@Article{taiwania2009544375,
AUTHOR = {Po-Wei Lin, Yuan-Li Huang, Shee-Uan Chen, Hsinyu Lee},
TITLE = {Lysophosphatidic Acid Up-regulates MT1-MMP Expression through a Gi –dependent Pathway in Human Umbilical Vein Endothelial Cells},
JOURNAL = {Taiwania},
VOLUME = {54},
YEAR = {2009},
ISSUE = {4},
PAGES = {375-380},
URL = {https://taiwania.ntu.edu.tw/abstract/935},
ABSTRACT = {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.},
DOI = {10.6165/tai.2009.54(4).375}
}