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3 results on '"hypoxia response"'

1. MafG controls the hypoxic response of cells by accumulating HIF-1α in the nuclei

Author

Ueda, Koji, Xu, Jing, Morimoto, Haruka, Kawabe, Atsumi, and Imaoka, Susumu

Subjects
*HYPOXEMIA, *PROTEINS, *CELL nuclei, *SURFACE plasmon resonance
Abstract

Abstract: We identified MafG as a protein that interacts with HIF-1α, a key factor in hypoxic response, using the yeast two-hybrid system. Interaction between MafG and HIF-1α was confirmed by surface plasmon resonance and by translocation to the nucleolus with the NoLS signal. A knockdown of MafG reduced erythropoietin (EPO) mRNA levels as well as luciferase reporter activity with the hypoxia response element. The knockdown of MafG did not change total HIF-1α protein, but reduced the accumulation of HIF-1α in the nuclei. These results suggest that MafG regulates the hypoxic response of cells by detaining HIF-1α in the nuclei. Structured summary: MINT-6550898: HIF1A (uniprotkb:Q16665) physically interacts (MI:0218) with MAFG (uniprotkb:Q9BRP3) by two hybrid (MI:0018) MINT-6550966: HIF1A (uniprotkb:Q16665) physically interacts (MI:0218) with HSP90 alpha (uniprotkb:P07900) by surface plasmon resonance (MI:0107) MINT-6550948: HIF1A (uniprotkb:Q16665) physically interacts (MI:0218) with MAFK (uniprotkb:A5PLQ5) by surface plasmon resonance (MI:0107) MINT-6550925: HIF1A (uniprotkb:Q16665) physically interacts (MI:0218) with MAFG (uniprotkb:Q9BRP3) by surface plasmon resonance (MI:0107) MINT-6550912: MAFG (uniprotkb:Q9BRP3) and HIF1A (uniprotkb:Q16665) physically interact (MI:0218) by fluorescence microscopy (MI:0416) MINT-6550980: HIF1A (uniprotkb:Q16665) physically interacts (MI:0218) with HSP90 beta (uniprotkb:P08238) by surface plasmon resonance (MI:0107) [Copyright &y& Elsevier]

Published
2008
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2. MafG controls the hypoxic response of cells by accumulating HIF-1α in the nuclei

Author

Haruka Morimoto, Atsumi Kawabe, Susumu Imaoka, Koji Ueda, and Jing Xu

Subjects
MafG Transcription Factor, Aryl hydrocarbon receptor nuclear translocator, Nucleolus, Biophysics, HIF-1α, Repressor, Biology, Biochemistry, Nrf2, Genes, Reporter, Structural Biology, RNA interference, Cell Line, Tumor, Two-Hybrid System Techniques, Genetics, medicine, Humans, Molecular Biology, Hypoxia response, Cell Nucleus, Gene knockdown, MafG, Cell Biology, Hypoxia-Inducible Factor 1, alpha Subunit, Molecular biology, Cell Hypoxia, Repressor Proteins, Cell nucleus, medicine.anatomical_structure, Cell culture, RNA Interference
Abstract

We identified MafG as a protein that interacts with HIF-1α, a key factor in hypoxic response, using the yeast two-hybrid system. Interaction between MafG and HIF-1α was confirmed by surface plasmon resonance and by translocation to the nucleolus with the NoLS signal. A knockdown of MafG reduced erythropoietin (EPO) mRNA levels as well as luciferase reporter activity with the hypoxia response element. The knockdown of MafG did not change total HIF-1α protein, but reduced the accumulation of HIF-1α in the nuclei. These results suggest that MafG regulates the hypoxic response of cells by detaining HIF-1α in the nuclei.Structured summaryMINT-6550898:HIF1A (uniprotkb:Q16665) physically interacts (MI:0218) with MAFG (uniprotkb:Q9BRP3) by two hybrid (MI:0018)MINT-6550966:HIF1A (uniprotkb:Q16665) physically interacts (MI:0218) with HSP90 alpha (uniprotkb:P07900) by surface plasmon resonance (MI:0107)MINT-6550948:HIF1A (uniprotkb:Q16665) physically interacts (MI:0218) with MAFK (uniprotkb:A5PLQ5) by surface plasmon resonance (MI:0107)MINT-6550925:HIF1A (uniprotkb:Q16665) physically interacts (MI:0218) with MAFG (uniprotkb:Q9BRP3) by surface plasmon resonance (MI:0107)MINT-6550912:MAFG (uniprotkb:Q9BRP3) and HIF1A (uniprotkb:Q16665) physically interact (MI:0218) by fluorescence microscopy (MI:0416)MINT-6550980:HIF1A (uniprotkb:Q16665) physically interacts (MI:0218) with HSP90 beta (uniprotkb:P08238) by surface plasmon resonance (MI:0107)

Published
2008

3. Hypoxia-induced miR-497 decreases glioma cell sensitivity to TMZ by inhibiting apoptosis

Author

Yajun Xue, Huairui Chen, Cong Han, Zhijian Wu, Sanhu Zhao, Jun Fang, Meiqing Lou, and Jin Lan

Subjects
Transcriptional Activation, Transcription, Genetic, Cell Survival, medicine.medical_treatment, Biophysics, Apoptosis, Drug resistance, Glioma cell, Response Elements, miR-497, Biochemistry, law.invention, Hypoxia response, Structural Biology, law, Cell Line, Tumor, Glioma, Temozolomide, Genetics, medicine, Humans, Antineoplastic Agents, Alkylating, Molecular Biology, Chemotherapy, Binding Sites, Base Sequence, PDCD4, Brain Neoplasms, Chemistry, RNA-Binding Proteins, Cell Biology, Hypoxia (medical), Hypoxia-Inducible Factor 1, alpha Subunit, medicine.disease, Cell Hypoxia, Dacarbazine, Gene Expression Regulation, Neoplastic, MicroRNAs, HEK293 Cells, Drug Resistance, Neoplasm, Cancer research, Suppressor, RNA Interference, Drug Screening Assays, Antitumor, medicine.symptom, Apoptosis Regulatory Proteins
Abstract

Understanding the resistance of glioma cells to chemotherapy has been an enormous challenge. In particular, mechanisms by which tumor cells acquire resistance to chemotherapy under hypoxic conditions are not fully understood. In this study, we have found that miR-497 is overexpressed in glioma and that hypoxia can induce the expression of miR-497 at the transcriptional level by binding with the hypoxia response element in the promoter. Ectopic overexpression of miR-497 promotes chemotherapy resistance in glioma cells by targeting PDCD4, a tumor suppressor that is involved in apoptosis. In contrast, the inhibition of miR-497 enhances apoptosis and increases the sensitivity of glioma cells to TMZ. These results suggest that miR-497 is a potential molecular target for glioma therapy.

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