Intraneuritic corpora amylacea

Anzil, A. P.; Herrlinger, H.; Blinzinger, K.; Kronski, D.

doi:10.1007/bf00432727

Cited by 56 publications

(9 citation statements)

References 9 publications

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“…Both types of inclusion become increasingly abundant with advancing age, reside in periventricular brain regions, and are largely astrocytic in origin (Anzil, 1974;Ramsay, 1965;Schipper, 1991). Small GAI may even coexist with one or more larger CA in the cytoplasm of individual GFAP-positive astrocytes (present study).…”

Section: Discussionmentioning

confidence: 56%

“…In Alzheimer's disease (Fleming and Rogers, 1986;Fleming et al, 1987) and other neuroedegenerative conditions (Behrman et al, 1969;Gambetti et al, 1971;Janeway et al, 1967;Robitaille et al, 1980), these inclusions are present in increased numbers relative to age-matched controls. CA predominate in astrocytic processes (Palmucci et al, 1982;Ramsay, 1965) and to a far lesser extent in neurons (Anzil et al, 1974;Averback, 1981;Takahashi et al, 1975). Although many of the tinctorial and histochemical properties of CA have been delineated, their subcellular origin remains unclear.…”

Section: Introductionmentioning

confidence: 99%

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Mitochondrial constituents of corpora amylacea and autofluorescent astrocytic inclusions in senescent human brain

Schipper

Cissé

1995

Glia

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Corpora amylacea (CA) are cytoplasmic inclusions that accumulate in human brain in the course of normal aging, and to an even greater extent, in Alzheimer's disease and other neurodegenerative conditions. In senescent and Alzheimer-diseased human brains, astrocytes in limbic and periventricular regions exhibit red autofluorescent inclusions, homologous to Gomori-positive astrocyte granules previously described in the brains of aging rodents and other vertebrates. We have shown that Gomori inclusions in situ and in culture are derived from autophagocytosed mitochondria exhibiting iron-mediated peroxidase activity. In the human brain, the autofluorescent inclusions share many properties with CA. Both types of inclusion progressively accumulate in periventricular regions with advancing age, are largely astrocytic in origin, and contain various heat shock proteins and ubiquitin. Using histochemistry in conjunction with cofocal microscopy, we demonstrated that both CA and the red autofluorescent granules exhibit non-enzymatic peroxidase activity and an affinity for CAH and PAS. The only major divergent histochemical feature between the Gomori-positive astrocyte granules and CA is the presence of orange-red autofluorescence in the former and the absence of endogenous fluorescence in the latter. On the basis of numerous shared topographic and histochemical features, we hypothesized that CA are largely derived from autofluorescent (Gomori-positive) astrocyte granules which reside in periventricular regions of the senescent CNS. Immunofluorescent labeling and laser scanning confocal microscopy demonstrated consistent colocalization of the mitochondrial proteins, sulfite oxidase, and heat shock protein 60, to both CA and the autofluorescent astroglial inclusions. In addition, both CA and the autofluorescent astrocyte granules exhibit staining for DNA which colocalizes to mitochondrial antigens and therefore likely represents mitochondrial nucleic acid in dual-labeled preparations. These observations suggest that a) Gomori-positive astrocyte granules in human brain are homologous to those described in rodents, b) Gomori-positive granules may be structural precursors of CA in senescent human brain, and c) in the aging human brain, degenerate mitochondria within periventricular astrocytes give rise to autofluorescent cytoplasmic granules and corpora amylacea.

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Section: Discussionmentioning

confidence: 56%

Section: Introductionmentioning

confidence: 99%

Mitochondrial constituents of corpora amylacea and autofluorescent astrocytic inclusions in senescent human brain

Schipper

Cissé

1995

Glia

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“…Whereas larger bodies >5 μm in diameter occur within the processes of astrocytes,6 9those less than this size have been seen principally within neurites6 7 and can be found at various points along both central and peripheral axons down to preterminal and terminal regions 78 11 Although commonly found in neurites in humans and in other species12 they have rarely, if ever, been seen within the perikarya of neurons.…”

Section: Discussionmentioning

confidence: 99%

“…However, this does contrast with the finding by Kubota et al 10 of complete loss of corpora amylacea from the optic nerve after glaucoma, which raises the question as to whether they in fact regularly “escape” from subpial regions. Sbarbati et al 6 have shown them apparently being released into the subpial space, but whether this is a regular route is not known. If they are not, it might be concluded that accumulation of corpora amylacea at various sites within the CNS is a means whereby potentially damaging waste materials they seem to be containing26 may be harmlessly sequestered.…”

Section: Discussionmentioning

confidence: 99%

Spinal corpora amylacea and motor neuron disease: a quantitative study

Cavanagh

1998

Journal of Neurology, Neurosurgery & Psychiatry

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Objective-To test the hypothesis that as there is growing evidence that corpora amylacea, or amyloid bodies, in the CNS are derived primarily from neurons, it might be expected that their numbers in the spinal cord would decline with loss of neurons in motor neuron degeneration as they do in the retina on destruction of ganglion cells by glaucoma. Methods-The numbers of corpora amylacea were counted in PAS stained transverse sections of the lumbar cord from 27 patients with motor neuron disease and 21 control subjects of similar age and sex mix. The numbers and sizes of corpora amylacea were determined both in the anterior horn grey matter and in the submeningeal white matter regions in each case. Results-In both groups the total numbers in the white matter and submeningeal regions ranged from 160 to more than 5000/section and there was minimal significant diVerence between the two groups. No relation with age was found in this narrow age range. The mean diameters of the corpora amylacea were significantly less in the grey matter of both groups than in the submeningeal regions. However, their densities in the grey matter of the anterior horn were significantly reduced in the spinal cord sections in the motor neuron disease group, but only where few motor neurons remained. Conclusions-These findings support the view that corpora amylacea may arise from neurons, and suggest that that there may be two compartments, one mobile and one static, the second most likely remaining in the periphery of the spinal cord for prolonged periods. (J Neurol Neurosurg Psychiatry 1998;65:488-491)

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“…However, the A4 peptide is most easily demonstrated by immunologic techniques in extracellular amyloid deposits and affected blood vessels of the AD brain (8)(9)(10)(11) (16,19). They have been associated with both neurons (20)(21)(22) and astrocytes (23). A distinct difference between A4 and P2 antigens was the presence of the latter in CA.…”

Section: Discussionmentioning

confidence: 99%

Identification of cellular and extracellular sites of amyloid precursor protein extracytoplasmic domain in normal and Alzheimer disease brains.

Tate-Ostroff

Majocha

Marotta

1989

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

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Information concerning the distribution of various subdomains of the amyloid precursor protein (APP) in brain may illuminate aspects of the normal metabolism of this membrane-associated protein, as well as putative abnormal processing that may occur in Alzheimer disease (AD). We prepared affinity-purified antibody, P2, against an extracytoplasmic APP site and applied it, along with monoclonal antibodies to the j3-peptide, or A4 region, in conjunction with selective cytochemical staining methods, to control and AD tissues. The following was noted: (i) in contrast to A4 epitopes, which are easily demonstrable primarily in extracellular senile plaques of AD patients, the extracytoplasmic P2 antigen was found in association with neurons, glia, and blood vessels in both normal and AD prefrontal cortex; (i) a subset of senile plaques contained both A4 and P2 antigens; (iU) in some instances, P2 antigen occurred as an extracellular deposit in the absence of A4; (iv) the P2 antigen, but not A4, was also associated with corpora amylacea. In addition to identifying the unique cellular distribution of the APP extracytoplasmic antigen, the results support the view that a segment of this domain undergoes processing and deposition at extracellular sites, including a subset of senile plaques.The structure of Alzheimer amyloid precursor protein (APP) cDNA has been determined (1-5) and shown to correspond to a protein of 695 amino acids that has features in common with glycosylated cell-surface receptors (1). Of the APP domains, the A4 (or P-peptide) region consisting of -42 amino acids appears to extend from the extracytoplasmic domain to the transmembrane site (1). Immunologic and biochemical data have firmly established that in the Alzheimer disease (AD) brain the A4 polypeptide is a major component of cerebrovascular and senile plaque amyloid (6)(7)(8)(9)(10)(11). However, no detailed information has been available concerning the cellular or extracellular localization of the extracytoplasmic domain (ECD) of the APP and its distribution with regard to A4 and senile plaques.The present report addresses the issue oflocalization ofthe ECD by means of an affinity-purified antibody, P2, raised to a unique peptide within the extracytoplasmic region of the APP. Both control and AD brains were stained with P2, anti-A4 monoclonal antibodies (mAbs) (10), and anti-glial fibrillary acidic protein, in addition to selective cytochemical counterstains. We report here that an extracytoplasmic APP domain has unique features in both control and AD brains that distinguish it from A4. We report, further, that certain senile plaques of the AD brain contain the extracytoplasmic P2 antigen in addition to the A4 domain and that the P2 antigen alone can accumulate extracellularly.A portion of these data were reported previously in preliminary form (12). (1) was prepared by methods previously described (10). The polypeptide was determined to have a unique sequence as indicated by searches facilitated by BIONET (IntelliGenetics) data bases....

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Intraneuritic corpora amylacea

Cited by 56 publications

References 9 publications

Mitochondrial constituents of corpora amylacea and autofluorescent astrocytic inclusions in senescent human brain

Mitochondrial constituents of corpora amylacea and autofluorescent astrocytic inclusions in senescent human brain

Spinal corpora amylacea and motor neuron disease: a quantitative study

Identification of cellular and extracellular sites of amyloid precursor protein extracytoplasmic domain in normal and Alzheimer disease brains.

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