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Visualization of the three-dimensional organization of hypoxia-inducible factor-1α and interacting cofactors in subnuclear structures

  • U. Berchner-Pfannschmidt , C. Wotzlaw , E. Merten , H. Acker and J. Fandrey
Published/Copyright: June 1, 2005
Biological Chemistry
From the journal Volume 385 Issue 3-4

Abstract

Cells need oxygen (O2) to meet their metabolic demands. Highly efficient systems of O2-sensing have evolved to initiate responses enabling cells to adapt their metabolism to reduced O2 availability. Of central importance is the activation of hypoxiainducible factor-1 (HIF-1), a transcription factor complex that controls the expression of genes the products of which regulate glucose uptake and metabolism, vasotonus and angiogenesis, oxygen capacity of the blood as well as cell growth and death. Activation of HIF-1 requires the accumulation and nuclear translocation of the HIF-1α subunit, its dimerization with HIF-1β and the binding of coactivator proteins such as p300. In this study we investigated the threedimensional (3D) distribution of HIF-1α within the nucleus and assigned its localization to known nuclear compartments. Using twophoton microscopy we determined the colocalization of HIF-1α and -β subunits within nuclear domains as well as overlaps between HIF-1α and p300. Our data provide information on the nuclear distribution of HIF-1α with respect to subnuclear domains that could serve as specific locations for hypoxiainduced gene expression.

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Published Online: 2005-06-01
Published in Print: 2004-04-13

Copyright © 2004 by Walter de Gruyter GmbH & Co. KG

Articles in the same Issue

  1. Oxygen and the Cell
  2. O2 sensing in the human ductus arteriosus: redox-sensitive K+ channels are regulated by mitochondria-derived hydrogen peroxide
  3. Oxidative stress in the systemic and cellular responses to intermittent hypoxia
  4. HIF hydroxylation and cellular oxygen sensing
  5. Visualization of the three-dimensional organization of hypoxia-inducible factor-1α and interacting cofactors in subnuclear structures
  6. Modulation of glucokinase expression by hypoxia-inducible factor 1 and upstream stimulatory factor 2 in primary rat hepatocytes
  7. Redox-sensitive regulation of the HIF pathway under non-hypoxic conditions in pulmonary artery smooth muscle cells
  8. Measurement of exhaled hydrogen peroxide from rabbit lungs
  9. Effects of reducing agents on glutathione metabolism and the function of carotid body chemoreceptor cells
  10. Expression of functional purinergic receptors in pulmonary neuroepithelial bodies and their role in hypoxia chemotransmission
  11. Remodelling of Ca2+ homeostasis in type I cortical astrocytes by hypoxia: evidence for association with Alzheimer's disease
  12. Simultaneous exposure of rats to dioxin and carbon monoxide reduces the xenobiotic but not the hypoxic response
  13. Structure and expression of two kininogen genes in mice
  14. The central domain of the matrix protein of HIV-1: influence on protein structure and virus infectivity
  15. Skin secretion of the toad Bombina variegata contains multiple insulin-releasing peptides including bombesin and entirely novel insulinotropic structures
  16. Inhibition of lentil copper/TPQ amine oxidase by the mechanism-based inhibitor derived from tyramine
  17. Enhanced expression of basolateral multidrug resistance protein isoforms Mrp3 and Mrp5 in rat liver by LPS
  18. Critical O2 and NO concentrations in NO-induced cell death in a rat liver sinusoidal endothelial cell line
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