Hepatocyte growth factor stimulates invasion across reconstituted basement membranes by a new human small intestinal cell line

1994 ◽  
Vol 12 (2) ◽  
pp. 143-154 ◽  
Author(s):  
Iruvanti Sunitha ◽  
Deborah L. Meighen ◽  
Dan -Paul Hartman ◽  
Erik W. Thompson ◽  
Stephen W. Byers ◽  
...  
Keyword(s):  
Growth Factor ◽  
Hepatocyte Growth Factor ◽  
Cell Line ◽  
Basement Membranes ◽  
Intestinal Cell ◽  
Intestinal Cell Line ◽  
Small Intestinal ◽  
Hepatocyte Growth

High levels of soluble syndecan-1 in myeloma-derived bone marrow: modulation of hepatocyte growth factor activity

Blood ◽  
2000 ◽  
Vol 96 (9) ◽  
pp. 3139-3146 ◽  
Author(s):  
Carina Seidel ◽  
Magne Børset ◽  
Øyvind Hjertner ◽  
Dianjun Cao ◽  
Niels Abildgaard ◽  
...  
Keyword(s):  
Bone Marrow ◽  
Growth Factor ◽  
Hepatocyte Growth Factor ◽  
Heparan Sulfate ◽  
Cell Line ◽  
Osteosarcoma Cell ◽  
Heparin Binding ◽  
Myeloma Cells ◽  
Hepatocyte Growth

Syndecan-1 is a heparan sulfate proteoglycan expressed on the surface of, and actively shed by, myeloma cells. Hepatocyte growth factor (HGF) is a cytokine produced by myeloma cells. Previous studies have demonstrated elevated levels of syndecan-1 and HGF in the serum of patients with myeloma, both of negative prognostic value for the disease. Here we show that the median concentrations of syndecan-1 (900 ng/mL) and HGF (6 ng/mL) in the marrow compartment of patients with myeloma are highly elevated compared with healthy controls and controls with other diseases. We show that syndecan-1 isolated from the marrow of patients with myeloma seems to exist in an intact form, with glucosaminoglycan chains. Because HGF is a heparan-sulfate binding cytokine, we examined whether it interacted with soluble syndecan-1. In supernatants from myeloma cells in culture as well as in pleural effusions from patients with myeloma, HGF existed in a complex with soluble syndecan-1. Washing myeloma cells with purified soluble syndecan-1 could effectively displace HGF from the cell surface, suggesting that soluble syndecan-1 can act as a carrier for HGF in vivo. Finally, using a sensitive HGF bioassay (interleukin-11 production from the osteosarcoma cell line Saos-2) and intact syndecan-1 isolated from the U-266 myeloma cell line, we found that the presence of high concentrations of syndecan-1 (more than 3 μg/mL) inhibited the HGF effect, whereas lower concentrations potentiated it. HGF is only one of several heparin-binding cytokines associated with myeloma. These data indicate that soluble syndecan-1 may participate in the pathology of myeloma by modulating cytokine activity within the bone marrow.

Hepatocyte Growth Factor/Scatter Factor Stimulates Mitogenesis and Migration of a Head and Neck Squamous Cell Carcinoma Cell Line

2002 ◽  
Vol 127 (4) ◽  
pp. 271-278 ◽  
Author(s):  
Jeffery Fleigel ◽  
Jack Sedwick ◽  
Lori J. Kornberg
Keyword(s):  
Squamous Cell Carcinoma ◽  
Growth Factor ◽  
Hepatocyte Growth Factor ◽  
Cell Carcinoma ◽  
Head And Neck ◽  
Cell Line ◽  
Squamous Cell ◽  
Cultured Cells ◽  
Scatter Factor ◽  
Hepatocyte Growth

OBJECTIVE: We sought to assess the effect of extracellular matrix and hepatocyte growth factor/scatter factor (HGF/SF) on the growth and motility of cultured squamous cell carcinoma of the head and neck (SCCHN) cells. METHODS: Cultured cells were incubated in the presence of HGF/SF. The effect of HFG/SF on cell growth, motility, and phosphorylation of the signaling proteins FAK and Erk was determined. RESULTS: HGF/SF is both mitogenic and motogenic to the human SCCHN cell line FaDu. Incubation of FaDu cells in the presence of HGF/SF led to a rapid increase in phosphorylation of both FAK and the growth-promoting kinase Erk. HGF/SF-induced phosphorylation of FAK and Erk was observed in both detached and attached SCCHN cells. However, phosphorylation was much greater in attached cells. CONCLUSIONS AND SIGNIFICANCE: The mitogenic and motogenic activities of HGF/SF may contribute to the pathogenesis of SCCHN in vivo.

Hepatocyte Growth Factor (HGF) Induces Interleukin-11 Secretion From Osteoblasts: A Possible Role for HGF in Myeloma-Associated Osteolytic Bone Disease

Blood ◽  
1999 ◽  
Vol 94 (11) ◽  
pp. 3883-3888 ◽  
Author(s):  
Øyvind Hjertner ◽  
Maria Lyngaas Torgersen ◽  
Carina Seidel ◽  
Henrik Hjorth-Hansen ◽  
Anders Waage ◽  
...  
Keyword(s):  
Growth Factor ◽  
Hepatocyte Growth Factor ◽  
Cell Line ◽  
Bone Disease ◽  
Myeloma Cell ◽  
Physical Contact ◽  
Myeloma Cell Line ◽  
Myeloma Cells ◽  
Hepatocyte Growth ◽  
Interleukin 11

Multiple myeloma is associated with unbalanced bone remodeling causing lytic bone lesions. Interleukin-11 (IL-11) promotes osteoclast formation and inhibits osteoblast activity and may, thus, be one factor involved in cancer-induced bone destruction. We have previously shown that myeloma cells produce hepatocyte growth factor (HGF). We now report that HGF induces IL-11 secretion from human osteoblast-like cells and from the osteosarcoma cell lines Saos-2 and HOS. In coculture experiments, both the myeloma cell line JJN-3 and primary myeloma cells from 3 patients induced IL-11 secretion from osteoblasts, whereas no induction was observed with the non-HGF producing myeloma cell line OH-2. Enhanced IL-11 induction was observed with physical contact between osteoblasts and myeloma cells as compared with experiments in which contact was prohibited by tissue inserts. Anti-HGF serum strongly reduced the myeloma cell-induced IL-11 secretion. Furthermore, we show that JJN-3 cells express HGF on the cell-surface. Removal of surface-bound HGF on JJN-3 cells reduced IL-11 production induced in cocultures. Transforming growth factor β1 and IL-1 potentiated the effect of HGF on IL-11 secretion, whereas an additive effect was observed with tumor necrosis factor. Thus, myeloma-derived HGF can influence the bone marrow environment both as a soluble and a surface-bound factor. Furthermore, HGF emerges as a possible factor involved in myeloma bone disease by its ability to induce IL-11.

Downregulation of cyclin a promoter activity and G1 accumulation in the HepG2 cell line by hepatocyte growth factor

2000 ◽  
Vol 118 (4) ◽  
pp. A907
Author(s):  
Masaya Furukawa ◽  
Yasushi Magami ◽  
Shinichiro Kokuno ◽  
Daiju Nakayama ◽  
Yoshihisa Tsukioka ◽  
...  
Keyword(s):  
Growth Factor ◽  
Hepatocyte Growth Factor ◽  
Cell Line ◽  
Hepg2 Cell ◽  
Promoter Activity ◽  
Cyclin A ◽  
Hepg2 Cell Line ◽  
Hepatocyte Growth

scholarly journals Defective posttranslational processing activates the tyrosine kinase encoded by the MET proto-oncogene (hepatocyte growth factor receptor).

1991 ◽  
Vol 11 (12) ◽  
pp. 6084-6092 ◽  
Author(s):  
A Mondino ◽  
S Giordano ◽  
P M Comoglio
Keyword(s):  
Growth Factor ◽  
Cell Surface ◽  
Hepatocyte Growth Factor ◽  
Tyrosine Kinase ◽  
Cell Line ◽  
Proteolytic Cleavage ◽  
Cdna Clones ◽  
Posttranslational Processing ◽  
Single Chain ◽  
Hepatocyte Growth

The MET proto-oncogene encodes a 190-kDa disulfide-linked heterodimeric receptor (p190 alpha beta) whose tyrosine kinase activity is triggered by the hepatocyte growth factor. The mature receptor is made of two subunits: an alpha chain of 50 kDa and a beta chain of 145 kDa, arising from proteolytic cleavage of a single-chain precursor of 170 kDa (pr170). In a colon carcinoma cell line (LoVo), the precursor is not cleaved and the Met protein is exposed at the cell surface as a single-chain polypeptide of 190 kDa (p190NC). The expression of the uncleaved Met protein is due to defective posttranslational processing, since in this cell line (i) the proteolytic cleavage site Lys-303-Arg-Lys-Lys-Arg-Ser-308 is present in the precursor, (ii) p190NC is sensitive to mild trypsin digestion of the cell surface, generating alpha and beta chains of the correct size, and (iii) the 205-kDa insulin receptor precursor is not cleaved as well. p190NC is a functional tyrosine kinase in vitro and is activated in vivo, as shown by constitutive autophosphorylation on tyrosine. The MET gene is neither amplified nor rearranged in LoVo cells. Overlapping cDNA clones selected from a library derived from LoVo mRNA were sequenced. No mutations were present in the MET-coding region. These data indicate that the tyrosine kinase encoded by the MET proto-oncogene can be activated as a consequence of a posttranslational defect.

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