Preferential localization of copper zinc superoxide dismutase in the vulnerable cortical neurons in Alzheimer's disease

Delacourte, André; Défossez, A.; Ceballos, I.; Nicole, Annie; Sinet, Pierre-Marie

doi:10.1016/0304-3940(88)90597-6

Cited by 82 publications

(14 citation statements)

References 20 publications

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“…Our immunocytochemical findings in human and primate hippocampus show some differences from previous studies that used in situ hybridization and immunocytochemistry to report similar levels in the distribution of SOD1 mRNA and protein in all regions of the cornu Ammonis and dentate gyrus (5,12). We have no explanation to account for the discrepancies with previous reports.…”

Section: Discussioncontrasting

confidence: 56%

“…Although SOD1 has been reported to be expressed in many different cells (1), examination of its distribution in the human or mouse nervous system has been limited to examination in the hippocampus (5,6,12) and the substantia nigra [by in situ hybrydization (7)]. Only a study in canine and rat brain has disclosed the extensive presence of SOD1 in various regions of the brain (8), but study of the spinal cord has not been reported.…”

Section: Discussionmentioning

confidence: 99%

“…It has been hypothesized that alterations in antioxidant systems, including SOD1, are implicated in neurodegenerative diseases (5,(11)(12)(13)(14)(15). In some cases of familial amyotrophic lateral sclerosis (FALS), mutations in SOD1 have been linked to disease (16)(17)(18), and at least two of these mutations can cause motor neuron disease when expressed in transgenic mice (ref.…”

Section: Introductionmentioning

confidence: 99%

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Superoxide dismutase is an abundant component in cell bodies, dendrites, and axons of motor neurons and in a subset of other neurons.

Pardo

Borchelt

et al. 1995

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

286

149

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Mutation in superoxide dismutase 1 (SODI), a Cu/Zn enzyme that removes oxygen radicals and protects against oxidative injury, has been implicated in some cases of familial amyotrophic lateral sclerosis (FALS). As a first approach to examining the mechanism(s) through which these mutations cause specific degeneration ofmotor neurons, we have used immunocytochemistry to identify the distribution of SODI in populations of cells in the peripheral and central nervous systems. In (02), yielding H202 and 02; subsequent removal of H202 is facilitated by catalase and glutathione peroxidase (2). Thus, SOD activity can protect against oxidative stress produced by oxygen radicals and may represent a first line of defense against oxidative damage mediated by oxygen radicals (1, 2).SODs are present in the central and peripheral nervous systems, but the cellular and intracellular distributions of SOD1 in neuronal populations are not well defined. Biochemical assays of SOD1 activity have not localized enzymatic activities to specific cells in the brain (3,4), and in situ hybridization and immunocytochemical studies have focused only on selected areas of the nervous system in either control (5-8) or diseased (9, 10) brain.It has been hypothesized that alterations in antioxidant systems, including SOD1, are implicated in neurodegenerative diseases (5,(11)(12)(13)(14)(15). In some cases of familial amyotrophic lateral sclerosis (FALS), mutations in SOD1 have been linked to disease (16)(17)(18), and at least two of these mutations can cause motor neuron disease when expressed in transgenic mice (ref. 19; unpublished observations). However, the mechanism(s) responsible for selective vulnerability to degeneration of motor neurons in FALS-linked SOD1 mutations is unknown. To identify events that lead to motor neuron death, it is critical to define the cellular distributions of SOD1 in the peripheral and central nervous systems. To this end, we have used protein blotting and immunocytochemistry at both light and electron microscopic levels to localize SOD1 in the mouse, nonhuman primate, and human nervous systems. MATERIALS AND METHODSGeneration and Characterization ofanti-SODI Antibody. A pentadecapeptide (CYDDLGDGGNEESTK) of which the C-terminal 13 amino acids correspond to residues 125-137 of mouse and human SOD1 was crosslinked to keyhole limpet hemocyanin (Pierce), emulsified in Freund's adjuvant, and used to immunize rabbits, as described (20) 954The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.

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Section: Discussioncontrasting

confidence: 56%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Superoxide dismutase is an abundant component in cell bodies, dendrites, and axons of motor neurons and in a subset of other neurons.

Pardo

Borchelt

et al. 1995

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

286

149

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“…Consequently, their further characterization and the search for experimental conditions able to produce such abnormal tau proteins might be useful to establish an in vitro model of nerve cell degeneration. For example, they might be produced in nerve cell cultures after the addition of aluminium salts [ 181, or in cells transfected with the Cu,Zn-superoxide dismutase gene [19]. This might be very suitable for the study of the early events that lead to the neurofibrillary degeneration and might help in the search for the primum movens of Alzheimer's disease.…”

Section: Discussionmentioning

confidence: 99%

Abnormal tau species are produced during Alzheimer's disease neurodegenerating process

Flament

Delacourte

1989

FEBS Letters

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Tau proteins were detected in human brain using two polyclonal antibodies: anti-paired helical filaments and anti-human native tau proteins. Both antisera detected identically the normal set of tau proteins in control brains. Moreover they detected two abnormal tau variants of 64 and 69 kDa exclusively in brain areas showing neurofibrillary tangles and senile plaques. Tau 64 and 69 were abnormally phosphorylated as revealed by the decrease in their molecular mass observed after alkaline phosphatase treatment. Therefore, tau 64 and 69 are specific markers of the neurofibrillary degeneration of the Alzheimer type and might be useful tools for studying the first pathological events that lead to neuronal death.

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“…Moreover, cultured neurons of transgenic SOD-1 mice with elevated SOD-1 activity exhibit a chronic prooxidant state, altered intracellular calcium homeostasis and higher susceptibility to excitotoxicity [BarPeled et al, 1996]. Finally, increased SOD-1 expression has been found in degenerating neurons in the AD brain [Delacourte et al, 1988;Furuta et al, 1995] suggesting a potential involvement of elevated SOD-1 activity in the degenerative process. Other factors relevant to the pathogenesis of AD in DS have included Ets-2 is a transcription factor, which is involved in multiple cellular processes including differentiation, maturation and activation of signaling cascades [Macleod et al, 1992;Wasylyk et al, 1993].…”

Section: Neurobiology Of Ad: the Role Of Oxidative Stressmentioning

confidence: 97%

Alzheimer's disease in Down syndrome: Neurobiology and risk

Zigman¹,

Lott²

2007

Ment. Retard. Dev. Disabil. Res. Rev.

244

221

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Down syndrome (DS) is characterized by increased mortality rates, both during early and later stages of life, and age-specific mortality risk remains higher in adults with DS compared with the overall population of people with mental retardation and with typically developing populations. Causes of increased mortality rates early in life are primarily due to the increased incidence of congenital heart disease and leukemia, while causes of higher mortality rates later in life may be due to a number of factors, two of which are an increased risk for Alzheimer's disease (AD) and an apparent tendency toward premature aging. In this article, we describe the increase in lifespan for people with DS that has occurred over the past 100 years, as well as advances in the understanding of the occurrence of AD in adults with DS. Aspects of the neurobiology of AD, including the role of amyloid, oxidative stress, Cu/ZN dismutase (SOD-1), as well as advances in neuroimaging are presented. The function of risk factors in the observed heterogeneity in the expression of AD dementia in adults with DS, as well as the need for sensitive and specific biomarkers of the clinical and pathological progressing of AD in adults with DS is considered.

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Preferential localization of copper zinc superoxide dismutase in the vulnerable cortical neurons in Alzheimer's disease

Cited by 82 publications

References 20 publications

Superoxide dismutase is an abundant component in cell bodies, dendrites, and axons of motor neurons and in a subset of other neurons.

Superoxide dismutase is an abundant component in cell bodies, dendrites, and axons of motor neurons and in a subset of other neurons.

Abnormal tau species are produced during Alzheimer's disease neurodegenerating process

Alzheimer's disease in Down syndrome: Neurobiology and risk

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