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  • 1
    Electronic Resource
    Electronic Resource
    Neuronotrophic Factors Released by C6 Glioma Cells (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 50 (1988), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Glial cells have been shown previously to release factors that promote survival of central and peripheral neurons [neuronotrophic factors (NTFs)]. We have investigated the release of NTFs by C6 cells, a rat glioma cell line, under different modes of conditioning. Media conditioned in the presence or absence of serum [C6 cell conditioned media (C6CMs)] were analyzed using biological, biochemical, and immunological assays. We report that (a) nuclear and cytoskeletal proteins were not present in C6CMs, indicating that C6CM proteins result from release by C6 cells rather than from cell death; (b) C6CM contained 1–3 μg protein/ml, corresponding to a secretion rate of about 0.5 pg protein per cell and day; (c) C6CM contained the neurite-promoting factor laminin and low amounts of nerve growth factor; (d) the presence of fetal calf serum in the culture medium was essential for synthesis and release of NTFs; and (e) our C6CM contained at least three NTFs differing by their temporal secretory patterns and three NTFs differing by biochemical properties, indicating that C6 cells produce and secrete six different NTFs. Within these, nerve growth factor seems to be the only established NTF.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1988.tb02474.x
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  • 2
    Electronic Resource
    Electronic Resource
    An Enzyme-Linked Immunoassay for Nerve Growth Factor (NGF): A Tool for Studying Regulatory Mechanisms Involved in NGF Production in Brain and in Peripheral Tissues (1987)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 48 (1987), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: A sensitive enzyme-linked immunosorbent assay (ELISA) for nerve growth factor (NGF) has been developed. The sensitivity of this assay (0.1 pg/well) permits the quantification of endogenous immunoreactive NGF in the peripheral nervous system and the CNS. Studies on the regulatory mechanisms involved in NGF production indicate that, in addition to neurally mediated mechanisms, other stimuli, e.g., inflammation, significantly contribute to NGF production.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1987.tb05736.x
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  • 3
    Electronic Resource
    Electronic Resource
    RELATIONSHIP BETWEEN THE RATE OF AXOPLASMIC TRANSPORT AND SUBCELLULAR DISTRIBUTION OF ENZYMES INVOLVED IN THE SYNTHESIS OF NOREPINEPHRINE (1973)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 20 (1973), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The net rate of proximo-distal transport of tyrosine hydroxylase, dopamine β-hydroxylase, DOPA decarboxylase and choline acetyltransferase was determined by measuring the accumulation of these enzymes proximal to a ligature of the rat sciatic nerve. The rate of accumulation was constant for at least 12 h. For the enzymes involved in the biosynthesis of norepinephrine the rate of transport was correlated to their subcellular distribution and a close correlation between these two parameters was found. Dopamine β-hydroxylase, an enzyme mainly localized in the particulate fraction of the sciatic nerve, showed the fastest rate of transport (1·94 mm/h) whereas DOPA decarboxylase, exclusively located in the high-speed supernatant fluid, gave the slowest (0·63 mm/h) rate of transport. Tyrosine hydroxylase, predominantly located in the non-particulate fraction of the sciatic nerve was transported much slower (0·75 mm/h) than dopamine β-hydroxylase but still significantly (P 〈 0.005) faster than DOPA decarboxylase. The subcellular distribution of dopamine β-hydroxylase in ganglia did not differ significantly (0·45 〉 P 〉 0·40) from that in the sciatic nerve, but in nerve endings a greater proportion of dopamine β-hydroxylase was localized in particulate fractions. Tyrosine hydroxylase and DOPA decarboxylase were found exclusively in the non-particulate fractions of ganglia. In the nerve endings of the effector organs a small but consistent portion of tyrosine hydroxylase was found in particulate fractions, whereas DOPA decarboxylase was exclusively localized in the high-speed supernatant fluid.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1973.tb00285.x
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  • 4
    Electronic Resource
    Electronic Resource
    ORGAN CULTURE OF THE RAT ADRENAL MEDULLA: A MODEL SYSTEM FOR THE STUDY OF TRANS-SYNAPTIC ENZYME INDUCTION (1975)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 25 (1975), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: —It was the aim of the present study to develop organ culture conditions for the rat adrenal medulla which are representative for the in vivo situation. This is a prerequisite for studying the complex processes involved in trans-synaptic enzyme induction. The processes of trans-synaptic enzyme induction initiated in vivo by injecting 5 mg/kg of reserpine 2 h prior to the removal of the adrenal medulla, continued in this culture system and final levels of tyrosine hydroxylase were comparable to those seen in vivo. That these culture conditions are representative for the in vivo induction is also supported by the fact that transection of the splanchnic fibres supplying the adrenal medulla or administration of actinomycin D prior to reserpine abolished the rise in tyrosine hydroxylase activity not only in vivo, but also in culture.The findings that high concentrations (0·29 mm) of corticosterone in the culture medium inhibited the increase in tyrosine hydroxylase activity caused by reserpine support the hypothesis that glucocorticoids act as modulatory agents in trans-synaptic enzyme induction. This inhibition was exhibited only when corticosterone was added at the initiation of the culture period. If added 2 or 4 h after the beginning of the culture period there was little or no effect on the subsequent increase of tyrosine hydroxylase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1975.tb04340.x
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  • 5
    Electronic Resource
    Electronic Resource
    EFFECT OF GLUCOCORTICOIDS ON NERVE GROWTH FACTOR-MEDIATED ENZYME INDUCTION IN ORGAN CULTURES OF RAT SYMPATHETIC GANGLIA: ENHANCED RESPONSE AND REDUCED TIME REQUIREMENT TO INITIATE ENZYME INDUCTION (1977)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 29 (1977), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— After previous studies had shown that nerve growth factor produces a very similar change in the enzyme pattern of adrenergic neurons as does an increased activity of the preganglionic cholinergic nerves, the present experiments revealed that the nerve growth factor-mediated selective induction of TH and DBH is enhanced by glucocorticoids in a way similar to that mediated by acetylcholine via nicotinic receptors. Corticosterone (5 μM) produced not only an increase in the maximal response to NGF but shifted the concentration response curve of TH to NGF to the left. The potentiation effect was shown to be specific for glucocorticoids, since other steroid hormones like testosterone, β-estradiol and progesterone had no effect. Moreover, the glucocorticoid effect could be antagonized by cortexolone, suggesting an effect via glucocorticoid receptors. In addition to the potentiation of the nerve growth factor-mediated enzyme induction, glucocorticoids reduced the exposure time to NGF, necessary to initiate maximal TH induction, from 4 h to 10 min. The glucocorticoid potentiation of NGF-mediated specific enzyme induction is discussed in relation to the site and mechanism of action of NGF.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1977.tb03925.x
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  • 6
    Electronic Resource
    Electronic Resource
    SYNTHESIS, SUBCELLULAR DISTRIBUTION AND TURNOVER OF DOPAMINE β-HYDROXYLASE IN ORGAN CULTURES OF SYMPATHETIC GANGLIA AND ADRENAL MEDULLAE (1976)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 27 (1976), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The synthesis, subcellular distribution and turnover of dopamine β-hydroxylase was studied in organ cultures of rat adrenal medullae and superior cervical ganglia. After exposure to [3H]leucine for 1 or 3 h, the tissues were homogenized at various time intervals and the amount of labelled dopamine β-hydroxylase in different subcellular fractions (cytosol, soluble and membrane-bound fraction of catecholamine storage vesicles) was determined by immunoprecipitation and subsequent electrophoresis. In cultured adrenal medullae, induction of dopamine β-hydroxylase initiated in vivo by administration of reserpine affected both soluble and membrane-bound pools of dopamine β-hydroxylase to a similar extent after pulse-labelling for 1 or 3 h. The half-lives of dopamine β-hydroxylase, which amounted to 6 h for the cytosol, 7.5 h for the soluble vesicular and 32 h for the membrane-bound vesicular pools were not altered by pretreatment with reserpine. In superior cervical ganglia the half-lives of the soluble pools were 2–3 times longer than in the adrenal medulla, whereas the half-life of the membrane-bound fraction was the same as in the adrenal medulla. In both organs the most heavily labelled fraction (both after a pulse of 1 or 3 h) was always that of the vesicular membrane, suggesting that newly-synthesized dopamine β-hydroxylase is immediately incorporated into the storage vesicles and not via release into the cytosol from the site of synthesis. The fact that the half-life of membrane-bound dopamine β-hydroxylase is markedly longer than that of the two soluble pools suggests that the single pools are not only independently supplied by newly-synthesized DBH but there is also no appreciable subsequent exchange between soluble and membrane-bound pools.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1976.tb00312.x
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  • 7
    Electronic Resource
    Electronic Resource
    INCREASED SYNTHESIS OF DOPAMINE β-HYDROXYLASE IN CULTURED RAT ADRENAL EDULLAE AFTER IN VIVO ADMINISTRATION OF RESERPINE (1976)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 27 (1976), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— The present experiments were designed to provide direct evidence that the increase in dopamine β-hydroxylase (DBH) activity after treatment with reserpme results from an augmented synthesis of new enzyme protein. After in vivo experiments had shown that DBH could not be labelled to a sufficient extent even after administration of high doses (8.3 mCi/kg) of [3H]leucine we took advantage of earlier observations that neuronally-mediated enzyme induction initiated in vivo progresses in organ cultures of adrenal medullae in a similar manner as in vivo. With that system it was possible to achieve a sufficient labelling of DBH molecules and to provide evidence that the increase in DBH activity produced by reserpine was really due to a specific increase in DBH synthesis. The fact that the half-life of DBH was identical in organ cultures of controls and reserpine-treated animals eliminated the possibility that the increased labelling of DBH after reserpine results from a slower rate of degradation.Both the experiments in vivo and in organ culture showed very clearly that the immunoprecipitation of labelled molecules has to be followed by additional purification by gel electrophoresis since in spite of the use of monospecific antibodies and careful washing of the immunoprecipitates contaminating coprecipitated labelled molecules accounted for up to 96% of the total precipitated radioactivity in whole adrenals (in vivo experiments) and up to 80% in adrenal medulla (organ culture experiments). The coprecipitation of contaminants most probably results from the addition of carrier proteins, used in order to make the precipitation of the small amounts of labelled proteins visible.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1976.tb01573.x
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  • 8
    Electronic Resource
    Electronic Resource
    Interleukin-6 and Interleukin-6 Receptor mRNA Expression in Rat Central Nervous System (1995)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 762 (1995), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1995.tb32348.x
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  • 9
    Electronic Resource
    Electronic Resource
    Stimulation of the pituitary-adrenocortical axis by nerve growth factor (1979)
    [s.l.] : Nature Publishing Group
    Nature 282 (1979), S. 413-414 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] NGF was prepared from submaxillary glands of adult male mice by the method of Bocchini and Angeletti8, as the 2.5S subunit, with the modifications of Suda et al9. The purity of NGF was controlled by SDS gel electrophoresis and its biological activity was determined as described by Fenton10. The ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/282413a0
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  • 10
    Electronic Resource
    Electronic Resource
    Expression of low-affinity NGF receptor and trkB mRNA in human SH-SY5Y neuroblastoma cells
    Amsterdam : Elsevier
    FEBS Letters 330 (1993), S. 287-292 
    Details
    ISSN: 0014-5793
    Keywords: Brain-derived neurotrophic factor ; Differentiation ; Gene expression ; Polymerase chain reaction
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0014-5793(93)80890-7
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