Lysophosphatidic acid receptor-5 negatively regulates cell motile and invasive activities of human sarcoma cell lines. 2014

Yan Dong, and Miku Hirane, and Mutsumi Araki, and Nobuyuki Fukushima, and Kanya Honoki, and Toshifumi Tsujiuchi
Division of Cancer Biology and Bioinformatics, Department of Life Science, Faculty of Science and Engineering, Kinki University, 3-4-1, Kowakae, Higashiƍsaka, Osaka, 577-8502, Japan.

LPA signaling via LPA receptors [LPA receptor-1 (LPA1)-LPA6] mediates the several cellular responses in cancer cells, including cell motility and invasion. In the present study, to investigate a role of LPA5 in the cell motile and invasive activities of sarcoma cells, LPAR5 knockdown (HOSL5 and HT1080L5) cells were generated from human osteosarcoma HOS and fibrosarcoma HT1080 cells, respectively. In cell motility assays with cell culture inserts, HOSL5 and HT1080L5 cells indicated the high cell motile activities, compared with control cells. The cell invasive activities of HOSL5 and HT1080L5 cells were significantly higher than those of control cells. Moreover, the activities of matrix metalloproteinase (MMP)-2 and MMP-9 were measured by gelatin zymography. MMP-2 was significantly activated in HOSL5 cells, but not MMP-9. The elevated activities of MMP-2 and MMP-9 were found in HT1080L5 cells, in comparison with control cells. These results suggest that LPA signaling via LPA5 negatively regulates the cell motile and invasive activities of human sarcoma cells.

UI MeSH Term Description Entries
D008246 Lysophospholipids Derivatives of PHOSPHATIDIC ACIDS that lack one of its fatty acyl chains due to its hydrolytic removal. Lysophosphatidic Acids,Lysophospholipid,Acids, Lysophosphatidic
D009361 Neoplasm Invasiveness Ability of neoplasms to infiltrate and actively destroy surrounding tissue. Invasiveness, Neoplasm,Neoplasm Invasion,Invasion, Neoplasm
D002465 Cell Movement The movement of cells from one location to another. Distinguish from CYTOKINESIS which is the process of dividing the CYTOPLASM of a cell. Cell Migration,Locomotion, Cell,Migration, Cell,Motility, Cell,Movement, Cell,Cell Locomotion,Cell Motility,Cell Movements,Movements, Cell
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D012509 Sarcoma A connective tissue neoplasm formed by proliferation of mesodermal cells; it is usually highly malignant. Sarcoma, Epithelioid,Sarcoma, Soft Tissue,Sarcoma, Spindle Cell,Epithelioid Sarcoma,Epithelioid Sarcomas,Sarcomas,Sarcomas, Epithelioid,Sarcomas, Soft Tissue,Sarcomas, Spindle Cell,Soft Tissue Sarcoma,Soft Tissue Sarcomas,Spindle Cell Sarcoma,Spindle Cell Sarcomas
D015398 Signal Transduction The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway. Cell Signaling,Receptor-Mediated Signal Transduction,Signal Pathways,Receptor Mediated Signal Transduction,Signal Transduction Pathways,Signal Transduction Systems,Pathway, Signal,Pathway, Signal Transduction,Pathways, Signal,Pathways, Signal Transduction,Receptor-Mediated Signal Transductions,Signal Pathway,Signal Transduction Pathway,Signal Transduction System,Signal Transduction, Receptor-Mediated,Signal Transductions,Signal Transductions, Receptor-Mediated,System, Signal Transduction,Systems, Signal Transduction,Transduction, Signal,Transductions, Signal
D045744 Cell Line, Tumor A cell line derived from cultured tumor cells. Tumor Cell Line,Cell Lines, Tumor,Line, Tumor Cell,Lines, Tumor Cell,Tumor Cell Lines
D049368 Receptors, Lysophosphatidic Acid A subfamily of lysophospholipid receptors with specificity for LYSOPHOSPHATIDIC ACIDS. LPA Receptor,Lysophosphatidic Acid Receptor,Lysophosphatidic Acid Receptors,EDG7 Protein,Edg-4 Receptor,Edg-7 Receptor,Edg2 Protein,Edg4 Protein,LPA Receptors,LPA-1 Receptor,LPA1 Receptor,LPA2 Receptor,LPA3 Receptor,Receptor, Lysophosphatidic Acid,edg-2 Receptor,vzg-1 Receptor,Acid Receptor, Lysophosphatidic,Acid Receptors, Lysophosphatidic,Edg 4 Receptor,Edg 7 Receptor,LPA 1 Receptor,Receptor, Edg-4,Receptor, Edg-7,Receptor, LPA,Receptor, LPA1,Receptor, LPA2,Receptor, LPA3,Receptor, edg-2,Receptor, vzg-1,Receptors, LPA,edg 2 Receptor,vzg 1 Receptor
D020778 Matrix Metalloproteinase 2 A secreted endopeptidase homologous with INTERSTITIAL COLLAGENASE, but which possesses an additional fibronectin-like domain. Gelatinase A,72-kDa Gelatinase,72-kDa Type IV Collagenase,MMP-2 Metalloproteinase,MMP2 Metalloproteinase,Matrix Metalloproteinase-2,72 kDa Gelatinase,72 kDa Type IV Collagenase,Gelatinase, 72-kDa,MMP 2 Metalloproteinase,Metalloproteinase 2, Matrix,Metalloproteinase, MMP-2,Metalloproteinase, MMP2
D020780 Matrix Metalloproteinase 9 An endopeptidase that is structurally similar to MATRIX METALLOPROTEINASE 2. It degrades GELATIN types I and V; COLLAGEN TYPE IV; and COLLAGEN TYPE V. Gelatinase B,92-kDa Gelatinase,92-kDa Type IV Collagenase,MMP-9 Metalloproteinase,MMP9 Metalloproteinase,Matrix Metalloproteinase-9,92 kDa Gelatinase,92 kDa Type IV Collagenase,MMP 9 Metalloproteinase,Metalloproteinase 9, Matrix,Metalloproteinase, MMP-9,Metalloproteinase, MMP9

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