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  • 1
    Online Resource
    Online Resource
    San Diego :Elsevier Science & Technology,
    Keywords: Neurobiology. ; Electronic books.
    Type of Medium: Online Resource
    Pages: 1 online resource (455 pages)
    Edition: 1st ed.
    ISBN: 9780080857701
    Series Statement: Issn Series
    DDC: 573.8
    Language: English
    Note: Front Cover -- International Review of Neurobiology, Volume 36 -- Copyright Page -- Contents -- Chapter 1. Ca2+, N-Methyl-D-aspartate Receptors, and AIDS-Related Neuronal Injury -- I. Introduction -- II. Neuronal Loss in the CNS of AIDS Patients -- III. gpl20-Induced Neuronal Injury Is Ameliorated by Calcium Channel Anotagonists -- IV. Involvement of the NMDA Receptor in gpl20-Induced Neuronal Injury -- V. Indirect Neuronal Injury Mediated by HIV-Infected or gp120-Stimulated Monocytic Cells -- VI. Possible Involvement of Astrocytes, Oligodendrocytes, and Other HIV-1 Proteins in Neuronal Injury -- VII. Overstimulation of NMDA Receptors, a Final Common Pathway -- VIII. Development of Clinically Tolerated NMDA Antagonists for HIV-Related Neuronal Injury -- IX. Excitatory Amino Acid Antagonist Treatments on the Horizon -- X. Conclusion -- References -- Chapter 2. Processing of Alzheimer Aβ-Amyloid Precursor Protein: Cell Biology, Regulation, and Role in Alzheimer Disease -- I. Introduction -- II. Alzheimer Disease Is Associated with an Intracranial Amyloidosis -- III. APP Structure Gives Clues to Some of Its Functions -- IV. APP Is Processed via Several Distinct Enzymatic and Subcellular Pathways -- V. "Alternative" Pathways of APP Metabolism Provide Clues to the Source of Aβ-Amyloid -- VI. Aβ-Amyloid Is a Normal Constituent of Body Fluids and the Conditioned Medium of Cultured Cells -- VII. Evidence Suggests the Existence of an Enzyme, β-Secretase, That Cleaves APP at the Amino Terminus of the Aβ-Amyloid Domain -- VIII. APP Mutations in Familial Cerebral Amyloidoses Occur within or near the Aβ-Amyloid Domain, Segregate with Disease in Affected Kindreds, and Yield APP Molecules That Display Some Proamyloidogenic Properties -- IX. Signal Transduction via Protein Phosphorylation Regulates the Relative Utilization of APP Processing Pathways. , X. Beyond Aβ-Amyloid: Other Molecular Factors in Amyloidogenesis and Factors Differentiating Aging-Related Cerebral Amyloidosis from Alzheimer Disease -- References -- Chapter 3. Molecular Neurobiology of the GABAA Receptor -- I. Introduction -- II. Pharmacology of the GABAA Receptor -- III. Biochemistry -- IV. Molecular Cloning of Receptor Subunits -- V. Characterization of the Receptor Family -- VI. The Future -- Reference -- Chapter 4. The Pharmacology and Function of Central GABAB Receptors -- I. Introduction -- II. Pharmacology of GABAB Receptors -- III. Properties of GABAB Receptors -- IV. Function of GABAB Receptors -- V. Summary and Conclusions -- References -- Chapter 5.The Role of the Amygdala in Emotional Learning -- I. Introduction -- II. Morphology -- III. Electrophysiology -- IV. Anatomical Connections between the Amygdala and Brain Areas Involved in Fear and Anxiety -- V. Elicitation of Fear by Electrical or Chemical Stimulation of the Amygdagdala -- VI. Effects of Amygdala Lesions on Conditioned Fear -- VII. Effects of Amygdala Lesions on Unconditioned Fear -- VIII. Effects of Local Infusion of Drugs into the Amygdala on Measures of Fear and Anxiety -- IX. The Role of the Amygdala in Attention -- X. The Amygdala Is Critical for the Fear-Potentiated Startle Effect -- XI. Are Aversive Memories Actually Stored in the Amygdala? -- XII. Is the Amygdala Absolutely Essential for Fear-Potentiated Startle? -- XIII. Can Initial Fear Conditioning Occur without the Amygdala? -- XIV. The Role of Excitatory Amino Acid Receptors in the Amygdala in Fear Conditioning -- XV. Conclusions -- References -- Chapter 6. Excitotoxicity and Neurological Disorders: Involvement of Membrane Phospholipids -- I. Introduction -- II. Classification of Excitatory Amino Acid Receptors. , III. Excitatory Amino Acid Receptors and Neural Membrane Phospholipid Metabolism . . . -- IV. Role of Enhanced Excitatory Amino Acid-Mediated Phospolipid Metabolism in Developing Brain -- V. Possible Mechanism of Cell Injury Caused by Excitatory Amino Acids -- VI. Excitatory Amino Acid Receptors, Phospholipid Metabolism, and Neurological Disorders -- VII. Excitatory Amino Acid Receptor Antagonists and the Treatment of Neurological Disorders -- VIII. Conclusion -- IX. Summary -- References -- Chapter 7. Injury-Related Behavior and Neuronal Plasticity: An Evolutionary Perspective on Sensitization, Hyperalgesia, and Analgesia -- I. Introduction -- II. Evolutionary Considerations -- III. Adaptive Behavioral Reactions to Injury -- IV. Classes of Injury-Related Behavioral Modifiability -- V. Injury Signals -- VI. Mechanisms of Rapid Nociceptive Sensitization -- VII. Mechanisms of Long-Term Nociceptive Sensitization -- VIII. Conclusions -- References -- Index -- Contents of Recent Volumes.
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  • 2
    Electronic Resource
    Electronic Resource
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 94 (1991), S. 4682-4683 
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 96 (1992), S. 7394-7401 
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: We consider the scattering of light from a molecule or a cluster. The scattering may be elastic or inelastic, but we limit ourselves to the special case of transitions from initial states having total angular momentum number J=0 to final states also having J=0. In practice, this covers elastic scattering from clusters as the rotational temperature drops toward absolute zero. This hypothesis allows us to do the orientation average at the amplitude level, a method fundamentally incorrect in the general case. Without approximation, we are able to deduce the pattern of the observable Mueller matrix M of the scattering. We find a new symmetry that reflects the spherical nature of the J=0 states: M11+M33=M22+M44. This result includes all multipole orders of the scattered light, and is therefore valid for clusters large compared to wavelength, as well as for small clusters. In an Appendix, we discuss a new generating function for orientation averages, which allows one to make exact tensor averages weighted by two plane waves (for scattering, one incoming and one outgoing).
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 93 (1990), S. 4493-4493 
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 63 (1994), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: GABAA and benzodiazepine receptors are allosterically coupled, and occupation of either receptor site increases the affinity of the other. Chronic exposure of primary neuronal cultures to benzodiazepine agonists reduces these allosteric interactions. Neurons express multiple GABAA receptor subunits, and it has been suggested that uncoupling is due to changes in the subunit composition of the receptor. To determine if uncoupling could be observed with expression of defined subunits, mouse Ltk− cells stably transfected with GABAA receptors (bovine α1, β1, and γ2L subunits) were treated with flunitrazepam (Flu) or clonazepam. The increase in [3H]Flu binding affinity caused by GABA (GABA shift or coupling) was significantly reduced in cells treated chronically with the benzodiazepines, whereas the KD and Bmax of [3H]Flu binding were unaffected. The uncoupling caused by clonazepam treatment occurred rapidly with a t1/2 of ∼30 min. The EC50 for clonazepam treatment was ∼0.3 µM, and cotreatment with the benzodiazepine antagonist Ro 15-1788 (5.6 µM) prevented the effect of clonazepam. The uncoupling observed in this system was not accompanied by receptor internalization, is unlikely to be due to changes in receptor subunit composition, and probably represents posttranslational changes. The rapid regulation of allosteric coupling by benzodiazepine treatment of the stably transfected cells should provide insights to the mechanisms of coupling between GABAA and benzodiazepine receptors as well as benzodiazepine tolerance.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Chronic ethanol treatment is known to alter the function of the γ-aminobutyric acidA (GABAA) benzodiazepine receptor complex. To determine if genetic differences in development of ethanol dependence are related to expression of GABAA receptor subunits, we measured whole brain levels of mRNA for the α1α3, α6, γ2s, γ2t, and γ3 receptor subunits in withdrawal seizure-prone and -resistant (WSP and WSR, respectively) mice fed an ethanol-containing liquid diet or a control diet Brain poly(A)+ RNA was converted to cDNA and amplified by the polymerase chain reaction using primers conserved among GABAA receptor subunits. Quantification was carried out by densitometric analysis of Southern blots generated using subunit-specific probes. Chronic ethanol treatment decreased the content of α1, mRNA in WSP but not WSR mice and decreased the content of α6 mRNA in WSR but not WSP mice. The content of γ3 mRNA was increased by chronic ethanol in both lines. In untreated mice, the WSP line had lower levels of α3 and α6 mRNA than the WSR line. Thus, a decrease in the content of α1 mRNA is most clearly linked with development of withdrawal signs, although the amounts of α6 and α3 may also be important in the genetic differences between WSP and WSR mice. In contrast, levels of mRNA for γ2S and γ2L subunits do not appear to be altered in ethanol dependence.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The effect of cyclic AMP (cAMP)-dependent protein phosphorylation on γ-aminobutyric acidA (GABAA) receptor function was examined using isolated brain membrane vesicles (microsacs). Muscimol-stimulated 36C1− uptake was studied in mouse brain microsacs permeabilized to introduce the catalytic subunit of cAMP- dependent protein kinase (PKA). At both submaximal and maximally effective concentrations of muscimol, PKA inhibited muscimol-stimulated 36C1− uptake by ∼25%. Jn parallel experiments, PKA and [γ-32P]ATP were introduced into the microsacs, and we attempted to immunoprecipitatc the entire GABAA receptor complex, under nondenaturing conditions, using an anti-α1-subunit antibody. Data from such experiments show that PKA increases the phosphorylation of several microsac proteins, including a 66-kDa polypeptide specifically immunoprecipitated with the GABAA receptor anti-α1 subunit antibody. Phosphopeptide mapping of the 66-kDa polypeptide demonstrated a 14-kDa fragment similar to that obtained with the purified, PKA-phosphorylated GABAA receptor. These results provide evidence that the catalytic subunit of PKA inhibits the function of brain G ABAAreceptors and demonstrate that this functional change is concomitant with an increase in protein phosphorylation.
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: The effect of calcium-phospholipid-dependent protein kinase (PKC) on GABAA receptor function was examined in Xenopus oocytes expressing recombinant human GABAA receptor using two-electrode voltage-clamp measurements. Phorbol 12-myristate 13-acetate (PMA), a potent activator of PKC, inhibited GABA-gated chloride currents by ∼72% in oocytes expressing αlβ1γ2L subunit cDNAs. Phorbol 12-monomyristate (PMM), a negative control analogue of PMA, did not alter GABAA receptor responses. To investigate whether activation of PKC could alter the modulatory responses of the receptor complex, the effect of PMA on benzodiazepine and barbiturate potentiation of GABA responses was assessed. In oocytes expressing αlβ1γ2s subunit cDNAs, diazepam (300 nM) potentiated GABA responses by ∼160%. Following PMA (5-25 nM/) treatment, diazepam potentiation was significantly increased to 333%. No effect of the inactive phorbol ester PMM (25 nM) was observed on diazepam potentiation of GABA responses. PMA enhancement of diazepam potentiation of GABA responses was also observed in oocytes expressing αlβ1γ2Ssubunit cDNAs, indicating that the unique PKC site present in the Tγ2LL subunit is not required for observing the PMA effect. PMA (5-25 nM) also enhanced pentobarbital potentiation of GABA responses. In oocytes expressing αlβ1γ2L subunit cDNAs, pentobarbital (25 μM) potentiated GABA receptor responses by ∼97%. Following treatment with PMA (5-25 nM), pentobarbital potentiation of GABA responses increased to ∼ 156%. The present results suggest that protein phosphorylation may alter the coupling between the allosteric modulatory sites within the GABAA receptor complex.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 60 (1993), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Using receptors expressed from mouse brain mRNA in Xenopus oocytes, we found that enhancement of type A γ-aminobutyric acid (GABAA) receptor-gated Cl− channel response is a common action of structurally diverse anesthetics, suggesting that the GABAA receptor plays an important role in anesthesia. To determine if GABAA receptor subunit composition influences actions of anesthetics, we expressed subunit cRNAs in Xenopus oocytes and measured effects of enflurane on GABA-activated Cl− currents. Potentiation of GABA-activated currents by enflurane was dependent on the composition of GABAA receptor protein subunits; the order of sensitivity was α1β1 〉 α1β1γ2s=α1β1γ2L 〉 total mRNA. The results suggest that anesthetics with simple structures may act on the GABAA receptor protein complex to modulate the Cl− channel activity and provide a molecular explanation for the synergistic clinical interactions between benzodiazepines and general anesthetics.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 58 (1992), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: The effects of acute and extended ethanol exposure on N-methyl-d-aspartate- and kainate-induced currents were examined electrophysiologically in Xenopus oocytes expressing rat hippocampal mRNA. Ethanol inhibited responses stimulated by low and high concentrations of N-methyl-d-aspartate to a similar degree. However, responses produced by low or high concentrations of kainate were differentially inhibited by ethanol. Low kainate concentration responses were much more sensitive to ethanol than high kainate concentrations (e.g., 50 mM ethanol inhibited 12.5 μM kainate responses by 45% compared to 15% inhibition of 400 μM kainate responses). In oocytes cultured in 100 mM ethanol for 1–5 days, the ethanol inhibition of maximum N-methyl-d-aspartate and kainate responses was not different from that in non–ethanol-exposed oocytes. Ethanol treatment, however, selectively decreased the ethanol sensitivity of low kainate concentration responses. Currents stimulated by N-methyl-d-aspartate or kainate were not different between control and ethanol-treated oocytes, indicating that ethanol exposure did not interfere with channel expression. The selective actions of acute and extended ethanol exposure on low kainate responses may indicate selective actions of ethanol on subtypes of kainate receptors expressed in oocytes.
    Type of Medium: Electronic Resource
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