Search

Your search keyword '"Borel, O"' showing total 45 results
Start Over Author "Borel, O"
45 results on '"Borel, O"'

2. New Biomarkers In Hand Osteoarthritis: The Micro-Rnas

Author

Auroux, M., primary, Millet, M., additional, Merle, B., additional, Fontanges, E., additional, Duvert, F., additional, Gineyts, E., additional, Rousseau, J.-C., additional, Borel, O., additional, Mercier, A., additional, Lespessailles, E., additional, and Chapurlat, R., additional

Published
2023
Full Text
View/download PDF

15. ELISA MEASUREMENT OF CIRCULATING PERIOSTIN IN ANIMAL MODELS OF BONE LOSS OR BONE FORMATION AND IDENTIFICATION OF CIRCULATING AND TISSUE-SPECIFIC ASSOCIATED FORMS OF PERIOSTIN

Author

Gineyts , E., Bonnet , N., Bertholon , C., Pagnon-Minot , A., Borel , O., Hartmann , D., Chapurlat , R. D., Ferrari , S., Garnero , P., CLEZARDIN , P., Rousseau , J. -C., Ostéoporose et Qualité osseuse (Site Laennec), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-IFR62-Institut National de la Santé et de la Recherche Médicale (INSERM), Hôpital Nord [CHU - APHM], Matériaux, ingénierie et science [Villeurbanne] (MATEIS), Université de Lyon-Université de Lyon-Institut National des Sciences Appliquées de Lyon (INSA Lyon), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS), Dipartimento di Scienze della Terra e dell'Ambiente [Pavia], Università degli Studi di Pavia, DLR Institut für Planetenforschung, Deutsches Zentrum für Luft- und Raumfahrt [Berlin] (DLR), Institut de biologie et chimie des protéines [Lyon] (IBCP), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), Université Claude Bernard Lyon 1 ( UCBL ), Université de Lyon-Université de Lyon-IFR62-Institut National de la Santé et de la Recherche Médicale ( INSERM ), Matériaux, ingénierie et science [Villeurbanne] ( MATEIS ), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique ( CNRS ) -Institut National des Sciences Appliquées de Lyon ( INSA Lyon ), Université de Lyon-Institut National des Sciences Appliquées ( INSA ) -Institut National des Sciences Appliquées ( INSA ), Università di Pavia [Pavia], Deutsches Zentrum für Luft- und Raumfahrt [Berlin] ( DLR ), Institut de biologie et chimie des protéines [Lyon] ( IBCP ), and Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique ( CNRS )

Subjects
animal structures, [ SPI.MAT ] Engineering Sciences [physics]/Materials, education, health care economics and organizations, [SPI.MAT]Engineering Sciences [physics]/Materials
Abstract

WCO-IOF-ESCEO World Congress on Osteoporosis, Osteoarthritis and Musculoskeletal Diseases, Malaga, SPAIN, APR 14-17, 2016; International audience

Published
2016

17. Centrality dependence of the pseudorapidity density distribution for charged particles in Pb-Pb collisions at √sNN = 2.76 TeV

Author

E. Abbas a, B. Abelev bt, J. Adam al, D. Adamová ca, A. M. Adare dz, M. M. Aggarwal ce, G. Aglieri Rinella ah, M. Agnello cv, A. G. Agocs dy, A. Agostinelli ab, Z. Ahammed dt, A. Ahmad Masoodi r, N. Ahmad r, S. U. Ahn bm, S. A. Ahn bm, I. Aimo y, cv, ck, M. Ajaz p, A. Akindinov ay, D. Aleksandrov cq, B. Alessandro cv, A. Alici cx, m, A. Alkin d, E. Almaráz Aviña bi, J. Alme aj, T. Alt an, V. Altini af, S. Altinpinar s, I. Altsybeev dv, C. Andrei bw, A. Andronic cn, V. Anguelov cj, J. Anielski bg, C. Anson t, T. Anticˇic ́ co, F. Antinori cw, P. Antonioli cx, L. Aphecetche dd, H. Appelshäuser be, N. Arbor bp, S. Arcelli ab, A. Arend be, N. Armesto q, R. Arnaldi cv, T. Aronsson dz, I. C. Arsene cn, M. Arslandok be, A. Asryan dv, A. Augustinus ah, R. Averbeck cn, T. C. Awes cb, J. Äystö aq, M. D. Azmi r, M. Bach an, A. Badalà cu, Y. W. Baek bo, R. Bailhache be, R. Bala ch, A. Baldisseri o, F. Baltasar Dos Santos Pedrosa ah, J. Bán az, R. C. Baral ba, R. Barbera aa, F. Barile af, G. G. Barnaföldi dy, L. S. Barnby cs, V. Barret bo, J. Bartke dh, M. Basile ab, N. Bastid bo, S. Basu dt, B. Bathen bg, G. Batigne dd, B. Batyunya bk, P. C. Batzing v, C. Baumann be, I. G. Bearden by, H. Beck be, N. K. Behera as, I. Belikov bj, F. Bellini ab, R. Bellwied dn, E. Belmont Moreno bi, G. Bencedi dy, S. Beole y, I. Berceanu bw, A. Bercuci bw, Y. Berdnikov cc, D. Berenyi dy, A. A. E. Bergognon dd, R. A. Bertens ax, D. Berzano y, L. Betev ah, A. Bhasin ch, A. K. Bhati ce, J. Bhom dr, N. Bianchi bq, L. Bianchi y, C. Bianchin ax, J. Bielcˇík al, J. Bielcˇíková ca, A. Bilandzic by, S. Bjelogrlic ax, F. Blanco k, F. Blanco dn, D. Blau cq, C. Blume be, M. Boccioli ah, S. Böttger bd, A. Bogdanov bu, H. Bøggild by, M. Bogolyubsky av, L. Boldizsár dy, M. Bombara am, J. Book be, H. Borel o, A. Borissov dx, F. Bossú cg, M. Botje bz, E. Botta y, E. Braidot bs, P. Braun Munzinger cn, M. Bregant dd, T. Breitner bd, T. A. Broker be, T. A. Browning cl, M. Broz ak, R. Brun ah, E. Bruna y, G. E. Bruno af, D. Budnikov cp, H. Buesching be, S. Bufalino y, P. Buncic ah, O. Busch cj, Z. Buthelezi cg, D. Caffarri ac, X. Cai h, H. Caines dz, E. Calvo Villar ct, V. Canoa Roman l, G. Cara Romeo cx, F. Carena ah, W. Carena ah, N. Carlin Filho dk, F. Carminati ah, A. Casanova Díaz bq, J. Castillo Castellanos o, J. F. Castillo Hernandez cn, E. A. R. Casula x, V. Catanescu bw, C. Cavicchioli ah, C. Ceballos Sanchez j, J. Cepila al, P. Cerello cv, B. Chang aq, S. Chapeland ah, J. L. Charvet o, S. Chattopadhyay dt, S. Chattopadhyay cr, M. Cherney cd, C. Cheshkov ah, B. Cheynis dm, V. Chibante Barroso ah, D. D. Chinellato dn, P. Chochula ah, M. Chojnacki by, S. Choudhury dt, P. Christakoglou bz, C. H. Christensen by, P. Christiansen ag, T. Chujo dr, S. U. Chung cm, C. Cicalo cy, L. Cifarelli ab, F. Cindolo cx, J. Cleymans cg, F. Colamaria af, D. Colella af, A. Collu x, G. Conesa Balbastre bp, Z. Conesa del Valle ah, M. E. Connors dz, G. Contin w, J. G. Contreras l, T. M. Cormier dx, Y. Corrales Morales y, P. Cortese ae, I. Cortés Maldonado c, M. R. Cosentino bs, F. Costa ah, M. E. Cotallo k, E. Crescio l, P. Crochet bo, E. Cruz Alaniz bi, R. Cruz Albino l, E. Cuautle bh, L. Cunqueiro bq, A. Dainese ac, H. H. Dalsgaard by, R. Dangh, A. Danubc, K. Dascr, I. Dasau, S. Dase, D. Dascr, A. Dashdl, S. Dashas, S. Dedt, G. O. V. de Barros dk, A. De Caro ad, G. de Cataldo da, J. de Cuveland an, A. De Falco x, D. De Gruttola ad, H. Delagrange dd, A. Deloff bv, N. De Marco cv, E. Dénes dy, S. De Pasquale ad, A. Deppman dk, G. D. Erasmo af, R. de Rooij ax, M. A. Diaz Corchero k, D. Di Bari af, T. Dietel bg, C. Di Giglio af, S. Di Liberto db, A. Di Mauro ah, P. Di Nezza bq, R. Divià ah, Ø. Djuvsland s, A. Dobrin dx, ag, ax, T. Dobrowolski bv, B. Dönigus cn, O. Dordic v, O. Driga dd, A. K. Dubey dt, A. Dubla ax, L. Ducroux dm, P. Dupieux bo, A. K. Dutta Majumdar cr, D. Elia da, D. Emschermann bg, H. Engel bd, B. Erazmus ah, H. A. Erdal aj, D. Eschweiler an, B. Espagnon au, M. Estienne dd, S. Esumi dr, D. Evans cs, S. Evdokimov av, G. Eyyubova v, D. Fabris ac, J. Faivre bp, D. Falchieri ab, A. Fantoni bq, M. Fasel cj, D. Fehlker s, L. Feldkamp bg, D. Felea bc, A. Feliciello cv, B. Fenton Olsen bs, G. Feofilov dv, A. Fernández Téllez c, A. Ferretti y, A. Festanti ac, J. Figiel dh, M. A. S. Figueredo dk, S. Filchagin cp, D. Finogeev aw, F. M. Fionda af, E. M. Fiore af, E. Floratos cf, M. Floris ah, S. Foertsch cg, P. Foka cn, S. Fokin cq, A. Francescon ah, U. Frankenfeld cn, U. Fuchs ah, C. Furget bp, M. Fusco Girard ad, J. J. Gaardhøje by, M. Gagliardi y, A. Gago ct, M. Gallio y, D. R. Gangadharan t, P. Ganoti cb, C. Garabatos cn, E. Garcia Solis n, C. Gargiulo ah, I. Garishvili bt, J. Gerhard an, M. Germain dd, C. Geuna o, A. Gheata ah, M. Gheata bc, B. Ghidini af, P. Ghosh dt, P. Gianotti bq, M. R. Girard dw, P. Giubellino ah, E. Gladysz Dziadus dh, P. Glässel cj, R. Gomez dj, l, E. G. Ferreiro q, L. H. González Trueba bi, P. González Zamora k, S. Gorbunov an, A. Goswami ci, S. Gotovac df, L. K. Graczykowski dw, R. Grajcarek cj, A. Grelli ax, A. Grigoras ah, C. Grigoras ah, V. Grigoriev bu, A. Grigoryan b, S. Grigoryan bk, B. Grinyov d, N. Grion cz, P. Gros ag, J. F. Grosse Oetringhaus ah, J. Y. Grossiord dm, R. Grosso ah, F. Guber aw, R. Guernane bp, B. Guerzoni ab, M. Guilbaud dm, K. Gulbrandsen by, H. Gulkanyan b, T. Gunji dq, R. Gupta ch, A. Gupta ch, R. Haake bg, Ø. Haaland s, C. Hadjidakis au, M. Haiduc bc, H. Hamagaki dq, G. Hamar dy, B. H. Han u, L. D. Hanratty cs, A. Hansen by, Z. Harmanová Tóthová am, J. W. Harris dz, M. Hartig be, A. Harton n, D. Hatzifotiadou cx, S. Hayashi dq, A. Hayrapetyan ah, b, S. T. Heckel be, M. Heide bg, H. Helstrup aj, A. Herghelegiu bw, G. Herrera Corral l, N. Herrmann cj, B. A. Hess ds, K. F. Hetland aj, B. Hicks dz, B. Hippolyte bj, Y. Hori dq, P. Hristov ah, I. Hrˇivnácˇová au, M. Huang s, T. J. Humanic t, D. S. Hwang u, R. Ichou bo, R. Ilkaev cp, I. Ilkiv bv, M. Inaba dr, E. Incani x, P. G. Innocenti ah, G. M. Innocenti y, M. Ippolitov cq, M. Irfan r, C. Ivan cn, V. Ivanov cc, A. Ivanov dv, M. Ivanov cn, O. Ivanytskyi d, A. Jachołkowski aa, P. M. Jacobs bs, C. Jahnke dk, H. J. Jang bm, M. A. Janik dw, P. H. S. Y. Jayarathna dn, S. Jena as, D. M. Jha dx, R. T. Jimenez Bustamante bh, P. G. Jones cs, H. Jung ao, A. Jusko cs, A. B. Kaidalov ay, S. Kalcher an, P. Kalinˇák az, T. Kalliokoski aq, A. Kalweit ah, J. H. Kang eb, V. Kaplin bu, S. Kar dt, A. Karasu Uysal ah, ea, bn, O. Karavichev aw, T. Karavicheva aw, E. Karpechev aw, A. Kazantsev cq, U. Kebschull bd, R. Keidel ec, B. Ketzer be, K. H. Khan p, M. M. Khan r, P. Khan cr, S. A. Khan dt, A. Khanzadeev cc, Y. Kharlov av, B. Kileng aj, M. Kim eb, S. Kim u, B. Kim eb, T. Kim eb, D. J. Kim aq, D. W. Kim ao, J. H. Kim u, J. S. Kim ao, M. Kim ao, S. Kirsch an, I. Kisel an, S. Kiselev ay, A. Kisiel dw, J. L. Klay g, J. Klein cj, C. Klein Bösing bg, M. Kliemant be, A. Kluge ah, M. L. Knichel cn, A. G. Knospe di, M. K. Köhler cn, T. Kollegger an, A. Kolojvari dv, M. Kompaniets dv, V. Kondratiev dv, N. Kondratyeva bu, A. Konevskikh aw, V. Kovalenko dv, M. Kowalski dh, S. Kox bp, G. Koyithatta Meethaleveedu as, J. Kral aq, I. Králik az, F. Kramer be, A. Kravcˇáková am, M. Krelina al, M. Kretz an, M. Krivda cs, F. Krizek aq, M. Krus al, E. Kryshen cc, M. Krzewicki cn, V. Kucera ca, Y. Kucheriaev cq, T. Kugathasan ah, C. Kuhn bj, P. G. Kuijer bz, I. Kulakov be, J. Kumar as, P. Kurashvili bv, A. Kurepin aw, A. B. Kurepin aw, A. Kuryakin cp, S. Kushpil ca, V. Kushpil ca, H. Kvaerno v, M. J. Kweon cj, Y. Kwon eb, P. Ladrón de Guevara bh, I. Lakomov au, R. Langoy s, S. L. La Pointe ax, C. Lara bd, A. Lardeux dd, P. La Rocca aa, M. Lechman ah, S. C. Lee ao, G. R. Lee cs, I. Legrand ah, J. Lehnert be, R. C. Lemmon dc, M. Lenhardt cn, V. Lenti da, H. León bi, M. Leoncino y, I. León Monzón dj, P. Lévai dy, S. Li bo, h, J. Lien s, R. Lietava cs, S. Lindal v, V. Lindenstruth an, C. Lippmann cn, M. A. Lisa t, H. M. Ljunggren ag, D. F. Lodato ax, P. I. Loenne s, V. R. Loggins dx, V. Loginov bu, D. Lohner cj, C. Loizides bs, K. K. Loo aq, X. Lopez bo, E. López Torres j, G. Løvhøiden v, X. G. Lu cj, P. Luettig be, M. Lunardon ac, J. Luo h, C. Luzzi ah, K. Ma h, R. Ma dz, D. M. Madagodahettige Don dn, A. Maevskaya aw, M. Mager bf, D. P. Mahapatra ba, A. Maire cj, M. Malaev cc, I. Maldonado Cervantes bh, Ludmila Malinina bk, 1, D. Mal’Kevich ay, P. Malzacher cn, A. Mamonov cp, L. Manceau cv, L. Mangotra ch, V. Manko cq, F. Manso bo, V. Manzari da, Y. Mao h, M. Marchisone bo, y, J. Mareš bb, A. Margotti cx, A. Marín cn, C. Markert di, M. Marquard be, I. Martashvili dp, N. A. Martin cn, P. Martinengo ah, M. I. Martínez c, G. Martínez García dd, Y. Martynov d, A. Mas dd, S. Masciocchi cn, M. Masera y, A. Masoni cy, L. Massacrier dd, A. Mastroserio af, A. Matyja dh, C. Mayer dh, J. Mazer dp, M. A. Mazzoni db, F. Meddi z, A. Menchaca Rocha bi, J. Mercado Pérez cj, M. Meres ak, Y. Miake dr, K. Mikhaylov bk, L. Milano ah, Jovan Milosevic v, 2, A. Mischke ax, A. N. Mishra ci, D. Mis ́kowiec cn, C. Mitu bc, S. Mizuno dr, J. Mlynarz dx, B. Mohanty dt, L. Molnar dy, L. Montaño Zetina l, M. Monteno cv, E. Montes k, T. Moon eb, M. Morando ac, D. A. Moreira De Godoy dk, S. Moretto ac, A. Morreale aq, A. Morsch ah, V. Muccifora bq, E. Mudnic df, S. Muhuri dt, M. Mukherjee dt, H. Müller ah, M. G. Munhoz dk, S. Murray cg, L. Musa ah, J. Musinsky az, B. K. Nandi as, R. Nania cx, E. Nappi da, C. Nattrass dp, T. K. Nayak dt, S. Nazarenko cp, A. Nedosekin ay, M. Nicassio af, M. Niculescu bc, B. S. Nielsen by, T. Niida dr, S. Nikolaev cq, V. Nikolic co, S. Nikulin cq, V. Nikulin cc, B. S. Nilsen cd, M. S. Nilsson v, F. Noferini cx, P. Nomokonov bk, G. Nooren ax, A. Nyanin cq, A. Nyatha as, C. Nygaard by, J. Nystrand s, A. Ochirov dv, H. Oeschler bf, ah, cj, S. Oh dz, S. K. Oh ao, J. Oleniacz dw, A. C. Oliveira Da Silva dk, C. Oppedisano cv, A. Ortiz Velasquez ag, A. Oskarsson ag, P. Ostrowski dw, J. Otwinowski cn, K. Oyama cj, K. Ozawa dq, Y. Pachmayer cj, M. Pachr al, F. Padilla y, P. Pagano ad, G. Paic ́ bh, F. Painke an, C. Pajares q, S. K. Pal dt, A. Palaha cs, A. Palmeri cu, V. Papikyan b, G. S. Pappalardo cu, W. J. Park cn, A. Passfeld bg, D. I. Patalakha av, V. Paticchio da, B. Paul cr, A. Pavlinov dx, T. Pawlak dw, T. Peitzmann ax, H. Pereira Da Costa o, E. Pereira De Oliveira Filho dk, D. Peresunko cq, C. E. Pérez Lara bz, D. Perrino af, W. Peryt dw, A. Pesci cx, Y. Pestov f, V. Petrácˇek al, M. Petran al, M. Petris bw, P. Petrov cs, M. Petrovici bw, C. Petta aa, M. Pikna ak, P. Pillot dd, O. Pinazza ah, L. Pinsky dn, N. Pitz be, D. B. Piyarathna dn, M. Planinic co, M. Płoskon ́ bs, J. Pluta dw, T. Pocheptsov bk, S. Pochybova dy, P. L. M. Podesta Lerma dj, M. G. Poghosyan ah, K. Polák bb, B. Polichtchouk av, N. Poljak ax, A. Pop bw, S. Porteboeuf Houssais bo, V. Pospíšil al, B. Potukuchi ch, S. K. Prasad dx, R. Preghenella cx, F. Prino cv, C. A. Pruneau dx, I. Pshenichnov aw, G. Puddu x, V. Punin cp, M. Putiš am, J. Putschke dx, H. Qvigstad v, A. Rachevski cz, A. Rademakers ah, T. S. Räihä aq, J. Rak aq, A. Rakotozafindrabe o, L. Ramello ae, S. Raniwala ci, R. Raniwala ci, S. S. Räsänen aq, B. T. Rascanu be, D. Rathee ce, W. Rauch ah, K. F. Read dp, J. S. Real bp, K. Redlich bv, 3, R. J. Reed dz, A. Rehman s, P. Reichelt be, M. Reicher ax, R. Renfordt be, A. R. Reolon bq, A. Reshetin aw, F. Rettig an, J. P. Revol ah, K. Reygers cj, L. Riccati cv, R. A. Ricci br, T. Richert ag, M. Richter v, P. Riedler ah, W. Riegler ah, F. Riggi aa, M. Rodríguez Cahuantzi c, A. Rodriguez Manso bz, K. Røed s, v, E. Rogochaya bk, D. Rohr an, D. Röhrich s, R. Romita cn, F. Ronchetti bq, P. Rosnet bo, S. Rossegger ah, A. Rossi ah, P. Roy cr, C. Roy bj, A. J. Rubio Montero k, R. Russo y, E. Ryabinkin cq, A. Rybicki dh, S. Sadovsky av, K. Šafarˇík ah, R. Sahoo at, P. K. Sahu ba, J. Saini dt, H. Sakaguchi ar, S. Sakai bs, D. Sakata dr, C. A. Salgado q, J. Salzwedel t, S. Sambyal ch, V. Samsonov cc, X. Sanchez Castro bj, L. Šándor az, A. Sandoval bi, M. Sano dr, G. Santagati aa, R. Santoro ah, J. Sarkamo aq, D. Sarkar dt, E. Scapparone cx, F. Scarlassara ac, R. P. Scharenberg cl, C. Schiaua bw, R. Schicker cj, H. R. Schmidt ds, C. Schmidt cn, S. Schuchmann be, J. Schukraft ah, T. Schuster dz, Y. Schutz ah, K. Schwarz cn, K. Schweda cn, G. Scioli ab, E. Scomparin cv, R. Scott dp, P. A. Scott cs, G. Segato ac, I. Selyuzhenkov cn, S. Senyukov bj, J. Seo cm, S. Serci x, E. Serradilla k, A. Sevcenco bc, A. Shabetai dd, G. Shabratova bk, R. Shahoyan ah, N. Sharma dp, S. Sharma ch, S. Rohni ch, K. Shigaki ar, K. Shtejer j, Y. Sibiriak cq, E. Sicking bg, S. Siddhanta cy, T. Siemiarczuk bv, D. Silvermyr cb, C. Silvestre bp, G. Simatovic bh, G. Simonetti ah, R. Singaraju dt, R. Singh ch, S. Singha dt, V. Singhal dt, B. C. Sinha dt, T. Sinha cr, B. Sitar ak, M. Sitta ae, T. B. Skaali v, K. Skjerdal s, R. Smakal al, N. Smirnov dz, R. J. M. Snellings ax, C. Søgaard ag, R. Soltz bt, M. Song eb, J. Song cm, C. Soos ah, F. Soramel ac, I. Sputowska dh, M. Spyropoulou Stassinaki cf, B. K. Srivastava cl, J. Stachel cj, I. Stan bc, G. Stefanek bv, M. Steinpreis t, E. Stenlund ag, G. Steyn cg, J. H. Stiller cj, D. Stocco dd, M. Stolpovskiy av, P. Strmen ak, A. A. P. Suaide dk, M. A. Subieta Vásquez y, T. Sugitate ar, C. Suire au, R. Sultanov ay, M. Šumbera ca, T. Susa co, T. J. M. Symons bs, A. Szanto de Toledo dk, I. Szarka ak, A. Szczepankiewicz dh, M. Szyman ́ ski dw, J. Takahashi dl, M. A. Tangaro af, J. D. Tapia Takaki au, A. Tarantola Peloni be, A. Tarazona Martinez ah, A. Tauro ah, G. Tejeda Muñoz c, A. Telesca ah, A. Ter Minasyan cq, C. Terrevoli af, J. Thäder cn, D. Thomas ax, R. Tieulent dm, A. R. Timmins dn, D. Tlusty al, A. Toia an, ac, cw, H. Torii dq, L. Toscano cv, V. Trubnikov d, D. Truesdale t, W. H. Trzaska aq, T. Tsuji dq, A. Tumkin cp, R. Turrisi cw, T. S. Tveter v, J. Ulery be, K. Ullaland s, J. Ulrich bl, A. Uras dm, G. M. Urciuoli db, G. L. Usai x, M. Vajzer al, M. Vala bk, L. Valencia Palomo au, P. Vande Vyvre ah, J. W. Van Hoorne ah, M. van Leeuwen ax, L. Vannucci br, A. Vargas c, R. Varma as, M. Vasileiou cf, A. Vasiliev cq, V. Vechernin dv, M. Veldhoen ax, M. Venaruzzo w, E. Vercellin y, S. Vergara c, R. Vernet i, M. Verweij ax, L. Vickovic df, G. Viesti ac, J. Viinikainen aq, Z. Vilakazi cg, O. Villalobos Baillie cs, Y. Vinogradov cp, L. Vinogradov dv, A. Vinogradov cq, T. Virgili ad, Y. P. Viyogi dt, A. Vodopyanov bk, M. A. Völkl cj, S. Voloshin dx, K. Voloshin ay, G. Volpe ah, B. von Haller ah, I. Vorobyev dv, D. Vranic cn, J. Vrláková am, B. Vulpescu bo, A. Vyushin cp, B. Wagner s, V. Wagner al, R. Wan h, Y. Wang h, M. Wang h, Y. Wang cj, K. Watanabe dr, M. Weber dn, J. P. Wessels ah, U. Westerhoff bg, J. Wiechula ds, J. Wikne v, M. Wilde bg, G. Wilk bv, M. C. S. Williams cx, B. Windelband cj, L. Xaplanteris Karampatsos di, C. G. Yaldo dx, Y. Yamaguchi dq, S. Yang s, P. Yang h, H. Yang o, S. Yasnopolskiy cq, J. Yi cm, Z. Yin h, I. K. Yoo cm, J. Yoon eb, W. Yu be, X. Yuan h, I. Yushmanov cq, V. Zaccolo by, C. Zach al, C. Zampolli cx, S. Zaporozhets bk, A. Zarochentsev dv, P. Závada bb, N. Zaviyalov cp, H. Zbroszczyk dw, P. Zelnicek bd, I. S. Zgura bc, M. Zhalov cc, H. Zhang h, X. Zhang bs, bo, h, Y. Zhang h, D. Zhou h, F. Zhou h, Y. Zhou ax, H. Zhu h, J. Zhu h, X. Zhu h, A. Zichichi ab, A. Zimmermann cj, G. Zinovjev d, Y. Zoccarato dm, M. Zynovyev d, M. Zyzak, CAMERINI, Paolo, FRAGIACOMO, ENRICO, LEA, RAMONA, LUPARELLO, GRAZIA, MARGAGLIOTTI, GIACOMO, PIANO, STEFANO, RUI, RINALDO, E., Abbas a, B., Abelev bt, J., Adam al, D., Adamová ca, A. M., Adare dz, M. M., Aggarwal ce, G., Aglieri Rinella ah, M., Agnello cv, Ck, A. G., Agocs dy, A., Agostinelli ab, Z., Ahammed dt, A., Ahmad Masoodi r, N., Ahmad r, S. U., Ahn bm, S. A., Ahn bm, I., Aimo y, Cv, Ck, M., Ajaz p, A., Akindinov ay, D., Aleksandrov cq, B., Alessandro cv, A., Alici cx, M, A., Alkin d, E., Almaráz Aviña bi, J., Alme aj, T., Alt an, V., Altini af, S., Altinpinar, I., Altsybeev dv, C., Andrei bw, A., Andronic cn, V., Anguelov cj, J., Anielski bg, C., Anson t, T., Anticˇic ́ co, F., Antinori cw, P., Antonioli cx, L., Aphecetche dd, H., Appelshäuser be, N., Arbor bp, S., Arcelli ab, A., Arend be, N., Armesto q, R., Arnaldi cv, T., Aronsson dz, I. C., Arsene cn, M., Arslandok be, A., Asryan dv, A., Augustinus ah, R., Averbeck cn, T. C., Awes cb, J., Äystö aq, M. D., Azmi r, Cg, M., Bach an, A., Badalà cu, Y. W., Baek bo, Ao, R., Bailhache be, R., Bala ch, Cv, A., Baldisseri o, F., Baltasar Dos Santos Pedrosa ah, J., Bán az, R. C., Baral ba, R., Barbera aa, F., Barile af, G. G., Barnaföldi dy, L. S., Barnby c, V., Barret bo, J., Bartke dh, M., Basile ab, N., Bastid bo, S., Basu dt, B., Bathen bg, G., Batigne dd, B., Batyunya bk, P. C., Batzing v, C., Baumann be, I. G., Bearden by, H., Beck be, N. K., Behera a, I., Belikov bj, F., Bellini ab, R., Bellwied dn, E., Belmont Moreno bi, G., Bencedi dy, S., Beole y, I., Berceanu bw, A., Bercuci bw, Y., Berdnikov cc, D., Berenyi dy, A. A. E., Bergognon dd, R. A., Bertens ax, D., Berzano y, L., Betev ah, A., Bhasin ch, A. K., Bhati ce, J., Bhom dr, N., Bianchi bq, L., Bianchi y, C., Bianchin ax, J., Bielcˇík al, J., Bielcˇíková ca, A., Bilandzic by, S., Bjelogrlic ax, F., Blanco k, F., Blanco dn, D., Blau cq, C., Blume be, M., Boccioli ah, S., Böttger bd, A., Bogdanov bu, H., Bøggild by, M., Bogolyubsky av, L., Boldizsár dy, M., Bombara am, J., Book be, H., Borel o, A., Borissov dx, F., Bossú cg, M., Botje bz, E., Botta y, E., Braidot b, P., Braun Munzinger cn, M., Bregant dd, T., Breitner bd, T. A., Broker be, T. A., Browning cl, M., Broz ak, R., Brun ah, E., Bruna y, G. E., Bruno af, D., Budnikov cp, H., Buesching be, S., Bufalino y, P., Buncic ah, O., Busch cj, Z., Buthelezi cg, D., Caffarri ac, Cw, X., Cai h, H., Caines dz, E., Calvo Villar ct, Camerini, Paolo, V., Canoa Roman l, G., Cara Romeo cx, F., Carena ah, W., Carena ah, N., Carlin Filho dk, F., Carminati ah, A., Casanova Díaz bq, J., Castillo Castellanos o, J. F., Castillo Hernandez cn, E. A. R., Casula x, V., Catanescu bw, C., Cavicchioli ah, C., Ceballos Sanchez j, J., Cepila al, P., Cerello cv, B., Chang aq, Eb, S., Chapeland ah, J. L., Charvet o, S., Chattopadhyay dt, S., Chattopadhyay cr, M., Cherney cd, C., Cheshkov ah, Dm, B., Cheynis dm, V., Chibante Barroso ah, D. D., Chinellato dn, P., Chochula ah, M., Chojnacki by, S., Choudhury dt, P., Christakoglou bz, C. H., Christensen by, P., Christiansen ag, T., Chujo dr, S. U., Chung cm, C., Cicalo cy, L., Cifarelli ab, F., Cindolo cx, J., Cleymans cg, F., Colamaria af, D., Colella af, A., Collu x, G., Conesa Balbastre bp, Z., Conesa del Valle ah, Au, M. E., Connors dz, G., Contin w, J. G., Contreras l, T. M., Cormier dx, Y., Corrales Morales y, P., Cortese ae, I., Cortés Maldonado c, M. R., Cosentino b, F., Costa ah, M. E., Cotallo k, E., Crescio l, P., Crochet bo, E., Cruz Alaniz bi, R., Cruz Albino l, E., Cuautle bh, L., Cunqueiro bq, A., Dainese ac, H. H., Dalsgaard by, R., Dangh, A., Danubc, K., Dascr, I., Dasau, S., Dase, D., Dascr, A., Dashdl, S., Dasha, S., Dedt, G. O. V., de Barros dk, A., De Caro ad, G., de Cataldo da, J., de Cuveland an, A., De Falco x, D., De Gruttola ad, H., Delagrange dd, A., Deloff bv, N., De Marco cv, E., Dénes dy, S., De Pasquale ad, A., Deppman dk, G. D., Erasmo af, R., de Rooij ax, M. A., Diaz Corchero k, D., Di Bari af, T., Dietel bg, C., Di Giglio af, S., Di Liberto db, A., Di Mauro ah, P., Di Nezza bq, R., Divià ah, Ø., Djuvsland, A., Dobrin dx, Ag, Ax, T., Dobrowolski bv, B., Dönigus cn, O., Dordic v, O., Driga dd, A. K., Dubey dt, A., Dubla ax, L., Ducroux dm, P., Dupieux bo, A. K., Dutta Majumdar cr, D., Elia da, D., Emschermann bg, H., Engel bd, B., Erazmus ah, Dd, H. A., Erdal aj, D., Eschweiler an, B., Espagnon au, M., Estienne dd, S., Esumi dr, D., Evans c, S., Evdokimov av, G., Eyyubova v, D., Fabris ac, J., Faivre bp, D., Falchieri ab, A., Fantoni bq, M., Fasel cj, D., Fehlker, L., Feldkamp bg, D., Felea bc, A., Feliciello cv, B., Fenton Olsen b, G., Feofilov dv, A., Fernández Téllez c, A., Ferretti y, A., Festanti ac, J., Figiel dh, M. A. S., Figueredo dk, S., Filchagin cp, D., Finogeev aw, F. M., Fionda af, E. M., Fiore af, E., Floratos cf, M., Floris ah, S., Foertsch cg, P., Foka cn, S., Fokin cq, Fragiacomo, Enrico, A., Francescon ah, Ac, U., Frankenfeld cn, U., Fuchs ah, C., Furget bp, M., Fusco Girard ad, J. J., Gaardhøje by, M., Gagliardi y, A., Gago ct, M., Gallio y, D. R., Gangadharan t, P., Ganoti cb, C., Garabatos cn, E., Garcia Solis n, C., Gargiulo ah, I., Garishvili bt, J., Gerhard an, M., Germain dd, C., Geuna o, A., Gheata ah, M., Gheata bc, Ah, B., Ghidini af, P., Ghosh dt, P., Gianotti bq, M. R., Girard dw, P., Giubellino ah, E., Gladysz Dziadus dh, P., Glässel cj, R., Gomez dj, L, E. G., Ferreiro q, L. H., González Trueba bi, P., González Zamora k, S., Gorbunov an, A., Goswami ci, S., Gotovac df, L. K., Graczykowski dw, R., Grajcarek cj, A., Grelli ax, A., Grigoras ah, C., Grigoras ah, V., Grigoriev bu, A., Grigoryan b, S., Grigoryan bk, B., Grinyov d, N., Grion cz, P., Gros ag, J. F., Grosse Oetringhaus ah, J. Y., Grossiord dm, R., Grosso ah, F., Guber aw, R., Guernane bp, B., Guerzoni ab, M., Guilbaud dm, K., Gulbrandsen by, H., Gulkanyan b, T., Gunji dq, R., Gupta ch, A., Gupta ch, R., Haake bg, Ø., Haaland, C., Hadjidakis au, M., Haiduc bc, H., Hamagaki dq, G., Hamar dy, B. H., Han u, L. D., Hanratty c, A., Hansen by, Z., Harmanová Tóthová am, J. W., Harris dz, M., Hartig be, A., Harton n, D., Hatzifotiadou cx, S., Hayashi dq, A., Hayrapetyan ah, B, S. T., Heckel be, M., Heide bg, H., Helstrup aj, A., Herghelegiu bw, G., Herrera Corral l, N., Herrmann cj, B. A., Hess d, K. F., Hetland aj, B., Hicks dz, B., Hippolyte bj, Y., Hori dq, P., Hristov ah, I., Hrˇivnácˇová au, M., Huang, T. J., Humanic t, D. S., Hwang u, R., Ichou bo, R., Ilkaev cp, I., Ilkiv bv, M., Inaba dr, E., Incani x, P. G., Innocenti ah, G. M., Innocenti y, M., Ippolitov cq, M., Irfan r, C., Ivan cn, V., Ivanov cc, A., Ivanov dv, M., Ivanov cn, O., Ivanytskyi d, A., Jachołkowski aa, P. M., Jacobs b, C., Jahnke dk, H. J., Jang bm, M. A., Janik dw, P. H. S. Y., Jayarathna dn, S., Jena a, D. M., Jha dx, R. T., Jimenez Bustamante bh, P. G., Jones c, H., Jung ao, A., Jusko c, A. B., Kaidalov ay, S., Kalcher an, P., Kalinˇák az, T., Kalliokoski aq, A., Kalweit ah, J. H., Kang eb, V., Kaplin bu, S., Kar dt, A., Karasu Uysal ah, Ea, Bn, O., Karavichev aw, T., Karavicheva aw, E., Karpechev aw, A., Kazantsev cq, U., Kebschull bd, R., Keidel ec, B., Ketzer be, Dg, K. H., Khan p, M. M., Khan r, P., Khan cr, S. A., Khan dt, A., Khanzadeev cc, Y., Kharlov av, B., Kileng aj, M., Kim eb, S., Kim u, B., Kim eb, T., Kim eb, D. J., Kim aq, D. W., Kim ao, Bm, J. H., Kim u, J. S., Kim ao, M., Kim ao, S., Kirsch an, I., Kisel an, S., Kiselev ay, A., Kisiel dw, J. L., Klay g, J., Klein cj, C., Klein Bösing bg, M., Kliemant be, A., Kluge ah, M. L., Knichel cn, A. G., Knospe di, M. K., Köhler cn, T., Kollegger an, A., Kolojvari dv, M., Kompaniets dv, V., Kondratiev dv, N., Kondratyeva bu, A., Konevskikh aw, V., Kovalenko dv, M., Kowalski dh, S., Kox bp, G., Koyithatta Meethaleveedu a, J., Kral aq, I., Králik az, F., Kramer be, A., Kravcˇáková am, M., Krelina al, M., Kretz an, M., Krivda c, Az, F., Krizek aq, M., Krus al, E., Kryshen cc, M., Krzewicki cn, V., Kucera ca, Y., Kucheriaev cq, T., Kugathasan ah, C., Kuhn bj, P. G., Kuijer bz, I., Kulakov be, J., Kumar a, P., Kurashvili bv, A., Kurepin aw, A. B., Kurepin aw, A., Kuryakin cp, S., Kushpil ca, V., Kushpil ca, H., Kvaerno v, M. J., Kweon cj, Y., Kwon eb, P., Ladrón de Guevara bh, I., Lakomov au, R., Langoy, Du, S. L., La Pointe ax, C., Lara bd, A., Lardeux dd, P., La Rocca aa, Lea, Ramona, M., Lechman ah, S. C., Lee ao, G. R., Lee c, I., Legrand ah, J., Lehnert be, R. C., Lemmon dc, M., Lenhardt cn, V., Lenti da, H., León bi, M., Leoncino y, I., León Monzón dj, P., Lévai dy, S., Li bo, H, J., Lien, R., Lietava c, S., Lindal v, V., Lindenstruth an, C., Lippmann cn, M. A., Lisa t, H. M., Ljunggren ag, D. F., Lodato ax, P. I., Loenne, V. R., Loggins dx, V., Loginov bu, D., Lohner cj, C., Loizides b, K. K., Loo aq, X., Lopez bo, E., López Torres j, G., Løvhøiden v, X. G., Lu cj, P., Luettig be, M., Lunardon ac, J., Luo h, Luparello, Grazia, C., Luzzi ah, K., Ma h, R., Ma dz, D. M., Madagodahettige Don dn, A., Maevskaya aw, M., Mager bf, D. P., Mahapatra ba, A., Maire cj, M., Malaev cc, I., Maldonado Cervantes bh, Ludmila Malinina, Bk, D., Mal’Kevich ay, P., Malzacher cn, A., Mamonov cp, L., Manceau cv, L., Mangotra ch, V., Manko cq, F., Manso bo, V., Manzari da, Y., Mao h, M., Marchisone bo, Y, J., Mareš bb, Margagliotti, Giacomo, Cz, A., Margotti cx, A., Marín cn, C., Markert di, M., Marquard be, I., Martashvili dp, N. A., Martin cn, P., Martinengo ah, M. I., Martínez c, G., Martínez García dd, Y., Martynov d, A., Mas dd, S., Masciocchi cn, M., Masera y, A., Masoni cy, L., Massacrier dd, A., Mastroserio af, A., Matyja dh, C., Mayer dh, J., Mazer dp, M. A., Mazzoni db, F., Meddi z, A., Menchaca Rocha bi, J., Mercado Pérez cj, M., Meres ak, Y., Miake dr, K., Mikhaylov bk, Ay, L., Milano ah, Jovan Milosevic, V, A., Mischke ax, A. N., Mishra ci, At, D., Mis ́kowiec cn, C., Mitu bc, S., Mizuno dr, J., Mlynarz dx, B., Mohanty dt, Bx, L., Molnar dy, Bj, L., Montaño Zetina l, M., Monteno cv, E., Montes k, T., Moon eb, M., Morando ac, D. A., Moreira De Godoy dk, S., Moretto ac, A., Morreale aq, A., Morsch ah, V., Muccifora bq, E., Mudnic df, S., Muhuri dt, M., Mukherjee dt, H., Müller ah, M. G., Munhoz dk, S., Murray cg, L., Musa ah, J., Musinsky az, B. K., Nandi a, R., Nania cx, E., Nappi da, C., Nattrass dp, T. K., Nayak dt, S., Nazarenko cp, A., Nedosekin ay, M., Nicassio af, Cn, M., Niculescu bc, B. S., Nielsen by, T., Niida dr, S., Nikolaev cq, V., Nikolic co, S., Nikulin cq, V., Nikulin cc, B. S., Nilsen cd, M. S., Nilsson v, F., Noferini cx, P., Nomokonov bk, G., Nooren ax, A., Nyanin cq, A., Nyatha a, C., Nygaard by, J., Nystrand, A., Ochirov dv, H., Oeschler bf, Ah, Cj, S., Oh dz, S. K., Oh ao, J., Oleniacz dw, A. C., Oliveira Da Silva dk, C., Oppedisano cv, A., Ortiz Velasquez ag, Bh, A., Oskarsson ag, P., Ostrowski dw, J., Otwinowski cn, K., Oyama cj, K., Ozawa dq, Y., Pachmayer cj, M., Pachr al, F., Padilla y, P., Pagano ad, G., Paic ́ bh, F., Painke an, C., Pajares q, S. K., Pal dt, A., Palaha c, A., Palmeri cu, V., Papikyan b, G. S., Pappalardo cu, W. J., Park cn, A., Passfeld bg, D. I., Patalakha av, V., Paticchio da, B., Paul cr, A., Pavlinov dx, T., Pawlak dw, T., Peitzmann ax, H., Pereira Da Costa o, E., Pereira De Oliveira Filho dk, D., Peresunko cq, C. E., Pérez Lara bz, D., Perrino af, W., Peryt dw, A., Pesci cx, Y., Pestov f, V., Petrácˇek al, M., Petran al, M., Petris bw, P., Petrov c, M., Petrovici bw, C., Petta aa, Piano, Stefano, M., Pikna ak, P., Pillot dd, O., Pinazza ah, L., Pinsky dn, N., Pitz be, D. B., Piyarathna dn, M., Planinic co, M., Płoskon ́ b, J., Pluta dw, T., Pocheptsov bk, S., Pochybova dy, P. L. M., Podesta Lerma dj, M. G., Poghosyan ah, K., Polák bb, B., Polichtchouk av, N., Poljak ax, Co, A., Pop bw, S., Porteboeuf Houssais bo, V., Pospíšil al, B., Potukuchi ch, S. K., Prasad dx, R., Preghenella cx, F., Prino cv, C. A., Pruneau dx, I., Pshenichnov aw, G., Puddu x, V., Punin cp, M., Putiš am, J., Putschke dx, H., Qvigstad v, A., Rachevski cz, A., Rademakers ah, T. S., Räihä aq, J., Rak aq, A., Rakotozafindrabe o, L., Ramello ae, S., Raniwala ci, R., Raniwala ci, S. S., Räsänen aq, B. T., Rascanu be, D., Rathee ce, W., Rauch ah, K. F., Read dp, J. S., Real bp, K., Redlich bv, R. J., Reed dz, A., Rehman, P., Reichelt be, M., Reicher ax, R., Renfordt be, A. R., Reolon bq, A., Reshetin aw, F., Rettig an, J. P., Revol ah, K., Reygers cj, L., Riccati cv, R. A., Ricci br, T., Richert ag, M., Richter v, P., Riedler ah, W., Riegler ah, F., Riggi aa, Cu, M., Rodríguez Cahuantzi c, A., Rodriguez Manso bz, K., Røed, V, E., Rogochaya bk, D., Rohr an, D., Röhrich, R., Romita cn, Dc, F., Ronchetti bq, P., Rosnet bo, S., Rossegger ah, A., Rossi ah, P., Roy cr, C., Roy bj, A. J., Rubio Montero k, Rui, Rinaldo, R., Russo y, E., Ryabinkin cq, A., Rybicki dh, S., Sadovsky av, K., Šafarˇík ah, R., Sahoo at, P. K., Sahu ba, J., Saini dt, H., Sakaguchi ar, S., Sakai b, D., Sakata dr, C. A., Salgado q, J., Salzwedel t, S., Sambyal ch, V., Samsonov cc, X., Sanchez Castro bj, L., Šándor az, A., Sandoval bi, M., Sano dr, G., Santagati aa, R., Santoro ah, J., Sarkamo aq, D., Sarkar dt, E., Scapparone cx, F., Scarlassara ac, R. P., Scharenberg cl, C., Schiaua bw, R., Schicker cj, H. R., Schmidt d, C., Schmidt cn, S., Schuchmann be, J., Schukraft ah, T., Schuster dz, Y., Schutz ah, K., Schwarz cn, K., Schweda cn, G., Scioli ab, E., Scomparin cv, R., Scott dp, P. A., Scott c, G., Segato ac, I., Selyuzhenkov cn, S., Senyukov bj, J., Seo cm, S., Serci x, E., Serradilla k, Bi, A., Sevcenco bc, A., Shabetai dd, G., Shabratova bk, R., Shahoyan ah, N., Sharma dp, S., Sharma ch, S., Rohni ch, K., Shigaki ar, K., Shtejer j, Y., Sibiriak cq, E., Sicking bg, S., Siddhanta cy, T., Siemiarczuk bv, D., Silvermyr cb, C., Silvestre bp, G., Simatovic bh, G., Simonetti ah, R., Singaraju dt, R., Singh ch, S., Singha dt, V., Singhal dt, B. C., Sinha dt, T., Sinha cr, B., Sitar ak, M., Sitta ae, T. B., Skaali v, K., Skjerdal, R., Smakal al, N., Smirnov dz, R. J. M., Snellings ax, C., Søgaard ag, R., Soltz bt, M., Song eb, J., Song cm, C., Soos ah, F., Soramel ac, I., Sputowska dh, M., Spyropoulou Stassinaki cf, B. K., Srivastava cl, J., Stachel cj, I., Stan bc, G., Stefanek bv, M., Steinpreis t, E., Stenlund ag, G., Steyn cg, J. H., Stiller cj, D., Stocco dd, M., Stolpovskiy av, P., Strmen ak, A. A. P., Suaide dk, M. A., Subieta Vásquez y, T., Sugitate ar, C., Suire au, R., Sultanov ay, M., Šumbera ca, T., Susa co, T. J. M., Symons b, A., Szanto de Toledo dk, I., Szarka ak, A., Szczepankiewicz dh, M., Szyman ́ ski dw, J., Takahashi dl, M. A., Tangaro af, J. D., Tapia Takaki au, A., Tarantola Peloni be, A., Tarazona Martinez ah, A., Tauro ah, G., Tejeda Muñoz c, A., Telesca ah, A., Ter Minasyan cq, C., Terrevoli af, J., Thäder cn, D., Thomas ax, R., Tieulent dm, A. R., Timmins dn, D., Tlusty al, A., Toia an, Ac, Cw, H., Torii dq, L., Toscano cv, V., Trubnikov d, D., Truesdale t, W. H., Trzaska aq, T., Tsuji dq, A., Tumkin cp, R., Turrisi cw, T. S., Tveter v, J., Ulery be, K., Ullaland, J., Ulrich bl, Bd, A., Uras dm, G. M., Urciuoli db, G. L., Usai x, M., Vajzer al, Ca, M., Vala bk, L., Valencia Palomo au, P., Vande Vyvre ah, J. W., Van Hoorne ah, M., van Leeuwen ax, L., Vannucci br, A., Vargas c, R., Varma a, M., Vasileiou cf, A., Vasiliev cq, V., Vechernin dv, M., Veldhoen ax, M., Venaruzzo w, E., Vercellin y, S., Vergara c, R., Vernet i, M., Verweij ax, L., Vickovic df, G., Viesti ac, J., Viinikainen aq, Z., Vilakazi cg, O., Villalobos Baillie c, Y., Vinogradov cp, L., Vinogradov dv, A., Vinogradov cq, T., Virgili ad, Y. P., Viyogi dt, A., Vodopyanov bk, M. A., Völkl cj, S., Voloshin dx, K., Voloshin ay, G., Volpe ah, B., von Haller ah, I., Vorobyev dv, D., Vranic cn, J., Vrláková am, B., Vulpescu bo, A., Vyushin cp, B., Wagner, V., Wagner al, R., Wan h, Y., Wang h, M., Wang h, Y., Wang cj, K., Watanabe dr, M., Weber dn, J. P., Wessels ah, Bg, U., Westerhoff bg, J., Wiechula d, J., Wikne v, M., Wilde bg, G., Wilk bv, M. C. S., Williams cx, B., Windelband cj, L., Xaplanteris Karampatsos di, C. G., Yaldo dx, Y., Yamaguchi dq, S., Yang, P., Yang h, H., Yang o, Ax, S., Yasnopolskiy cq, J., Yi cm, Z., Yin h, I. K., Yoo cm, J., Yoon eb, W., Yu be, X., Yuan h, I., Yushmanov cq, Zaccolo by, V., C., Zach al, C., Zampolli cx, S., Zaporozhets bk, A., Zarochentsev dv, P., Závada bb, N., Zaviyalov cp, H., Zbroszczyk dw, P., Zelnicek bd, I. S., Zgura bc, M., Zhalov cc, H., Zhang h, X., Zhang b, Bo, H, Y., Zhang h, D., Zhou h, F., Zhou h, Y., Zhou ax, H., Zhu h, J., Zhu h, X., Zhu h, A., Zichichi ab, A., Zimmermann cj, G., Zinovjev d, Y., Zoccarato dm, M., Zynovyev d, and M., Zyzak

Subjects
Charged-particle density, Heavy-ion collisions, LHC, Wide rapidity coverage, Nuclear and High Energy Physics, HEAVY-ION COLLISIONS, Charged-Particle Density, Heavy ions collisions, charged-particle density, Nuclear Experiment
Abstract

We present the first wide-range measurement of the charged-particle pseudorapidity density distribution, for different centralities (the 0–5%, 5–10%, 10–20%, and 20–30% most central events) in Pb–Pb collisions at √sNN = 2.76 TeV at the LHC. The measurement is performed using the full coverage of the ALICE detectors, −5.0 < η < 5.5, and employing a special analysis technique based on collisions arising from LHC ‘satellite’ bunches. We present the pseudorapidity density as a function of the number of participating nucleons as well as an extrapolation to the total number of produced charged particles (Nch = 17 165 ± 772 for the 0–5% most central collisions). From the measured dNch/dη distribution we derive the rapidity density distribution, dNch/dy, under simple assumptions. The rapidity density distribution is found to be significantly wider than the predictions of the Landau model. We assess the validity of longitudinal scaling by comparing to lower energy results from RHIC. Finally the mechanisms of the underlying particle production are discussed based on a comparison with various theoretical models.

Published
2013

28. The collagenolytic activity of cathepsin K is unique among mammalian proteinases.

Author

Garnero, P, Borel, O, Byrjalsen, I, Ferreras, M, Drake, F H, McQueney, M S, Foged, N T, Delmas, P D, and Delaissé, J M

Abstract

Type I collagen fibers account for 90% of the organic matrix of bone. The degradation of this collagen is a major event during bone resorption, but its mechanism is unknown. A series of data obtained in biological models strongly suggests that the recently discovered cysteine proteinase cathepsin K plays a key role in bone resorption. Little is known, however, about the actual action of cathepsin K on type I collagen. Here, we show that the activity of cathepsin K alone is sufficient to dissolve completely insoluble collagen of adult human cortical bone. We found that the collagenolytic activity of cathepsin K is directed both outside the helical region of the molecule, i.e. the typical activity of cysteine proteinases, and at various sites inside the helical region, hitherto believed to resist all mammalian proteinases but the collagenases of the matrix metalloproteinase family and the neutrophil elastase. This property of cathepsin K is unique among mammalian proteinases and is reminiscent of bacterial collagenases. It is likely to be responsible for the key role of cathepsin K in bone resorption.

Published
1998

29. Variation du niveau circulant de périostine dans l'ostéogenèse imparfaite.

Author

Mercier, A., Gineyts, E., Millet, M., Borel, O., Szulc, P., Sornay-Rendu, E., Rousseau, J.C., Fontanges, E., and Chapurlat, R.

Abstract

La périostine (POSTN) interagit avec le collagène de type 1 et la voie Wnt-β-caténine, ce qui suggère son implication dans la physiopathologie de l'ostéogenèse imparfaite (OI). Des niveaux élevés de POSTN ont été associés au risque de fractures chez les femmes ménopausées. Il n'existe actuellement aucun biomarqueur pour évaluer la gravité de l'OI, et la POSTN apparaît comme un candidat prometteur en raison de la simplicité de sa mesure dans le sérum via une méthode standardisée. L'objectif principal est d'étudier s'il existe une dérégulation de la POSTN dans l'OI. L'objectif secondaire est de déterminer si les niveaux de POSTN sont corrélés à la gravité de la maladie ainsi qu'à diverses caractéristiques cliniques et biologiques. Il s'agit d'une analyse secondaire de 60 patients adultes issus de la cohorte miROI, incluant les types 1 et 3 d'OI. Ces patients ont été comparés à 60 individus témoins appariés selon l'âge, le sexe et l'indice de masse corporelle. Les mesures ont été effectuées à l'aide d'un test ELISA sur des échantillons de sérum. Un test t a été utilisé pour la comparaison principale, et le coefficient de corrélation de Pearson a été calculé pour identifier les corrélations potentielles entre les niveaux sériques de POSTN et les caractéristiques cliniques et biologiques (Fig. 1). Les niveaux sériques de POSTN étaient significativement plus élevés dans le groupe OI par rapport au groupe témoin (moyenne = 798 vs 712 ng/mL ; p = 0,016). Aucune corrélation n'a été observée avec des variables de gravité telles que le nombre de fractures sévères prévalentes, le rapport taille/envergure, ou la sévérité de la scoliose. Cependant, une association significative avec la présence de la dentinogenèse imparfaite (DI) a été observée (moyenne = 819 vs 685 ng/mL ; p = 0,03). Nous avons constaté que les niveaux sériques de POSTN étaient plus élevés chez les patients atteints d'OI que chez les témoins et étaient particulièrement associés à la présence de DI. Compte tenu du rôle de la POSTN dans la stabilité du collagène et la dentinogenèse, elle pourrait être considérée comme un facteur dans la physiopathologie de l'OI et un biomarqueur potentiel. [ABSTRACT FROM AUTHOR]

Published
2024
Full Text
View/download PDF

30. Evaluation of circulating microRNA signature in patients with erosive hand osteoarthritis: The HOAmiR study.

Author

Auroux M, Millet M, Merle B, Fontanges E, Duvert F, Gineyts E, Rousseau JC, Borel O, Mercier-Guery A, Lespessailles E, and Chapurlat R

Subjects
Humans, Male, Female, Aged, Middle Aged, Hand Joints, Case-Control Studies, Down-Regulation, Biomarkers blood, MicroRNAs blood, Osteoarthritis genetics, Osteoarthritis blood, Circulating MicroRNA blood, Circulating MicroRNA genetics
Abstract

Objectives: To identify circulating micro-RNAs differentially expressed in patients with erosive hand osteoarthritis (HOA) compared to patients with non-erosive HOA and patients without HOA., Methods: In the screening phase, 768 well-characterized micro-RNAs using Taqman low-density array cards were measured in 30 sera from 10 patients with erosive HOA, 10 patients with non-erosive HOA, and 10 controls without HOA, matched for age and body mass index (BMI). In a second step, we validated the micro-RNAs identified at the screening phase (adjusted p value < 0.05 after false discovery rate correction using Benjamini-Hochberg method and literature review) in larger samples (60 patients with erosive HOA and 60 patients without HOA matched for age and BMI)., Results: In the screening phase, we identified 21 down-regulated and 4 up-regulated micro-RNAs of interest between erosive HOA and control groups. Among these, 9 micro-RNAs (miR-373-3p, miR-558, miR-607, miR-653-5p, miR-137 and miR448 were down-regulated, and miR-142-3p, miR-144-3p and miR-34a-5p were up-regulated) were previously described in chondrocytes homeostasis or OA. We found only one significantly down-regulated micro-RNA between erosive and non-erosive HOA. In the validation phase, we showed replication of a single micro-RNA the significant downregulation of miR-196-5p, that had been previously identified in the screening phase among patients with erosive HOA compared to those without HOA. After reviewing the literature and the miRNA-gene interaction prediction model, we found that this microRNA could interact with bone homeostasis and HOXC8, which could explain its role in osteoarthritis., Conclusions: We found that miR-196-5p was down-regulated in patients with erosive HOA and some of its targets could explain a role in OA., (Copyright © 2024 Osteoarthritis Research Society International. Published by Elsevier Ltd. All rights reserved.)

Published
2024
Full Text
View/download PDF

31. Dysregulation of MicroRNAs in Adult Osteogenesis Imperfecta: The miROI Study.

Author

Mercier-Guery A, Millet M, Merle B, Collet C, Bagouet F, Borel O, Sornay-Rendu E, Szulc P, Vignot E, Gensburger D, Fontanges E, Croset M, and Chapurlat R

Subjects
Humans, Adult, Collagen Type I, alpha 1 Chain, Collagen Type I genetics, Minerals, Mutation, Osteogenesis Imperfecta genetics, MicroRNAs genetics
Abstract

As epigenetic regulators of gene expression, circulating micro-RiboNucleic Acids (miRNAs) have been described in several bone diseases as potential prognostic markers. The aim of our study was to identify circulating miRNAs potentially associated with the severity of osteogenesis imperfecta (OI) in three steps. We have screened by RNA sequencing for the miRNAs that were differentially expressed in sera of a small group of OI patients versus controls and then conducted a validation phase by RT-qPCR analysis of sera of a larger patient population. In the first phase of miROI, we found 79 miRNAs that were significantly differentially expressed. We therefore selected 19 of them as the most relevant. In the second phase, we were able to validate the significant overexpression of 8 miRNAs in the larger OI group. Finally, we looked for a relationship between the level of variation of the validated miRNAs and the clinical characteristics of OI. We found a significant difference in the expression of two microRNAs in those patients with dentinogenesis imperfecta. After reviewing the literature, we found 6 of the 8 miRNAs already known to have a direct action on bone homeostasis. Furthermore, the use of a miRNA-gene interaction prediction model revealed a 100% probability of interaction between 2 of the 8 confirmed miRNAs and COL1A1 and/or COL1A2. This is the first study to establish the miRNA signature in OI, showing a significant modification of miRNA expression potentially involved in the regulation of genes involved in the physiopathology of OI. © 2023 The Authors. Journal of Bone and Mineral Research published by Wiley Periodicals LLC on behalf of American Society for Bone and Mineral Research (ASBMR)., (© 2023 The Authors. Journal of Bone and Mineral Research published by Wiley Periodicals LLC on behalf of American Society for Bone and Mineral Research (ASBMR).)

Published
2023
Full Text
View/download PDF

32. Serum Col3-4: A new type III and IV collagen biochemical marker of synovial tissue turnover in patients with rheumatoid arthritis.

Author

Gineyts E, Millet M, Borel O, Coutant F, Rousseau JC, Chapurlat R, Marotte H, and Garnero P

Subjects
Humans, Female, Middle Aged, Male, Collagen Type IV metabolism, Synovial Membrane metabolism, Biomarkers, Matrix Metalloproteinase 9 metabolism, Arthritis, Rheumatoid metabolism
Abstract

The objective of this study was to develop a serum biochemical marker of the degradation of type III and IV collagens, as an index of synovium turnover, and evaluate its performance in patients with rheumatoid arthritis (RA). An enzyme-linked immunosorbent assay for serum synovial collagen fragments (Col3-4) was developed using an antibody recognizing a specific sequence from human type III collagen, which shares 70% homology with type IV collagen. Immunohistochemistry was performed to localize Col3-4 and the matrix metalloprotease MMP-9 which is upregulated in RA synovial fibroblasts in the synovial tissue from a RA patient. Serum Col3-4 was measured in patients with RA (n = 66, 73% women, mean age 62 years, median disease activity score 28 with erythrocyte sedimentation rate (DAS28-ESR) 2.6) and in sex and age matched healthy controls (n = 70, 76% women, mean age 59 years). Col3-4 immunoassay demonstrated adequate analytical performances and recognized a circulating neoepitope resulting from the cleavage of type III and IV collagens. In RA synovium tissue, Col3-4 fragments were localized in the lining layer where destructive fibroblasts are present and around blood vessels rich in type IV collagen. MMP-9 colocalized with Col3-4 staining and efficiently released Col3-4 fragments from type III and type IV collagen digestion. Serum Col3-4 was markedly increased in patients with RA (+240% vs controls, p < 0.0001) and correlated with DAS28-ESR (r = 0.53, p < 0.0001). Patients with RA and active disease (DAS28-ESR > 3.2, n = 20) had 896% (p < 0.0001) higher levels than subjects with low activity (n = 46). Serum Col3-4 is a specific and sensitive biochemical marker reflecting MMP- mediated type III and IV collagen degradation from synovial tissue. Serum Col3-4 levels are markedly increased in patients with RA, particularly in those with active disease, suggesting that it may be useful for the clinical investigation of RA., Competing Interests: The authors have declared that no competing interests exist., (Copyright: © 2023 Gineyts et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.)

Published
2023
Full Text
View/download PDF

33. Circulating autotaxin levels in healthy teenagers: Data from the Vitados cohort.

Author

Méaux MN, Regnier M, Portefaix A, Borel O, Alioli C, Peyruchaud O, Legrand M, and Bacchetta J

Abstract

Autotaxin (ATX) is a secreted enzyme with a lysophospholipase D activity, mainly secreted by adipocytes and widely expressed. Its major function is to convert lysophosphatidylcholine (LPC) into lysophosphatidic acid (LPA), an essential bioactive lipid involved in multiple cell processes. The ATX-LPA axis is increasingly studied because of its involvement in numerous pathological conditions, more specifically in inflammatory or neoplastic diseases, and in obesity. Circulating ATX levels gradually increase with the stage of some pathologies, such as liver fibrosis, thus making them a potentially interesting non-invasive marker for fibrosis estimation. Normal circulating levels of ATX have been established in healthy adults, but no data exist at the pediatric age. The aim of our study is to describe the physiological concentrations of circulating ATX levels in healthy teenagers through a secondary analysis of the VITADOS cohort. Our study included 38 teenagers of Caucasian origin (12 males, 26 females). Their median age was 13 years for males and 14 years for females, ranging from Tanner 1 to 5. BMI was at the 25th percentile for males and 54th percentile for females, and median blood pressure was normal. ATX median levels were 1,049 (450-2201) ng/ml. There was no difference in ATX levels between sexes in teenagers, which was in contrast to the male and female differences described in the adult population. ATX levels significantly decreased with age and pubertal status, reaching adult levels at the end of puberty. Our study also suggested positive correlations between ATX levels and blood pressure (BP), lipid metabolism, and bone biomarkers. However, except for LDL cholesterol, these factors were also significantly correlated with age, which might be a confounding factor. Still, a correlation between ATX and diastolic BP was described in obese adult patients. No correlation was found between ATX levels and inflammatory marker C-reactive protein (CRP), Body Mass Index (BMI), and biomarkers of phosphate/calcium metabolism. In conclusion, our study is the first to describe the decline in ATX levels with puberty and the physiological concentrations of ATX levels in healthy teenagers. It will be of utmost importance when performing clinical studies in children with chronic diseases to keep these kinetics in mind, as circulating ATX might become a non-invasive prognostic biomarker in pediatric chronic diseases., Competing Interests: The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest., (© 2023 Méaux, Regnier, Portefaix, Borel, Alioli, Peyruchaud, Legrand and Bacchetta.)

Published
2023
Full Text
View/download PDF

34. A Signature of Circulating miRNAs Associated With Fibrous Dysplasia of Bone: the mirDys Study.

Author

Legrand MA, Millet M, Merle B, Rousseau JC, Hemmendinger A, Gineyts E, Sornay-Rendu E, Szulc P, Borel O, Croset M, and Chapurlat R

Subjects
Adult, Biomarkers blood, Epigenesis, Genetic, Female, GTP-Binding Protein alpha Subunits, Gs genetics, Humans, Male, Circulating MicroRNA genetics, Fibrous Dysplasia of Bone genetics
Abstract

Fibrous dysplasia (FD) is a rare bone disease caused by activating mutations of GNAS encoding the Gsα protein, enhancing cyclic adenosine monophosphate (cAMP) production by overstimulation of adenylyl cyclase and impairing osteoblastic differentiation. The clinical presentation ranges from asymptomatic to polyostotic forms with severe disability, explained by the mosaic distribution of the GNAS mutation. Physicians have to deal with the gap of knowledge in FD pathogenesis, the absence of prognostic markers and the lack of specific treatment. The identification of specific biomarkers for FD is an important step to improve the clinical and therapeutic approaches. An epigenetic regulation driven by microRNAs (miRNAs), known as promising biomarkers in bone disease, could be involved in FD. We have sought circulating miRNAs that are differentially expressed in FD patients compared to controls and would reflect dysregulations of osteogenesis-related genes and bone disorder. The global miRNA profiling was performed using Next Generation Sequencing in patient serum collected from a discovery cohort of 20 patients (10 polyostotic and 10 monostotic) and 10 controls. From these, we selected 19 miRNAs for a miRNA validation phase from serum of 82 patients and 82 controls, using real-time qPCR. Discovery screening identified 111 miRNAs differentially expressed in patient serum, after adjusting for the false discovery rate (FDR). Among the 82 patients, 55% were polyostotic, and 73% were women with a mean age of 42 years. Six miRNAs (miR-25-3p, miR-93-5p, miR-182-5p, miR-324-5p, miR-363-3p, and miR-451a) were significantly overexpressed in serum, with FDR <0.05. The expression level of these six miRNAs was not associated with the FD severity. In conclusion, we identified a signature of circulating miRNAs associated with FD. These miRNAs are potential negative regulators of gene expression in bone cell progenitors, suggesting their activity in FD by interfering with osteoblastic and osteoclastic differentiation to impair bone mineralization and remodeling processes. © 2020 American Society for Bone and Mineral Research., (© 2020 American Society for Bone and Mineral Research.)

Published
2020
Full Text
View/download PDF

35. Association of circulating microRNAs with prevalent and incident knee osteoarthritis in women: the OFELY study.

Author

Rousseau JC, Millet M, Croset M, Sornay-Rendu E, Borel O, and Chapurlat R

Subjects
Aged, Circulating MicroRNA analysis, Cohort Studies, Female, High-Throughput Nucleotide Sequencing, Humans, Incidence, Prevalence, Biomarkers blood, MicroRNAs blood, Osteoarthritis, Knee blood
Abstract

Objectives: In the context of the scarcity of biomarkers for knee osteoarthritis (OA), we examined the associations of prevalent and incident OA with the expression levels of serum miRNAs in subjects with and without OA., Methods: With a next-generation sequencing approach, we compared the miRome expression of 10 women with knee OA and 10 age-matched healthy subjects. By real-time qPCR, we analyzed the expression levels of 19 miRNAs at baseline selecting 43 women with prevalent knee OA (Kellgren Lawrence score of 2/3), 23 women with incident knee OA over a 4-year follow-up and 67 healthy subjects without prevalent or incident OA matched for age and body mass index., Results: Serum miR-146a-5p was significantly increased in the group of prevalent knee OA compared with controls (relative quantification (RQ); median [Interquartile range] 1.12 [0.73; 1.46] vs 0.85 [0.62; 1.03], p = 0.015). The likelihood of prevalent knee OA was significantly increased (odds ratio [95% confidence interval (CI)] 1.83 [1.21-2.77], p = 0.004) for each quartile increase in serum miR-146a-5p. The women with miR-146a-5p levels above the median (0.851) had a higher risk of prevalent knee OA compared to those below the median [95% CI] 4.62 [1.85-11.5], p = 0.001. Moreover, we found a significant association between the baseline level of serum miR-186-5p and the risk of incident knee OA (Q4 vs Q1-3; odds ratio [95% CI] 6.13 [1.14-32.9], p = 0.034)., Conclusion: We showed for the first time that miR-146a-5p and miR-186-5p are significantly associated with prevalent and incident knee OA, respectively.

Published
2020
Full Text
View/download PDF

36. Selected serum microRNA, abdominal aortic calcification and risk of osteoporotic fracture.

Author

Pickering ME, Millet M, Rousseau JC, Croset M, Szulc P, Borel O, Sornay Rendu E, and Chapurlat R

Subjects
Aged, Aorta, Abdominal metabolism, Aorta, Abdominal pathology, Biomarkers blood, Calcinosis blood, Calcinosis diagnosis, Calcinosis pathology, Case-Control Studies, Female, Humans, MicroRNAs blood, Middle Aged, Odds Ratio, Osteoporosis, Postmenopausal blood, Osteoporosis, Postmenopausal diagnosis, Osteoporosis, Postmenopausal pathology, Osteoporotic Fractures blood, Osteoporotic Fractures diagnosis, Osteoporotic Fractures pathology, Polymerase Chain Reaction, Postmenopause blood, Postmenopause genetics, Prognosis, Prospective Studies, Risk, Calcinosis genetics, MicroRNAs genetics, Osteoporosis, Postmenopausal genetics, Osteoporotic Fractures genetics
Abstract

Context: MicroRNA (miRNA) regulate post-transcriptionally the expression of osteogenesis and angiogenesis associated genes and emerge as potential non-invasive biomarkers in vascular and bone diseases. Severe abdominal aortic calcification (AAC) is associated with higher risk of cardiovascular event and of fragility fracture., Objective: To identify miRNA linked to the aggravation of AAC and to incident osteoporotic fracture., Design: Postmenopausal women (>50 years) with available serum at inclusion and data for each outcome (Kauppila score and incident fracture) were selected from the OFELY prospective cohort. We conducted a case-control study in 434 age-matched women, 50% with incident osteoporotic fracture over 20 years of follow-up and a second study in 183 women to explore AAC over 17 years., Methods: Serum expression of three miRNA involved in vascular calcification and bone turnover regulation (miRs-26a-5p,-34a-5p, and -223-5p) was quantified at baseline by TaqMan Advanced miRNA technology and expressed by relative quantification. Outcomes were the association of miRNA levels with (1) incident osteoporotic fractures during 20 years, (2) AAC aggravation during 17 years., Results: MiRNA level was not associated with incident fractures (miR-26a-5p: 1.06 vs 0.99, p = 0.07; miR-34a-5p: 1.15 vs 1.26, p = 0.35; miR-223a-5p: 1.01 vs 1.05, p = 0.32). 93 women had an increase in Kauppila score over 17 years while 90 did not. None of the miRNAs was associated with an aggravation in AAC (miR-26a-5p: 1.09 vs 1.10, p = 0.95; miR-34a-5p: 0.78 vs 0.73, p = 0.90; miR-223-5p: 0.97 vs 0.78, p = 0.11)., Conclusions: Circulating miR-26a-5p, -34a-5p and -223-5p are not significantly associated with incident fracture and AAC aggravation., Competing Interests: The authors have declared that no competing interests exist.

Published
2019
Full Text
View/download PDF

37. The C-Terminal Intact Forms of Periostin (iPTN) Are Surrogate Markers for Osteolytic Lesions in Experimental Breast Cancer Bone Metastasis.

Author

Gineyts E, Bonnet N, Bertholon C, Millet M, Pagnon-Minot A, Borel O, Geraci S, Bonnelye E, Croset M, Suhail A, Truica C, Lamparella N, Leitzel K, Hartmann D, Chapurlat R, Lipton A, Garnero P, Ferrari S, Clézardin P, and Rousseau JC

Subjects
Adult, Aged, Animals, Cell Adhesion Molecules metabolism, Disease Models, Animal, Female, Humans, Mice, Middle Aged, Biomarkers, Tumor blood, Bone Neoplasms diagnosis, Bone Neoplasms secondary, Breast Neoplasms pathology, Cell Adhesion Molecules blood, Osteolysis diagnosis
Abstract

Periostin is an extracellular matrix protein that actively contributes to tumor progression and metastasis. Here, we hypothesized that it could be a marker of bone metastasis formation. To address this question, we used two polyclonal antibodies directed against the whole molecule or its C-terminal domain to explore the expression of intact and truncated forms of periostin in the serum and tissues (lung, heart, bone) of wild-type and periostin-deficient mice. In normal bones, periostin was expressed in the periosteum and specific periostin proteolytic fragments were found in bones, but not in soft tissues. In animals bearing osteolytic lesions caused by 4T1 cells, C-terminal intact periostin (iPTN) expression disappeared at the invasive front of skeletal tumors where bone-resorbing osteoclasts were present. In vitro, we found that periostin was a substrate for osteoclast-derived cathepsin K, generating proteolytic fragments that were not recognized by anti-periostin antibodies directed against iPTN. In vivo, using an in-house sandwich immunoassay aimed at detecting iPTN only, we observed a noticeable reduction of serum periostin levels (- 26%; P < 0.002) in animals bearing osteolytic lesions caused by 4T1 cells. On the contrary, this decrease was not observed in women with breast cancer and bone metastases when periostin was measured with a human assay detecting total periostin. Collectively, these data showed that mouse periostin was degraded at the bone metastatic sites, potentially by cathepsin K, and that the specific measurement of iPTN in serum should assist in detecting bone metastasis formation in breast cancer.

Published
2018
Full Text
View/download PDF

38. Osteocalcin levels on oral glucose load in women being investigated for polycystic ovary syndrome.

Author

Schwetz V, Lerchbaum E, Schweighofer N, Hacker N, Trummer O, Borel O, Pieber TR, Chapurlat R, and Obermayer-Pietsch B

Subjects
Adult, Body Mass Index, Collagen Type I blood, Cross-Sectional Studies, Female, Glucose Tolerance Test, Humans, Insulin Resistance, Peptide Fragments blood, Peptides blood, Procollagen blood, Osteocalcin blood, Polycystic Ovary Syndrome blood
Abstract

Objective: Osteocalcin (OC) might play a hormone-like role in energy metabolism and the regulatory circuit between the pancreas and osteoblasts. Effects of a 75-g oral glucose tolerance test (OGTT) on total OC, undercarboxylated (ucOC), and carboxylated osteocalcin (cOC) in insulin-resistant (IR) and noninsulin-resistant (nIR) premenopausal women was evaluated, and the relationships of changes in OC, ucOC, and cOC with area under the curve (AUC) insulin and the Matsuda index were examined., Methods: In this cross-sectional study, 105 premenopausal women underwent OGTT; 18 were IR (homeostatic model assessment of insulin resistance [HOMA-IR] > 2.6; (2 with type 2 diabetes, 2 with impaired glucose tolerance), and 87 were nIR (3 with impaired glucose tolerance). Changes in total OC, ucOC, and cOC were evaluated 60 and 120 minutes after glucose loading., Results: At baseline, IR subjects had significantly lower levels of total OC, cOC, and ucOC. In nIR women, total OC decreased by 19% from 18.0 ng/mL (14.5-24.7) at baseline to 14.6 ng/mL (10.9-17.8) after 120 minutes, ucOC decreased by 22% from 3.2 ng/mL (2.1-4.5) to 2.5 ng/mL (1.7-3.5), and cOC decreased by 26% from 14.9 ng/mL (12.1-20.4) to 11.1 ng/mL (9.0-14.5) (P < .001, respectively). No significant decreases were noted in IR subjects. The declines in OC and cOC predicted AUCinsulin (ΔOC: β = 0.301, P = .001; ΔcOC: β = 0.315, P < .001) and the Matsuda index (ΔOC: β = -0.235, P = .003; ΔcOC: β = -0.245, P = .002)., Conclusions: Glucose intake lowers levels of OC, ucOC, and cOC in nIR women, the extent of which predicts IR and insulin sensitivity in premenopausal women. OC parameters seem suppressed in IR women. There might be a differential osteoblast response to oral glucose in IR and nIR women, with OC reflecting this finding.

Published
2014
Full Text
View/download PDF

39. Lower fracture risk in older men with higher sclerostin concentration: a prospective analysis from the MINOS study.

Author

Szulc P, Bertholon C, Borel O, Marchand F, and Chapurlat R

Subjects
Adaptor Proteins, Signal Transducing, Aged, Bone Density, Bone and Bones pathology, Follow-Up Studies, Fractures, Bone mortality, Fractures, Bone physiopathology, France epidemiology, Genetic Markers, Humans, Incidence, Male, Multivariate Analysis, Prospective Studies, Risk Factors, Bone Morphogenetic Proteins blood, Fractures, Bone blood, Fractures, Bone epidemiology
Abstract

Sclerostin is synthesized by osteocytes and inhibits bone formation. We measured serum sclerostin levels in 710 men aged 50 years and older. Bone mineral density (BMD) was measured at the lumbar spine, hip, and distal forearm. Serum sclerostin increased with age (unadjusted r = 0.30, p < 0.001). After adjustment for age, weight, and bioavailable 17β-estradiol, serum sclerostin correlated positively with BMD (r = 0.24 to 0.35, p < 0.001) and negatively with the levels of bone turnover markers (r = - 0.09 to - 0.23, p < 0.05 to 0.001). During a 10-year follow-up, 75 men sustained fragility fractures. Fracture risk was lower in the two upper quintiles of sclerostin combined versus three lower quintiles combined (6.1 versus 13.5%, p < 0.01). We compared fracture risk in the two highest quintiles combined versus three lower quintiles combined using the Cox model adjusted for age, weight, leisure physical activity, BMD, bone width (tubular bones), prevalent fracture, prevalent falls, ischemic heart disease, and severe abdominal aortic calcification. Men with higher sclerostin concentration had lower fracture risk (adjusted for hip BMD, hazard ratio [HR] = 0.55, 95% confidence interval [CI] 0.31 to 0.96, p < 0.05). The results were similar in 47 men with major fragility fractures (adjusted for lumbar spine BMD: HR = 0.39, 95% CI 0.17 to 0.90, p < 0.05). Men who had higher sclerostin and higher BMD (two highest quintiles) had lower risk of fracture compared with men who had lower BMD and lower sclerostin levels (three lower quintiles) (HR = 0.24, 95% CI 0.10 to 0.62, p < 0.005). Circulating sclerostin was not associated with mortality rate or the incidence of major cardiovascular events. Thus, in older men, higher serum sclerostin levels are associated with lower risk of fracture, higher BMD, and lower bone turnover rate., (Copyright © 2013 American Society for Bone and Mineral Research.)

Published
2013
Full Text
View/download PDF

40. Cathepsin K preferentially solubilizes matured bone matrix.

Author

Borel O, Gineyts E, Bertholon C, and Garnero P

Subjects
Amino Acids metabolism, Animals, Arginine analogs & derivatives, Arginine metabolism, Bone Density, Cattle, Collagen metabolism, Collagen Type I metabolism, Humans, Isomerism, Lysine analogs & derivatives, Lysine metabolism, Peptides metabolism, Bone Matrix metabolism, Cathepsin K metabolism
Abstract

Bone collagen undergoes a series of enzymatic and nonenzymatic posttranslational modifications with maturation. The aim of this study was to analyze the collagenolytic efficiency of cathepsin K in relation to the extent of bone collagen age. Bone collagen posttranslational maturation was induced in vitro by preincubating bovine fetal cortical bone specimens at 37 °C for different times. The collagen enzymatic cross-links pyridinoline (PYD) and deoxypyridinoline (DPD), the advanced glycation end product pentosidine (PEN), and the native (α) and β-isomerized C-telopeptide (CTX) isomers were measured in each bone specimen. After extraction, bone collagen was incubated with human recombinant cathepsin K at different concentrations and its collagenolytic activity was measured by the release of hydroxyproline. To assess the affinity of cathepsin K for isomerized and nonisomerized CTX isomers, incubation with cathepsin K was also performed in the presence of various concentrations of a specific inhibitor. We showed that preincubation of bone collagen at 37 °C induces a marked increase in the bone concentration of PYD, DPD, and PEN and of CTX isomerization as reflected by the ratio of α-/βCTX. This increase was associated with a parallel increase in the efficiency of cathepsin K to solubilize bone collagen. When cathepsin K was incubated in the presence of an inhibitor, the β-isomerized form of collagen from 3-month- and 8-year-old bovine bone was more susceptible to degradation than the native α form. These results suggest that the collagenolytic activity of cathepsin K may be increased toward more matured bone collagen.

Published
2012
Full Text
View/download PDF

41. Extracellular post-translational modifications of collagen are major determinants of biomechanical properties of fetal bovine cortical bone.

Author

Garnero P, Borel O, Gineyts E, Duboeuf F, Solberg H, Bouxsein ML, Christiansen C, and Delmas PD

Subjects
Absorptiometry, Photon, Animals, Biomechanical Phenomena, Bone Density, Bone and Bones metabolism, Cattle, Collagen Type I analysis, Femur embryology, Femur metabolism, In Vitro Techniques, Isomerism, Microscopy, Polarization, Minerals metabolism, Peptides, Temperature, Time Factors, Bone and Bones embryology, Collagen Type I metabolism, Extracellular Matrix metabolism, Protein Processing, Post-Translational
Abstract

Mechanical behavior of bone depends on its mass and architecture, and on the material properties of the matrix, which is composed of a mineral phase and an organic component mainly constituted of type I collagen. Mineral accounts largely for the stiffness of bone, whereas type I collagen provides bone its ductility and toughness, i.e., its ability to undergo deformation and absorb energy after it begins to yield. The molecular mechanisms underlying the effect of alterations in type I collagen on bone mechanical properties are unclear. We used an in vitro model of fetal bovine cortical bone specimens (n = 44), where the extent of type I collagen cross-linking was modified by incubation at 37 degrees C for 0, 60, 90 and 120 days, keeping constant the architecture and the mineral content. At each incubation time, the following parameters were determined: (1) the bone concentration of enzymatic (pyridinoline; PYD and deoxypyridinoline, DPD) and non-enzymatic (pentosidine) crosslinks by HPLC, (2) the extent of aspartic acid isomerization of the type I collagen C-telopeptide (CTX) by ELISA of native (alpha CTX) and isomerized (beta CTX) forms, (3) the mineral density by DXA, (4) the porosity by micro-computed tomography and (5) the bending and compressive mechanical properties. Incubation of bone specimens at 37 degrees C for 60 days increased the level (per molecule of collagen) of PYD (+98%, P = 0.005), DPD (+42%, P = 0.013), pentosidine (+55-fold, P = 0.005), and the degree of type I collagen C-telopeptide isomerization (+4.9-fold, P = 0.005). These biochemical changes of collagen were associated with a 30% decrease in bending and compressive yield stress and a 2.5-fold increase in compressive post-yield energy absorption (P < 0.02 for all), with no significant change of bone stiffness. In multivariate analyses, the level of collagen cross-linking was associated with yield stress and post-yield energy absorption independently of bone mineral density, explaining up to 25% of their variance. We conclude that the extent and nature of collagen cross-linking contribute to the mechanical properties of fetal bovine cortical bone independently of bone mineral density.

Published
2006
Full Text
View/download PDF

42. Evaluation of a fully automated serum assay for C-terminal cross-linking telopeptide of type I collagen in osteoporosis.

Author

Garnero P, Borel O, and Delmas PD

Subjects
Adult, Aged, Aged, 80 and over, Autoanalysis, Collagen Type I, Enzyme-Linked Immunosorbent Assay, Female, Fractures, Bone diagnosis, Humans, Middle Aged, Osteoporosis, Postmenopausal blood, Postmenopause, Predictive Value of Tests, Premenopause, Prospective Studies, Collagen blood, Osteoporosis blood, Peptides blood
Abstract

Background: Biochemical markers of bone turnover can provide prognostic information about the risk of osteoporotic fracture and are useful tools for monitoring efficacy of antiresorptive therapy. A serum-based automated assay may be of better clinical value than urinary markers because of lower imprecision and day-to-day within-person variability. Our aim was to evaluate the technical and clinical performances of a new, fully automated assay for serum C-terminal cross-linking telopeptide of type I collagen (CTX), a marker of bone resorption., Methods: Serum CTX was measured on the Elecsys 2010 automated analyzer (Roche). Results were compared with those of the manual ELISA. We measured serum CTX concentrations in 728 healthy women, ages 31-89 years. We investigated the ability of this assay to predict the rate of postmenopausal forearm bone loss evaluated by four repeated bone mineral density measurements using dual-x-ray absorptiometry in 305 women followed prospectively for 4 years. Finally, in a cohort of healthy, untreated, postmenopausal women, we compared baseline serum CTX in 55 women who subsequently had a fracture (20 vertebral and 35 peripheral fractures) with values in the 380 women who did not fracture during a mean 5 years of follow-up., Results: The within- (n = 21) and between-run (n = 21) CVs were <4.1% and 5.7%, respectively. In 728 healthy women, serum CTX concentrations (automated) correlated with those of the manual ELISA (r = 0.82; P<0.0001). The median long-term within-person variability assessed by four repeated measurements over 3 months in 18 postmenopausal women was 9.4%. Compared with 254 premenopausal women, serum CTX was 39% (P<0.0001) higher in 45 perimenopausal women and 86% (P<0.0001) higher in 429 postmenopausal women (mean age, 64 years). Baseline serum CTX correlated negatively with changes of bone mass measured at the mid (r = -0.23; P<0.0001) and distal (r = -0.27; P<0001) radius. Postmenopausal women with serum CTX greater than the mean + 2 SD values in premenopausal women accounted for 42% of the population, lost bone at the mid radius on average eightfold more rapidly than the other women (-0.27% +/- 2.92% vs. -2.25% +/- 3.95%; P<0.0001), and had increased risk of fracture with a relative risk (95% confidence interval) of 1.8 (1.01-3.1) after adjustment for physical activity., Conclusions: The automated assay for serum CTX is precise and predicts rate of bone loss and fracture risk in postmenopausal women. Because it is convenient to use and has high throughput, this serum bone resorption marker may be useful for the investigation of patients with osteoporosis.

Published
2001

43. Racemization and isomerization of type I collagen C-telopeptides in human bone and soft tissues: assessment of tissue turnover.

Author

Gineyts E, Cloos PA, Borel O, Grimaud L, Delmas PD, and Garnero P

Subjects
Aged, Aged, 80 and over, Aging physiology, Amino Acids analysis, Amino Acids metabolism, Collagen chemistry, Connective Tissue chemistry, Cross-Linking Reagents chemistry, Female, Humans, Isomerism, Kinetics, Male, Middle Aged, Peptide Fragments chemistry, Bone and Bones metabolism, Collagen metabolism, Connective Tissue metabolism, Peptide Fragments metabolism
Abstract

Urinary excretion of the type I collagen C-telopeptide (CTx) has been shown to be a sensitive index of the rate of bone resorption. The human type I collagen sequence A(1209)HDGGR(1214) of CTx can undergo racemization of the aspartic acid residue Asp(1211) and isomerization of the bond between this residue and Gly(1212). These spontaneous non-enzymic chemical reactions takes place in vivo in bone, and the degree of racemization and isomerization of CTx molecules may be an index of the biological age and the remodelling of bone. The aim of the present study was to investigate the degree of racemization and isomerization of type I collagen in human connective soft tissues, in order to estimate the rate of collagen turnover in adult tissues and compare it with that of bone. We also performed a systematic evaluation of the pyridinium cross-link content in adult human tissues. Using antibodies raised against the different CTx forms, we found that bone and dermis are the tissues that show most racemization and isomerization. The type I collagen of arteries, lung, intestine, kidney, skeletal muscle and heart shows significantly less racemization and isomerization than that of bone, suggesting that these soft tissues have a faster turnover than bone. We also found that pyridinoline and, to a lesser degree, deoxypyridinoline are distributed throughout the different tissues investigated. Because bone type I collagen is characterized by a high degree of both racemization/isomerization and deoxypyridinoline cross-linking, the concomitant assessment of these two post-translational modifications is likely to result in a highly specific marker of bone resorption.

Published
2000

44. Vitamin D receptor gene polymorphisms are not related to bone turnover, rate of bone loss, and bone mass in postmenopausal women: the OFELY Study.

Author

Garnero P, Borel O, Sornay-Rendu E, Arlot ME, and Delmas PD

Subjects
Absorptiometry, Photon, Aged, Biomarkers analysis, Bone Density physiology, Calcium blood, Calcium metabolism, Female, Genotype, Humans, Middle Aged, Polymorphism, Genetic, Prospective Studies, Time Factors, Osteoporosis, Postmenopausal physiopathology, Receptors, Calcitriol genetics
Abstract

Vitamin D receptor (VDR) gene polymorphisms have been reported to account for most of the well established genetic influence on bone mineral density (BMD). However, discordant studies have been published and it is still not clear whether VDR genotypes influence bone mass accretion and/or postmenopausal bone loss. In this study, we analyzed VDR gene polymorphisms, i.e., that of BsmI, ApaI, and TaqI restriction enzymes in 268 untreated postmenopausal women 1-26 years postmenopausal. There were 37 BBAA homozygote (absence of BsmI and ApaI restriction sites on both alleles), 55 bbaa homozygote (presence of restriction sites on both alleles), and 176 heterozygotes. At baseline, women between the three genotypes did not differ significantly in age, years since menopause, body mass index (BMI), nor dietary calcium intake. We found no relationship between VDR genotypes and bone turnover assessed by three serum markers of bone formation and three urinary bone resorption markers, nor with BMD measured at the spine, hip, forearm, and whole body by dual-energy X-ray absorptiometry (DXA). Rates of bone loss assessed by repeated DXA measurements over 2 years were highly significant (p = 0.02-0.0001) at all skeletal sites except for the lumbar spine but did not differ between genotypes at any sites either before or after adjustment for potential confounding factors such as years since menopause, BMI, calcium intake, serum 25 hydroxyvitamin D levels, and baseline BMD. When we restricted the analysis to early postmenopausal women, within 10 years of menopause (n = 128), lumbar spine bone loss became significant, but no significant difference between VDR genotypes in the rate of bone loss measured at any site was found. We conclude that VDR genotypes are not predictive of bone turnover, rate of postmenopausal bone loss, and bone mass in either early or late postmenopausal women. In a subgroup of women with a low calcium intake (below 600 mg/day), we also found no significant differences between genotypes in BMD and the rate of bone loss measured at any site, although the sample size (n = 64) may be too small to detect small differences. In conclusion, these data, along with the absence of relationships between VDR gene polymorphisms and peak bone mass that we recently reported, suggest that the determination of VDR genotypes is probably not a useful clinical test for the risk assessment of osteoporosis.

Published
1996
Full Text
View/download PDF

45. Vitamin D receptor gene polymorphisms do not predict bone turnover and bone mass in healthy premenopausal women.

Author

Garnero P, Borel O, Sornay-Rendu E, and Delmas PD

Subjects
Adult, Female, Genotype, Humans, Middle Aged, Prognosis, Prospective Studies, Reference Values, Bone Density genetics, Bone Resorption genetics, Polymorphism, Genetic, Premenopause metabolism, Receptors, Calcitriol genetics
Abstract

Bone mineral density (BMD) is under strong genetic control. Polymorphisms at the vitamin D receptor (VDR) gene have been recently suggested to account for up to 75% of this genetic effect. We analyzed these polymorphisms, i.e., that of BsmI, TaqI, and ApaI restriction enzymes by PCR of the DNA in 189 healthy premenopausal women aged 31 to 57 years. For the BsmI polymorphism they were 17% BB homozygotes, 51% Bb heterozygotes, and 32% bb homozygotes, genotype frequencies that are very similar to those previously reported in other Caucasian populations of north European ancestry. Women in the three genotypes for any of the three polymorphisms were matched for age and did not differ in body weight, height, physical activity, nor smoking habits. We found no relationship between the genotype for any of the three polymorphisms nor bone formation and resorption rate assessed by five specific biochemical markers of bone turnover nor with BMD measured at the spine, proximal femur, forearm, and whole body by dual-energy X-ray absorptiometry (DXA). We concluded that these polymorphisms are not predictive of bone turnover nor BMD in a sample of healthy premenopausal women drawn from the French population.

Published
1995
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results