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  • 1
    Digitale Medien
    Digitale Medien
    Concerted CMP-Dependent [3H]Inositol Labeling of Phosphoinositides and Agonist Activation of Phospholipase C in Rat Brain Cortical Membranes (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 58 (1992), S. 0 
    Details
    ISSN: 1471-4159
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: Abstract: [3H]Inositol ([3H]Ins) labeling of phosphoinositides was studied in rat brain cortical membranes. [3H]Ins was incorporated into a common lipid pool through both CMP-dependent and independent mechanisms. These are as follows: (1) a reverse reaction catalyzed by phosphatidyl-inositol (PtdIns) synthase, and (2) the reaction performed by the PtdIns headgroup exchange enzyme, respectively. Membrane phosphoinositides prelabeled in either CMP-dependent or independent fashions were hydrolyzed by guan-osine 5′-O-(3-thiotriphosphate) (GTPγS)- and carbachol-stimulated phospholipase C. Unlike CMP-dependent labeling, however, CMP-independent incorporation of [3H]Ins into lipids was inhibited by 1 mM (0.04%) sodium deoxy-cholate. Thus, when PtdIns labeling and phospholipase C stimulation were studied in a concerted fashion, [3H]Ins was incorporated into lipids primarily through the Ptdlns synthase-catalyzed reaction because of the presence of deoxy-cholate required to observe carbachol-stimulation of phospholipase C. Little direct breakdown of [3H]PtdIns was detected because production of myo-[3H]inositol 1-mono- phosphate was minimal and myo-[3H]inositol 1,4-bisphos-phate was the predominant product. Although PtdIns labeling and 3Hpolyphosphoinositide formation were unaffected by GTPγS and carbachol and had no or little lag period, GTPγS- and carbachol-stimulated appearance of 3H-Ins phosphates exhibited an appreciable lag (10 min). Also, flux of label from [3H]Ins to 3H-Ins phosphates was restricted to a narrow range of free calcium concentrations (10–300 nM). These results show the concerted activities of Ptdlns synthase, Ptdlns 4-kinase, and phospholipase C, and constitute a simple assay for guanine nucleotide-dependent agonist stimulation of phospholipase C in a brain membrane system using [3H]Ins as labeled precursor.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1471-4159.1992.tb10958.x
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  • 2
    Digitale Medien
    Digitale Medien
    Silicon-directed Nazarov cyclizations. 8. Stereoelectronic control of torquoselectivity (1990)
    s.l. : American Chemical Society
    The @journal of organic chemistry 55 (1990), S. 5543-5545 
    Details
    ISSN: 1520-6904
    Quelle: ACS Legacy Archives
    Thema: Chemie und Pharmazie
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1021/jo00308a001
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  • 3
    Digitale Medien
    Digitale Medien
    Transmembrane signaling through phospholipase C in human cortical membranes (1993)
    Springer
    Neurochemical research 18 (1993), S. 139-145 
    Details
    ISSN: 1573-6903
    Schlagwort(e): Phospholipase C ; dopamine ; serotonin ; carbachol ; Parkinson's disease ; Alzheimer's disease ; schizophrenia ; G proteins
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Abstract Stimulation of phosphoinositide-specific phospholipase C (PLC) by carbachol, dopamine and serotonin was measured by supplying exogenous [3H]phosphatidylinositol 4,5-bisphosphate to membranes prepared from human cortex dissected and frozen at autopsy. Subjects with Alzheimer's disease, Parkinson's disease or schizophrenia were compared to age-matched controls with no known neurological disorders. Stimulation of PLC by the neurotransmitters was dependent on the presence of GTPγS. Carbachol elicited the greatest stimulations of PLC followed by serotonin and then dopamine. The maximal stimulations of PLC evoked by a neurotransmitter were similar for the various categories of subjects except in Parkinson's patients, where dopamine failed to stimulate PLC beyond the activity attained with carbachol. In the presence of carbachol, the sensitivity of PLC to GTPγS was significantly increased in Alzheimer's membranes, but not in age-matched controls or Parkinson's. Overall, the experiments demonstrate the feasibility for using the exogenous substrate assay to study the functionality of the phosphoinositide transmembrane signaling system in human brain.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF01474676
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  • 4
    Digitale Medien
    Digitale Medien
    Alpha-Adrenergic Stimulation of Phosphatidylinositol Synthesis in Human Platelets as an Alpha-2 Effect Secondary to Platelet Aggregation (1982)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 18 (1982), S. 213-220 
    Details
    ISSN: 0730-2312
    Schlagwort(e): phosphatidylinositol ; human platelets ; alpha catecholamines ; clonidine ; yohimbine ; prazosin ; Life and Medical Sciences ; Cell & Developmental Biology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie , Chemie und Pharmazie , Medizin
    Notizen: Epinephrine and adenosine diphosphate (ADP) stimulated 3H-glycerol uptake into phosphatidylinositol of human platelets. Yohimbine, an alpha-2 adrenoceptor antagonist, markedly reduced epinephrine-stimulated 3H-glycerol uptake into phosphatidylinositol; while prazosin, an alpha-1 antagonist, was without effect. Likewise, yohimbine, but not prazosin, blocked epinephrine-induced platelet aggregation. Furthermore, clonidine, a specific agonist for alpha-2 adrenoceptors, stimulated incorporation of-3H-glycerol into phosphatidylinositol and promoted platelet aggregation in the presence of low concentrations of ADP. These studies indicate that the effects of epinephrine on platelet aggregation and phosphatidylinositol synthesis are mediated through alpha-2 adrenoceptors. Further, since the stimulation of phosphatidylinositol synthesis seen with epinephrine was also observed with ADP, this suggests that the increased 3H-glycerol labeling is an indirect result of platelet aggregation.
    Zusätzliches Material: 3 Ill.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/jcb.1982.240180208
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