Heme oxygenase-1/carbon monoxide: from basic science to therapeutic applications. Review uri icon

Overview

MeSH

  • Animals
  • Environment
  • Enzyme Induction
  • Gene Expression Regulation
  • Heme Oxygenase (Decyclizing)
  • Humans
  • Isoenzymes
  • Signal Transduction
  • Stress, Physiological

MeSH Major

  • Carbon Monoxide
  • Heme Oxygenase-1

abstract

  • The heme oxygenases, which consist of constitutive and inducible isozymes (HO-1, HO-2), catalyze the rate-limiting step in the metabolic conversion of heme to the bile pigments (i.e., biliverdin and bilirubin) and thus constitute a major intracellular source of iron and carbon monoxide (CO). In recent years, endogenously produced CO has been shown to possess intriguing signaling properties affecting numerous critical cellular functions including but not limited to inflammation, cellular proliferation, and apoptotic cell death. The era of gaseous molecules in biomedical research and human diseases initiated with the discovery that the endothelial cell-derived relaxing factor was identical to the gaseous molecule nitric oxide (NO). The discovery that endogenously produced gaseous molecules such as NO and now CO can impart potent physiological and biological effector functions truly represented a paradigm shift and unraveled new avenues of intense investigations. This review covers the molecular and biochemical characterization of HOs, with a discussion on the mechanisms of signal transduction and gene regulation that mediate the induction of HO-1 by environmental stress. Furthermore, the current understanding of the functional significance of HO shall be discussed from the perspective of each of the metabolic by-products, with a special emphasis on CO. Finally, this presentation aspires to lay a foundation for potential future clinical applications of these systems.

publication date

  • April 2006

has subject area

  • Animals
  • Carbon Monoxide
  • Environment
  • Enzyme Induction
  • Gene Expression Regulation
  • Heme Oxygenase (Decyclizing)
  • Heme Oxygenase-1
  • Humans
  • Isoenzymes
  • Signal Transduction
  • Stress, Physiological

Research

keywords

  • Journal Article
  • Review

Identity

Language

  • eng

Digital Object Identifier (DOI)

  • 10.1152/physrev.00011.2005

PubMed ID

  • 16601269

Additional Document Info

start page

  • 583

end page

  • 650

volume

  • 86

number

  • 2