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Calcium‐activated, phospholipid‐dependent protein kinase in cultured rat mesangial cells
Author(s) -
Orita Yoshimasa,
Fujiwara Yoshihiro,
Ochi Satoshi,
Tanaka Yoshimu,
Kamada Takenobu
Publication year - 1985
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(85)80063-6
Subject(s) - diacylglycerol kinase , protein kinase c , phosphatidylinositol , protein kinase a , angiotensin ii , phospholipid , mesangial cell , chemistry , biochemistry , intracellular , kinase , biology , microbiology and biotechnology , in vitro , receptor , membrane
The analysis of the 1 × g supernatant fraction of cultured rat glomerular mesangial cells with DEAE‐cellulose ion‐exchange chromatography revealed a large peak showing the activity of a protein kinase (protein kinase C) which depended on phospholipid and diolein as well as Ca 2+ Furthermore, it was shown that angiotensin II (AII) (10 −6 M) induced rapid hydrolysis of phosphatidylinositol 4,5‐bisphosphate, leading to production of diacylglycerol rich in arachidonic acid, in the cultured rat mesangial cells. These results suggest that activation of protein kinase C resulting from enhancement of phosphoinositide metabolism may be important as an intracellular regulatory mechanism of AII upon cultured mesangial cells.