Immunocytochemical localization of manganese superoxide dismutase (Mn-SOD) in the hippocampus of the rat

Akai, Fumiharu; Maeda, Masayuki; Suzuki, Keiichiro; Inagaki, Shinobu; Takagi, Hiroshi; Taniguchi, Naoyuki

doi:10.1016/0304-3940(90)90510-g

Cited by 51 publications

(28 citation statements)

References 14 publications

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“…Unfortunately, complete maps of other enzyme systems involved in these processes are presently not available, since immunohistochemical studies on these enzymes have focused on restricted brain regions (37)(38)(39).…”

Section: Functional' Consideration^mentioning

confidence: 99%

Immunocytochemical localization of catalase in the central nervous system of the rat.

Moreno¹,

Mugnaini²,

Cerù³

1995

J Histochem Cytochem.

100

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Catalase is a marker for peroxisomes, which are ubiquitous cytoplasmic organelles. Although the distribution and features of peroxisomes are well known in liver and kidney, these organelles have been rarely studied in neural tissues. Catalase is an important scavenging enzyme against reactive oxygen species, as it removes H202 produced during metabolic processes. Reactive oxygen species are involved in a number of brain lesions and in brain aging. We investigated the distribution of catalase in rat central nervous system by means of a newly developed immunocytochemical procedure for signal enhancement, using an affinity-purified polyclonal antiserum. The data show that catalase immunoreactivity is present in all neural cells, both neuronal and glial, albeit at different concentrations. Among glial cells, ependymal cells and tanycytes of the third ventride and the median eminence show the most intense immunoreaction; positivity is also found in oligodendrocytes and astrocytes. In general, neurons in the brainstem are relatively more immunoreactive than those in the forebrain although, within these respective brain regions, there are areas with low and high staining intensity. Moreover, within the same area, certain types

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Section: Functional' Consideration^mentioning

confidence: 99%

Immunocytochemical localization of catalase in the central nervous system of the rat.

Moreno¹,

Mugnaini²,

Cerù³

1995

J Histochem Cytochem.

100

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“…The latter is subsequently converted to water via catalase or glutathione peroxidase, thereby effectively neutralizing the potentially damaging effects of reactive oxygen species within this vital organelle. Increased levels of MnSOD protein, mRNA, and enzymatic activity have been amply documented in the rodent central nervous sytem (CNS) as a consequence of normal aging (Vanella et al, 1982;Williams et al, 1993), ischemia (Akai et al, 1990;Liu et al, 1993;Ohtsuki et al, 1993), hyperoxia and prooxidant drug exposure . Mn-SOD expression is also reportedly augmented in the substantia nigra of subjects with idiopathic Parkinson disease (Saggu et al, 1989), Alzheimer-diseased hippocampal astrocytes (Shibata et al, 1993), the spinal cord of patients with amyotrophic lateral sclerosis (Blaauwgeers et al, 1996), and certain rare neurodegenerative disorders of childhood (Shibata et al, 1995).…”

mentioning

confidence: 99%

Role of heme oxygenase-1 in the regulation of manganese superoxide dismutase gene expression in oxidatively-challenged astroglia

2000

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Manganese superoxide dismutase (MnSOD) is an antioxidant enzyme that reduces superoxide anion to hydrogen peroxide in cell mitochondria. MnSOD is overexpressed in normal aging brain and in various central nervous system disorders; however, the mechanisms mediating the upregulation of MnSOD under these conditions remain poorly understood. We previously reported that cysteamine (CSH) and other pro-oxidants rapidly induce the heme oxygenase-1 (HO-1) gene in cultured rat astroglia followed by late upregulation of MnSOD in these cells. In the present study, we demonstrate that antecedent upregulation of HO-1 is necessary and sufficient for subsequent induction of the MnSOD gene in neonatal rat astroglia challenged with CSH or dopamine, and in astroglial cultures transiently transfected with full-length human HO-1 cDNA. Treatment with potent antioxidants attenuates MnSOD expression in HO-1-transfected astroglia, strongly suggesting that intracellular oxidative stress signals MnSOD gene induction in these cells. Activation of this HO-1-MnSOD axis may play an important role in the pathogenesis of Alzheimer disease, Parkinson disease and other free radical-related neurodegenerative disorders. In these conditions, compensatory upregulation of MnSOD may protect mitochondria from oxidative damage accruing from heme-derived free iron and carbon monoxide liberated by the activity of HO-1.

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“…We succeeded in developing specific antibodies against human and rat Mn-SODs (JIzuKA et al, 1984;KAWAGUCHI et al, 1989;AKAI et al, 1990), and examining the distribution of Mn-SOD in the rat stomach at the light microscopic level. In the rat stomach, Mn-SOD was predominantly localized in the cells of the gastric gland (Fig.…”

Section: Results and Commentsmentioning

confidence: 99%

Post-Embedding Immuno-Electron Microscopy with Rapid Freezing and Freeze-Substitution Techniques for the Localization of Manganese Superoxide Dismutase.

Tatsumi

Suzuki

Senda

et al. 1991

Archives of Histology and Cytology

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Immunocytochemical localization of manganese superoxide dismutase (Mn-SOD) in the hippocampus of the rat

Cited by 51 publications

References 14 publications

Immunocytochemical localization of catalase in the central nervous system of the rat.

Immunocytochemical localization of catalase in the central nervous system of the rat.

Role of heme oxygenase-1 in the regulation of manganese superoxide dismutase gene expression in oxidatively-challenged astroglia

Post-Embedding Immuno-Electron Microscopy with Rapid Freezing and Freeze-Substitution Techniques for the Localization of Manganese Superoxide Dismutase.

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