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Protein kinase C‐regulated production of prostacyclin by rat endothelium is increased in the presence of lipoxin A4
Author(s) -
Leszczynski Dariusz,
Ustinov Jarkko
Publication year - 1990
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(90)80718-x
Subject(s) - prostacyclin , kinase , endothelium , protein kinase a , microbiology and biotechnology , protein kinase c , endothelial stem cell , chemistry , pharmacology , biology , biochemistry , endocrinology , in vitro
Prostacyclin is generated by cultured rat endothelial cells. Compound blocking activity of protein kinase C and cyclic nucleotide‐dependent protein kinases (H7) and compound blocking interaction between Ca 2+ and calmodulin (W7) diminish generation of prostacyclin in rat endothelial cells. These compounds give a synergistic effect when they are introduced to the endothelial cell cultures simultaneously. Compound HA1004, an inhibitor ofcAMP‐ and cGMP‐dependent protein kinases has no effect on prostacyclin generation. Lipoxin A4, a potent direct stimulator of protein kinase C, rapidly induces prostacyclin generation in rat endothelium in a dose‐ and time‐dependent fashion. Lipoxin A4‐induced generation of prostacyclin can be inhibited by H7 and W7 but not by HA1004. Lipoxin B4 has no significant effect on prostacyclin generation in rat endothelium. In conclusion, our results demonstrate that generation of prostacyclin by rat endothelial cells is regulated via a pathway involving protein kinase C and Ca 2+ .