TY -JOUR AU -Po-Wei Lin AU -Yuan-Li Huang AU -Shee-Uan Chen AU -Hsinyu Lee TI -Lysophosphatidic Acid Up-regulates MT1-MMP Expression through a Gi –dependent Pathway in Human Umbilical Vein Endothelial Cells PY -2009 DA -2009-11-30 JO -Taiwania VL -54 IS -4 SP -375 EP -380 UR -https://taiwania.ntu.edu.tw/abstract/935 AB -Lysophosphatidic acid (LPA) is a low molecular weight lysophospholipid (LPL). Through binding to its specific G protein-coupled receptor family, LPA regulates various cellular functions, including proliferation, migration, invasion, and differentiation. Matrix-metalloproteinases (MMPs) are zinc-dependent protease and play important roles in regulating the interaction between cells and extracellular matrix (ECM). Among these MMPs, membrane type 1-metalloproteinase (MT1-MMP) not only degrades ECM protein but also activates metalloproteinase-2 (MMP-2, Gelatinase A), which are important to endothelial cell migration. Our previous study showed that LPA enhances MMP-2 expression and activity in human umbilical vein endothelial cells (HUVECs). In this study, we further revealed that LPA also induce MT1-MMP mRNA and protein expressions in HUVECs through real-time PCR and Western blotting, respectively. Furthermore, by applying chemical inhibitors, we found that LPA-induced MT1-MMP expression is mainly through a Gi- and partially through a Gq-dependent pathway. Our results provide new evidence that LPA might modulate ECM through regulating the expression of MT1-MMP. DO -10.6165/tai.2009.54(4).375