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  • 1
    Electronic Resource
    Electronic Resource
    Endothelin 1 Stimulates Na+,K+-ATPase and Na+-K+-Cl− Cotransport Through ETA Receptors and Protein Kinase C-Dependent Pathway in Cerebral Capillary Endothelium (1995)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 65 (1995), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: The effect of endothelins (ET-1 and ET-3) on 86Rb+ uptake as a measure of K+ uptake was investigated in cultured rat brain capillary endothelium. ET-1 or ET-3 dose-dependently enhanced K+ uptake (EC50 = 0.60 ± 0.15 and 21.5 ± 4.1 nM, respectively), which was inhibited by the selective ETA receptor antagonist BQ 123 (cyclo-d-Trp-d-Asp-Pro-d-Val-Leu). Neither the selective ETB agonists IRL 1620 [N-succinyl-(Glu9,-Ala11,15)-ET-1] and sarafotoxin S6c, nor the ETB receptor antagonist IRL 1038 [(Cys11,Cys15)-ET-1] had any effect on K+ uptake. Ouabain (inhibitor of Na+,K+-ATPase) and bumetanide (inhibitor of Na+-K+-Cl− cotransport) reduced (up to 40% and up to 70%, respectively) the ET-1-stimulated K+ uptake. Complete inhibition was seen with both agents. Phorbol 12-myristate 13-acetate (PMA), activator of protein kinase C (PKC), stimulated Na+,K+-ATPase and Na+-K+-Cl− cotransport. ET-1-but not PMA-stimulated K+ uptake was inhibited by 5-(N-ethyl-N-isopropyl)amiloride (inhibitor of Na+/H+ exchange system), suggesting a linkage of Na+/H+ exchange with ET-1-stimulated Na+,K+-ATPase and Na+-K+-Cl− cotransport activity that is not mediated by PKC.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.1995.65041588.x
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  • 2
    Electronic Resource
    Electronic Resource
    In Vivo Striatal Dopamine Release by M1 Muscarinic Receptors Is Induced by Activation of Protein Kinase C (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: Abstract: Islet-activating protein was unilaterally microinjected into rat stratum, and a dialysis cannula was implanted into the same area under anesthesia. After 2 days, various agents were perfused continuously into the striatum through the dialysis membrane, under freely moving conditions. Isletactivating protein (2 μg/2 μ1) treatment alone did not change in vivo striatal dopamine (DA) release and metabolism, but completely abolished the increase of striatal DA release evoked in vivo by the M1-selective agonist McN-A-343 (10−7M). Forskolin (10−5M), an adenylate cyclase activator, increased DA release and showed an additive effect on the DA release evoked by McN-A-343. Polymyxin B, a rather selective inhibitor of protein kinase C, decreased DA release and completely blocked the effect of McN-A-343. These results suggest that in vivo striatal DA release elicited by M1 muscarinic receptors is coupled with interaction with a G protein and is induced by activation of protein kinase C.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1990.tb04891.x
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  • 3
    Electronic Resource
    Electronic Resource
    Endothelin-1 Receptor Binding and Cellular Signal Transduction in Cultured Human Brain Endothelial Cells (1994)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 62 (1994), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: The kinetic properties of endothelin-1 (ET-1) binding sites and the production of inositol phosphates (IPs; IP1, IP2, IP3), cyclic AMP, thromboxane B2, and prostaglandin F2α induced by various endothelins (ET-1, ET-2, ET-3, and sarafotoxin S6b) were examined in endothelial cells derived from human brain microvessels (HBECs). The presence of both high- and low-affinity binding sites for ET-1 with KD1 = 122 pM and KD2 = 31 nM, and Bmax1 = 124 fmol/mg of protein and Bmax2 = 909 fmol/mg of protein, respectively, was demonstrated on intact HBECs. ET-1 dose-dependently stimulated IP accumulation with EC50 (IP3) = 0.79 nM, whereas ET-3 was ineffective. The order of potency for displacing ET-1 from high-affinity binding sites (ET-1 〉 ET-2 〉 sarafotoxin S6b 〉 ET-3) correlated exponentially with the ability of respective ligands to induce IP3 formation. ET-1-induced IP3 formation by HBEC was inhibited by the ETA receptor antagonist, BQ123. The protein kinase C activator phorbol myristate ester dose-dependently inhibited the ET-1-stimulated production of IPs, whereas pertussis toxin was ineffective. Cyclic AMP production by HBECs was enhanced by both phorbol myristate ester and ET-1, and potentiated by combined treatment with ET-1 and phorbol myristate ester. Data indicate that protein kinase C plays a role in regulating the ET-1-induced activation of phospholipase C, whereas interaction of different messenger systems may regulate ET-1-induced accumulation of cyclic AMP. ET-1 also stimulated endothelial prostaglandin F2α production, suggesting that activation of phospholipase A2 is most likely secondary to IP3-mediated intracellular calcium mobilization because both ET-1-induced IP3 and prostaglandin F2α were inhibited by BQ123. These findings are the first demonstration of ET-1 (ETA-type) receptors linked to phospholipase C and phospholipase A2 activation in HBECs.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.1994.62020592.x
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  • 4
    Electronic Resource
    Electronic Resource
    Formation of a Persistent Inhibitory State of Brain Adenylate Cyclase by GTP Analogs (1983)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 40 (1983), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Addition of 10μM guanyl-5′-ylimidodiphos phate at 30° or 0° to guinea pig brain particulates instantaneously evoked nearly 50% inhibition of adenylate cyclase activity as determined after removal of the GTP analog by washing of the particulates. The inhibitory state, once formed, persisted for at least 60 min as long as the preparation was kept either in a medium devoid of the analog (0-30°) or in its presence at 0°. During incubation at 30° in the presence of the analog, however, the inhibited or nontreated enzyme showed a gradual increase in enzyme activity. Both the inhibitory and the activating effects of the analog were saturable, with a half-maximal concentration of about 1.0 μM, and were antagonized by simultaneous addition of GTP, GDP, and GMP (in decreasing order). The persistently inhibited enzyme enabled the detection of marked stimulation by norepinephrine and histamine, whereas these amines showed only marginal stimulation of the enzyme before treatment with the analog. Formation of such a persistent inhibitory state appears to be specific to brain cyclase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1983.tb08027.x
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  • 5
    Electronic Resource
    Electronic Resource
    Non-aminergic Effects of Amphetamine on the NMDA Receptor in Primary Cultured Cortical Cells (1996)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 801 (1996), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1996.tb17453.x
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  • 6
    Electronic Resource
    Electronic Resource
    Substrates for adenosine 3′,5′-monophosphate (cAMP)-dependent protein kinase in the rat pituitary gland (1988)
    Springer
    Cellular and molecular neurobiology 8 (1988), S. 71-83 
    Details
    ISSN: 1573-6830
    Keywords: pituitary gland ; adenosine 3′,5′-monophosphate (cAMP) ; protein kinase ; intermediate lobe
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary 1. Substrates for cAMP-dependent protein kinase were investigated in anterior, intermediate, and neural lobes of the rat pituitary gland. In a cell-free assay system, cAMP increased phosphorylation of 17 K, 33 K, and 60 K macromolecules of the anterior lobe, 17 K, 33 K, 60 K, and 80 K macromolecules of the intermediate lobe, and 60 K, 80 K, and 85 K macromolecules of the neural lobe. 2. Other nucleotides were tested in the intermediate lobe; 8 Br-cAMP mimicked cAMP, cGMP was much less effective than cAMP or 8 Br-cAMP, and 5′-AMP showed no significant effect. The purified catalytic subunit of cAMP-dependent protein kinase evoked the same phosphorylation pattern as the endogenous kinase. 3. Maximum cAMP-dependent phosphorylation occurred at between 1 and 2 min of incubation; after 20 min, phosphorylation was reduced by 80%. This suggests the presence of phosphatase activity in the intermediate lobe. 4. When tested upon dispersed intermediate lobe cells permeabilized by high-voltage electrical discharges, cAMP increased phosphorylation of the 17 K and 33 K macromolecules.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00712913
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  • 7
    Electronic Resource
    Electronic Resource
    Effects of Chronic Administration of Interferon α A/D on Serotonergic Receptors in Rat Brain (1999)
    Springer
    Neurochemical research 24 (1999), S. 359-363 
    Details
    ISSN: 1573-6903
    Keywords: Interferon ; neuropsychiatric complications ; depression ; serotonin ; 5-HT7
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The effects of chronic administration of interferon (IFN; recombinant human IFN -αA/D) on serotonergic binding sites in rat brain were investigated. IFN was injected daily for 2 weeks at a dose of 100000 I.U./kg, (i.p.) in male Wistar rats. IFN did not alter either [3H]ketanserin binding to 5-HT2A receptors or [3H]paroxetine binding to 5-HT transporters. Scatchard analysis of [3H]8-hydroxy-dipropylaminotetraline (8-OH-DPAT) binding to 5-HT1A receptors demonstrated the presence of high- and low-affinity binding sites in both treatment and control groups. IFN significantly increased both Kd and Bmax measures of [3H]8-OH-DPAT binding at low-affinity binding sites, but not at the high-affinity sites. These results suggest that IFN affects the low-affinity 5-HT1A receptors sites and may be involved in the development of IFN-induced psychiatric disturbances.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1020929415443
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