Induction of in Vitro Tumor Cell Invasion of Cellular Monolayers by Lysophosphatidic Acid or Phospholipase D

Imamura, Fumio; Horai, Takeshi; Mukai, Mutsuko; Shinkai, Kiyoko; Sawada, Machiko; Akedo, Hitoshi

doi:10.1006/bbrc.1993.1651

Cited by 171 publications

(110 citation statements)

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“…We added fibronectin or vitronectin at almost comparable concentrations to those in 1% FBS into the FBS-free assay medium; however, neither of them could stimulate phagokinetic motility of the integrin β3-or HOXD3-transfectants (unpublished data). It is well known that FBS contains several potent motility-stimulating factors, some of which are lysophosphatidic acid (LPA), insulin, epidermal growth factor (EGF), insulin-like growth factor-I (IGF-I), platelet derived growth factor (PDGF), and hepatocyte growth factor (HGF) [27]. LPA, EGF and HGF are unlikely to be a motility-stimulating factor for A549 cells because we have evidence that these molecules do not stimulate the phagokinetic motility of any of the transfectants used here (unpublished data).…”

Section: Hoxd3-transfectants Fibronectin Is a Ligand For A Variety Omentioning

confidence: 99%

HOXD3-overexpression increases integrin αvβ3 expression and deprives E-cadherin while it enhances cell motility in A549 cells

Ohta

Hamada

Tada

et al. 2006

Clin Exp Metastasis

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We have previously shown that transduction of HOXD3, one of homeobox genes, into human lung cancer A549 cells enhances cell motility, invasion and metastasis. In the present study, we examined the roles of integrin β3 which was up-regulated by HOXD3-overexpression in the HOXD3-induced motility of A549 cells. We first established integrin β3-transfectants and compared their motile activity to those of the HOXD3-transfected, control-transfected and parental cells by three different assays.The integrin β3-transfectants as well as the HOXD3-transfectants formed heterodimer with integrin αv subunit, and showed highly motile activities assessed by haptotaxis or phagokinetic track assay compared to the control transfectants or parental cells. In vitro wound-healing assay revealed that migratory activities were graded as the HOXD3-transfectants > the integrin β3-transfectants > the control transfectants or parental cells. E-cadherin was expressed in the integrin β3-transfectants but not expressed in the HOXD3-transfectants. An addition of function-blocking antibody to E-cadherin into the wound-healing assay promoted the migratory activity of the integrin β3-transfectants, suggesting that E-cadherin prevented the cells from dissociating from the wound edges. These results indicate that increased expression of integrin αv β3 and loss of E-cadherin by HOXD3-overexpression are responsible for the enhanced motility and dissociation.

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Section: Hoxd3-transfectants Fibronectin Is a Ligand For A Variety Omentioning

confidence: 99%

HOXD3-overexpression increases integrin αvβ3 expression and deprives E-cadherin while it enhances cell motility in A549 cells

Ohta

Hamada

Tada

et al. 2006

Clin Exp Metastasis

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“…(Imamura et al, 1991), lysophosphatidic acid (Imamura et al, 1993), an unknown factor from rat and bovine livers (invasion inhibiting peptide-2) (Shinkai et al, 1988;Isoai et al, 1990;Isoai et al, 1992) and transmethylation inhibitors modify the capacity of cancer cells to invade mesothelial cell monolayers, but the factors influencing the mesothelial barrier are not well studied. It is generally agreed that transmesothelial penetration by cancer cells occurs at the junctional region between adjacent cells.…”

Section: Ter Measurementsmentioning

confidence: 99%

Enhanced paracellular barrier function of rat mesothelial cells partially protects against cancer cell penetration

Tobioka

Sawada²,

Zhong³

et al. 1996

Br J Cancer

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“…A potential role of LPA and its receptors in the pathogenesis of human cancer, however, is a relatively new concept. LPA was implicated in human tumorigenesis from studies showing that LPA increases the motility and invasiveness of different types of cells (Imamura et al, 1993;Stam et al, 1998). LPA has been shown to be accumulated in ascitic fluids from patients with intraperitoneal malignancies, particularly ovarian cancer and pancreatic cancer (Xu et al, 1995;Westermann et al, 1998;Yamada et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

Role of p38 mitogen-activated kinase and c-Jun terminal kinase in migration response to lysophosphatidic acid and sphingosine-1-phosphate in glioma cells

et al. 2005

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A potential role for 1-oleoyl-sn-glycero-3-phosphate or lysophosphatidic acid (LPA) and sphingosine-1-phosphate (S1P) in the regulation of malignant diseases has been widely considered. In this study, we found that in transformed astroglial cells, the expression profile of lysophospholipid receptor mRNA and the action modes of LPA and S1P on cell motility were changed: there was a change in the acquisition of the ability of LPA to stimulate cell migration and a change in the migratory response to S1P from stimulation through S1P 1 to inhibition through S1P 2 . LPA-induced cell migration was almost completely inhibited by either pertussis toxin, LPA 1 receptor antagonists including Ki16425 (3-(4-[4-([1-(2-chlorophenyl)ethoxy]carbonyl amino)-3-methyl-5-isoxazolyl] benzylsulfonyl)propanoic acid) or an inhibitor of phosphatidylinositol 3-kinase (PI3K) wortmannin. The LPA-induced action was also suppressed, although incompletely, by several specific inhibitors for intracellular signaling pathways including Rac1, Cdc42, p38 mitogen-activated protein kinase (p38MAPK) and c-Jun terminal kinase (JNK), but not extracellular signalregulated kinase. Nearly complete inhibition of migration response to LPA, however, required simultaneous inhibition of both the p38MAPK and JNK pathways. Inhibition of Rac1 suppressed JNK but not p38MAPK, while the activity of p38MAPK was abolished by a dominantnegative form of Cdc42. These findings suggest that, in glioma cells, the PI3K/Cdc42/p38MAPK and PI3K/ Rac1/JNK pathways are equally important for LPA 1 receptor-mediated migration.

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Induction of in Vitro Tumor Cell Invasion of Cellular Monolayers by Lysophosphatidic Acid or Phospholipase D

Cited by 171 publications

References 0 publications

HOXD3-overexpression increases integrin αvβ3 expression and deprives E-cadherin while it enhances cell motility in A549 cells

HOXD3-overexpression increases integrin αvβ3 expression and deprives E-cadherin while it enhances cell motility in A549 cells

Enhanced paracellular barrier function of rat mesothelial cells partially protects against cancer cell penetration

Role of p38 mitogen-activated kinase and c-Jun terminal kinase in migration response to lysophosphatidic acid and sphingosine-1-phosphate in glioma cells

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