Endogenous receptor bound ur019nase mediates tissue invasion of human monocytes

Kirchheimer, Johannes C.; Remold, Heinz G.

doi:10.1016/0268-9499(89)90083-0

Cited by 51 publications

(73 citation statements)

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“…In these cases, the interaction of uPAR with integrin may be responsible for the observed phenomena. On the other hand, with the amnion invasion assay, in which ECM is required, occupancy of uPAR with endogenous uPA enhances human monocyte migration, and PAI-2, an inhibitor of endogenously uPAR-associated uPA, inhibits this migration [41]. In addition to leukocytes, uPARbound uPA is also required for an integrin (␣ v ␤ 5 )-mediated tumor cell migration [42].…”

Section: Regulation Of Leukocyte Transendothelial Migration By the Upmentioning

confidence: 99%

Regulation of leukocyte adherence and migration by glycosylphosphatidyl-inositol-anchored proteins

Sendo

Araki

1999

Journal of Leukocyte Biology

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Leukocyte extravasation is essential for subsequent inflammation and the immune response. Extravasation can be divided into at least three steps; rolling, firm adhesion, and transendothelial migration. Although the mechanisms involved in the first two steps have been fairly well documented, the last step is complex and largely remains to be clarified. This review focuses on the possible role of GPI-anchored proteins on leukocytes in the regulation of their transendothelial migration. In addition to regulation by urokinase and its receptor, which has been regarded as the main modulator, we draw attention to a novel GPI-anchored protein (GPI-80) on human phagocytes that may be involved in regulating leukocyte adhesion and migration. The high degree of homology of GPI-80 with vanin-1, which is expressed on vascular tissues and is involved in prethymic cell homing into the thymus, raises the possibility that there is a family of molecules, including GPI-80 and vanin-1, that may be involved in leukocyte transendothelial migration. The possible role of soluble GPI-anchored proteins in this process is also discussed. J. Leukoc. Biol. 66: 369-374; 1999.

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Section: Regulation Of Leukocyte Transendothelial Migration By the Upmentioning

confidence: 99%

Regulation of leukocyte adherence and migration by glycosylphosphatidyl-inositol-anchored proteins

Sendo

Araki

1999

Journal of Leukocyte Biology

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“…It has been reported that the activated N-ras gene is crucial for keeping the transformed phenotypes of HT1080 cells (Hall et al, 1983;Paterson et al, 1987) and that the elevated levels of expression of urokinase-type plasminogen activator (uPA) are associated with cell migration and malignant transformation in several types of tumour cells (Kirchheimer and Remold, 1989;Chambers et al, 1995). Therefore, we examined whether PU.…”

Section: Expression Of Pu1 Protein In Pu1-transfected Ht1080 Cellsmentioning

confidence: 99%

Enhanced expression of the urokinase-type plasminogen activator gene and reduced colony formation in soft agar by ectopic expression of PU.1 in HT1080 human fibrosarcoma cells

Kondoh

Yamada²,

Kihara-Negishi³

et al. 1998

Br J Cancer

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Summary To investigate the cell biological function of PU.1, a member of the Ets family of transcription factors, a vector capable of expressing the protein was transfected into HT1080 human fibrosarcoma cells. Exogenous expression of PU.1 in HT1080 cells reduced colony-forming efficiency but stimulated cell migration in soft agar, although it did not affect cell growth in adherent culture. Expression of the urokinase-type plasminogen activator (uPA) mRNA, which is known to be correlated with cell migration and invasion, was enhanced in PU. 1 transfectants compared with mock transfectants. Run-on analysis demonstrated that uPA transcription was unaffected by PU.1, suggesting that this enhancement mainly occurs at a post-transcriptional level. On the other hand, treatment of HT1080 cells with the synthetic glucocorticoid dexamethasone (DEX; 10-7 M) significantly reduced uPA gene expression at a transcriptional level. Furthermore, DEX inhibited cell migration in soft agar without affecting cell growth. These negative effects of DEX on uPA expression and cell migration were alleviated by the expression of PU.1 in HT1080 cells, whereas expression of the N-ras oncogene, which is responsible for maintenance of the transformed phenotypes in HT1080 cells, was unaffected by PU.1 expression or DEX treatment in the cells. Our results suggest that expression of PU.1 can stimulate uPA gene expression at the post-transcriptional level, which may subsequently lead to activation of cell motility and/or reduced cell-cell adhesion, but reduces anchorage-independent growth of HT1080 cells.

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“…The uPAR protein is inducible in monocytes by the tumor promoter, phorbol myristate acetate (PMA) [10] and by the cytokines, interferon gamma (IFN-y) and tumor necrosis factor alpha (TNFc 0 [11]. uPAR biosynthesis, the uPAR mRNA level and gene transcription are also increased by transforming growth factor beta (TGFfl) and dexamethasone in A549 lung carcinoma cells [12], but reports of transcriptional regulation of uPAR mRNA expression by TNF~ in any cell type are *Corresponding author.…”

Section: Introductionmentioning

confidence: 99%

Human urokinase receptor expression is inhibited by amiloride and induced by tumor necrosis factor and phorbol ester in colon cancer cells

et al. 1994

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The modulation of urokinase plasminogen activator receptor (uPAR) gene expression by tumor necrosis factor alpha (TNF~), phorbol ester (PMA) and amiloride was studied in three colon cancer cell lines, uPAR mRNA and protein were induced by TNF~ and by PMA but were inhibited by amiloride at concentrations of 0.1 to 1 mM in the presence or absence of TNFc~ and PMA. Nuclear run-on transcription assay indicated that the effects of amiloride and TNF~ were mediated at least in part at the transcriptional level, whereas PMA may act in part via a posttranscriptional mechanism. These results suggested that uPAR gene expression is modulated by multiple signal transduction pathways.

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Endogenous receptor bound ur019nase mediates tissue invasion of human monocytes

Cited by 51 publications

References 0 publications

Regulation of leukocyte adherence and migration by glycosylphosphatidyl-inositol-anchored proteins

Regulation of leukocyte adherence and migration by glycosylphosphatidyl-inositol-anchored proteins

Enhanced expression of the urokinase-type plasminogen activator gene and reduced colony formation in soft agar by ectopic expression of PU.1 in HT1080 human fibrosarcoma cells

Human urokinase receptor expression is inhibited by amiloride and induced by tumor necrosis factor and phorbol ester in colon cancer cells

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