Cooperation of fibronectin with lysophosphatidic acid induces motility and transcellular migration of rat ascites hepatoma cells. Biochim Biophys Acta 2000 Jan 10;1495(1):40-50
Date
01/15/2000Pubmed ID
10634931DOI
10.1016/s0167-4889(99)00153-6Scopus ID
2-s2.0-0033962365 (requires institutional sign-in at Scopus site) 21 CitationsAbstract
We have previously shown that the transcellular migration of rat ascites hepatoma (AH130-MM1) cells through a cultured mesothelial cell monolayer (MCL) is triggered with lysophosphatidic acid (LPA) that stimulates actin polymerization and myosin light chain phosphorylation through the activation of Rho-ROCK (Rho-kinase) cascade. When, however, the motility of MM1 cells on a glass surface was tested by phagokinetic track motility assay, LPA failed to induce the motility. Nevertheless, when the glass had been coated with fibronectin (FN), LPA could induce phagokinetic motility which was accompanied by transformation of MM1 cells to fusiform-shape and assembly of focal adhesion. beta1 integrin, the counter receptor of FN, was expressed on MM1 cells. Anti-FN antibody, anti-beta1 integrin antibody and cyclo-GRGDSPA remarkably suppressed LPA-induced phagokinetic motility. These antibodies suppressed LPA-induced transcellular migration through MCL, as well. These results indicate that actin polymerization and phosphorylation of myosin light chain through Rho activation are insufficient for inducing motility but the cooperative FN/beta1 integrin-mediated adhesion is necessary for both the phagokinetic motility and transcellular migration of MM1 cells.
Author List
Ayaki M, Mukai M, Imamura F, Iwasaki T, Mammoto T, Shinkai K, Nakamura H, Akedo HAuthor
Tadanori Mammoto MD, PhD Associate Professor in the Pediatrics department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
AnimalsAntibodies
Carcinoma, Hepatocellular
Cell Movement
Fibronectins
Integrin beta1
Liver Neoplasms
Lysophospholipids
Rats
Tumor Cells, Cultured
