Phosphatidylinositol 4,5-Bisphosphate Phospholipase C and Phosphomonoesterase in Dunaliella salina Membranes
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چکیده
منابع مشابه
Phosphatidylinositol-specific phospholipase C in fetal membranes and uterine decidua.
An assay procedure was developed in which phosphatidyl[2-(3)H]inositol was employed as substrate for the measurement of phosphatidylinositol-specific phospholipase C activity. Employing this assay, phosphatidylinositol-specific phospholipase C activity in human fetal membranes and uterine decidua was identified and characterized. The specific activity of this enzyme in amnion (4.4 mumol x mg(-1...
متن کاملInteraction of cerebral-cortical membranes with exogenously added phosphatidylinositol 4,5-bisphosphate. Effects on measured phospholipase C activity.
Exogenously added phosphatidylinositol 4,5-bisphosphate (PtdInsP2) is rapidly associated with cerebral-cortical membranes. Substrate association with membranes was promoted by Mg2+, but inhibited by bivalent chelators. Once associated with the membrane, the PtdInsP2 was resistant to displacement by EDTA. The apparent phospholipase C activity was dependent on the degree of association of substra...
متن کاملCeramide kinase regulates phospholipase C and phosphatidylinositol 4, 5, bisphosphate in phototransduction.
Phosphoinositide-specific phospholipase C (PLC) is a central effector for many biological responses regulated by G-protein-coupled receptors including Drosophila phototransduction where light sensitive channels are activated downstream of NORPA, a PLCbeta homolog. Here we show that the sphingolipid biosynthetic enzyme, ceramide kinase, is a novel regulator of PLC signaling and photoreceptor hom...
متن کاملPhosphatidylinositol 4,5-bisphosphate modifies tubulin participation in phospholipase Cbeta1 signaling.
Tubulin forms the microtubule and regulates certain G-protein-mediated signaling pathways. Both functions rely on the GTP-binding properties of tubulin. Signal transduction through Galpha(q)-regulated phospholipase Cbeta1 (PLCbeta1) is activated by tubulin through a direct transfer of GTP from tubulin to Galpha(q). However, at high tubulin concentrations, inhibition of PLCbeta1 is observed. Thi...
متن کاملPresynaptic inhibition via a phospholipase C- and phosphatidylinositol bisphosphate-dependent regulation of neuronal Ca2+ channels.
Presynaptic inhibition of transmitter release is commonly mediated by a direct interaction between G protein betagamma subunits and voltage-activated Ca2+ channels. To search for an alternative pathway, the mechanisms by which presynaptic bradykinin receptors mediate an inhibition of noradrenaline release from rat superior cervical ganglion neurons were investigated. The peptide reduced noradre...
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ژورنال
عنوان ژورنال: Plant Physiology
سال: 1989
ISSN: 0032-0889,1532-2548
DOI: 10.1104/pp.90.3.1115