Highly Sensitive Immunoassays for Three Forms of Rat Brain Enolase

Kato, Kanefusa; Suzuki, Fujiko; Umeda, Yumiko

doi:10.1111/j.1471-4159.1981.tb01663.x

Cited by 70 publications

(26 citation statements)

References 13 publications

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“…This last value is in the same range as that found for rat brain ey mRNA by ourselves (Marks et al, 1980) and by others (Walker and ZomzelyNeurath, 1980;Sakimura et al, 1980). The levels of oa and y antigens in rodent brain (Marangos et al, 1979;Pin-Scarna, 1980;Kato et al, 1981) are I%, while we find that the levels of corresponding mRNAs are smaller by an order of magnitude, as has also been shown by others (Walker and Zomzely-Neurath, 1980) The relative increase of a and -y antigens during development appears to depend upon the accumulation of the corresponding translatable mRNA. However, the proportion of adult a mRNA is three times higher than that of -y mRNA while the relative amounts of the corresponding antigens in adult rat brain , or mouse brain (PinScarna, 1980) are similar.…”

supporting

confidence: 79%

Developmental changes in translatable mRNAs for the cerebral enolase isozymes alphaalpha and gammagamma.

et al. 1983

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Using the rabbit reticulocyte cell-free translation system we have estimated during ontogenesis the proportions of in vitro translatable a and oy brain enolase mRNAs, which are two minor mRNA species. No polypeptide precursor to these enzyme subunits appears to be synthesized during translation in vitro. During brain development, the changes in translatable a and 'y mRNA content seem to parallel those of the corresponding antigens. The proportion of each of the enolase mRNAs is highest in adult mouse brain. Mechanisms controlling a and -y antigen expression are discussed. In order to prepare the specific cDNA probes, purification of a and -y mRNAs was undertaken.

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supporting

confidence: 79%

Developmental changes in translatable mRNAs for the cerebral enolase isozymes alphaalpha and gammagamma.

et al. 1983

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“…The fixed preparations were transferred to a 100 mm plastic dish, in which a wet filter paper had been set. The cells were then treated for 40 min at room temperature with 100 p1 1 in 1000 diluted rabbit anti-68K-neurofilament IgG (Monosan), anti-glial fibrillary acidic protein IgG (DAKO), antis-100 (@) IgG or anti-yy-enolase IgG (Liem et al, 1978;Dahl & Bignami, 1979;Isobe & Okuyama, 1978;Kato et al, 1981). Antibodies against S-100 and yy-enolase were provided by K. Kato, Department of Biochemistry, Institute for Developmental Research, Aichi Prefectural Colony, Japan.…”

Section: Methodsmentioning

confidence: 99%

Binding and Cytotoxic Effects of Clostridium botulinum Type A, C1 and E Toxins in Primary Neuron Cultures from Foetal Mouse Brains

Kurokawa¹,

Oguma²,

Yokosawa³

et al. 1987

Microbiology

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Binding of purified Clostridium botulinum type A, C1 and E toxins to cultured cells was studied by an immunocytochemical method. Type A and C1 toxins bound strongly to neuron cultures prepared from brains of foetal mice, but binding of type E toxin was weak. None of the toxin types bound to the feeder layer, composed of non-neuronal cells. The heavy-chain component of the type C1 toxin bound to neurons, but the light chain component did not. Type C1 toxin also bound only to cell lines of neuronal origin. When type C1 toxin [final concentration 4 x 10(2) LD50 (10 ng) per well] was added to primary neuron cultures in 96-well plates, degeneration of neuronal processes and rounding of neuronal somas were observed, but type A and E toxins did not produce such changes. The binding and cytotoxic activities of type C1 toxin were blocked by heat treatment (80 degrees C for 30 min) or by preincubation of the toxin with polyclonal anti-C1 IgG and some of the monoclonal antibodies which neutralized the toxin activity in mice. In the neuronal processes treated with C1 toxin, many degenerated mitochondria, membranous dense bodies and vesicles were observed by electron microscopy; these ultrastructural changes were similar to those of Wallerian degeneration in vivo.

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“…9). Although this was also the case in pri mary malignant brain tumors, here it could be influenced by the tissue from which the primary tumor emerges, as in most organs total enolase activity is lower than in the brain, with the exception of skeletal muscle, kidney and liver [7,28].…”

Section: Resultsmentioning

confidence: 99%

Enolase Isoenzymes in Human Cerebral Metastasis

Doel¹,

Roholl²,

Rijksen³

et al. 1989

Tumor Biol

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γ-Enolase [one of the three possible subunits of the dimeric enzyme enolase (EC 4.2.1.11)] has been reported as a marker for human neurons, neuroendocrine cells and tumors derived from these cells. In recent years, however, its presence has been reported in nonneuronal tumors. For employment in the histopathologic diagnosis of tumors of the nervous system, exact knowledge of the enolase isoenzyme patterns occurring in these tumors is a prerequisite. In human gliomas, the presence of varying quantities of γ-enolase has been demonstrated. The present study examines the enolase isoenzyme pattern in human cerebral metastases of various primary progeny, using electrophoresis of tumor tissue extracts as well as immunohistochemistry. Additionally, a number of primary tumors of nonneuroepithelial tissue was examined by immunohistochemistry. The presence of γ-enolase was demonstrated in a significant number of brain metastases. A relation between enolase isoenzyme pattern and survival after operation for brain metastasis could not be found. For histopathologic diagnosis of tumors of the adult human central nervous system, analysis of the enolase isoenzyme pattern is not reliable.

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Highly Sensitive Immunoassays for Three Forms of Rat Brain Enolase

Cited by 70 publications

References 13 publications

Developmental changes in translatable mRNAs for the cerebral enolase isozymes alphaalpha and gammagamma.

Developmental changes in translatable mRNAs for the cerebral enolase isozymes alphaalpha and gammagamma.

Binding and Cytotoxic Effects of Clostridium botulinum Type A, C1 and E Toxins in Primary Neuron Cultures from Foetal Mouse Brains

Enolase Isoenzymes in Human Cerebral Metastasis

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