TAILIEUCHUNG - Báo cáo khoa học: Expression and function of Noxo1c, an alternative splicing form of the NADPH oxidase organizer 1

Activation of the superoxide-producing NADPH oxidase Nox1 requires both the organizer protein Noxo1 and the activator protein Noxa1. Here we describe an alternative splicing form of Noxo1, Noxo1c, which is expressed in the testis and fetal brain. | ỊFEBS Journal Expression and function of Noxo1y an alternative splicing form of the NADPH oxidase organizer 1 Ryu Takeya1 2 Masahiko Taura1 Tomoko Yamasaki1 Seiji Naito3 and Hideki Sumimoto1 2 1 Medical institute of Bioregulation Kyushu University Fukuoka Japan 2 CREST Japan Science and Technology Agency Saitama Japan 3 Department of Urology Kyushu University Graduate Schoolof MedicalSciences Fukuoka Japan Keywords NADPH oxidase Nox1 Nox organiser 1 Noxo1 PX domain phosphoinositide Correspondence H. Sumimoto Medical institute of Bioregulation Kyushu University Fukuoka 812-8582 Japan Fax 81 92 642 6807 Tel 81 92 642 6806 E-mail hsumi@ Received 31 May 2006 accepted 12 June 2006 doi Activation of the superoxide-producing NADPH oxidase Nox1 requires both the organizer protein Noxo1 and the activator protein Noxa1. Here we describe an alternative splicing form of Noxo1 Noxo1y which is expressed in the testis and fetal brain. The Noxo1y protein contains an additional five amino acids in the N-terminal PX domain a phosphoinositide-binding module the domain plays an essential role in supporting superoxide production by NADPH oxidase Nox family oxidases including Nox1 gp91phox Nox2 and Nox3 as shown in this study. The PX domain isolated from Noxo1y shows a lower affinity for phosphoinositides than that from the classical splicing form Noxo1p. Consistent with this in resting cells Noxo1y is poorly localized to the membrane and thus less effective in activating Nox1 than Noxo1p which is constitutively present at the membrane. On the other hand cell stimulation with phorbol 12-myristate 13-acetate PMA an activator of Nox1-3 facilitates membrane translocation of Noxo1y as a result Noxo1y is equivalent to Noxo1p in Nox1 activation in PMA-stimulated cells. The effect of the five-amino-acid insertion in the Noxo1 PX domain appears to depend on the type of Nox in activation of gp91phox Nox2 Noxo1y is less active than Noxo1p even

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