Immunohistochemistry of Nervous System-Specific Antigens

Eng, Lawrence F.; Bigbee, John W.

doi:10.1007/978-1-4615-8240-3_2

Cited by 109 publications

(34 citation statements)

References 222 publications

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“…5,6,and 8). This pattern of labeling is typical of the ultrastructural localization of GFA (Eng and Bigbee, 1978;Maunoury et al, 1979;Schachner et al, 1977). The present study was not designed to precisely localize GFA within cytoplasmic organelles or to determine the site of its synthesis.…”

Section: Electron Microscopic Examinationmentioning

confidence: 65%

“…The sensitivity and specificity of the GFA antibody and the immunohistochemical methods utilized here for the localization of glial cells are well documented (Eng and Kosec, 1974;Levitt and Rakic, 1980;Ludwin et al, 1976). There is little doubt concerning the specificity of GFA as a major constituent of astroglial filaments (Bignami et al, 1972;Bignami and Dahl, 1974;Eng, 1980;Eng and Bigbee, 1978;Eng and Kosec, 1974). In the results presented below, the ultrastructural localization of the immuno- peroxidase reaction product within the embryonic glial cells correlates closely with previous electron microscopic characterizations in mature astrocytes (Maunoury et al, 1979;Schachner et al, 1977).…”

Section: Methodsmentioning

confidence: 93%

“…1, Jan. 19811971, 1972Schmechel and Rakic, 1979). More recently, immunocytochemical staining for the specific glial librillary acid protein (GFA) (Bignami et al, 1972;Eng, 1980;Eng and Bigbee, 1978;Eng et al, 1971;Ludwin et al, 1976) provided more direct evidence of the presence of radial glial cells during early periods of neurogenesis in the human cerebrum (Antanitus et al, 1976;Choi and Lapham, 1978) and in all major subdivisions of the fetal monkey central nervous system (Levitt and Rakic, 1980). This method showed that the number of radial glial cells increases during periods of peak neuronal proliferation and subsides only after neuronal migration ceases (Levitt and Rakic, 1980).…”

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confidence: 99%

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Coexistence of neuronal and glial precursor cells in the cerebral ventricular zone of the fetal monkey: an ultrastructural immunoperoxidase analysis

Levitt¹,

Cooper²,

Rakić³

1981

J. Neurosci.

362

134

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Section: Electron Microscopic Examinationmentioning

confidence: 65%

Section: Methodsmentioning

confidence: 93%

mentioning

confidence: 99%

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Coexistence of neuronal and glial precursor cells in the cerebral ventricular zone of the fetal monkey: an ultrastructural immunoperoxidase analysis

Levitt¹,

Cooper²,

Rakić³

1981

J. Neurosci.

362

134

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“…Immun olabeling of cultured celIs grown on 9-mm coverslips was performed using mouse anti-GC MAb (a ceIl type-specific marker for OL) (9), rabbit anti-GFAP antibody (a cell type-specific marker for astrocytes) (12), and rat anti-N F 150-kOa triplet protein MAb (a ceIl type-specific marker for neurons) (13) as described previously (14). Coverslips were incubated with mouse anti-GC MAb (1:2) for 30 min at room tem perature.…”

Section: Resultsmentioning

confidence: 99%

Psychosine Cytotoxicity in Rat Neural Cell Cultures and Protection by Phorbol Ester and Dimethyl Sulfoxide

et al. 1990

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ABSTRACT. In Krabbe's disease (globoid cell leukodystrophy), galactosylsphingosine (psychosine) is considered to be a causative agent of the pathology found in the nervous system of the patients. In our study, we examined the cytotoxic effect of psychosine in neural cell cultures derived from the rat nervous system. The concentration of toxic thresholds varied from cell type to cell type. The 50% of toxic doses for oligodendrocytes, astrocytes, and the sensory neurons of the dorsal root ganglia were 8, 20, and 30 JLg/mL, respectively. Oligodendrocytes, therefore, appeared to show a higher sensitivity to psychosine than did astrocytes or neurons. When phorbol ester or DMSO was applied simultaneously with psychosine as protective agents in enriched cultures of rat oligodendrocytes, the total number of live cells and galactocerebroside-positive cells and the 2'3'-cyclic nucleotide 3'-phosphohydrolase activity in these cultures were considerably higher as compared with their levels in the experimental cultures treated with psychosine alone. These results indicate that phorbol ester and DMSO could serve as protective agents for psychosine neurotoxicity. (Pediatr Res 28: 473-476, 1990) Abbreviations GLD, globoid cell leukodystrophy EMEM, Eagle's minimum essential medium PDB, 4-iJ-phorbol-12, 13-dibutyrate OL, oligodendrocyte CNP, 2'3'-cyclic nucleotide 3'-phosphohydrolase GC, galactocerebroside GF AP, glial fibrillary acidic protein NF, neurofilament TD so , 50% toxic dose Krabbe's disease (OLD) is an inherited neurologic disorder in children caused by galactosylceramide-d-galactosidase deficiency (l ). In OLD, unlike in other sphingolipid storage diseases, galactosylceramide, the natural substrate of the deficient enzyme, does not accumulate in the CNS, and the overall concentration in the brain is much lower than normal (2), An abnormal accumulation in the brains of OLD patients of galactosylsphingosine (psychosine), which is also a substrate for the missing enzyme, was demonstrated by Svennerholm et at. (3), These authors confirmed the "psychosine hypothesis" proposed by Miyatake and Suzuki (4) that psychosine is highly cytotoxic and responsible for the extensive pathology of the disease (5), Received December 18, 1989: accepted June 28, 1990. Correspondence: Seung U. Kim, MD., PhD., Division of Neurology, University Hospital. University of British Columbia, Vancouver, B.c., V6T IW5, Canada.Previous studies have reported that psychosine is cytotoxic in the cell culture system (4) and in vivo when it is injected intracerebrally (6). In OLD, the affected organ is almost exclusively the nervous system, which shows dysmyelination of the CNS and the peripheral nerve. To facilitate our understanding of how psychosine elicits dysmyelination of the CNS, we examined its cytotoxic effect on the neural cell cultures derived from newborn rat brain and dorsal root ganglion. In addition, attempts were made to neutralize psychosine cytotoxicity in rat brain cultures by supplementing two reagents, DMSO and phorbol ester PDB, as...

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“…S-100 protein, first described by Moore in 1965 [I], is one of those specific proteins which is located primarily in glial cells [2]. The function of this protein is unknown, although there is a theory about its role in learning process [3].…”

mentioning

confidence: 99%

Structural Relation of Two S-100 Proteins in Bovine Brain; Subunit Composition of S-100 a Protein

Isobe

Ishioka

Okuyama

2005

European Journal of Biochemistry

154

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Dodecyl sulfate/urea/polyacrylamide gel electrophoresis of S-100a protein, one of the two major components of the brain-specific S-100 protein, indicated the presence of two different subunits in the protein.These subunits (a and fl subunits) were purified from the aminoethylated protein by column chromatography on Sephadex G-75, and the purified subunits were subjected to analyses. The results have shown that S-100a protein is a dimer of ci and B subunits, with each subunit having a molecular weight of approximately 10500.Structural comparison of these subunits with the subunit of S-100b protein, the other component of S-100 protein consisting of two identical subunits with known amino acid sequence, has revealed that the [ j subunit and the subunit of S-100b protein are identical, so that S-100a protein is related to S-100b protein by sharing one of the subunits as a common structural constituent.

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Immunohistochemistry of Nervous System-Specific Antigens

Cited by 109 publications

References 222 publications

Coexistence of neuronal and glial precursor cells in the cerebral ventricular zone of the fetal monkey: an ultrastructural immunoperoxidase analysis

Coexistence of neuronal and glial precursor cells in the cerebral ventricular zone of the fetal monkey: an ultrastructural immunoperoxidase analysis

Psychosine Cytotoxicity in Rat Neural Cell Cultures and Protection by Phorbol Ester and Dimethyl Sulfoxide

Structural Relation of Two S-100 Proteins in Bovine Brain; Subunit Composition of S-100 a Protein

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