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Modulation of Phosphoinositide Hydrolysis by NaF and Aluminum in Rat Cortical Slices
Author(s) -
Jope Richard S.
Publication year - 1988
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1988.tb01152.x
Subject(s) - inositol , inositol phosphate , carbachol , chemistry , inositol trisphosphate , stimulation , medicine , endocrinology , incubation , intracellular , receptor , biochemistry , biology
Abstract: NaF stimulated phosphoinositide hydrolysis in rat cortical slices. The production of [ 3 H]inositol monophosphate was rapid for the first 15 min of incubation with NaF, followed by a plateau. The major product detected was [ 3 H]inositol monophosphate, although significant amounts of [ 3 H]inositol bisphosphate and [ 3 H]inositol trisphosphate were also produced. The stimulation of [ 3 H]inositol monophosphate production by NaF was concentration dependent between 2 and 20 μ M NaF. Addition of 10 or 100 μ M A1C1 3 or aluminum maltol did not alter the effect of NaF, whereas at 500 μ M , these aluminum preparations resulted in significant inhibition. Increasing the concentration of K + from 5 to 20 μ M potentiated [ 3 H]inositol monophosphate production induced by carbachol but not by NaF. Incubation with 1 μ M phorbol 12–myristate 13–acetate, a phorbol ester, inhibited carbachol‐induced, but not NaF‐induced, [ 3 H]inositol monophosphate production. These results further support the hypothesis that a guanine nucleotide binding protein that can be activated by NaF is involved in phosphoinositide hydrolysis in brain. The use of NaF provides a means to bypass receptors to study intracellular regulatory sites of phosphoinositide metabolism without disrupting cells.