The role of lysophosphatidylcholine acyltransferase 2 in osteoblastic differentiation of C2C12 cells

Glycerophospholipids, a primary component of cellular membranes, play important structural and functional roles in cells. In the remodelling pathway (Lands' cycle), the concerted actions of phospholipase As and lysophospholipid acyltransferases (LPLATs) contribute to the incorporation of diverse fatty acids in glycerophospholipids in an asymmetric manner, which differ between cell types. In this study, the role of LPLATs in osteoblastic differentiation of C2C12 cells was investigated. Gene and protein expression levels of lysophosphatidylcholine acyltransferase 2 (LPCAT2), one of the LPLATs, increased during osteoblastic differentiation in C2C12 cells. LPCAT2 knockdown in C2C12 cells downregulated the expression of osteoblastic differentiation markers and the number and size of lipid droplets (LDs) and suppressed the phosphorylation of Smad1/5/9. In addition, LPCAT2 knockdown inhibited Snail1 and the downstream target of Runx2 and vitamin D receptor (VDR). These results suggest that LPCAT2 modulates osteoblastic differentiation in C2C12 cells through the bone morphogenetic protein (BMP)/Smad signalling pathway. Protein expression of lysophosphatidylcholine acyltransferase 2 (LPCAT2, also LPLAT9), which is a phospholipid biosynthetic enzyme increased during osteoblastic differentiation in C2C12 cells. In addition, LPCAT2 knockdown in C2C12 cells suppressed the expression of osteoblastic differentiation markers, growth of lipid droplets (LDs), and the phosphorylation of Smad1/5/9. These results suggest that LPCAT2 possibly modulates osteoblastic differentiation in C2C12 cells.