TAILIEUCHUNG - Báo cáo khoa học: Inhibitor of nuclear factor-kappaB alpha derepresses hypoxia-inducible factor-1 during moderate hypoxia by sequestering factor inhibiting hypoxia-inducible factor from hypoxia-inducible factor 1a

Hypoxia and inflammation often develop concurrently in numerous diseases, and both hypoxia-inducible factor (HIF)-1aand nuclear factor-kappaB (NF-jB) are key transcription factors of stress response genes. An NF-jB inhibitor, inhibitor of NF-jBa(IjBa), was found to interact with factor inhibiting HIF (FIH) and to be hydroxylated by FIH. | Inhibitor of nuclear factor-kappaB alpha derepresses hypoxia-inducible factor-1 during moderate hypoxia by sequestering factor inhibiting hypoxia-inducible factor from hypoxia-inducible factor 1a Dong Hoon Shin1 z Shan Hua Li1 Seung-Won Yang1 Byung Lan Lee2 Myung Kyu Lee3 and Jong-Wan Park1 1 Department of Pharmacology Ischemic Hypoxic Disease Institute SeoulNationalUniversity College of Medicine Korea 2 Department of Anatomy Ischemic Hypoxic Disease Institute SeoulNationalUniversity College of Medicine Korea 3 Omics and Integration Research Center KRIBB Yuseong Daejeon Korea Keywords factor inhibiting hypoxia-inducible factor FIH hypoxia-inducible factor-1 HIF-1 IkB nuclear factor-kappaB NF-kB protein interaction Correspondence . Park Department of Pharmacology SeoulNationalUniversity College of Medicine Seoul Korea Fax 82 2 7457996 Tel 82 2 7408289 E-mail parkjw@ These authors contributed equally to this work Received 11 January 2009 revised 17 March 2009 accepted 21 April 2009 doi Hypoxia and inflammation often develop concurrently in numerous diseases and both hypoxia-inducible factor HIF -la and nuclear factor-kappaB NF-kB are key transcription factors of stress response genes. An NF-kB inhibitor inhibitor of NF-KBa IkBm was found to interact with factor inhibiting HIF FIH and to be hydroxylated by FIH. However FIH did not functionally regulate IkBm and the consequence of the FIH-IkBm interaction thus remains uncertain. In the present study we tested the possibility that IkBm regulates FIH. FIH-IkBm binding was confirmed by yeast two-hybrid and coimmunoprecipitation analyses. Functionally IkBm expression further enhanced the transcriptional activity of HIF-1a under hypoxic conditions. Furthermore IkBm knockdown repressed HIF-1a activity. Mechanistically IkBm derepressed HIF-1a activity by inhibiting the FIH-mediated Asn803 hydroxylation of HIF-1a. It was also found that IkBm activated HIF-1a by sequestering FIH .

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