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Suppression of Lysophosphatidylcholine‐Induced Human Aortic Smooth Muscle Cell Calcification by Protein Kinase A Inhibition
Author(s) -
Toita Riki,
Asai Daisuke,
Otani Kentaro,
Kawano Takahito,
Murata Masaharu,
Kang JeongHun
Publication year - 2019
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1002/lipd.12178
Subject(s) - lysophosphatidylcholine , calcification , vascular smooth muscle , chemistry , alkaline phosphatase , protein kinase a , phospholipase , medicine , biochemistry , endocrinology , microbiology and biotechnology , kinase , smooth muscle , phosphatidylcholine , biology , enzyme , phospholipid , membrane
Abstract Lysophosphatidylcholine (lysoPtdCho) is produced mainly by the phospholipase A2‐dependent hydrolysis of phosphatidylcholine (PtdCho) and can induce inflammatory activation and osteogenic gene expression in vascular smooth muscle cells. However, the mechanisms mediating these processes have not been fully elucidated. In this study, we investigated whether inhibition of protein kinase A (PKA) signaling suppressed lysoPtdCho‐induced calcification of human aortic smooth muscle cells (HASMC). Calcium levels and alkaline phosphatase activity were significantly increased in HASMC treated with lysoPtdCho, but not PtdCho, compared with those in phosphate‐buffered saline‐treated HASMC. However, the addition of a PKA inhibitor (H‐89) or PKA siRNA blocked lysoPtdCho‐induced HASMC calcification. These results showed that lysoPtdCho could activate PKA‐mediated HASMC calcification and that PKA may be a therapeutic target for lysoPtdCho‐mediated vascular smooth muscle cell calcification.