[3H]PtdIns hydrolysis in postmortem human brain membranes is mediated by the G-proteins Gq/11 and phospholipase C-β
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چکیده
منابع مشابه
Phospholipase C - mediated Hydrolysis of Phosphatidylcholine
We have investigated the effect of cis-diamminedichloroplatinum(II) (CDDP) on signal transduction pathways. CDDP treatment did not cause any change in the binding of 1H1phorbol dibutyrate to PC-9 (human lung adenocarcinoma cell line) cells, a measure of protein kinase C activation. However, 2-h CDDP treatment (20 gg/ml) caused 200% increase in 1,2-sn-diacylglycerol (DAG) production and 50% decr...
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The phospholipase C-catalysed breakdown of inositol-containing phospholipids is an important source of diacylglycerol in cells stimulated by several agonists. However, recent experimental evidence suggests that major phospholipids such as phosphatidylcholine may also be substrates of the phosphodiesteratic hydrolysis activated by hormones, growth factors and oncogene products. We show here that...
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Grillone, L. R., Clark, M. A., Godfrey, R. W., Stassen, F. & Crooke, S. T. (1988) J. Biol. Chem. 263, Received 13 December 199
متن کاملPhospholipase C–mediated hydrolysis of PIP2 releases ERM proteins from lymphocyte membrane
Mechanisms controlling the disassembly of ezrin/radixin/moesin (ERM) proteins, which link the cytoskeleton to the plasma membrane, are incompletely understood. In lymphocytes, chemokine (e.g., SDF-1) stimulation inactivates ERM proteins, causing their release from the plasma membrane and dephosphorylation. SDF-1-mediated inactivation of ERM proteins is blocked by phospholipase C (PLC) inhibitor...
متن کاملSerotonin-mediated palmitoylation and depalmitoylation of G alpha proteins in rat brain cortical membranes.
We investigated serotonin stimulated palmitoylation of G alpha subunits in rat brain cerebrocortical membranes. Serotonin dose dependently stimulated palmitoylation of membrane G alpha proteins. The highest [3H] palmitate incorporation observed was by G alpha-q (7-fold), followed by G alpha-o (5-fold), G alpha-i (4-fold) and G alpha-s (3-fold) and these increases in palmitoylation were blocked ...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1994
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj3040655