102 results on '"Satriano, J A"'
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2. Kidney growth, hypertrophy and the unifying mechanism of diabetic complications
- Author
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Satriano, J.
- Published
- 2007
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3. Primary kidney growth and its consequences at the onset of diabetes mellitus
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Satriano, J. and Vallon, V.
- Published
- 2006
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4. Arginine pathways and the inflammatory response: Interregulation of nitric oxide and polyamines: Review article
- Author
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Satriano, J.
- Published
- 2004
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5. Biological effects of arginine metabolites
- Author
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BLANTZ, R C, SATRIANO, J, GABBAI, F, and KELLY, C
- Published
- 2000
6. Erratum to: Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition) (Autophagy, 12, 1, 1-222, 10.1080/15548627.2015.1100356
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Klionsky, D.J. Abdelmohsen, K. Abe, A. Abedin, M.J. Abeliovich, H. Arozena, A.A. Adachi, H. Adams, C.M. Adams, P.D. Adeli, K. Adhihetty, P.J. Adler, S.G. Agam, G. Agarwal, R. Aghi, M.K. Agnello, M. Agostinis, P. Aguilar, P.V. Aguirre-Ghiso, J. Airoldi, E.M. Ait-Si-Ali, S. Akematsu, T. Akporiaye, E.T. Al-Rubeai, M. Albaiceta, G.M. Albanese, C. Albani, D. Albert, M.L. Aldudo, J. Algül, H. Alirezaei, M. Alloza, I. Almasan, A. Almonte-Beceril, M. Alnemri, E.S. Alonso, C. Altan-Bonnet, N. Altieri, D.C. Alvarez, S. Alvarez-Erviti, L. Alves, S. Amadoro, G. Amano, A. Amantini, C. Ambrosio, S. Amelio, I. Amer, A.O. Amessou, M. Amon, A. An, Z. Anania, F.A. Andersen, S.U. Andley, U.P. Andreadi, C.K. Andrieu-Abadie, N. Anel, A. Ann, D.K. Anoopkumar-Dukie, S. Antonioli, M. Aoki, H. Apostolova, N. Aquila, S. Aquilano, K. Araki, K. Arama, E. Aranda, A. Araya, J. Arcaro, A. Arias, E. Arimoto, H. Ariosa, A.R. Armstrong, J.L. Arnould, T. Arsov, I. Asanuma, K. Askanas, V. Asselin, E. Atarashi, R. Atherton, S.S. Atkin, J.D. Attardi, L.D. Auberger, P. Auburger, G. Aurelian, L. Autelli, R. Avagliano, L. Avantaggiati, M.L. Avrahami, L. Azad, N. Awale, S. Bachetti, T. Backer, J.M. Bae, D.-H. Bae, J.-S. Bae, O.-N. Bae, S.H. Baehrecke, E.H. Baek, S.-H. Baghdiguian, S. Bagniewska-Zadworna, A. Bai, H. Bai, J. Bai, X.-Y. Bailly, Y. Balaji, K.N. Balduini, W. Ballabio, A. Balzan, R. Banerjee, R. Bánhegyi, G. Bao, H. Barbeau, B. Barrachina, M.D. Barreiro, E. Bartel, B. Bartolomé, A. Bassham, D.C. Bassi, M.T. Bast, R.C., Jr. Basu, A. Batista, M.T. Batoko, H. Battino, M. Bauckman, K. Baumgarner, B.L. Bayer, K.U. Beale, R. Beaulieu, J.-F. Beck, G.R., Jr. Becker, C. Beckham, J.D. Bédard, P.-A. Bednarski, P.J. Begley, T.J. Behl, C. Behrends, C. Behrens, G.M.N. Behrns, K.E. Bejarano, E. Belaid, A. Belleudi, F. Bénard, G. Berchem, G. Bergamaschi, D. Bergami, M. Berkhout, B. Berliocchi, L. Bernard, A. Bernard, M. Bernassola, F. Bertolotti, A. Bess, A.S. Besteiro, S. Bettuzzi, S. Bhalla, S. Bhattacharyya, S. Bhutia, S.K. Biagosch, C. Bianchi, M.W. Biard-Piechaczyk, M. Billes, V. Bincoletto, C. Bingol, B. Bird, S.W. Bitoun, M. Bjedov, I. Blackstone, C. Blanc, L. Blanco, G.A. Blomhoff, H.K. Boada-Romero, E. Böckler, S. Boes, M. Boesze-Battaglia, K. Boise, L.H. Bolino, A. Boman, A. Bonaldo, P. Bordi, M. Bosch, J. Botana, L.M. Botti, J. Bou, G. Bouché, M. Bouchecareilh, M. Boucher, M.-J. Boulton, M.E. Bouret, S.G. Boya, P. Boyer-Guittaut, M. Bozhkov, P.V. Brady, N. Braga, V.M.M. Brancolini, C. Braus, G.H. Bravo-San-Pedro, J.M. Brennan, L.A. Bresnick, E.H. Brest, P. Bridges, D. Bringer, M.-A. Brini, M. Brito, G.C. Brodin, B. Brookes, P.S. Brown, E.J. Brown, K. Broxmeyer, H.E. Bruhat, A. Brum, P.C. Brumell, J.H. Brunetti-Pierri, N. Bryson-Richardson, R.J. Buch, S. Buchan, A.M. Budak, H. Bulavin, D.V. Bultman, S.J. Bultynck, G. Bumbasirevic, V. Burelle, Y. Burke, R.E. Burmeister, M. Bütikofer, P. Caberlotto, L. Cadwell, K. Cahova, M. Cai, D. Cai, J. Cai, Q. Calatayud, S. Camougrand, N. Campanella, M. Campbell, G.R. Campbell, M. Campello, S. Candau, R. Caniggia, I. Cantoni, L. Cao, L. Caplan, A.B. Caraglia, M. Cardinali, C. Cardoso, S.M. Carew, J.S. Carleton, L.A. Carlin, C.R. Carloni, S. Carlsson, S.R. Carmona-Gutierrez, D. Carneiro, L.A.M. Carnevali, O. Carra, S. Carrier, A. Carroll, B. Casas, C. Casas, J. Cassinelli, G. Castets, P. Castro-Obregon, S. Cavallini, G. Ceccherini, I. Cecconi, F. Cederbaum, A.I. Ceña, V. Cenci, S. Cerella, C. Cervia, D. Cetrullo, S. Chaachouay, H. Chae, H.-J. Chagin, A.S. Chai, C.-Y. Chakrabarti, G. Chamilos, G. Chan, E.Y.W. Chan, M.T.V. Chandra, D. Chandra, P. Chang, C.-P. Chang, R.C.-C. Chang, T.Y. Chatham, J.C. Chatterjee, S. Chauhan, S. Che, Y. Cheetham, M.E. Cheluvappa, R. Chen, C.-J. Chen, G. Chen, G.-C. Chen, G. Chen, H. Chen, J.W. Chen, J.-K. Chen, M. Chen, M. Chen, P. Chen, Q. Chen, Q. Chen, S.-D. Chen, S. Chen, S.S.-L. Chen, W. Chen, W.-J. Chen, W.Q. Chen, W. Chen, X. Chen, Y.-H. Chen, Y.-G. Chen, Y. Chen, Y. Chen, Y. Chen, Y.-J. Chen, Y.-Q. Chen, Y. Chen, Z. Chen, Z. Cheng, A. Cheng, C.H.K. Cheng, H. Cheong, H. Cherry, S. Chesney, J. Cheung, C.H.A. Chevet, E. Chi, H.C. Chi, S.-G. Chiacchiera, F. Chiang, H.-L. Chiarelli, R. Chiariello, M. Chieppa, M. Chin, L.-S. Chiong, M. Chiu, G.N.C. Cho, D.-H. Cho, S.-G. Cho, W.C. Cho, Y.-Y. Cho, Y.-S. Choi, A.M.K. Choi, E.-J. Choi, E.-K. Choi, J. Choi, M.E. Choi, S.-I. Chou, T.-F. Chouaib, S. Choubey, D. Choubey, V. Chow, K.-C. Chowdhury, K. Chu, C.T. Chuang, T.-H. Chun, T. Chung, H. Chung, T. Chung, Y.-L. Chwae, Y.-J. Cianfanelli, V. Ciarcia, R. Ciechomska, I.A. Ciriolo, M.R. Cirone, M. Claerhout, S. Clague, M.J. Cl� ria, J. Clarke, P.G.H. Clarke, R. Clementi, E. Cleyrat, C. Cnop, M. Coccia, E.M. Cocco, T. Codogno, P. Coers, J. Cohen, E.E.W. Colecchia, D. Coletto, L. Coll, N.S. Colucci-Guyon, E. Comincini, S. Condello, M. Cook, K.L. Coombs, G.H. Cooper, C.D. Cooper, J.M. Coppens, I. Corasaniti, M.T. Corazzari, M. Corbalan, R. Corcelle-Termeau, E. Cordero, M.D. Corral-Ramos, C. Corti, O. Cossarizza, A. Costelli, P. Costes, S. Cotman, S.L. Coto-Montes, A. Cottet, S. Couve, E. Covey, L.R. Cowart, L.A. Cox, J.S. Coxon, F.P. Coyne, C.B. Cragg, M.S. Craven, R.J. Crepaldi, T. Crespo, J.L. Criollo, A. Crippa, V. Cruz, M.T. Cuervo, A.M. Cuezva, J.M. Cui, T. Cutillas, P.R. Czaja, M.J. Czyzyk-Krzeska, M.F. Dagda, R.K. Dahmen, U. Dai, C. Dai, W. Dai, Y. Dalby, K.N. Valle, L.D. Dalmasso, G. D'amelio, M. Damme, M. Darfeuille-Michaud, A. Dargemont, C. Darley-Usmar, V.M. Dasarathy, S. Dasgupta, B. Dash, S. Dass, C.R. Davey, H.M. Davids, L.M. Dávila, D. Davis, R.J. Dawson, T.M. Dawson, V.L. Daza, P. de Belleroche, J. de Figueiredo, P. de Figueiredo, R.C.B.Q. de la Fuente, J. De Martino, L. De Matteis, A. De Meyer, G.R.Y. De Milito, A. De Santi, M. de Souza, W. De Tata, V. De Zio, D. Debnath, J. Dechant, R. Decuypere, J.-P. Deegan, S. Dehay, B. Del Bello, B. Del Re, D.P. Delage-Mourroux, R. Delbridge, L.M.D. Deldicque, L. Delorme-Axford, E. Deng, Y. Dengjel, J. Denizot, M. Dent, P. Der, C.J. Deretic, V. Derrien, B. Deutsch, E. Devarenne, T.P. Devenish, R.J. Di Bartolomeo, S. Di Daniele, N. Di Domenico, F. Di Nardo, A. Di Paola, S. Di Pietro, A. Di Renzo, L. Di Antonio, A. Díaz-Araya, G. Díaz-Laviada, I. Diaz-Meco, M.T. Diaz-Nido, J. Dickey, C.A. Dickson, R.C. Diederich, M. Digard, P. Dikic, I. Dinesh-Kumar, S.P. Ding, C. Ding, W.-X. Ding, Z. Dini, L. Distler, J.H.W. Diwan, A. Djavaheri-Mergny, M. Dmytruk, K. Dobson, R.C.J. Doetsch, V. Dokladny, K. Dokudovskaya, S. Donadelli, M. Dong, X.C. Dong, X. Dong, Z. Donohue, T.M., Jr. Donohue-Jr, T.M. Doran, K.S. D'orazi, G. Dorn, G.W., II Dosenko, V. Dridi, S. Drucker, L. Du, J. Du, L.-L. Du, L. du Toit, A. Dua, P. Duan, L. Duann, P. Dubey, V.K. Duchen, M.R. Duchosal, M.A. Duez, H. Dugail, I. Dumit, V.I. Duncan, M.C. Dunlop, E.A. Dunn, W.A., Jr. Dupont, N. Dupuis, L. Durán, R.V. Durcan, T.M. Duvezin-Caubet, S. Duvvuri, U. Eapen, V. Ebrahimi-Fakhari, D. Echard, A. Eckhart, L. Edelstein, C.L. Edinger, A.L. Eichinger, L. Eisenberg, T. Eisenberg-Lerner, A. Eissa, N.T. El-Deiry, W.S. El-Khoury, V. Elazar, Z. Eldar-Finkelman, H. Elliott, C.J.H. Emanuele, E. Emmenegger, U. Engedal, N. Engelbrecht, A.-M. Engelender, S. Enserink, J.M. Erdmann, R. Erenpreisa, J. Eri, R. Eriksen, J.L. Erman, A. Escalante, R. Eskelinen, E.-L. Espert, L. Esteban-Martínez, L. Evans, T.J. Fabri, M. Fabrias, G. Fabrizi, C. Facchiano, A. Færgeman, N.J. Faggioni, A. Fairlie, W.D. Fan, C. Fan, D. Fan, J. Fang, S. Fanto, M. Fanzani, A. Farkas, T. Faure, M. Favier, F.B. Fearnhead, H. Federici, M. Fei, E. Felizardo, T.C. Feng, H. Feng, Y. Feng, Y. Ferguson, T.A. Fernández, Á.F. Fernandez-Barrena, M.G. Fernandez-Checa, J.C. Fernández-López, A. Fernandez-Zapico, M.E. Feron, O. Ferraro, E. Ferreira-Halder, C.V. Fesus, L. Feuer, R. Fiesel, F.C. Filippi-Chiela, E.C. Filomeni, G. Fimia, G.M. Fingert, J.H. Finkbeiner, S. Finkel, T. Fiorito, F. Fisher, P.B. Flajolet, M. Flamigni, F. Florey, O. Florio, S. Floto, R.A. Folini, M. Follo, C. Fon, E.A. Fornai, F. Fortunato, F. Fraldi, A. Franco, R. Francois, A. François, A. Frankel, L.B. Fraser, I.D.C. Frey, N. Freyssenet, D.G. Frezza, C. Friedman, S.L. Frigo, D.E. Fu, D. Fuentes, J.M. Fueyo, J. Fujitani, Y. Fujiwara, Y. Fujiya, M. Fukuda, M. Fulda, S. Fusco, C. Gabryel, B. Gaestel, M. Gailly, P. Gajewska, M. Galadari, S. Galili, G. Galindo, I. Galindo, M.F. Galliciotti, G. Galluzzi, L. Galluzzi, L. Galy, V. Gammoh, N. Gandy, S. Ganesan, A.K. Ganesan, S. Ganley, I.G. Gannagé, M. Gao, F.-B. Gao, F. Gao, J.-X. Nannig, L.G. Véscovi, E.G. Garcia-Macía, M. Garcia-Ruiz, C. Garg, A.D. Garg, P.K. Gargini, R. Gassen, N.C. Gatica, D. Gatti, E. Gavard, J. Gavathiotis, E. Ge, L. Ge, P. Ge, S. Gean, P.-W. Gelmetti, V. Genazzani, A.A. Geng, J. Genschik, P. Gerner, L. Gestwicki, J.E. Gewirtz, D.A. Ghavami, S. Ghigo, E. Ghosh, D. Giammarioli, A.M. Giampieri, F. Giampietri, C. Giatromanolaki, A. Gibbings, D.J. Gibellini, L. Gibson, S.B. Ginet, V. Giordano, A. Giorgini, F. Giovannetti, E. Girardin, S.E. Gispert, S. Giuliano, S. Gladson, C.L. Glavic, A. Gleave, M. Godefroy, N. Gogal, R.M., Jr. Gokulan, K. Goldman, G.H. Goletti, D. Goligorsky, M.S. Gomes, A.V. Gomes, L.C. Gomez, H. Gomez-Manzano, C. Gómez-Sánchez, R. Gonçalves, D.A.P. Goncu, E. Gong, Q. Gongora, C. Gonzalez, C.B. Gonzalez-Alegre, P. Gonzalez-Cabo, P. González-Polo, R.A. Goping, I.S. Gorbea, C. Gorbunov, N.V. Goring, D.R. Gorman, A.M. Gorski, S.M. Goruppi, S. Goto-Yamada, S. Gotor, C. Gottlieb, R.A. Gozes, I. Gozuacik, D. Graba, Y. Graef, M. Granato, G.E. Grant, G.D. Grant, S. Gravina, G.L. Green, D.R. Greenhough, A. Greenwood, M.T. Grimaldi, B. Gros, F. Grose, C. Groulx, J.-F. Gruber, F. Grumati, P. Grune, T. Guan, J.-L. Guan, K.-L. Guerra, B. Guillen, C. Gulshan, K. Gunst, J. Guo, C. Guo, L. Guo, M. Guo, W. Guo, X.-G. Gust, A.A. Gustafsson, Å.B. Gutierrez, E. Gutierrez, M.G. Gwak, H.-S. Haas, A. Haber, J.E. Hadano, S. Hagedorn, M. Hahn, D.R. Halayko, A.J. Hamacher-Brady, A. Hamada, K. Hamai, A. Hamann, A. Hamasaki, M. Hamer, I. Hamid, Q. Hammond, E.M. Han, F. Han, W. Handa, J.T. Hanover, J.A. Hansen, M. Harada, M. Harhaji-Trajkovic, L. Harper, J.W. Harrath, A.H. Harris, A.L. Harris, J. Hasler, U. Hasselblatt, P. Hasui, K. Hawley, R.G. Hawley, T.S. He, C. He, C.Y. He, F. He, G. He, R.-R. He, X.-H. He, Y.-W. He, Y.-Y. Heath, J.K. Hébert, M.-J. Heinzen, R.A. Helgason, G.V. Hensel, M. Henske, E.P. Her, C. Herman, P.K. Hernández, A. Hernandez, C. Hernández-Tiedra, S. Hetz, C. Hiesinger, P.R. Higaki, K. Hilfiker, S. Hill, B.G. Hill, J.A. Hill, W.D. Hino, K. Hofius, D. Hofman, P. Höglinger, G.U. Höhfeld, J. Holz, M.K. Hong, Y. Hood, D.A. Hoozemans, J.J.M. Hoppe, T. Hsu, C. Hsu, C.-Y. Hsu, L.-C. Hu, D. Hu, G. Hu, H.-M. Hu, H. Hu, M.C. Hu, Y.-C. Hu, Z.-W. Hua, F. Hua, Y. Huang, C. Huang, H.-L. Huang, K.-H. Huang, K.-Y. Huang, S. Huang, S. Huang, W.-P. Huang, Y.-R. Huang, Y. Huang, Y. Huber, T.B. Huebbe, P. Huh, W.-K. Hulmi, J.J. Hur, G.M. Hurley, J.H. Husak, Z. Hussain, S.N.A. Hussain, S. Hwang, J.J. Hwang, S. Hwang, T.I.S. Ichihara, A. Imai, Y. Imbriano, C. Inomata, M. Into, T. Iovane, V. Iovanna, J.L. Iozzo, R.V. Ip, N.Y. Irazoqui, J.E. Iribarren, P. Isaka, Y. Isakovic, A.J. Ischiropoulos, H. Isenberg, J.S. Ishaq, M. Ishida, H. Ishii, I. Ishmael, J.E. Isidoro, C. Isobe, K.-I. Isono, E. Issazadeh-Navikas, S. Itahana, K. Itakura, E. Ivanov, A.I. Iyer, A.K.V. Izquierdo, J.M. Izumi, Y. Izzo, V. Jäättelä, M. Jaber, N. Jackson, D.J. Jackson, W.T. Jacob, T.G. Jacques, T.S. Jagannath, C. Jain, A. Jana, N.R. Jang, B.K. Jani, A. Janji, B. Jannig, P.R. Jansson, P.J. Jean, S. Jendrach, M. Jeon, J.-H. Jessen, N. Jeung, E.-B. Jia, K. Jia, L. Jiang, H. Jiang, H. Jiang, L. Jiang, T. Jiang, X. Jiang, X. Jiang, Y. Jiang, Y. Jiménez, A. Jin, C. Jin, H. Jin, L. Jin, M. Jin, S. Jinwal, U.K. Jo, E.-K. Johansen, T. Johnson, D.E. Johnson, G.V.W. Johnson, J.D. Jonasch, E. Jones, C. Joosten, L.A.B. Jordan, J. Joseph, A.-M. Joseph, B. Joubert, A.M. Ju, D. Ju, J. Juan, H.-F. Juenemann, K. Juhász, G. Jung, H.S. Jung, J.U. Jung, Y.-K. Jungbluth, H. Justice, M.J. Jutten, B. Kaakoush, N.O. Kaarniranta, K. Kaasik, A. Kabuta, T. Kaeffer, B. Kågedal, K. Kahana, A. Kajimura, S. Kakhlon, O. Kalia, M. Kalvakolanu, D.V. Kamada, Y. Kambas, K. Kaminskyy, V.O. Kampinga, H.H. Kandouz, M. Kang, C. Kang, R. Kang, T.-C. Kanki, T. Kanneganti, T.-D. Kanno, H. Kanthasamy, A.G. Kantorow, M. Kaparakis-Liaskos, M. Kapuy, O. Karantza, V. Karim, M.R. Karmakar, P. Kaser, A. Kaushik, S. Kawula, T. Kaynar, A.M. Ke, P.-Y. Ke, Z.-J. Kehrl, J.H. Keller, K.E. Kemper, J.K. Kenworthy, A.K. Kepp, O. Kern, A. Kesari, S. Kessel, D. Ketteler, R. Kettelhut, I.C. Khambu, B. Khan, M.M. Khandelwal, V.K.M. Khare, S. Kiang, J.G. Kiger, A.A. Kihara, A. Kim, A.L. Kim, C.H. Kim, D.R. Kim, D.-H. Kim, E.K. Kim, H.Y. Kim, H.-R. Kim, J.-S. Kim, J.H. Kim, J.C. Kim, J.H. Kim, K.W. Kim, M.D. Kim, M.-M. Kim, P.K. Kim, S.W. Kim, S.-Y. Kim, Y.-S. Kim, Y. Kimchi, A. 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Lamark, T. Lancel, S. Landowski, T.H. Lane, D.J.R. Lane, J.D. Lanzi, C. Lapaquette, P. Lapierre, L.R. Laporte, J. Laukkarinen, J. Laurie, G.W. Lavandero, S. Lavie, L. Lavoie, M.J. Law, B.Y.K. Law, H.K.-W. Law, K.B. Layfield, R. Lazo, P.A. Le Cam, L. Le Roch, K.G. Le Stunff, H. Leardkamolkarn, V. Lecuit, M. Lee, B.-H. Lee, C.-H. Lee, E.F. Lee, G.M. Lee, H.-J. Lee, H. Lee, J.K. Lee, J. Lee, J.-H. Lee, J.H. Lee, M. Lee, M.-S. Lee, P.J. Lee, S.W. Lee, S.-J. Lee, S.-J. Lee, S.Y. Lee, S.H. Lee, S.S. Lee, S.-J. Lee, S. Lee, Y.-R. Lee, Y.J. Lee, Y.H. Leeuwenburgh, C. Lefort, S. Legouis, R. Lei, J. Lei, Q.-Y. Leib, D.A. Leibowitz, G. Lekli, I. Lemaire, S.D. Lemasters, J.J. Lemberg, M.K. Lemoine, A. Leng, S. Lenz, G. Lenzi, P. Lerman, L.O. Barbato, D.L. Leu, J.I.J. Leung, H.Y. Levine, B. Lewis, P.A. Lezoualch, F. Li, C. Li, F. Li, F.-J. Li, J. Li, K. Li, L. Li, M. Li, Q. Li, R. Li, S. Li, W. Li, X. Li, Y. Lian, J. Liang, C. Liang, Q. Liao, Y. Liberal, J. Liberski, P.P. Lie, P. Lieberman, A.P. 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7. Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition). Autophagy
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- Published
- 2016
8. Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)
- Author
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Klionsky, D.J. Abdelmohsen, K. Abe, A. Abedin, M.J. Abeliovich, H. Arozena, A.A. Adachi, H. Adams, C.M. Adams, P.D. Adeli, K. Adhihetty, P.J. Adler, S.G. Agam, G. Agarwal, R. Aghi, M.K. Agnello, M. Agostinis, P. Aguilar, P.V. Aguirre-Ghiso, J. Airoldi, E.M. Ait-Si-Ali, S. Akematsu, T. Akporiaye, E.T. Al-Rubeai, M. Albaiceta, G.M. Albanese, C. Albani, D. Albert, M.L. Aldudo, J. Algül, H. Alirezaei, M. Alloza, I. Almasan, A. Almonte-Beceril, M. Alnemri, E.S. Alonso, C. Altan-Bonnet, N. Altieri, D.C. Alvarez, S. Alvarez-Erviti, L. Alves, S. Amadoro, G. Amano, A. Amantini, C. Ambrosio, S. Amelio, I. Amer, A.O. Amessou, M. Amon, A. An, Z. Anania, F.A. Andersen, S.U. Andley, U.P. Andreadi, C.K. Andrieu-Abadie, N. Anel, A. Ann, D.K. Anoopkumar-Dukie, S. Antonioli, M. Aoki, H. Apostolova, N. Aquila, S. Aquilano, K. Araki, K. Arama, E. Aranda, A. Araya, J. Arcaro, A. Arias, E. Arimoto, H. Ariosa, A.R. Armstrong, J.L. Arnould, T. Arsov, I. Asanuma, K. Askanas, V. Asselin, E. Atarashi, R. 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- Published
- 2016
9. Erratum to: Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition) (Autophagy, 12, 1, 1-222, 10.1080/15548627.2015.1100356
- Author
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Robin, Higaki, Katsumi, Hilfiker, Sabine, Hill, Bradford G., Hill, Joseph A., Hill, William D., Hino, Keisuke, Hofius, Daniel, Hofman, Paul, Höglinger, Günter U., Höhfeld, Jörg, Holz, Marina K., Hong, Yonggeun, Hood, David A., Hoozemans, Jeroen J.M., Hoppe, Thorsten, Hsu, Chin, Hsu, Chin-Yuan, Hsu, Li-Chung, Hu, Dong, Hu, Guochang, Hu, Hong-Ming, Hu, Hongbo, Hu, Ming Chang, Hu, Yu-Chen, Hu, Zhuo-Wei, Hua, Fang, Hua, Ya, Huang, Canhua, Huang, Huey-Lan, Huang, Kuo-How, Huang, Kuo-Yang, Huang, Shile, Huang, Shiqian, Huang, Wei-Pang, Huang, Yi-Ran, Huang, Yong, Huang, Yunfei, Huber, Tobias B., Huebbe, Patricia, Huh, Won-Ki, Hulmi, Juha J., Hur, Gang Min, Hurley, James H., Husak, Zvenyslava, Hussain, Sabah N.A., Hussain, Salik, Hwang, Jung Jin, Hwang, Seungmin, Hwang, Thomas I.S., Ichihara, Atsuhiro, Imai, Yuzuru, Imbriano, Carol, Inomata, Megumi, Into, Takeshi, Iovane, Valentina, Iovanna, Juan L., Iozzo, Renato V., Ip, Nancy Y., Irazoqui, Javier E., Iribarren, Pablo, Isaka, Yoshitaka, Isakovic, Aleksandra J., Ischiropoulos, Harry, Isenberg, Jeffrey S., Ishaq, Mohammad, Ishida, Hiroyuki, Ishii, Isao, Ishmael, Jane E., Isidoro, Ciro, Isobe, Ken-Ichi, Isono, Erika, Issazadeh-Navikas, Shohreh, Itahana, Koji, Itakura, Eisuke, Ivanov, Andrei I., Iyer, Anand Krishnan V., Izquierdo, José M., Izumi, Yotaro, Izzo, Valentina, Jäättelä, Marja, Jaber, Nadia, Jackson, Daniel John, Jackson, William T., Jacob, Tony George, Jacques, Thomas S., Jagannath, Chinnaswamy, Jain, Ashish, Jana, Nihar Ranjan, Jang, Byoung Kuk, Jani, Alkesh, Janji, Bassam, Jannig, Paulo Roberto, Jansson, Patric J., Jean, Steve, Jendrach, Marina, Jeon, Ju-Hong, Jessen, Niel, Jeung, Eui-Bae, Jia, Kailiang, Jia, Lijun, Jiang, Hong, Jiang, Hongchi, Jiang, Liwen, Jiang, Teng, Jiang, Xiaoyan, Jiang, Xuejun, Jiang, Ying, Jiang, Yongjun, Jiménez, Alberto, Jin, Cheng, Jin, Hongchuan, Jin, Lei, Jin, Meiyan, Jin, Shengkan, Jinwal, Umesh Kumar, Jo, Eun-Kyeong, Johansen, Terje, Johnson, Daniel E., Johnson, Gail V.W., Johnson, James D., Jonasch, Eric, Jones, Chri, Joosten, Leo A.B., Jordan, Joaquin, Joseph, Anna-Maria, Joseph, Bertrand, Joubert, Annie M., Ju, Dianwen, Ju, Jingfang, Juan, Hsueh-Fen, Juenemann, Katrin, Juhász, Gábor, Jung, Hye Seung, Jung, Jae U., Jung, Yong-Keun, Jungbluth, Heinz, Justice, Matthew J., Jutten, Barry, Kaakoush, Nadeem O., Kaarniranta, Kai, Kaasik, Allen, Kabuta, Tomohiro, Kaeffer, Bertrand, Kågedal, Katarina, Kahana, Alon, Kajimura, Shingo, Kakhlon, Or, Kalia, Manjula, Kalvakolanu, Dhan V., Kamada, Yoshiaki, Kambas, Konstantino, Kaminskyy, Vitaliy O., Kampinga, Harm H., Kandouz, Mustapha, Kang, Chanhee, Kang, Rui, Kang, Tae-Cheon, Kanki, Tomotake, Kanneganti, Thirumala-Devi, Kanno, Haruo, Kanthasamy, Anumantha G., Kantorow, Marc, Kaparakis-Liaskos, Maria, Kapuy, Orsolya, Karantza, Vassiliki, Karim, Md Razaul, Karmakar, Parimal, Kaser, Arthur, Kaushik, Susmita, Kawula, Thoma, Kaynar, A. Murat, Ke, Po-Yuan, Ke, Zun-Ji, Kehrl, John H., Keller, Kate E., Kemper, Jongsook Kim, Kenworthy, Anne K., Kepp, Oliver, Kern, Andrea, Kesari, Santosh, Kessel, David, Ketteler, Robin, Kettelhut, Isis do Carmo, Khambu, Bilon, Khan, Muzamil Majid, Khandelwal, Vinoth K.M., Khare, Sangeeta, Kiang, Juliann G., Kiger, Amy A., Kihara, Akio, Kim, Arianna L., Kim, Cheol Hyeon, Kim, Deok Ryong, Kim, Do-Hyung, Kim, Eung Kweon, Kim, Hye Young, Kim, Hyung-Ryong, Kim, Jae-Sung, Kim, Jeong Hun, Kim, Jin Cheon, Kim, Jin Hyoung, Kim, Kwang Woon, Kim, Michael D., Kim, Moon-Moo, Kim, Peter K., Kim, Seong Who, Kim, Soo-Youl, Kim, Yong-Sun, Kim, Yonghyun, Kimchi, Adi, Kimmelman, Alec C., Kimura, Tomonori, King, Jason S., Kirkegaard, Karla, Kirkin, Vladimir, Kirshenbaum, Lorrie A., Kishi, Shuji, Kitajima, Yasuo, Kitamoto, Katsuhiko, Kitaoka, Yasushi, Kitazato, Kaio, Kley, Rudolf A., Klimecki, Walter T., Klinkenberg, Michael, Klucken, Jochen, Knævelsrud, Helene, Knecht, Erwin, Knuppertz, Laura, Ko, Jiunn-Liang, Kobayashi, Satoru, Koch, Jan C., Koechlin-Ramonatxo, Christelle, Koenig, Ulrich, Koh, Young Ho, Köhler, Katja, Kohlwein, Sepp D., Koike, Masato, Komatsu, Masaaki, Kominami, Eiki, Kong, Dexin, Kong, Hee Jeong, Konstantakou, Eumorphia G., Kopp, Benjamin T., Korcsmaros, Tama, Korhonen, Laura, Korolchuk, Viktor I., Koshkina, Nadya V., Kou, Yanjun, Koukourakis, Michael I., Koumenis, Constantino, Kovács, Attila L., Kovács, Tibor, Kovacs, Werner J., Koya, Daisuke, Kraft, Claudine, Krainc, Dimitri, Kramer, Helmut, Kravic-Stevovic, Tamara, Krek, Wilhelm, Kretz-Remy, Carole, Krick, Roswitha, Krishnamurthy, Malathi, Kriston-Vizi, Jano, Kroemer, Guido, Kruer, Michael C., Kruger, Rejko, Ktistakis, Nicholas T., Kuchitsu, Kazuyuki, Kuhn, Christian, Kumar, Addanki Pratap, Kumar, Anuj, Kumar, Ashok, Kumar, Deepak, Kumar, Dhiraj, Kumar, Rakesh, Kumar, Sharad, Kundu, Mondira, Kung, Hsing-Jien, Kuno, Atsushi, Kuo, Sheng-Han, Kuret, Jeff, Kurz, Tino, Kwok, Terry, Kwon, Taeg Kyu, Kwon, Yong Tae, Kyrmizi, Irene, La Spada, Albert R., Lafont, Frank, Lahm, Tim, Lakkaraju, Aparna, Lam, Truong, Lamark, Trond, Lancel, Steve, Landowski, Terry H., Lane, Darius J.R., Lane, Jon D., Lanzi, Cinzia, Lapaquette, Pierre, Lapierre, Louis R., Laporte, Jocelyn, Laukkarinen, Johanna, Laurie, Gordon W., Lavandero, Sergio, Lavie, Lena, Lavoie, Matthew J., Law, Betty Yuen Kwan, Law, Helen Ka-Wai, Law, Kelsey B., Layfield, Robert, Lazo, Pedro A., Le Cam, Laurent, Le Roch, Karine G., Le Stunff, Hervé, Leardkamolkarn, Vijittra, Lecuit, Marc, Lee, Byung-Hoon, Lee, Che-Hsin, Lee, Erinna F., Lee, Gyun Min, Lee, He-Jin, Lee, Hsinyu, Lee, Jae Keun, Lee, Jongdae, Lee, Ju-Hyun, Lee, Jun Hee, Lee, Michael, Lee, Myung-Shik, Lee, Patty J., Lee, Sam W., Lee, Seung-Jae, Lee, Shiow-Ju, Lee, Stella Y., Lee, Sug Hyung, Lee, Sung Sik, Lee, Sung-Joon, Lee, Sunhee, Lee, Ying-Ray, Lee, Yong J., Lee, Young H., Leeuwenburgh, Christiaan, Lefort, Sylvain, Legouis, Renaud, Lei, Jinzhi, Lei, Qun-Ying, Leib, David A., Leibowitz, Gil, Lekli, Istvan, Lemaire, Stéphane D., Lemasters, John J., Lemberg, Marius K., Lemoine, Antoinette, Leng, Shuilong, Lenz, Guido, Lenzi, Paola, Lerman, Lilach O., Barbato, Daniele Lettieri, Leu, Julia I. 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Sue, Menna-Barreto, Rubem F.S., Menon, Manoj B., Meraz-Ríos, Marco A., Merla, Giuseppe, Merlini, Luciano, Merlot, Angelica M., Meryk, Andrea, Meschini, Stefania, Meyer, Joel N., Mi, Man-Tian, Miao, Chao-Yu, Micale, Lucia, Michaeli, Simon, Michiels, Carine, Migliaccio, Anna Rita, Mihailidou, Anastasia Susie, Mijaljica, Dalibor, Mikoshiba, Katsuhiko, Milan, Enrico, Miller-Fleming, Leonor, Mills, Gordon B., Mills, Ian G., Minakaki, Georgia, Minassian, Berge A., Ming, Xiu-Fen, Minibayeva, Farida, Minina, Elena A., Mintern, Justine D., Minucci, Saverio, Miranda-Vizuete, Antonio, Mitchell, Claire H., Miyamoto, Shigeki, Miyazawa, Keisuke, Mizushima, Noboru, Mnich, Katarzyna, Mograbi, Baharia, Mohseni, Simin, Moita, Luis Ferreira, Molinari, Marco, Molinari, Maurizio, Møller, Andreas Buch, Mollereau, Bertrand, Mollinedo, Faustino, Mongillo, Marco, Monick, Martha M., Montagnaro, Serena, Montell, Craig, Moore, Darren J., Moore, Michael N., Mora-Rodriguez, Rodrigo, Moreira, Paula I., Morel, Etienne, Morelli, Maria Beatrice, Moreno, Sandra, Morgan, Michael J., Moris, Arnaud, Moriyasu, Yuji, Morrison, Janna L., Morrison, Lynda A., Morselli, Eugenia, Moscat, Jorge, Moseley, Pope L., Mostowy, Serge, Motori, Elisa, Mottet, Deni, Mottram, Jeremy C., Moussa, Charbel E.-H., Mpakou, Vassiliki E., Mukhtar, Hasan, Levy, Jean M. 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- Subjects
Molecular Biology ,Cell Biology ,Settore BIO/06 - Anatomia Comparata E Citologia - Abstract
non presente
- Published
- 2016
10. Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition).
- Author
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Yang, Wy, Yang, X, Yang, Y, Yang, Z, Yao, Mc, Yao, Pj, Yao, X, Yao, Z, Yasui, L, Ye, M, Yedvobnick, B, Yeganeh, B, Yeh, E, Yeyati, Pl, Yi, F, Yi, L, Yin, Xm, Yip, Ck, Yoo, Ym, Yoo, Yh, Yoon, Sy, Yoshida, K, Yoshimori, T, Young, Kh, Yu, H, Yu, Jj, Yu, Jt, Yu, J, Yu, L, Yu, Wh, Yu, Xf, Yu, Z, Yuan, J, Yuan, Zm, Yue, By, Yue, J, Yue, Z, Zacks, Dn, Zacksenhaus, E, Zaffaroni, N, Zaglia, T, Zakeri, Z, Zecchini, V, Zeng, J, Zeng, M, Zeng, Q, Zervos, A, Zhang, Dd, Zhang, F, Zhang, G, Zhang, Gc, Zhang, H, Zhang, J, Zhang, Jp, Zhang, L, Zhang, My, Zhang, X, Zhang, Xd, Zhang, Y, Zhao, M, Zhao, Wl, Zhao, X, Zhao, Yg, Zhao, Y, Zhao, Yx, Zhao, Z, Zhao, Zj, Zheng, D, Zheng, Xl, Zheng, X, Zhivotovsky, B, Zhong, Q, Zhou, Gz, Zhou, G, Zhou, H, Zhou, Sf, Zhou, Xj, Zhu, H, Zhu, Wg, Zhu, W, Zhu, Xf, Zhu, Y, Zhuang, Sm, Zhuang, X, Ziparo, E, Zois, Ce, Zoladek, T, Zong, Wx, Zorzano, A, Zughaier, Sm., Giordano A (ORCID:0000-0002-6978-0880), and Viscomi MT (ORCID:0000-0002-9096-4967)
- Abstract
In 2008 we published the first set of guidelines for standardizing research in autophagy. Since then, research on this topic has continued to accelerate, and many new scientists have entered the field. Our knowledge base and relevant new technologies have also been expanding. Accordingly, it is important to update these guidelines for monitoring autophagy in different organisms. Various reviews have described the range of assays that have been used for this purpose. Nevertheless, there continues to be confusion regarding acceptable methods to measure autophagy, especially in multicellular eukaryotes. For example, a key point that needs to be emphasized is that there is a difference between measurements that monitor the numbers or volume of autophagic elements (e.g., autophagosomes or autolysosomes) at any stage of the autophagic process versus those that measure flux through the autophagy pathway (i.e., the complete process including the amount and rate of cargo sequestered and degraded). In particular, a block in macroautophagy that results in autophagosome accumulation must be differentiated from stimuli that increase autophagic activity, defined as increased autophagy induction coupled with increased delivery to, and degradation within, lysosomes (in most higher eukaryotes and some protists such as Dictyostelium) or the vacuole (in plants and fungi). In other words, it is especially important that investigators new to the field understand that the appearance of more autophagosomes does not necessarily equate with more autophagy. In fact, in many cases, autophagosomes accumulate because of a block in trafficking to lysosomes without a concomitant change in autophagosome biogenesis, whereas an increase in autolysosomes may reflect a reduction in degradative activity. It is worth emphasizing here that lysosomal digestion is a stage of autophagy and evaluating its competence is a crucial part of the evaluation of autophagic flux, or complete autophagy. Here, we prese
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- 2016
11. Effects of agmatine on rotenone-induced damage in SH-SY5Y neuroblastoma cells
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Condello, S, Curro', Monica, Ferlazzo, Nadia, Caccamo, Daniela, Satriano, J, and Ientile, Riccardo
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- 2009
12. Transport of agmatine in brain mitochondria
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Battaglia, V., Grancara, S., Mancon, M., Cravanzola, C., Satriano, J., Agostinelli, Enzo, and Toninello, A.
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- 2009
13. Autophagy and metabolic changes in obesity-related chronic kidney disease
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Satriano, J., primary and Sharma, K., additional
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- 2013
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14. Agmatine prevents the Ca2+-dependent induction of permeability transition in rat brain mitochondria
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Battaglia, V., primary, Grancara, S., additional, Satriano, J., additional, Saccoccio, S., additional, Agostinelli, E., additional, and Toninello, A., additional
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- 2009
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15. Inhibition of constitutive nitric oxide synthase (NOS) by nitric oxide generated by inducible NOS after lipopolysaccharide administration provokes renal dysfunction in rats.
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Schwartz, D, primary, Mendonca, M, additional, Schwartz, I, additional, Xia, Y, additional, Satriano, J, additional, Wilson, C B, additional, and Blantz, R C, additional
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- 1997
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16. Agmatine affects glomerular filtration via a nitric oxide synthase-dependent mechanism
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Schwartz, D., primary, Peterson, O. W., additional, Mendonca, M., additional, Satriano, J., additional, Lortie, M., additional, and Blantz, R. C., additional
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- 1997
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17. Regulation of RANTES and ICAM-1 expression in murine mesangial cells.
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Satriano, J A, primary, Banas, B, additional, Luckow, B, additional, Nelson, P, additional, and Schlondorff, D O, additional
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- 1997
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18. Agmatine, a bioactive metabolite of arginine. Production, degradation, and functional effects in the kidney of the rat.
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Lortie, M J, primary, Novotny, W F, additional, Peterson, O W, additional, Vallon, V, additional, Malvey, K, additional, Mendonca, M, additional, Satriano, J, additional, Insel, P, additional, Thomson, S C, additional, and Blantz, R C, additional
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- 1996
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19. Identification ot a Prostaglandin Transporter
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Kanai, N., primary, Lu, R., additional, Chan, B., additional, Bao, Y., additional, Satriano, J., additional, and Schuster, V.L., additional
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- 1996
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20. Activation and attenuation of transcription factor NF-kB in mouse glomerular mesangial cells in response to tumor necrosis factor-alpha, immunoglobulin G, and adenosine 3':5'-cyclic monophosphate. Evidence for involvement of reactive oxygen species.
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Satriano, J, primary and Schlondorff, D, additional
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- 1994
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21. Oxygen radicals as second messengers for expression of the monocyte chemoattractant protein, JE/MCP-1, and the monocyte colony-stimulating factor, CSF-1, in response to tumor necrosis factor-alpha and immunoglobulin G. Evidence for involvement of reduced nicotinamide adenine dinucleotide phosphate (NADPH)-dependent oxidase.
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Satriano, J A, primary, Shuldiner, M, additional, Hora, K, additional, Xing, Y, additional, Shan, Z, additional, and Schlondorff, D, additional
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- 1993
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22. Regulation of monocyte chemoattractant protein-1 and macrophage colony-stimulating factor-1 by IFN-gamma, tumor necrosis factor-alpha, IgG aggregates, and cAMP in mouse mesangial cells.
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Satriano, J A, primary, Hora, K, additional, Shan, Z, additional, Stanley, E R, additional, Mori, T, additional, and Schlondorff, D, additional
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- 1993
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23. Receptors for IgG complexes activate synthesis of monocyte chemoattractant peptide 1 and colony-stimulating factor 1.
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Hora, K, primary, Satriano, J A, additional, Santiago, A, additional, Mori, T, additional, Stanley, E R, additional, Shan, Z, additional, and Schlondorff, D, additional
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- 1992
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24. Signal Processing For Wide Swath Bathymetric Sonars.
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Satriano, J. H. and Smith, L. C.
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- 1991
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25. Agmatine prevents the Ca2+-dependent induction of permeability transition in rat brain mitochondria.
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Battaglia, V., Grancara, S., Satriano, J., Saccoccio, S., Agostinelli, E., and Toninello, A.
- Subjects
AGMATINE ,MITOCHONDRIA ,CALCIUM ions ,REACTIVE oxygen species ,BRAIN - Abstract
The arginine metabolite agmatine is able to protect brain mitochondria against the drop in energy capacity by the Ca
2+ -dependent induction of permeability transition (MPT) in rat brain mitochondria. At normal levels, the amine maintains the respiratory control index and ADP/O ratio and prevents mitochondrial colloid-osmotic swelling and any electrical potential (ΔΨ) drop. MPT is due to oxidative stress induced by the interaction of Ca2+ with the mitochondrial membrane, leading to the production of hydrogen peroxide and, subsequently, other reactive oxygen species (ROS) such as hydroxyl radicals. This production of ROS induces oxidation of sulfhydryl groups, in particular those of two critical cysteines, most probably located on adenine nucleotide translocase, and also oxidation of pyridine nucleotides, resulting in transition pore opening. The protective effect of agmatine is attributable to a scavenging effect on the most toxic ROS, i.e., the hydroxyl radical, thus preventing oxidative stress and consequent bioenergetic collapse. [ABSTRACT FROM AUTHOR]- Published
- 2010
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26. Effects of nonenzymatic glycosylation of mesangial matrix on proliferation of mesangial cells
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Crowley, S. T., primary, Brownlee, M., additional, Edelstein, D., additional, Satriano, J. A., additional, Mori, T., additional, Singhal, P. C., additional, and Schlondorff, D. O., additional
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- 1991
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27. HIV service provision for people with severe mental illness in outpatient mental health care settings in New York.
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Satriano J, McKinnon K, and Adoff S
- Abstract
People with severe mental illness evidence significantly higher rates of HIV infection than the general population in the United States. Frequently, the only access to health care for this population is through their outpatient mental health care providers. In order to determine how these providers were dealing with the increased risk of HIV infection among this group, a survey of all licensed and certified outpatient mental health care centers in New York State was conducted. The data were compared to a similar previous survey conducted in 1997. [ABSTRACT FROM AUTHOR]
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- 2007
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28. Mouse mesangial cells produce colony-stimulating factor-1 (CSF-1) and express the CSF-1 receptor.
- Author
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Mori, T, primary, Bartocci, A, additional, Satriano, J, additional, Zuckerman, A, additional, Stanley, R, additional, Santiago, A, additional, and Schlondorff, D, additional
- Published
- 1990
- Full Text
- View/download PDF
29. Effects of vasoactive agents on uptake of immunoglobulin G complexes by mesangial cells
- Author
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Singhal, P. C., primary, Santiago, A., additional, Satriano, J., additional, Hays, R. M., additional, and Schlondorff, D., additional
- Published
- 1990
- Full Text
- View/download PDF
30. Public health matters. HIV testing policy and serious mental illness.
- Author
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Walkup J, Satriano J, Barry D, Sadler D, and Cournos F
- Abstract
OBJECTIVES: Using opinion data from experts, we examined the context of the argument for mandatory testing of psychiatric patients. METHODS: Vignettes were distributed to experts on HIV and mental illness. Respondents were asked to provide appropriateness ratings for different hypothetical clinical decisions regarding HIV management. RESULTS: Respondents were reluctant to impose testing without informed consent in most circumstances. The presence of risk factors or danger to another increased appropriateness ratings modestly. CONCLUSIONS: Despite experts' tendency to emphasize individual rights, public reluctance to mandate testing is unlikely to extend to people with serious mental illness. No argument for mandatory testing can be persuasive if improved voluntary testing can achieve adequate detection rates. Voluntary testing protocols should be studied to determine which successfully identify infected individuals. [ABSTRACT FROM AUTHOR]
- Published
- 2002
- Full Text
- View/download PDF
31. Angiotensin II Causes Formation of Platelet Activating Factor in Cultured Rat Mesangial Cells.
- Author
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Neuwirth, R., Satriano, J. A., DeCandido, S., Clay, K., and Schlondorff, D.
- Published
- 1989
32. Effects of vasoactive agents on uptake of immunoglobulin G complexes by mesangial cells.
- Author
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SINGHAL, P. C., SANTIAGO, A., SATRIANO, J., HAYS, R. M., and SCHLONDORFF, D.
- Published
- 1990
33. Relationship of GTP-binding proteins, phospholipase C, and PGE2 synthesis in rat glomerular mesangial cells.
- Author
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SCHLONDORFF, D., SINGHAL, P., HASSID, A., SATRIANO, J. A., and DECANDIDO, S.
- Published
- 1989
34. In vivo demonstration of glomerular PGE2 responses to physiological manipulations and experimental agents.
- Author
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SCHLONDORFF, D., AYNEDJIAN, H. S., SATRIANO, J. A., and BANK, N.
- Published
- 1987
35. Production of platelet-activating factor in glomeruli and cultured glomerular mesangial cells.
- Author
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SCHLONDORFF, D., GOLDWASSER, P., NEUWIRTH, R., SATRIANO, J. A., and CLAY, K. L.
- Published
- 1986
36. Synthesis of prostaglandin E2 in different segments of isolated collecting tubules from adult and neonatal rabbits.
- Author
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SCHLONDORFF, D., SATRIANO, J. A., and SCHWARTZ, G. J.
- Published
- 1985
37. Differential stimulation of PGE2 synthesis in mesangial cells by angiotensin and A23187.
- Author
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SCHLONDORFF, D., PEREZ, J., and SATRIANO, J. A.
- Published
- 1985
- Full Text
- View/download PDF
38. Mapping the substrate binding site of the prostaglandin transporter PGT by cysteine scanning mutagenesis.
- Author
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Chan, B S, Satriano, J A, and Schuster, V L
- Abstract
We have identified a cDNA, PGT, that encodes a widely expressed transporter for prostaglandin (PG) E(2), PGF(2alpha), PGD(2), 8-iso-PGF(2alpha), and thromboxane B(2). To begin to understand the molecular mechanisms of transporter function, we have initiated a structure-function analysis of PGT to identify its substrate-binding region. We have found that by introducing the small, water-soluble, thiol-reactive anion Na(2-sulfonatoethyl)methanethiosulfonate (MTSES) into the substrate pathway, we were able to cause inhibition of transport that could be reversed with dithiothreitol. Importantly, co-incubation with PGE(2) protected PGT from this inhibition, suggesting that MTSES gains access to the aqueous pore pathway of PGT to form a mixed disulfide near the substrate-binding site. To identify the susceptible cysteine, we mutated, one at a time, all six of the putative transmembrane cysteines to serine. Only the mutation of Cys-530 to serine within putative transmembrane 10 became resistant to inhibition by MTSES. Thus, Cys-530 is the substrate-protectable, MTSES-inhibitable residue. To identify other residues that may be lining the substrate-binding site, we initiated cysteine-scanning mutagenesis of transmembrane 10 using Cys-530 as an entry point. On a C530S, MTSES-resistant background, residues in the N- and C-terminal directions were individually mutated to cysteine (Ala-513 to His-536), one at a time, and then analyzed for MTSES inhibition. Of the 24 cysteine-substituted mutants generated, 6 were MTSES-sensitive and, among these, 4 were substrate-protectable. The pattern of sensitivity to MTSES places these residues on the same face of an alpha-helix. The results of cysteine-scanning mutagenesis and molecular modeling of putative transmembrane 10 indicate that the substrate binding of PGT is formed among its membrane-spanning segments, with 4 residues along the cytoplasmic end of helix 10 contributing to one surface of the binding site.
- Published
- 1999
39. Agmatine suppresses proliferation by frameshift induction of antizyme and attenuation of cellular polyamine levels.
- Author
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Satriano, J, Matsufuji, S, Murakami, Y, Lortie, M J, Schwartz, D, Kelly, C J, Hayashi, S, and Blantz, R C
- Abstract
Polyamines are required for entry and progression of the cell cycle. As such, augmentation of polyamine levels is essential for cellular transformation. Polyamines are autoregulated through induction of antizyme, which represses both the rate-limiting polyamine biosynthetic enzyme ornithine decarboxylase and cellular polyamine transport. In the present study we demonstrate that agmatine, a metabolite of arginine via arginine decarboxylase (an arginine pathway distinct from that of the classical polyamines), also serves the dual regulatory functions of suppressing polyamine biosynthesis and cellular polyamine uptake through induction of antizyme. The capacity of agmatine to induce antizyme is demonstrated by: (a) an agmatine-dependent translational frameshift of antizyme mRNA to produce a full-length protein and (b) suppression of agmatine-dependent inhibitory activity by either anti-antizyme IgG or antizyme inhibitor. Furthermore, agmatine administration depletes intracellular polyamine levels to suppress cellular proliferation in a transformed cell line. This suppression is reversible with polyamine supplementation. We propose a novel regulatory pathway in which agmatine acts as an antiproliferative molecule and potential tumor suppressor by restricting the cellular polyamine supply required to support growth.
- Published
- 1998
40. Differential stimulation of PGE2 synthesis in mesangial cells by angiotensin and A23187
- Author
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Schlondorff, D., Perez, J., and Satriano, J. A.
- Abstract
The mechanism of arachidonic acid release and prostaglandin E2 (PGE2) synthesis was studied in cultured mesangial cells from rat kidneys. Both the ionophore A23187 and angiotensin II stimulated radioimmunoassayable PGE2 synthesis. The effect of angiotensin occurred within minutes, with half-maximal stimulation around 10(-9) M. In cells prelabeled with [14C]arachidonate, A23187 caused release of [14C]-arachidonate from all phospholipids. In contrast, angiotensin II caused preferential release of [14C]arachidonate from phosphatidylinositol, associated with a significant increase in 14C-labeled phosphatidic acid, mono- and diacylglyceride, and arachidonate. These results indicate that angiotensin preferentially, but not exclusively, stimulates a phosphatidylinositol-specific phospholipase C, whereas A23187 results in unspecific stimulation of phospholipases. The tight coupling between an angiotensin-responsive phospholipid-arachidonate pool and cyclooxygenase may be responsible for the specificity of the response to angiotensin.
- Published
- 1985
- Full Text
- View/download PDF
41. Angiotensin II stimulates phospholipases C and A2 in cultured rat mesangial cells
- Author
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Schlondorff, D., DeCandido, S., and Satriano, J. A.
- Abstract
Angiotensin II stimulates prostaglandin (PG) E2 formation in mesangial cells cultured from rat renal glomeruli. The interactions between angiotensin II and PGE2 are important in modulating glomerular function. We examined the mechanism for stimulation of PGE2 production in mesangial cells using the putative diacylglycerol-lipase inhibitor RHC 80267 and trifluoperazine (TFP), an agent interfering with Ca2+-CaM-mediated processes. Although RHC 80267 inhibited diacylglycerol-lipase activity in mesangial cells, it did not influence PGE2 production in response to either angiotensin II or A23187. In contrast, TFP (50 microM) inhibited basal PGE2 production and stimulation by angiotensin II and A23187. TFP also decreased 14C release in response to angiotensin from cells prelabeled with [14C]arachidonic acid, which was associated with inhibition of 14C loss from phosphatidylinositol. In cells prelabeled with 32P, orthophosphate angiotensin II caused a rapid hydrolysis of phosphatidylinositol 4,5-bisphospate. TFP enhanced 32P labeling of phosphatidylinositides, but did not prevent the loss of phosphatidylinositol 4,5-bisphosphate in response to angiotensin. This was verified in cells prelabeled with myo-[3H]inositol where angiotensin stimulated formation of [3H]inositol trisphosphate. TFP enhanced formation of [3H]inositol trisphosphate both under basal- and angiotensin II-stimulated conditions. Thus TFP did not inhibit phospholipase C activation by angiotensin. Angiotensin II caused marked increases in [32P]lysophospholipids, indicating activation of also phospholipase A2. This process was inhibited by TFP. Taken together, these results are consistent with stimulation of both phospholipase C and A2 by angiotensin, the latter step responsible for the release of arachidonic acid and PGE2 formation. The activation of phospholipase A2, but not that of phospholipase C, is inhibited by TFP, perhaps by interference with calmodulin-dependent steps.
- Published
- 1987
- Full Text
- View/download PDF
42. Mechanism of prostaglandin E2 transport across the plasma membrane of HeLa cells and Xenopus oocytes expressing the prostaglandin transporter "PGT".
- Author
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Chan, B S, Satriano, J A, Pucci, M, and Schuster, V L
- Abstract
We recently identified a novel prostaglandin transporter called PGT (Kanai, N., Lu, R., Satriano, J. A., Bao, Y., Wolkoff, A. W., and Schuster, V. L. (1995) Science 268, 866-869). Based on initial functional studies, we have hypothesized that PGT might mediate the release of newly synthesized prostaglandins (PG), epithelial transport of PGs, or metabolic clearance of PGs. Here we examined the mechanism of PGT transport as expressed in HeLa cells and Xenopus oocytes, using isotopic PG influx and efflux studies. In both native HeLa cells and oocytes, cell membranes were poorly permeable to PGs. In contrast, in oocytes injected with PGT mRNA, the PG influx permeability coefficient was 90-157 times that of oocytes injected with water. The rank order substrate profile was PGF2alpha approximately PGE2 > TXB2 >> 6 keto-PGF1alpha. PG influx displayed an overshoot with rapid accumulation of tracer PGE2, followed by a gradual return to baseline. Based on estimated oocyte volumes, the PGT-mediated accumulation of PGE2 reached steady state at intra-oocyte concentrations 25-fold higher than the external media. The accumulation of PG was not due to intracellular binding or metabolism. PGT-mediated uptake was ATP- and temperature-dependent, but not sodium-dependent, and was inhibited by disulfonic stilbenes, niflumic acid, and the thiol reactive anion MTSES (Na(2-sulfonatoethyl)methanethiosulfonate). [3H]PGE2 efflux from PGT-transfected HeLa cells was stimulated by external (trans) PGE2 in a dose-dependent fashion and was inhibited by bromcresol green and 4,4'-diisothiocyanatostilbene-2,2'-disulfonate. Membrane depolarization inhibited uptake of [3H]PGE2, consistent with a model of net outward movement of negative charge during the translocation event. These findings suggest that PGT mediates [3H]PGE2 accumulation via obligatory, electrogenic anion exchange.
- Published
- 1998
43. Effect of platelet activating factor antagonists on cultured rat mesangial cells.
- Author
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Neuwirth, R, Singhal, P, Satriano, J A, Braquet, P, and Schlondorff, D
- Abstract
Platelet activating factor (PAF; 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine) is a lipid mediator of inflammation produced by inflammatory cells and also by renal glomerular mesangial cells. PAF may play a role in glomerular function and disease. Previously the authors reported that glomerular mesangial cells respond to PAF by increasing prostaglandin E2 (PGE2) synthesis and by cell contraction. This paper examines the specificity of BN52021, SRI 63-072 and kadsurenone on the effects of PAF on cultured rat glomerular mesangial cells. Both BN52021 and SRI 63-072 specifically decreased PAF (1 X 10(-6) M)-stimulated PGE2 production in a dose-dependent fashion (10(-7)-10(-5) M) without affecting the stimulation by angiotensin II (AII) or the calcium ionophore A23187. Kadsurenone also decreased PAF-stimulated PGE2 production, but in a less specific manner, as it also decreased AII- and A23187-stimulated PGE2 production. In order to examine the site of antagonism of PAF-induced PGE2 synthesis by BN52021 and SRI 63-072, the authors prelabeled cells with [14C]arachidonic acid. Both agents diminished the release of [14C]arachidonate from these prelabeled cells in response to PAF in a dose-dependent fashion, though not decreasing release in response to AII or A23187, indicating that they blocked the effect of PAF on phospholipase activation, consistent with receptor blocking activity. BN52021 and SRI 63-072 also inhibited PAF-induced contraction of cultured mesangial cells without an effect on basal tone of the cells or the contractile response to AII.(ABSTRACT TRUNCATED AT 250 WORDS)
- Published
- 1987
44. The effects of amrinone on transport and cyclic AMP metabolism in toad urinary bladder.
- Author
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Levine, S D, Jacoby, M, Satriano, J A, and Schlondorff, D
- Abstract
Amrinone is a new noncatechol, nonglycoside agent with cardiotonic and vasodilator properties. This paper examines the effects of amrinone in the toad urinary bladder, a tissue whose function may be altered by many factors which also change cardiovascular activity. Amrinone enhanced the effect of vasopressin and cyclic AMP on water and urea permeabilities, as well as the effect of vasopressin on sodium transport. Consistent with these actions, amrinone inhibited cyclic AMP phosphodiesterase activity in epithelial homogenates and increased both cyclic AMP content and the protein kinase activity ratio measured in intact epithelial cells. The inhibitory effect of amrinone on phosphodiesterase may be relevant to its cardiostimulatory and vasodilator activities.
- Published
- 1981
45. Prostaglandin synthesis by isolated cells from the outer medulla and from the thick ascending loop of Henle of rabbit kidney.
- Author
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Schlondorff, D, Zanger, R, Satriano, J A, Folkert, V W, and Eveloff, J
- Published
- 1982
46. Atrial natriuretic peptide and nitroprusside cause relaxation of cultured rat mesangial cells
- Author
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Singhal, P. C., DeCandido, S., Satriano, J. A., Schlondorff, D., and Hays, R. M.
- Abstract
These studies evaluate the effects of atrial natriuretic peptide (ANP) and nitroprusside (NP) on cultured mesangial cells (MC) grown on a flexible silicone rubber surface. The basal tone of the MC produced wrinkles on the silicone rubber surface. A decrease in number or magnitude of wrinkles was considered to represent cell relaxation, whereas an increase represented cell contraction. ANP (10(-9) M) produced a relaxation in greater than 60% of the cells by 10 min. The percentage of cells showing a decrease of wrinkles was significantly higher (P less than 0.05 at 5 min and P less than 0.001 at 10 min) during the ANP-treated period than during the control period. NP (10(-5) M) caused a decrease of wrinkles in greater than 80% of cells (P less than 0.02 at 5 min and P less than 0.01 at 10 min) compared with a 5% decrease in the control period. Dibutyryl guanosine 3',5'-cyclic monophosphate (DBcGMP; 10(-4) M) also produced a decrease of wrinkles in 81% of the cells (P less than 0.02) compared with a 9% decrease in the control period. MC treated with ANP, NP, or DBcGMP and then labeled with 7-nitrobenz-2-oxa-1,3-diazol-4-yl (NBD)-phallacidin did not show obvious alteration of morphology of actin filaments compared with untreated cells. ANP could inhibit as well as partially reverse the agonist (angiotensin II)-induced contractile response. ANP (10(-10)-10(-8) M) as well as NP (10(-5) M) increased intracellular cGMP content of MC (P less than 0.005) compared with control cells.(ABSTRACT TRUNCATED AT 250 WORDS)
- Published
- 1989
- Full Text
- View/download PDF
47. A specific Fc gamma receptor on cultured rat mesangial cells.
- Author
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Santiago, A, primary, Satriano, J, additional, DeCandido, S, additional, Holthofer, H, additional, Schreiber, R, additional, Unkeless, J, additional, and Schlondorff, D, additional
- Published
- 1989
- Full Text
- View/download PDF
48. Effect of platelet-activating factor and serum-treated zymosan on prostaglandin E2 synthesis, arachidonic acid release, and contraction of cultured rat mesangial cells.
- Author
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Schlondorff, D, primary, Satriano, J A, additional, Hagege, J, additional, Perez, J, additional, and Baud, L, additional
- Published
- 1984
- Full Text
- View/download PDF
49. Prostaglandin synthesis by isolated rat glomeruli: effect of angiotensin II
- Author
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Schlondorff, D., primary, Roczniak, S., additional, Satriano, J. A., additional, and Folkert, V. W., additional
- Published
- 1980
- Full Text
- View/download PDF
50. Multiple sites for interaction of prostaglandin and vasopressin in toad urinary bladder
- Author
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Schlondorff, D., primary, Carvounis, C. P., additional, Jacoby, M., additional, Satriano, J. A., additional, and Levine, S. D., additional
- Published
- 1981
- Full Text
- View/download PDF
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