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  • 1
    Online Resource
    Online Resource
    Nicotinic Acetylcholine Receptor Signaling in Neuroprotection (2018)
    Singapore : Springer Singapore Pte. Limited
    Details Availability
    Keywords: Electronic books
    Description / Table of Contents: Intro -- Preface -- Acknowledgement -- Contents -- Chapter 1: Overview -- 1.1 Introduction -- 1.2 Structural and Pharmacological Characterization of Nicotinic Acetylcholine Receptors -- 1.3 Neuroprotection Mediated by Nicotinic Acetylcholine Receptors -- 1.4 Intracellular Signal Transduction Triggered by Nicotinic Acetylcholine Receptors -- 1.5 Acetylcholinesterase Inhibitors Used for Treatment of Alzheimer' Disease -- 1.6 Conclusion -- References -- Chapter 2: In Vivo Imaging of Nicotinic Acetylcholine Receptors in the Central Nervous System -- 2.1 Introduction -- 2.2 Nuclear Medical Imaging Modality -- 2.2.1 Positron Emission Tomography (PET) -- 2.2.2 Single-Photon Emission Computed Tomography (SPECT) -- 2.3 Imaging Probes for Nicotinic Acetylcholine Receptors -- 2.3.1 Imaging Probes for the α4β2 Subtype -- 2.3.1.1 Nicotine Derivatives -- 2.3.1.2 A-85380 Derivatives -- A-85380-Derived SPECT Probe -- A-85380-Derived PET Probes -- 2.3.1.3 Epibatidine Derivatives -- 2.3.2 Imaging Probes for the α7 Subtype -- 2.4 Nicotinic Acetylcholine Receptor Imaging in Human Brain -- 2.4.1 (S)-11C-Nicotine -- 2.4.2 123I-5IA -- 2.4.3 18F-2FA -- 2.4.4 (−)-18F-Flubatine -- 2.4.5 α7-nAChR Imaging Probes -- 2.5 Alteration of Nicotinic Acetylcholine Receptor Density -- 2.5.1 Alzheimer's Disease (AD) -- 2.5.2 Other Causes of Dementia -- 2.5.3 Parkinson's Disease (PD) -- 2.5.4 Other Diseases -- 2.5.4.1 Alcohol Abuse -- 2.5.4.2 Autosomal Dominant Nocturnal Frontal Lobe Epilepsy -- 2.5.4.3 Major Depressive Disorders -- 2.5.5 Smokers -- 2.6 Nicotinic Acetylcholine Receptor Imaging in Mouse Brain -- References -- Chapter 3: A New Aspect of Cholinergic Transmission in the Central Nervous System -- 3.1 Introduction -- 3.2 Intracellular Distribution of AChRs -- 3.2.1 Muscarinic AChRs -- 3.2.2 Nicotinic AChRs -- 3.3 Incorporation of ACh into Postsynaptic Neurons.
    Type of Medium: Online Resource
    Pages: 1 online resource (196 pages)
    ISBN: 9789811084881
    URL: https://ebookcentral.proquest.com/lib/kxp/detail.action?docID=6422622
    Language: English
    Note: Description based on publisher supplied metadata and other sources
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  • 2
    Online Resource
    Online Resource
    Nicotinic Acetylcholine Receptor Signaling in Neuroprotection (2018)
    Singapore : Springer
    Details Availability
    Keywords: Medicine ; Biomedicine ; Toxicology ; Pharmacology ; Neurosciences ; Neurology ; Receptors, Nicotinic metabolism ; Signal Transduction physiology ; Neuroprotective Agents
    Description / Table of Contents: This open access book presents the roles and mechanisms of signal transduction triggered by nicotinic acetylcholine receptors (nAChRs) stimulation in neuroprotection against toxic effects of risk factors of neurodegenerative diseases. Accumulating evidence suggests that nAChRs in the CNS play important roles not only in excitatory neurotransmission but also in neuronal survival and related functions. Neuroprotection mediated by nAChRs in neurodegenerative diseases such as Alzheimer's disease is the major topic of this book. In response to rapidly evolving areas in clinical and laboratory neuropharmacology and neurochemistry, this volume provides in-depth coverage of neuroprotection in basic research and future developments in the clinical application of effective neuroprotective strategies in neurodegenerative diseases. This work appeals to both basic and clinical researchers in several fields, such as neuroscience, neurology, and pharmacology. This book is published with open access under a CC BY 4.0 license
    Type of Medium: Online Resource
    Pages: Online-Ressource (X, 191 p. 62 illus., 20 illus. in color, online resource)
    ISBN: 9789811084881
    Series Statement: SpringerLink
    URL: http://dx.doi.org/10.1007/978-981-10-8488-1
    URL: https://doi.org/10.1007/978-981-10-8488-1
    DOI: 10.1007/978-981-10-8488-1
    Language: English
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  • 3
    Electronic Resource
    Electronic Resource
    Different Modulation of Protein Kinase C Isozymes in Dibutyryl Cyclic AMP-Differentiated PC12h Cells (1994)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 63 (1994), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: PC12h cells can be differentiated into sympathetic neuron-like cells by various agents, including nerve growth factor, basic fibroblast growth factor, cyclic AMP analogues, and protein kinase C (PKC) activators. To study the involvement of PKC in the process of PC12h cell differentiation by cyclic AMP treatment, PKC isozymes (α, βI, βII, and γ) were analyzed using column chromatography and immunoblotting. Two PKC isozymes, PKC(α) and PKC(βII), were predominantly detected in PC12h cells. When stimulated by dibutyryl cyclic AMP, PKC(α) levels declined in the cytosolic fraction of the cells, whereas PKC(βII) levels increased. Increased PKC(βII) levels were also detected in the particulate fraction, whereas particulate PKC(α) levels did not change. The total PKC activity decreased in the cytosolic fraction following cyclic AMP stimulation of PC12h cells, whereas it stayed constant in the particulate fraction. Fractionation on a hydroxyapatite column showed a decreased level of PKC(α) activity and a transient increase followed by a decreased level of PKC(βII) activity. This discrepancy between increased PKC(βII) immunoreactivity and reduced PKC(βII) activity suggested the presence of nonactivatable PKC(βII) in cyclic AMP-treated PC12h extract. These findings indicate that PKC(α) and PKC(βII) are differentially regulated during the differentiation of PC12h cells. In addition, the differentiation of PC12h cells triggered by cyclic AMP seems to involve characteristic alterations of PKC isozymes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.1994.63010125.x
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  • 4
    Electronic Resource
    Electronic Resource
    Ca2+-Dependent and Ca2+-Independent Protein Kinase C Changes in the Brains of Patients with Alzheimer's Disease (1996)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 67 (1996), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: We examined protein kinase C (PKC) activity in Ca2+-dependent PKC (Ca2+-dependent PKC activities) and Ca2+-independent PKC (Ca2+-independent PKC activities) assay conditions in brains from Alzheimer's disease (AD) patients and age-matched controls. In cytosolic and membranous fractions, Ca2+-dependent and Ca2+-independent PKC activities were significantly lower in AD brain than in control brain. In particular, reduction of Ca2+-independent PKC activity in the membranous fraction of AD brain was most enhanced when cardiolipin, the optimal stimulator of PKC-ε, was used in the assay; whereas Ca2+-independent PKC activity stimulated by phosphatidylinositol, the optimal stimulator of PKC-δ, was not significantly reduced in AD. Further studies on the protein levels of Ca2+-independent PKC-δ, PKC-ε, and PKC-ζ in AD brain revealed reduction of the PKC-ε level in both cytosolic and membranous fractions, although PKC-δ and PKC-ζ levels were not changed. These findings indicated that Ca2+-dependent and Ca2+-independent PKC are changed in AD, and that among Ca2+-independent PKC isozymes, the alteration of PKC-ε is a specific event in AD brain, suggesting its crucial role in AD pathophysiology.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.1996.67010317.x
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  • 5
    Electronic Resource
    Electronic Resource
    Biochemical Characterization of α-Adrenergic Receptors in Human Brain and Changes in Alzheimer-Type Dementia (1986)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 47 (1986), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract Using ligand binding techniques, we studied α-adrenergic receptors in brains obtained at autopsy from seven histologically normal controls and seven patients with histopathologically verified Alzheimer-type dementia (ATD). Binding of the α-adrenergic antagonists [3H]prazosin and [3H]yohimbine to membranes of human brains exhibited characteristics compatible with α1- and α2-adrenergic receptors, respectively. Binding of both ligands was saturable and reversible, with dissociation constants of 0.15 nM for [3H]prazosin and 5.5 nM for [3H]yohimbine. [3H]Prazosin binding was highest in the hippocampus and frontal cortex and lowest in the caudate and putamen in the control brains. [3H]Yohimbine binding was highest in the nucleus basalis of Meynert (NbM) and frontal cortex and lowest in the caudate and cerebellar hemisphere in the control brains. Compared with values for the controls, [3H]prazosin binding sites were significantly reduced in number in the hippocampus and cerebellar hemisphere, and [3H]yohimbine binding sites were significantly reduced in number in the NbM in the ATD brains. These results suggest that α1 and α2-adrenergic receptors are present in the human brain and that there are significant changes in numbers of both receptors in selected regions in patients with ATD.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1986.tb00753.x
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  • 6
    Electronic Resource
    Electronic Resource
    Changes in Nicotinic and Muscarinic Cholinergic Receptors in Alzheimer-Type Dementia (1986)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 46 (1986), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Nicotinic and muscarinic cholinergic receptors were studied in autopsied brains from four histologically normal controls and five histopathologically verified cases of Alzheimer-type dementia (ATD), using ligand binding techniques. Nicotinic and muscarinic cholinergic receptors were assessed by (–)-[3H]nicotine and [3H]quinuclidinyl benzilate ([3H]QNB), respectively. Compared with the controls, (–)-[3H]nicotine binding sites in the ATD brain regions examined were significantly reduced in the putamen and the nucleus basalis of Meynert (NbM). [3H]QNB binding was significantly reduced in the hippocampus and NbM. These findings suggest that there are significant changes of nicotinic and muscarinic cholinergic receptors in selected regions of ATD brains.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1986.tb12960.x
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  • 7
    Electronic Resource
    Electronic Resource
    Alteration of Phospholipase C-δ Protein Level and Specific Activity in Alzheimer's Disease (1995)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 64 (1995), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Phosphoinositide-specific phospholipase C (PLC) is a key enzyme in signal transduction. We have previously demonstrated that an antibody to an isozyme of PLC, PLC-δ, produced intense staining of neurofibrillary tangles in the brains of patients with Alzheimer's disease. In the present study, we investigated the protein level and activity of this enzyme in control and Alzheimer brains. Western blot analysis using a specific antibody for PLC-δ showed that the concentration of PLC-δ protein was significantly higher in the cytosolic fraction of Alzheimer's disease cortical tissue than in control brains. The activity of PLC-δ, which hydrolyzes phosphatidylinositol, was also investigated, and we found that PLC-δ activity was not significantly different in the Alzheimer and control cytosolic fractions. These results indicate that the specific activity of PLC-δ is decreased in Alzheimer brains and suggest that inactivation of PLC-δ might be related to the pathophysiology of this disease.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.1995.64062629.x
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  • 8
    Electronic Resource
    Electronic Resource
    [3H]N-[1-(2-Thienyl)cyclohexyl]-3,4-Piperidine ([3H]TCP) Binding in Human Frontal Cortex: Decreases in Alzheimer-Type Dementia (1990)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 54 (1990), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: We studied [3H]N-[1-(2-thienyl)cyclohexyl]-3,4-piperidine ([3H]TCP) binding to human frontal cortex obtained at autopsy from 10 histologically normal controls and eight histopathologically verified cases with Alzheimer-type dementia (ATD). Extensively washed membrane preparations were used to minimize the effects of endogenous substances. In ATD frontal cortex, the total concentration (Bmax) of [3H]TCP binding sites was significantly reduced by 40–50%. The apparent dissociation constant (KD) values showed no significant change. The reduction in binding capacity was also apparent in Triton X-100–treated membrane preparations, and there was a linear correlation between the number of [3H]TCP binding sites and that of N-methyl-D-aspartate (NMDA)-sensitive [3H]glutamate binding sites. [3H]TCP binding sites spared in ATD brains retained the affinity for the ligand and the reactivity to NMDA, L-glutamate, and glycine. These results suggest that the primary change in NMDA receptor-ion channel complex in ATD brains is the reduction of its number, possibly reflecting the loss of neurons bearing these receptor complexes, and that the functional linkage within the receptor complexes spared in ATD brains remains normal.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1990.tb01903.x
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  • 9
    Electronic Resource
    Electronic Resource
    Changes in β-Adrenergic Receptor Subtypes in Alzheimer-Type Dementia (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: Using ligand binding techniques, we studied β-adrenergic receptor subtypes in brains obtained at autopsy from seven histologically normal controls and seven histopathologically verified cases with Alzheimer-type dementia (ATD). Inhibition of [3H]dihydroalprenolol ([3H]DHA) binding by the selective β, antagonist, metoprolol, results in nonlinear Hofstee plots, suggesting the presence of the two receptor subtypes in the human brain. The calculated ratios of β1/β2-adrenergic receptors in control brains are as follows: frontal cortex, 49:51; temporal cortex, 31:69; hippocampus, 66:34; thalamus, 23:77; putamen, 70:30; caudate, 48:52; nucleus basalis of Meynert (NbM), 43:57; cerebellar hemisphere, 25:75. Compared with the controls, total concentrations of β-adrenergic receptors were significantly reduced only in the thalamus of the ATD brains. β1-Adrener gic receptor concentrations were significantly reduced in the hippocampus and increased in the NbM and cerebellar hemisphere, whereas β2-adrenergic receptor concentrations were significantly reduced in the thalamus, NbM, and cerebellar hemisphere and increased in the hippocampus and putamen of the ATD brains. These results suggest that β1-and β2-adrenergic receptors are present in the human brain and that there are significant changes in both receptor subtypes in selected brain regions in patients with ATD.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1987.tb05649.x
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  • 10
    Electronic Resource
    Electronic Resource
    Neuroprotective Mechanism of Glial Cell Line-Derived Neurotrophic Factor in Mesencephalic Neurons (2000)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 74 (2000), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Glial cell line-derived neurotrophic factor (GDNF) provides neuroprotection, but its neuroprotective mechanism has not been resolved. We investigated the neuroprotective mechanism of GDNF using primary culture of the rat mesencephalon. Bleomycin sulfate (BLM) and L-buthionine-[S,R]-sulfoximine (BSO) caused apoptosis in both dopaminergic and nondopaminergic neurons, as revealed by the presence of chromatin condensation, and positive staining by terminal deoxynucleotidyl transferase-mediated deoxyuridine triphosphate nick end-labeling (TUNEL). GDNF preincubation blocked the neurotoxicity and reduced the number of the TUNEL-positive cells caused by BLM and BSO exposure. In contrast, GDNF did not provide neuroprotection against glutamate toxicity, which was not accompanied by these apoptotic features. The neuroprotection was mediated by phosphatidylinositol 3-kinase, an effector downstream from c-Ret, because it was blocked by LY294002. GDNF pretreatment caused up-regulation of Bcl-2 and Bcl-x. Furthermore, GDNF suppressed oxygen radical accumulation caused by BLM. Apoptosis induced by BLM and BSO was blocked by a caspase-3 inhibitor. Caspase-3 activity was elevated by BLM and suppressed by GDNF pretreatment. These findings indicate that GDNF has no effect on necrosis but exerts protection against apoptosis by activation of phosphatidylinositol 3-kinase and the subsequent up-regulation of Bcl-2 and Bcl-x, which suppresses accumulation of oxygen radicals followed by caspase-3 activation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.2000.741175.x
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