Differential expression of heme oxygenase-1 in cultured cortical neurons and astrocytes determined by the aid of a new heme oxygenase antibody. Response to oxidative stress

Heme oxygenase exists as two isoenzymes designated heme oxygenase-1 (HO-1)and heme oxygenase-2 (HO-2). HO-2 is made constitutively in many cell types whereas HO-1 is a stress protein inducible by heat, heavy metals, ultraviolet irradiation, and oxidative stress. Recombinant rat HO-1 was expressed in...

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Published in:Brain research. Molecular brain research. 1995-05, Vol.30 (1), p.37-47
Main Authors: Dwyer, Barney E., Nishimura, Robert N., Lu, Shi-Yi
Format: Article
Language:English
Subjects:
Antibodies - immunology
Astrocyte
Astrocytes - enzymology
Astrocytes - metabolism
Autoradiography
Biological and medical sciences
Blotting, Western
Cells, Cultured
Electrophoresis
Fundamental and applied biological sciences. Psychology
Heat shock protein
Heme oxygenase
Heme Oxygenase (Decyclizing) - biosynthesis
Heme Oxygenase (Decyclizing) - genetics
Immunohistochemistry
Isolated neuron and nerve. Neuroglia
Neuron
Neuronal injury
Neurons - enzymology
Neurons - metabolism
Oxidative injury
Oxidative Stress - physiology
Polymerase Chain Reaction
Recombinant Proteins
Stress protein
Vertebrates: nervous system and sense organs
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Summary:Heme oxygenase exists as two isoenzymes designated heme oxygenase-1 (HO-1)and heme oxygenase-2 (HO-2). HO-2 is made constitutively in many cell types whereas HO-1 is a stress protein inducible by heat, heavy metals, ultraviolet irradiation, and oxidative stress. Recombinant rat HO-1 was expressed in bacteria and antiserum designated HO-1713 was raised against the purified protein. HO-1713 detected recombinant rat HO-1 and recombinant rat HO-2. In rat tissues it detected HO-1 and a second, unidentified band designated HO-L (heme oxygenase-like immunoreactivity)which was not HO-2. Cultured rat cortical neurons and forebrain astrocytes were exposed to hydrogen peroxide (0.14-0.7 micromolar for 30 or 60 min). Neurons which contained little detectable HO-1 and which were sensitive to hydrogen peroxide at the high end of the dose curve failed to induce HO-1 by Western blot analysis. In contrast, cultured rat forebrain astrocytes which contained HO-1 under normal culture conditions and which were resistant to injury by hydrogen peroxide, increased their content of immunoreactive HO-1 by 7-fold within 3 h after exposure. Our results support a protective role for HO-1 in oxidative injury and suggest that the relative inability of neurons to increase HO-1 after oxidative stress may contribute to their selective vulnerability vis-a-vis astrocytes. They also suggest that differential expression of heme oxygenase in studies utilizing CNS cultures may alter normal cell physiology and cell survival.
ISSN:0169-328X
1872-6941
DOI:10.1016/0169-328X(94)00273-H