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

被引：131

作者：

DWYER, BE

NISHIMURA, RN

LU, SY

机构：

[1] DEPT VET AFFAIRS MED CTR,MOLEC NEUROBIOL LAB,SEPULVEDA,CA 91343

[2] DEPT VET AFFAIRS MED CTR,INVITRO REMYELINAT LAB,SEPULVEDA,CA 91343

[3] UNIV CALIF LOS ANGELES,SCH MED,DEPT NEUROL,LOS ANGELES,CA 90024

[4] UNIV CALIF LOS ANGELES,SCH MED,BRAIN RES INST,LOS ANGELES,CA 90024

来源：

MOLECULAR BRAIN RESEARCH | 1995年 / 30卷 / 01期

关键词：

HEME OXYGENASE; NEURON; NEURONAL INJURY; ASTROCYTE; OXIDATIVE INJURY; STRESS PROTEIN; HEAT SHOCK PROTEIN;

D O I：

10.1016/0169-328X(94)00273-H

中图分类号：

Q189 [神经科学];

学科分类号：

071006 ;

摘要：

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.

引用

页码：37 / 47

页数：11

共 47 条

[1] Chomczynski, Sacchi, Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction, Anal. Biochem., 162, pp. 156-159, (1987)
[2] Cohen, Catalase, glutathione peroxidase, superoxide dismutase, and cytochrome P-450, Handbook of Neurochemistry, 4, pp. 315-330, (1983)
[3] Cole, de Vellis, Preparation of astrocyte and oligodendrocyte cultures from primary rat glial cultures, A Dissection Manual of the Nervous System, pp. 121-133, (1989)
[4] Dwyer, Nishimura, Heat shock proteins in hypoxic-ischemic brain injury: a perspective, Brain Pathol., 2, pp. 245-251, (1992)
[5] Dwyer, Nishimura, Heat shock proteins and neuroprotection in CNS culture, Heat Shock or Cell Stress Proteins and the Nervous System, pp. 99-121, (1994)
[6] Dwyer, Nishimura, de Vellis, Clegg, Regulation of heat shock protein synthesis in rat astrocytes, J. Neurosci. Res., 28, pp. 352-358, (1991)
[7] Dwyer, Nishimura, de Vellis, Yoshida, Heme oxygenase is a heat shock protein and PEST protein in rat astroglial cells, Glia, 5, pp. 300-305, (1992)
[8] Dwyer, Nishimura, Lu, Heme oxygenase in traumatic brain injury, Soc. Neurosci. Abstr., 20, (1994)
[9] Ewing, Maines, In situ hybridization and immunohistochemical localization of heme oxygenase-2 mRNA and protein in normal rat brain: differential distribution of isozyme 1 and 2, Mol. Cell. Neurosci., 3, pp. 559-570, (1992)
[10] Ewing, Maines, Glutathione depletion induces heme oxygenase-1 (HSP-32)mRNA and protein in rat brain, J. Neurochem., 60, pp. 1512-1519, (1993)

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