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Phosphoinositide hydrolysis in permeabilized SH‐SY5Y human neuroblastoma cells is inhibited by mastoparan
Author(s) -
Wojcikiewicz Richard J.H.,
Nahorski Stefan R.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81366-3
Subject(s) - mastoparan , inositol , inositol phosphate , sh sy5y , phospholipase c , chemistry , biochemistry , inhibitory postsynaptic potential , microbiology and biotechnology , g protein , neuroblastoma , biology , cell culture , endocrinology , enzyme , receptor , genetics
The effects of mastoparan on phospholipase C‐catalysed phosphoinositide hydrolysis were examined in [ 3 H]inositol‐labelled human neuroblastoma SH‐SY5Y cells. [ 3 H]Inositol phosphate formation in intact cells was not altered by 20 μM mastoparan. In contrast, [ 3 H]inositol phosphate formation in electrically permeabilized cells stimulated with guanosine 5′[γ‐thio]triphosphate and/or carbachol was inhibited by mastoparan with half‐maximal effects at approx. 3 μM. The peptide was much less effective in inhibiting stimulatory effects of Ca 2+ . Similar but less potent inhibitory effects were observed with the cations, neomycin and spermine, indicating that direct interaction of mastoparan with polyphosphoinositides might account for its inhibitory effects on inositol phosphate formation.