plasma lipids and atherogenesis in response to diet.
- Published
- 2000
45. Low level expression of hormone-sensitive lipase in arterial macrophage-derived foam cells: potential explanation for low rates of cholesteryl ester hydrolysis
- Author
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Harte, R. A., Hulten, L. M., Lindmark, H., Reue, K., Schotz, M. C., Khoo, J., and Rosenfeld, M. E.
- Published
- 2000
- Full Text
- View/download PDF
46. Paradoxical effect on atherosclerosis of hormone-sensitive lipase overexpression in macrophages.
- Author
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Escary, J L, Choy, H A, Reue, K, Wang, X P, Castellani, L W, Glass, C K, Lusis, A J, and Schotz, M C
- Abstract
Foam cells formed from receptor-mediated uptake of lipoprotein cholesterol by macrophages in the arterial intima are critical in the initiation, progression, and stability of atherosclerotic lesions. Macrophages accumulate cholesterol when conditions favor esterification by acyl-CoA:cholesterol acyltransferase (ACAT) over cholesteryl-ester hydrolysis by a neutral cholesteryl-ester hydrolase, such as hormone-sensitive lipase (HSL), and subsequent cholesterol efflux mediated by extracellular acceptors. We recently made stable transfectants of a murine macrophage cell line, RAW 264.7, that overexpressed a rat HSL cDNA and had a 5-fold higher rate of cholesteryl-ester hydrolysis than control cells. The current study examined the effect of macrophage-specific HSL overexpression on susceptibility to diet-induced atherosclerosis in mice. A transgenic line overexpressing the rat HSL cDNA regulated with a macrophage-specific scavenger receptor promoter-enhancer was established by breeding with C57BL/6J mice. Transgenic peritoneal macrophages exhibited macrophage-specific 7-fold overexpression of HSL cholesterol esterase activity. Total plasma cholesterol levels in transgenic mice fed a chow diet were modestly elevated 16% compared to control littermates. After 14 weeks on a high-fat, high-cholesterol diet, total cholesterol increased 3-fold, with no difference between transgenics and controls. However, HSL overexpression resulted in thicker aortic fatty lesions that were 2.5-times larger in transgenic mice. HSL expression in the aortic lesions was shown by immunocytochemistry. Atherosclerosis was more advanced in transgenic mice exhibiting raised lesions involving the aortic wall, along with lipid accumulation in coronary arteries occurring only in transgenics. Thus, increasing cholesteryl-ester hydrolysis, without concomitantly decreasing ACAT activity or increasing cholesterol efflux, is not sufficient to protect against atherosclerosis. hormone-sensitive lipase overexpression in macrophages.
- Published
- 1999
47. Altered gene expression pattern in the fatty liver dystrophy mouse reveals impaired insulin-mediated cytoskeleton dynamics.
- Author
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Klingenspor, M, Xu, P, Cohen, R D, Welch, C, and Reue, K
- Abstract
The mouse fatty liver dystrophy (fld) mutation is characterized by transient hypertriglyceridemia and fatty liver during the neonatal period, followed by development of a peripheral neuropathy. To uncover the metabolic pathway that is disrupted by the fld mutation, we analyzed the altered pattern of gene expression in the fatty liver of fld neonates by representational difference analysis of cDNA. Differentially expressed genes detected include a novel member of the Ras superfamily of small GTP-binding proteins, a novel Ser/Thr kinase, and several actin cytoskeleton-associated proteins including actin, profilin, alpha-actinin, and myosin light chain. Because these proteins have a potential functional link in the propagation of hormone signals, we investigated cytoskeleton dynamics in fld cells in response to hormone treatment. These studies revealed that preadipocytes from fld mice exhibit impaired formation of actin membrane ruffles in response to insulin treatment. These findings suggest that the altered mRNA expression levels detected in fld tissue represent a compensatory response for the nonfunctional fld gene and that the fld gene product may be required for development of normal insulin response.
- Published
- 1999
48. Human apolipoprotein CIII gene expression is regulated by positive and negative cis-acting elements and tissue-specific protein factors.
- Author
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Reue, K, Leff, T, and Breslow, J L
- Abstract
Apolipoprotein CIII (apoCIII) is a major protein constituent of triglyceride-rich lipoproteins and is synthesized primarily in the liver. Cis-acting DNA elements required for liver-specific apoCIII gene transcription were identified with transient expression assays in the human hepatoma (HepG2) and epithelial carcinoma (HeLa) cell lines. In liver cells, 821 nucleotides of the human apoCIII gene 5'-flanking sequence were required for maximum levels of gene expression, while the proximal 110 nucleotides alone were sufficient. No expression was observed in similar studies with HeLa cells. The level of expression was modulated by a combination of positive and negative cis-acting sequences, which interact with distinct sets of proteins from liver and HeLa cell nuclear extracts. The proximal positive regulatory region shares homology with similarly located sequences of other genes strongly expressed in the liver, including alpha 1-antitrypsin and other apolipoprotein genes. The negative regulatory region is strikingly homologous to the human beta-interferon gene regulatory element. The distal positive region shares homology with some viral enhancers and has properties of a tissue-specific enhancer. The regulation of the apoCIII gene is complex but shares features with other genes, suggesting shuffling of regulatory elements as a common mechanism for cell type-specific gene expression.
- Published
- 1988
- Full Text
- View/download PDF
49. The fatty liver dystrophy mutant mouse: microvesicular steatosis associated with altered expression levels of peroxisome proliferator-regulated proteins.
- Author
-
Rehnmark, S, Giometti, C S, Slavin, B G, Doolittle, M H, and Reue, K
- Abstract
Fatty liver dystrophy ( fld) is an autosomal recessive mutation in mice characterized by hypertriglyceridemia and fatty liver during neonatal development. The fatty liver in fld/fld mice spontaneously resolves between the age of 14-18 days, at which point the animals develop a neuropathy associated with abnormal myelin formation in peripheral nerve. We have investigated the morphological and biochemical alterations that occur in the fatty liver of neonatal fld/fld mice. Studies at the light and electron microscopic level demonstrated the accumulation of lipid droplets and hypertrophic parenchymal cells in fld neonates, with no apparent liver pathology after resolution of the fatty liver. To better characterize the biochemical basis for the development of fatty liver in fld mice, we compared protein expression patterns in the fatty liver of fld mice and in the liver of phenotypically normal (wild-type) littermates using quantitative two-dimensional gel electrophoresis. We detected 24 proteins with significantly altered expression levels (P < 0.001) in the fld fatty liver, 15 of which are proteins that are altered in abundance by peroxisome proliferating chemicals. As these compounds characteristically elicit changes in the expression of mitochondrial and peroxisomal enzymes involved in fatty acid oxidation, we quantitated rates of fatty acid oxidation in hepatocytes isolated from fld and wild-type mice. These studies revealed that hepatic fatty acid oxidation in fld neonates is reduced by 60% compared to wild-type littermates. In hepatocytes from adult fld mice that no longer exhibit a fatty liver, oxidation rates were similar to those in hepatocytes from age-matched wild-type mice. These findings indicate that altered expression of proteins involved in fatty acid oxidation is associated with triglyceride accumulation in the fld fatty liver.
- Published
- 1998
50. Lipid-protein interactions during ricin toxin insertion into membranes. Evidence for A and B chain penetration.
- Author
-
Ishida, B, Cawley, D B, Reue, K, and Wisnieski, B J
- Published
- 1983
- Full Text
- View/download PDF
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