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Multicellular organisms contain a variety of structurally and functionally distinct cell types, but the DNA in all the cells originated from the same parent cells. The differences in the cells can be attributed to the differential gene expression. Liver cells, whose functions include detoxification of blood, production of bile to metabolize fats, and synthesis of proteins essential for metabolism, must express a specific set of genes to perform their functions. Gene expression also varies with...
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Hemin induces neuroglobin expression in neural cells.

Yonghua Zhu1, Yunjuan Sun, Kunlin Jin

  • 1Buck Institute for Age Research, Novato, CA 94945, USA.

Blood
|September 20, 2002
PubMed
Summary

Neuroglobin, a brain protein, is induced by hemin, a molecule similar to those in hemoglobin. This process involves specific signaling pathways, distinct from how hypoxia affects neuroglobin.

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Biochemistry

Background:

  • Neuroglobin is a recently discovered vertebrate globin found in cerebral neurons.
  • Neuronal neuroglobin expression is upregulated by hypoxia and ischemia, offering neuroprotection.
  • Hemoglobin and myoglobin, like neuroglobin, can have their expression induced.

Purpose of the Study:

  • To investigate the induction of neuroglobin expression by hemin.
  • To elucidate the signaling pathways involved in hemin-mediated neuroglobin induction.
  • To compare the mechanisms of hemin and hypoxia in regulating neuroglobin expression.

Main Methods:

  • Neuroglobin mRNA and protein levels were measured following hemin treatment.
  • The effects of protein kinase G and soluble guanylate cyclase inhibitors (KT5823, LY83583) were assessed.

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  • The impact of 8-bromo-cyclic guanosine 3',5'-monophosphate and PD98059 on neuroglobin expression was evaluated.

    • Main Results:

    • Hemin induced neuroglobin expression in a concentration- and time-dependent manner, peaking at 50 microM hemin and 8-24 hours.
    • Hemin-induced neuroglobin expression was mediated by protein kinase G and soluble guanylate cyclase, evidenced by inhibitor effects and increased cGMP levels.
    • Hypoxic induction of neuroglobin was blocked by PD98059, indicating a different regulatory pathway than hemin.

    Conclusions:

    • Hemin induces neuroglobin expression through a pathway involving protein kinase G and soluble guanylate cyclase.
    • Hypoxia and hemin utilize distinct signal transduction pathways to regulate neuroglobin expression.
    • Neuroglobin expression is controlled by at least two different signaling mechanisms.