Regional and subcellular distribution of superoxide dismutase in brain

Loomis, T. C.; Yee, Gayle M.; Stahl, William L.

doi:10.1007/bf01937382

Cited by 33 publications

(12 citation statements)

References 10 publications

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“…For liver, brain, and heart, no significant changes with age in SODase specific activity are seen. SODase specific activity in gray matter of brain appears similar to whole brain tissue, as has been reported (48). MLP Table 1. changes for liver, brain, and heart are evident, although a slight decrease is seen in liver and heart (Fig.…”

supporting

confidence: 78%

Superoxide dismutase: correlation with life-span and specific metabolic rate in primate species.

Tolmasoff¹,

Ono²,

Cutler³

1980

Proc. Natl. Acad. Sci. U.S.A.

313

112

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Much evidence now suggests that superoxide dismutase (superoxide:superoxide oxidoreductase, EC 1.15.1.1) may be a major intracellular protective enzyme against oxygen toxicity by catalyzing the removal of the superoxide radical. We examined the possible role this enzyme may have in determining the life-span of primate species. Superoxide dismutase specific activity levels were measured in cytoplasmic fractions of liver, brain, and heart of 2 rodent and 12 primate species. These species had maximum life-span potentials ranging from 3.5 to 95 years. Liver, brain, and heart had similar specific activity levels for a given species, but the levels for different species varied over 2-fold, with man having the highest level.No general correlation was found in the levels with life-span.However, the ratio of superoxide dismutase specific activity to specific metabolic rate of the tissue or of the whole adult organism was found to increase with increasing maximum lifespan potential for all the species. This correlation suggests that longer-lived species have a higher degree of protection against by-products of oxygen metabolism.A wide range exists in maximum life-span potential (MLP) of different mammalian species which may be the result of relatively small biological differences (1-3). Much of the evolution of mammalian species may have been the result of alterations in the temporal and quantitative expression of a conserved set of structural genes (4-6). Consistent with this view is the high rate of increase in MLP during the evolution of the primates, particularly along the hominid ancestral-descendant sequence (7). This high rate implies that relatively few genetic alterations may have been necessary to substantially prolong the period of general health maintenance (8, 9). These and other data have suggested that, as in the evolution of morphology and other characteristics of a species, modifications in gene regulation may be involved in the evolution of longevity or health maintenance (7, 10).We are testing this hypothesis by searching for a correlation between the level of expression of potentially important genetic repair and protective processes and the MLP of mammalian species. There is compelling evidence that superoxide dismutase (SODase; superoxide:superoxide oxidoreductase, EC 1.15.1.1) is a major protective enzyme against oxygen toxicity, which acts by catalyzing the removal of the superoxide radical (11-13). In this paper we show the relative level of SODase specific activity as a function of MLP in liver, brain, and heart for 2 rodent and 12 primate species. Results indicate an excellent positive correlation between the ratio of SODase specific activity to specific metabolic rate (SMR) and MLP for these species. MATERIALS AND METHODS

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supporting

confidence: 78%

Superoxide dismutase: correlation with life-span and specific metabolic rate in primate species.

Tolmasoff¹,

Ono²,

Cutler³

1980

Proc. Natl. Acad. Sci. U.S.A.

313

112

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“…However, since in the former studies, where multiple enzyme activity determinations were made, simply applying Student's t-test is not appropriate to identify regional differences, the proposed regionally different distributions of SOD, GSH-PX and catalase remain uncertain. In human brains, both the limited previous available evidence (Loomis et al, 1976;Marklund et al, 1983Marklund et al, , 1985Ansari et al, 1985) and our own findings suggest that SOD, GSSG-RD, catalase, and cytosolic GSH-PX activities are distributed fairly evenly in different brain regions. The only exception was the uneven occurrence of particulate fraction GSH-PX activity, with high activities in the basal nucleus and amygdala and low activities in the calcarine fissure, hippocampus, thalamus, and dentate nucleus.…”

Section: Discussionmentioning

confidence: 46%

“…In experimental animals, the distribution of SOD activity in different brain areas has been found to be uniform (Danh et al, 1983), or some concentration has been noted on the pons, substantia nigra, striatum and hypothalamus (Thomas et al, 1976;Ledig et al, 1982;Mizuno and Ohta, 1986). In humans, the regional distribution of SOD activity is not known, but the limited evidence suggests rather similar SOD activities in different brain regions (Loomis et al, 1976;Marklund et al, 1983Marklund et al, , 1985. GSH-PX activity in the rat brain has been noted to be somewhat higher in the striatum and substantia nigra than in other brain regions (Brannan et al, 1980;Mizuno and Ohta, 1986), and a similar, although very slight regional difference has also been seen in GSSG-RD activity (Mizuno and Ohta, 1986).…”

Section: Introductionmentioning

confidence: 99%

Oxygen toxicity protecting enzymes in the human brain

Marttila

Röyttä

Lorentz

et al. 1988

J. Neural Transmission

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Regional distribution of superoxide dismutase, catalase, glutathione peroxidase, and glutathione reductase activities were studied in 22 anatomic sites of 5 human brains. No significant regional differences were observed in cytosolic activities of any enzyme studied, nor in particulate activities of superoxide dismutase, catalase and glutathione reductase, whereas particulate glutathione peroxidase activities were distributed unevenly, the highest activities observed in the basal nucleus and amygdala. There were significant interindividual differences in the activities of each enzyme. This was shown to result partly from the decrease of cytosolic superoxide dismutase and catalase activities with age, concurrently with age-related decrease of particulate glutathione peroxidase and glutathione reductase activities.

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“…In other regions (i.e., substantia nigra, caudate-putamen) the enzyme activity steadily declines with age. These markedly different age-related profiles of superoxide dismutase activity with age in the different brain regions could explain the controversial data of the literature (5,10,59,60). In caudate-putamen and, particularly, in substantia nigra the enzyme activity is increased by both dihydroergocristine and dihydroergocriptine chronic treatments during age, the other brain regions being practically unaffected.…”

Section: Discussionmentioning

confidence: 94%

Changes induced by aging and drug treatment on cerebral enzymatic antioxidant system

1988

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The age-related modifications of the participants to the cerebral enzymatic antioxidant system (superoxide dismutase, glutathione peroxidase, glutathione reductase, glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase) were evaluated in four brain regions from male Wistar rats aged 5, 10, 15, 20, 25, 30, and 35 months. Both the specific enzyme activity and the profile of any enzyme tested markedly differ with age according to the region examined: parieto-temporal cortex, caudate-putamen, substantia nigra and thalamus. This inhomogeneous age-related profile of enzyme activities could explain both the controversial data of literature and the different regional vulnerability of the brain tissue to damage with aging. In rats aged 10, 20, or 30 months, the chronic i.p. treatment for two months with papaverine or ergot alkaloids (dihydroergocristine, dihydroergocornine, dehydroergocriptine) suggests that the antioxidant enzyme activities may be influenced according to the agent utilized, the brain region tested, and the age of the animal. In any case, small differences in the drug structure support marked differences in the type and extent of the intervention on the antioxidant enzymatic system.

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Regional and subcellular distribution of superoxide dismutase in brain

Cited by 33 publications

References 10 publications

Superoxide dismutase: correlation with life-span and specific metabolic rate in primate species.

Superoxide dismutase: correlation with life-span and specific metabolic rate in primate species.

Oxygen toxicity protecting enzymes in the human brain

Changes induced by aging and drug treatment on cerebral enzymatic antioxidant system

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