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A significant increase of lysophosphatidylinositol 4‐phosphate with insulin in isolated rat fat cells
Author(s) -
Kuroda Yoshihiko,
Nakayama Hidetaka,
Ishibashi Teruo,
Aoki Shin,
Tushima Satoshi,
Nakagawa Shoichi
Publication year - 1987
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(87)80437-4
Subject(s) - insulin , phosphatidylinositol , medicine , endocrinology , insulin receptor , phospholipase c , hydrolysis , phospholipase , phospholipid , thin layer chromatography , chemistry , insulin receptor substrate , phosphate , receptor , biochemistry , biology , chromatography , enzyme , insulin resistance , signal transduction , membrane
We studied the effects of insulin on the incorporation of 32 P i into phospholipids in rat fat cells. When the cells were treated with insulin, a new radioactive phospholipid was detected on thin layer chromatography. The substance migrated slower than phosphatidylinositol 4,5‐bisphosphate and was hardly detectable in the absence of insulin. This effect of insulin was both time‐ and dose‐dependent with half‐maximal stimulation at 120 μU/ml. Pretreatment of insulin with anti‐insulin antibody or the cells with anti‐insulin receptor anti‐body inhibited the effect of insulin. The product of phosphatidylinositol 4‐phosphate hydrolysed by phospholipase A 2 was coincided with the substance on thin layer chromatography. Quinacrine inhibited the formation of the substance in a dose‐dependent manner. These results suggested that insulin stimulates the generation of lysophosphatidylinositol 4‐phosphate through the insulin‐receptor interaction.