GLORIA

GEOMAR Library Ocean Research Information Access

feed icon rss

Ihre E-Mail wurde erfolgreich gesendet. Bitte prüfen Sie Ihren Maileingang.

Leider ist ein Fehler beim E-Mail-Versand aufgetreten. Bitte versuchen Sie es erneut.

Vorgang fortführen?

Exportieren
  • 1
    Online-Ressource
    Online-Ressource
    San Diego :Elsevier Science & Technology,
    Schlagwort(e): Calcium in the body. ; Electronic books.
    Materialart: Online-Ressource
    Seiten: 1 online resource (417 pages)
    Ausgabe: 1st ed.
    ISBN: 9780080552736
    Serie: Issn Series
    Sprache: Englisch
    Anmerkung: Front Cover -- Calcium Regulation of Cellular Function -- Copyright Page -- Contents -- Contributing Authors -- Preface -- Chapter 1. Intracellular Calcium Waves -- Chapter 2. Regulation of Calcium Channels in the Heart -- Chapter 3. Determinants that Govern High Affinity Calcium Binding -- Chapter 4. Calcium Regulation of Smooth Muscle Contractile Proteins -- Chapter 5. Calcium-Dependent Protein Kinases in Learning and Memory -- Chapter 6. Calcium-Dependent Regulation of Protein Synthesis -- Chapter 7. Calcium Regulation of Gene Expression -- Chapter 8. Calcium Regulation of Apoptosis -- Chapter 9. Role of Calcium in T-Lymphocyte Activation -- Chapter 10. Regulation of the Cell Division Cycle by Inositol Triphosphate and the Calcium Signalling Pathway -- Chapter 11. The Regulation of Calcium in Paramecium -- Chapter 12. Calcium in Saccharomyces cerevisiae -- Chapter 13. Calcium Regulation of Drosophila Development -- Subject Index.
    Standort Signatur Einschränkungen Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 2
    Online-Ressource
    Online-Ressource
    San Diego :Elsevier Science & Technology,
    Schlagwort(e): Periodicals. ; Electronic books.
    Materialart: Online-Ressource
    Seiten: 1 online resource (339 pages)
    Ausgabe: 1st ed.
    ISBN: 9780080526454
    Serie: Issn Series
    DDC: 571.6
    Sprache: Englisch
    Anmerkung: Front Cover -- Ion Channel Regulation -- Copyright Page -- Contents -- Contributing Authors -- Prologue -- Part I: Protein Phosphorylation -- Chapter 1. Modulation of Ion Channels by Protein Phosphorylation: How the Brain Works -- Chapter 2. Regulation of Voltage-Sensitive Sodium and Calcium Channels by Phosphorylation -- Chapter 3. Regulation of Ligand-Gated Ion Channels by Protein Phosphorylation -- Chapter 4. Regulation of CFTR C1-Ion Channels by Phosphorylation and Dephosphorylation -- Chapter 5. Ion Channels as Physiological Effectors for Growth Factor Receptor and Ras/ERK Signaling Pathways -- Part II: Closely Associated Proteins -- Chapter 6. Voltage-Dependent Modulation of N-Type Calcium Channels: Role of G Protein Subunits -- Chapter 7. L-Type Calcium Channel Modulation -- Chapter 8. G Protein Gated Potassium Channels -- Chapter 9. The Company They Keep: Ion Channels and Their Intracellular Regulatory Partners -- Part III: Second Messengers -- Chapter 10. Cyclic Nucleotide Gated Channels -- Chapter 11. Cyclic GMP and Ion Channel Regulation -- Chapter 12. Store-Operated Calcium Channels -- Subject Index.
    Standort Signatur Einschränkungen Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 3
    Publikationsdatum: 2022-05-25
    Beschreibung: Author Posting. © Society for Neuroscience, 2005. This article is posted here by permission of Society for Neuroscience for personal use, not for redistribution. The definitive version was published in Journal of Neuroscience 25 (2005): 2658-2669, doi:10.1523/JNEUROSCI.4278-04.2005.
    Beschreibung: Synapsins are a family of neuron-specific phosphoproteins that regulate neurotransmitter release by associating with synaptic vesicles. Synapsins consist of a series of conserved and variable structural domains of unknown function. We performed a systematic structure-function analysis of the various domains of synapsin by assessing the actions of synapsin fragments on neurotransmitter release, presynaptic ultrastructure, and the biochemical interactions of synapsin. Injecting a peptide derived from domain A into the squid giant presynaptic terminal inhibited neurotransmitter release in a phosphorylation-dependent manner. This peptide had no effect on vesicle pool size, synaptic depression, or transmitter release kinetics. In contrast, a peptide fragment from domain C reduced the number of synaptic vesicles in the periphery of the active zone and increased the rate and extent of synaptic depression. This peptide also slowed the kinetics of neurotransmitter release without affecting the number of docked vesicles. The domain C peptide, as well as another peptide from domain E that is known to have identical effects on vesicle pool size and release kinetics, both specifically interfered with the binding of synapsins to actin but not with the binding of synapsins to synaptic vesicles. This suggests that both peptides interfere with release by preventing interactions of synapsins with actin. Thus, interactions of domains C and E with the actin cytoskeleton may allow synapsins to perform two roles in regulating release, whereas domain A has an actin-independent function that regulates transmitter release in a phosphorylation-sensitive manner.
    Beschreibung: This work was supported by grants from The Fisher Center for Alzheimer’s Disease Research (P.G., F.B.), National Institutes of Health Grants NS-21624 (G.J.A.) and MH39327 (P.G.), the Italian Ministry of Education (F.B.), Consorzio Italiano Biotecnologie (F.B.), and a Ramon y Cajal fellowship (S.H.).
    Schlagwort(e): Synapsin ; Release ; Regulation ; Neurotransmitter ; Actin ; Cytoskeleton ; Depression
    Repository-Name: Woods Hole Open Access Server
    Materialart: Article
    Format: application/pdf
    Standort Signatur Einschränkungen Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 4
    ISSN: 1471-4159
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: Abstract: DARPP-32 (dopamine- and cyclic AMP-regulated phosphoprotein of Mr= 32,000) and phosphatase inhibitor-1, two previously characterized inhibitors of protein phosphatase-1, were identified in both the neostriatum and the substantia nigra. Phosphatase inhibitor-1 was partially purified from bovine caudate nucleus and found to be distinct from DARPP-32 in some of its biochemical properties. The neuronal localization of DARPP-32 and phosphatase inhibitor-1 within the rat neostriatum and substantia nigra was investigated by studying the effects of kainic acid. Injection into the neostriatum of kainic acid, which destroys striatonigral neurons and striatonigral fibers, decreased the amounts of DARPP-32 and phosphatase inhibitor-1 to the same extent, both in the lesioned neostriatum and in the ipsilateral substantia nigra. The specific activity of protein phosphatase-1 in the neostriatum was unaffected by kainic acid. The results indicate that, in rat brain, DARPP-32 and phosphatase inhibitor-1 are both present in striatal neurons and in striatonigral fibers, and that they probably coexist in at least a subpopulation of striatonigral neurons. In contrast, protein phosphatase-1 does not appear to be enriched in any specific neuronal subpopulation in the neostriatum.
    Materialart: Digitale Medien
    Standort Signatur Einschränkungen Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 5
    ISSN: 1471-4159
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: Abstract: The distribution of inhibitor-1, a cyclic AMP-regulated inhibitor of protein phosphatase-1, was analyzed in various brain regions and peripheral tissues of various species by immunolabeling of sodium dodecyl sulfate-polyacrylamide gel transfers using specific antibodies. The distribution of inhibitor-1 was directly compared to that of DARPP-32, a structurally related cyclic AMP-regulated inhibitor of protein phosphatase-1. In rat CNS, a single immunoreactive protein of Mr 30,000, identified as inhibitor-1, was widely distributed. In contrast, DARPP-32 was highly concentrated in the basal ganglia. Inhibitor-1 was detected in brain tissue from frog (Mr 27,000), turtle (Mr 29,000/33,000), canary (Mr 26,000), pigeon (Mr 28,000), mouse (Mr 30,500), rabbit (Mr 26,500), cow (Mr 27,000), and monkey (Mr 27,500), but not from goldfish. Inhibitor-1 was detected at various levels in most peripheral tissues of the species studied; however, it was not detectable in certain tissues of particular species (e.g., rat and cow liver). DARPP-32 was detected in brain tissue of all the species tested except frog and goldfish, but was not detectable in most peripheral tissues. Both inhibitor-1 and DARPP-32 were concentrated in the cytosol and synaptosomal cytosol of rat striatum. The developmental expressions of inhibitor-1 and DARPP-32 in rat striatum differed: the level of inhibitor-1 peaked in the first postnatal week and then declined by the third postnatal week, whereas the level of DARPP-32 increased to a peak level by the third postnatal week and remained elevated thereafter. Because inhibitor-1 and DARPP-32 have distinct but partially overlapping regional distributions and developmental expression in rat CNS and have distinct tissue distributions in a number of species, it appears that their functions are not fully interchangeable.
    Materialart: Digitale Medien
    Standort Signatur Einschränkungen Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 6
    ISSN: 1471-4159
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: Abstract: Treatment of PC12 cells with nerve growth factor (NGF), epidermal growth factor (EGF), or agents that raise intracellular cyclic AMP (cAMP) levels (e.g., forskolin) reduces the activity of calmodulin-dependent protein kinase III (CaM-PK III) over a period of 8 h. The mechanism of this effect of NGF has now been examined in more detail, making use of a mutant PC12 cell line (A126-1B2) that is deficient in cAMP-dependent protein kinase activity. Control experiments showed that A 126-1B2 cells retain other NGF-mediated responses (e.g., the induction of ornithine decarboxylase, a cAMP-independent event) and contain a complement of CaM-PK III and its substrate, elongation factor-2, comparable to that of wild-type cells. The ability of NGF or forskolin, but not of EGF, to down-regulate CaM-PK III was markedly attenuated in A 126-1B2 compared to wildtype cells. Treatment of wild-type cells with the cAMP phosphodiesterase inhibitor, isobutylmethylxanthine, enhanced the effects of NGF, but not of EGF. The possibility that NGF led to a stimulation of cAMP-dependent protein kinase activity in wild-type cells was assessed by measurement of the “activation ratio’(-cAMP/+cAMP) of this enzyme before and at various times after NGF addition. A small, but significant, increase in the activation ratio from 0.3 to 0.48 was observed, reaching a peak 5 min after NGF treatment. EGF had no effect on the activation ratio in wild-type cells. These experiments support the hypothesis that NGF, but not EGF, achieves its effects on CaM-PK III by activation of a cAMP-dependent protein kinase and suggest that other actions of NGF may be mediated by the same mechanism.
    Materialart: Digitale Medien
    Standort Signatur Einschränkungen Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 7
    Digitale Medien
    Digitale Medien
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Pharmacology 44 (2004), S. 269-296 
    ISSN: 0362-1642
    Quelle: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Thema: Medizin , Chemie und Pharmazie
    Notizen: Dopamine- and cAMP-regulated phosphoprotein, Mr 32 kDa (DARPP-32), was identified initially as a major target for dopamine and protein kinase A (PKA) in striatum. However, recent advances now indicate that regulation of the state of DARPP-32 phosphorylation provides a mechanism for integrating information arriving at dopaminoceptive neurons, in multiple brain regions, via a variety of neurotransmitters, neuromodulators, neuropeptides, and steroid hormones. Activation of PKA or PKG stimulates DARPP-32 phosphorylation at Thr34 and thereby converts DARPP-32 into a potent inhibitor of protein phosphatase-1 (PP-1). DARPP-32 is also phosphorylated at Thr75 by Cdk5 and this converts DARPP-32 into an inhibitor of PKA. Thus, DARPP-32 has the unique property of being a dual-function protein, acting either as an inhibitor of PP-1 or of PKA. The state of phosphorylation of DARPP-32 at Thr34 depends on the phosphorylation state of two serine residues, Ser102 and Ser137, which are phosphorylated by CK2 and CK1, respectively. By virtue of its ability to modulate the activity of PP-1 and PKA, DARPP-32 is critically involved in regulating electrophysiological, transcriptional, and behavioral responses to physiological and pharmacological stimuli, including antidepressants, neuroleptics, and drugs of abuse.
    Materialart: Digitale Medien
    Standort Signatur Einschränkungen Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 8
    Digitale Medien
    Digitale Medien
    s.l. : American Chemical Society
    Biochemistry 26 (1987), S. 4471-4474 
    ISSN: 1520-4995
    Quelle: ACS Legacy Archives
    Thema: Biologie , Chemie und Pharmazie
    Materialart: Digitale Medien
    Standort Signatur Einschränkungen Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 9
    ISSN: 1471-4159
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: Spinophilin is a protein phosphatase-1 (PP-1)- and actin-binding protein that is enriched in dendritic spines. Phosphorylation of the actin-binding domain of rat spinophilin at one or more sites by protein kinase A (PKA) inhibits actin binding. Here, we investigated the regulation of mouse spinophilin that contains only a single PKA-site (Ser94) within its actin-binding domain. In vitro phosphorylation of Ser94 resulted in the dissociation of spinophilin from actin filaments. In mouse neostriatal slices, phospho-Ser94 (p-Ser94) was dephosphorylated mainly by PP-1 and also by PP-2A. Activation of dopamine D1 receptors in striatonigral medium spiny neurons, and of adenosine A2A receptors in striatopallidal medium spiny neurons increased, whereas activation of dopamine D2 receptors in striatopallidal neurons decreased, spinophilin Ser94 phosphorylation. In neostriatal slices from DARPP-32 (dopamine- and cAMP-regulated phosphoprotein of 32 kDa) knockout mice, the effects of D1, D2 and A2A receptors were largely attenuated. Activation of NMDA receptors decreased Ser94 phosphorylation in a PP-2A-dependent, but DARPP-32-independent, manner. These results suggest that PKA-dependent phosphorylation of spinophilin at Ser94 in both striatonigral and striatopallidal neurons requires synergistic contributions from the PKA and DARPP-32/PP-1 pathways. In addition, PP-2A plays a role in Ser94 dephosphorylation in response to activation of both D2 and NMDA receptors.
    Materialart: Digitale Medien
    Standort Signatur Einschränkungen Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 10
    ISSN: 1471-4159
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: Methylphenidate (MPH), a dopamine uptake inhibitor, is the most commonly prescribed drug for the treatment of attention-deficit/hyperactivity disorder (ADHD) in children. We examined the effect of MPH on dopamine- and cAMP-regulated phosphoprotein, Mr 32 kDa (DARPP-32) phosphorylation at Thr34 (PKA-site) and Thr75 (Cdk5-site) using neostriatal slices from young (14–15- and 21–22-day-old) and adult (6–8-week-old) mice. MPH increased DARPP-32 Thr34 phosphorylation and decreased Thr75 phosphorylation in slices from adult mice. The effect of MPH was blocked by a dopamine D1 antagonist, SCH23390. In slices from young mice, MPH did not affect DARPP-32 phosphorylation. As with MPH, cocaine stimulated DARPP-32 Thr34 phosphorylation in slices from adult, but not from young mice. In contrast, a dopamine D1 agonist, SKF81297, regulated DARPP-32 phosphorylation comparably in slices from young and adult mice, as did methamphetamine, a dopamine releaser. The results suggest that dopamine synthesis and the dopamine transporter are functional at dopaminergic terminals in young mice. In contrast, the lack of effect of MPH in young mice is likely attributable to immature development of the machinery that regulates vesicular dopamine release.
    Materialart: Digitale Medien
    Standort Signatur Einschränkungen Verfügbarkeit
    BibTip Andere fanden auch interessant ...
Schließen ⊗
Diese Webseite nutzt Cookies und das Analyse-Tool Matomo. Weitere Informationen finden Sie hier...