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  • 1
    Electronic Resource
    Electronic Resource
    Characterization of Transcripts from the Synapsin III Gene Locus (1999)
    Oxford UK : Blackwell Science Ltd.
    Journal of neurochemistry 73 (1999), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract : Synapsin III, the most recently described member of the synapsin gene family, displays a gene structure and protein domain structure similar to those of synapsins I and II. In this report, however, we describe major differences in the temporal- and tissue-specific expressions of synapsin III. Whereas synapsins I and II each give rise to two isoforms that are expressed predominantly in adult brain, there are at least six synapsin III transcripts (synapsin IIIa-IIIf) that differ with respect to tissue- and developmental stage-specific expression. Three of the neuronal transcripts are detected in fetal and to a lesser extent in adult brain (IIIa-IIIc), whereas one (IIId) is detected only in fetal brain. Two additional transcripts (IIIe and IIIf) are detected only in nonneuronal tissues. A putative second promoter, which is contained within an intron in the synapsin III gene locus, appears to generate the nonneuronal synapsin IIIe and IIIf transcripts. This level of genome complexity is far greater than that described previously for the synapsin I and II genes and suggests that synapsin III may have functions distinct from those described for synapsins I and II.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.1999.0732266.x
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  • 2
    Electronic Resource
    Electronic Resource
    Dopamine D1 Receptor-Induced Gene Transcription Is Modulated by DARPP-32 (2000)
    Oxford UK : Blackwell Science Ltd.
    Journal of neurochemistry 75 (2000), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract : The role of the dopamine- and cyclic AMP-regulated phosphoprotein of Mr 32,000 (DARPP-32) in dopaminergic regulation of gene transcription in striatum and globus pallidus was examined. Mice with targeted disruption of the gene encoding DARPP-32, its homologue, inhibitor-1, or both, were used. Pharmacological characterization showed that mutant mice had normal basal levels of dopamine D1 and D2 receptors and adenosine A2A receptors. Basal expression levels of the striatonigral-specific neuropeptides substance P and prodynorphin and the immediate early genes c-fos and NGFI-A were also unaltered in mutant mice. A full D1 receptor agonist, SKF 82958, up-regulated the expression of these neuropeptides and immediate early genes significantly more in wild-type mice than in mice lacking DARPP-32. Moreover, the additive stimulation of SKF 82958 and quinelorane, a D2 receptor agonist, on c-fos mRNA in globus pallidus was significantly decreased in DARPP-32 and DARPP-32/I-1 knockout mice. No changes in dopamine receptor-induced gene expression were found in I-1 knockout mice. These results demonstrate an important involvement of DARPP-32 in dopamine receptor-mediated regulation of gene expression both in striatal neurons, which are enriched in DARPP-32, and in pallidal neurons, which do not contain DARPP-32.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.2000.0750248.x
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  • 3
    Electronic Resource
    Electronic Resource
    A 127-kDa Protein (UV-DDB) Binds to the Cytoplasmic Domain of the Alzheimer's Amyloid Precursor Protein (1999)
    Oxford UK : Blackwell Science Ltd.
    Journal of neurochemistry 72 (1999), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract : Alzheimer amyloid precursor protein (APP) is an integralmembrane protein with a short cytoplasmic domain of 47 amino acids. It ishoped that identification of proteins that interact with the cytoplasmicdomain will provide new insights into the physiological function of APP and,in turn, into the pathogenesis of Alzheimer's disease. To identify proteinsthat interact with the cytoplasmic domain of APP, we employed affinitychromatography using an immobilized synthetic peptide corresponding toresidues 645-694 of APP695 and identified a protein of ~130 kDa inrat brain cytosol. Amino acid sequencing of the protein revealed the proteinto be a rat homologue of monkey UV-DDB (UV-damaged DNA-binding protein,calculated molecular mass of 127 kDa). UV-DDB/p127 co-immunoprecipitated withAPP using an anti-APP antibody from PC12 cell lysates. APP alsoco-immunoprecipitated with UV-DDB/p127 using an anti-UV-DDB/p127 antibody.These results indicate that UV-DDB/p127, which is present in the cytosolicfraction, forms a complex with APP through its cytoplasmic domain. In vitrobinding experiments using a glutathione S-transferase-APP cytoplasmic domain fusion protein and several mutants indicated that the YENPTY motif within the APP cytoplasmic domain, which is important in the internalization of APP and amyloid β protein secretion, may be involved in the interaction between UV-DDB/p127 and APP.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.1999.0720549.x
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  • 4
    Electronic Resource
    Electronic Resource
    Neuron-Specific Phosphorylation of Alzheimer's β-Amyloid Precursor Protein by Cyclin-Dependent Kinase 5 (2000)
    Oxford UK : Blackwell Science Ltd.
    Journal of neurochemistry 75 (2000), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: The mature form of Alzheimer's β-amyloid precursor protein (APP) is phosphorylated specifically at Thr668 in neurons. In mature neurons, phosphorylated APP is detected in neurites, with dephosphorylated APP being found mostly in the cell body. In vitro, active cyclin-dependent kinase 5 (Cdk5) phosphorylated the cytoplasmic domain of APP at Thr668. Treatment of mature neurons with an antisense oligonucleotide to Cdk5 suppressed Cdk5 expression and significantly diminished the level of phosphorylated APP. The expression of APP was unaffected in antisense-treated neurons. These results indicate that in neurons APP is phosphorylated by Cdk5, and that this may play a role in its localization.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.2000.0751085.x
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  • 5
    Electronic Resource
    Electronic Resource
    Regulation of Na+, K+ -ATPase Isoforms in Rat Neostriatum by Dopamine and Protein Kinase C (1999)
    Oxford UK : Blackwell Science Ltd.
    Journal of neurochemistry 73 (1999), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract : Our previous studies showed that dopamine inhibits Na+, K+ -ATPase activity in acutely dissociated neurons from striatum. In the present study, we have found that in this preparation, dopamine inhibited significantly (by ~25%) the activity of the α3 and/or α2 isoforms, but not the α1 isoform, of Na+, K+ -ATPase. Dopamine, via D1 receptors, activates cyclic AMP-dependent protein kinase (PKA) in striatal neurons. Dopamine is also known to activate the calcium- and phospholipid-dependent protein kinase (PKC) in a number of different cell types. The PKC activator phorbol 12,13-dibutyrate reduced the activity of Na+, K+ -ATPase α3 and/or α2 isoforms (by ~30%) as well as the α1 isoform (by ~15%). However, dopamine-mediated inhibition of Na+, K+ -ATPase activity was unaffected by calphostin C, a PKC inhibitor. Dopamine did not affect the phosphorylation of Na+, K+ -ATPase isoforms at the PKA-dependent phosphorylation site. Phorbol ester treatment did not alter the phosphorylation of α2 or α3 isoforms of Na+, K+ -ATPase in neostriatal neurons but did increase the phosphorylation of the α1 isoform. Thus, in rat neostriatal neurons, treatment with either dopamine or PKC activators results in inhibition of the activity of specific (α3 and/or α2) isoforms of Na+, K+ -ATPase, but this is not apparently mediated through direct phosphorylation of the enzyme. In addition, PKC is unlikely to mediate inhibition of rat Na+, K+ -ATPase activity by dopamine in neostriatal neurons.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.1999.0731492.x
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