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Lysophospholipids Enhance Membrane Type‐1 Matrix Metalloproteinase Expression Activity in Human Endothelial Cells
Author(s) -
Lee Hsinyu,
Lin ChiIou,
Lin PoWei
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.6.a858-a
Subject(s) - matrix metalloproteinase , angiogenesis , microbiology and biotechnology , extracellular matrix , lysophosphatidic acid , s1pr1 , chemistry , endothelial stem cell , biology , western blot , umbilical vein , receptor , biochemistry , vascular endothelial growth factor a , cancer research , vascular endothelial growth factor , in vitro , gene , vegf receptors
Lysophosphatidic acid (LPA) and sphingosine 1‐phosphate (S1P) are both low molecular weight lysophospholipids (LPLs), which promote cell proliferation, migration, and invasion via interaction with a family of specific G protein‐coupled receptors. Matrix metalloproteinases (MMPs) are zinc‐dependent proteolytic enzymes, which are involved in degradation of the extracellular matrix. Among members of the MMP family, membrane type 1‐MMP (MT1‐MMP) has been recognized as an essential enzyme involved in matrix remodeling and in the migration of endothelial cells, which facilitates angiogenesis process. In our present study, we examined the effects of LPA and S1P on MT1‐MMP expression and activity in human umbilical cord vein endothelial cells. By Western Blot analysis and Biotrak activity assay, we showed that both LPA and S1P enhanced MT1‐MMP protein expression and enzymatic activity in a dose‐ and time‐dependent manner. Maximal expression appeared at 1 μM post‐ligand treatment at 4 h. These observations suggest that lysophospholipids might play important roles in endothelial cell invasion by regulating the expression and activity of MT1‐MMP.