ZIB

1

Digitale Medien

MEASUREMENT OF NEURON-SPECIFIC (NSE) AND NON-NEURONAL (NNE) ISOENZYMES OF ENOLASE IN RAT, MONKEY AND HUMAN NERVOUS TISSUE (1979)

Marangos, P. J. ; Schmechel, D. ; Parma, A. M. ; [weitere]

Oxford, UK : Blackwell Publishing Ltd

Journal of neurochemistry 33 (1979), S. 0

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ISSN: 1471-4159

Quelle: Blackwell Publishing Journal Backfiles 1879-2005

Thema: Medizin

Notizen: Four double antibody solid-phase radioimmunoassay systems are described for the measurement of neuron-specific enolase (NSE) and non-neuronal enolase (NNE) from rat, monkey and human brain tissue. NSE and NNE are antigenically distinct, making their respective assays specific. The levels of neuronal and non-neuronal enolase (an enolase recently shown to be localized in glial cells) are determined in various regions of rat, monkey and human nervous system. Both neuronal and glial enolases are major proteins of brain tissue with each representing about 1.5% of total brain soluble protein. NSE levels are highest and NNE levels lowest in brain areas having a high proportion of grey matter, such as the cerebral cortex. The reverse is true for areas high in white matter, such as the pyramidal tract and the corpus callosum. Peripheral nervous system levels of NSE are much lower than those of brain with the spinal cord intermediate between the two.Radioimmunological and immunocytochemical data show that neuron-specific enolase is also present in neuroendocrine cells located in non-nervous tissue, which include pinealocytes, parafollicular cells of the thyroid, adrenal medullary chromaffin cells, glandular cells of the pituitary and Islet of Langerhans cells in the pancreas. Unlike neurons, these cells also contain non-neuronal enolase in high amounts.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1111/j.1471-4159.1979.tb11735.x

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2

Digitale Medien

STRUCTURAL AND IMMUNOLOGICAL PROPERTIES OF NEURON SPECIFIC PROTEIN (NSP) FROM RAT, CAT AND HUMAN BRAIN: COMPARISON TO BOVINE 14-3-2 (1977)

Marangos, P. J. ; Zomzely-Neurath, Claire ; Goodwin, F. K.

Oxford, UK : Blackwell Publishing Ltd

Journal of neurochemistry 28 (1977), S. 0

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ISSN: 1471-4159

Quelle: Blackwell Publishing Journal Backfiles 1879-2005

Thema: Medizin

Notizen: Abstract— Neuron specific protein (NSP) has been isolated from cat (NSP-C) and human (NSP-H) brain utilizing the purification procedure described for rat brain 14-3-2 (Marangoset al., 1975a,b,c), a protein which is now designated NSP-R. The protein as isolated from cat and human brain has a molecular weight of approx 80,000 as determined by sedimentation equilibrium. Sedimentation studies done in the presence of 6mg-HCl and 0.2%β mercaptoethanol yields a protomer M.W. of approx 40,000 for both preparations establishing the dimeric nature of each. The subunits appear identical in each case since one band is observed upon electrophoresis of either preparation in the presence of 8 M-urea. NSP-C and NSP-H have identical isoelectric points of 4.7 making them slightly more acidic than NSP-R (pi = 5.0).Comparison of NSP-C and NSP-H with NSP-R and bovine 14-3-2 by electrophoretic and immunological criteria revealed that the cat, human and bovine proteins were very similar. NSP-R can be distinguished from the other three preparations electrophoretically and immunologically. The protomer unit of NSP-R differs in amino acid composition from that of the cat, human or bovine proteins since the former can be completely resolved from any of the latter three preparations on 8 M-urea polyacrylamide gels. The data indicate that NSP and bovine 14-3-2 are probably homologous proteins, and establish the general structural properties of NSP.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1111/j.1471-4159.1977.tb10674.x

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3

Digitale Medien

FUNCTIONAL PROPERTIES OF NEURONAL AND GLIAL ISOENZYMES OF BRAIN ENOLASE (1978)

Marangos, P. J. ; Parma, A. M. ; Goodwin, F. K.

Oxford, UK : Blackwell Publishing Ltd

Journal of neurochemistry 31 (1978), S. 0

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ISSN: 1471-4159

Quelle: Blackwell Publishing Journal Backfiles 1879-2005

Thema: Medizin

Notizen: Two of the major brain enolase (EC 4.2.1.11) isoenzymes exist as cell specific forms. The neuron specific enolase (NSE) is localized in neurons and the non-neuronal enolase (NNE) in glial cells. A third enolase containing one subunit from each of the above species is also present in brain and has been designated hybrid enolase. The stabilities of the brain enolases towards incubation with chloride and bromide salts is markedly different. NNE is rapidly inactivated upon incubation in 0.5 M-KCI or KBr while NSE is minimally effected and the hybrid has an intermediate stability. The inactivation is temperature dependent and reversible by salt removal. Magnesium exerts a stabilizing effect on each enzyme form. The mechanism of the reversible salt inactivation involves dissociation of the enolase subunits with reassociation occurring during reactivation.The brain enolases also display marked stability differences during incubation in 3 M-urea. with the neuronal form again being more stable. The urea inactivation was highly reversible for NNE but only marginally so for NSE. The neuronal enolase is also by far the most stable of the brain enolases at 50°C.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1111/j.1471-4159.1978.tb07847.x

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4

Digitale Medien

The Role of the Lithium Ion in Medicine (1982)

Rosenthal, N E ; Goodwin, F K

Palo Alto, Calif. : Annual Reviews

Annual Review of Medicine 33 (1982), S. 555-568

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ISSN: 0066-4219

Quelle: Annual Reviews Electronic Back Volume Collection 1932-2001ff

Thema: Medizin

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1146/annurev.me.33.020182.003011

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5

Digitale Medien

Characterization of [3H]Ouabain Binding Sites in Human Brain, Platelet, and Erythrocyte (1985)

Hauger, R. ; Luu, H. M. D. ; Goodwin, F. K. ; [weitere]

Oxford, UK : Blackwell Publishing Ltd

Journal of neurochemistry 44 (1985), S. 0

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ISSN: 1471-4159

Quelle: Blackwell Publishing Journal Backfiles 1879-2005

Thema: Medizin

Notizen: [3H]Ouabain binding was investigated in membranes prepared from human brain, erythrocyte, and platelet. Scatchard analysis of [3H]ouabain binding to human hypothalamic membranes revealed a single class of noninteracting binding sites with an apparent affinity constant (KD) of 21 nM. Though the number of [3H]ouabain binding sites was lower in human platelets than in erythrocytes, both tissues exhibited a single class of high-affinity binding sites with an apparent KD similar to that found in human brain. Specific [3H]ouabain binding in basal ganglia tissue from patients with Huntington's disease was more than 50% lower than in tissue from age- and sex-matched controls. These results, along with previous findings in rat brain, suggest that high-affinity [3H]ouabain binding labels the neuronal form of Na,K-ATPase in human brain, and may prove useful in quantitating this enzyme in postmortem brain samples.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1111/j.1471-4159.1985.tb07157.x

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6

Digitale Medien

Characterization of “High-Affinity”[3H]Ouabain Binding in the Rat Central Nervous System (1985)

Hauger, R. ; Luu, H. M. D. ; Meyer, D. K. ; [weitere]

Oxford, UK : Blackwell Publishing Ltd

Journal of neurochemistry 44 (1985), S. 0

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ISSN: 1471-4159

Quelle: Blackwell Publishing Journal Backfiles 1879-2005

Thema: Medizin

Notizen: The characteristics of [3H]ouabain binding were examined in various areas of rat brain. In the striatum, Scatchard analysis revealed a single class of “high-affinity” binding sites with an apparent binding affinity (KD) of 10.4 ± 0.9 nM and an estimated binding capacity (Bmax) of 7.6 ± 1.9 pmol/mg protein. Similar monophasic Scatchard plots were found in the brainstem, cerebellum, hypothalamus, and frontal cerebral cortex. [3H]Ouabain binding to rat brain was sodium- and ATP-dependent and strongly inhibited by potassium. Proscillariden A was the most potent cardiac glycoside tested in inhibiting specific [3H]ouabain binding to brain membranes, and the rank order of inhibitory potencies for a series of cardiac glycosides was similar to that previously reported for inhibition of heart Na,K-ATPase. To assess whether the high-affinity binding sites for [3H]ouabain were localized to neuronal or nonneuronal membranes, the effect of discrete kainic acid lesions on striatal [3H]ouabain binding was examined. Kainic acid lesions of the striatum reduced [3H]ouabain binding to striatal homogenates by 79.6 ± 1.6%. This suggests that the “high-affinity”[3H]ouabain binding sites measured in our experiments are localized to neuronal elements. Thus, the high-affinity binding of [3H]ouabain to brain membranes may selectively label a neuronal form or conformation of Na,K-ATPase.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1111/j.1471-4159.1985.tb07158.x

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7

Digitale Medien

Effect of serum from depressed and manic patients on maze behavior of rats (1972)

Post, R. M. ; Kotin, J. ; Matzen, M. ; [weitere]

Springer

Cellular and molecular life sciences 28 (1972), S. 1471-1472

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ISSN: 1420-9071

Quelle: Springer Online Journal Archives 1860-2000

Thema: Biologie , Medizin

Notizen: Zusammenfassung Serum von depressiven und manischen Patienten und von normalen Kontrollen wurde in die Venen von Ratten injiziert und deren Labyrinthlaufen beobachtet. Bedeutende Unterschiede bei Laufzeit und Fehlern wurden nicht festgestellt.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1007/BF01957859

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8

Digitale Medien

The effect of orally administered cocaine on sleep of depressed patients (1974)

Post, R. M. ; Gillin, J. C. ; Wyatt, R. J. ; [weitere]

Springer

Psychopharmacology 37 (1974), S. 59-66

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ISSN: 1432-2072

Schlagwort(e): Cocaine ; Stimulants ; Depression ; Sleep ; Dreaming ; Electroencephalograph

Quelle: Springer Online Journal Archives 1860-2000

Thema: Medizin

Notizen: Abstract Cocaine was administered orally on a double-blind basis to depressed patients and effects on EEG-monitored sleep were assessed. In doses which did not produce consistent effects on vital signs or mood, cocaine significantly reduced total sleep and rapid eye movement (REM) sleep. The REM sleep supression with cocaine administration and rebound upon cocaine discontinuation was dose related; there was a greater effect at higher doses. Two properties of cocaine appear to closely correspond to those of many other drugs which suppress REM sleep in man—enhancement of functional catecholamines and/or high drug-abuse potential.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1007/BF00426683

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