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, , 2013.
Il a été précédemment montré au sein de notre équipe que la GalT-I (?4GalT7) transfère de manière efficace le galactose sur le xylose non modifié, par contre ce transfert est totalement inhibé quand le xylose est phosphorylé en position 2-O, 2005. ,
Ben) phosphorylé, alors qu'il est incapable de transférer le galactose sur le disaccharide ,
, , 2014.
Cependant, d'autres travaux ont montré que les souris invalidées pour le gène de la EXTL2 produisent plus de GAGs comparées aux souris sauvages, la phosphorylation du xylose régulerait la biosynthèse des PGs à HS, 1968. ,
, Les différentes lignées cellulaires (PgsA-745, PgsB-618, CHO-KI, HEK-293
La région codante de chaque gène est excisée et liguée dans le vecteur d'expression. Les vecteurs d'expression utilisés sont pCMV, pcDNA, pEGFP. Le d'ExGen500 (Euromedex). La XT-I, la XT-II et leurs mutants sont transfectés de façon stable dans les cellules CHO-PgsA-745. Le shRNA-Fam20B est également transfecté de manière stable dans les cellules HEK-293. Dans le cas de la transfection stable, les cellules sont la fois l'activité du rapporteur (CAGA)12-Lux et la Renilla Luciferase ,
, Par la suite, les cellules ont été rincées avec du PBS et fixées avec 4% de paraformaldéhyde. Les cellules sont perméabilisées avec 0,1% de Triton-X100 et bloquées avec 0,2% de gélatine et hybridées avec l'anticorps primaire pendant 20 minutes, Après plusieurs lavages, les cellules sont hybridées avec l'anticorps secondaire et les noyaux sont colorés avec du colorant de Hoechst. Enfin, les lamelles sont montées sur lames dans du Moviol
, Buts et objectifs Les principaux objectifs de cette étude sont
, Golgi, cependant la localisation des XTs est encore controversée, en particulier celle de la XT-I
, Nous avons étudié la localisation subcellulaire de la XT-I et la XT-II et avons montré que les deux isoformes présentent des localisations différentes. En effet, la XT-I est co-localisée avec le marqueur du RE, la calnexine et la XT-II est co-localisée avec un marqueur du cis-Golgi
, Cependant, l'efficacité d'initiation de la synthèse par la XT-I semble être réduite par rapport à celle de la XT-II. De façon intéressante, nous avons montré que les chaînes de GAGs amorcées par la XT-I sont de tailles plus longues, comparées à celles initiées par la XTla taille des chaînes de GAGs dans les cellules exprimant la XT-I, alors qu'il est sans effet sur les chaînes initiées par la XT-II. Nous avons ensuite montré que la XT-II est clivée par la ?-sécrétase et sécrétée dans le milieu extracellulaire, contrairement à la XT-I, En utilisant la décorine et le syndécane 4 comme protéines rapporteurs des PGs à CS et HS, respectivement, nous avons montré que la XT-I et la XT-II sont capables d'initier la synthèse des deux types de PGs
, Tous les mutants XT-I étudiés sont localisés dans le RE, mais la synthèse de GAG est moins importante comparée à l'enzyme sauvage. La XT-II et ses mutants sont sécrétés dans la MEC. Cependant, deux mutants de la XT-II sont localisés dans le RE et sont inactifs et ne sont pas sécrétés. Les souris XT-II/KO sont viables et présentent une polykystose principalement dans le foie et dans une moindre mesure dans les reins. Cependant, les souris XT-I/KO n'ont pas encore été décrites, Nous avons montré dans un premier temps que la XT-I est localisée dans le RE alors que la XT-II est localisée dans le Golgi et que les chaînes de GAG initiées par les deux isoformes sont différentes
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