Internalization and degradation of hepatocyte growth factor in hepatocytes with down‐regulation of the receptor/c‐<i>Met</i>

Naka, Daiji; Shimomura, Takeshi; Yoshiyama, Yoshiko; Sato, Maki; Sato, Mutsumi; Ishii, Takuro; Hara, Hiroto

doi:10.1016/0014-5793(93)80212-d

Cited by 36 publications

(22 citation statements)

References 28 publications

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“…Consistent with others' results [33][34][35], in HBEpCs HGF (25 ng/ml) treatment for 30 min induced c-Met internalization from plasma membrane to cytoplasm and perinuclear compartment in a dose-dependent fashion (Fig. 7A).…”

Section: The Effect Of Lpa On Hgf / C-met-mediated C-met Internalizatsupporting

confidence: 92%

“…Ligand-dependent endocytosis of RTKs was the common mechanism of receptor inactivation and recycling [30][31][32][33][34][35]44,45]. Consistent to the study in HeLa cells [35], the binding of HGF to c-Met triggers internalization and redistribution of c-Met to the perinulear compartment in HBEpCs.…”

Section: Discussionmentioning

confidence: 63%

“…HGF induces c-Met endocytosis and intracellular traffic has been demonstrated in variety of cell types [33][34][35]. Here we examined the c-Met redistribution by LPA treatment in HBEpCs.…”

Section: Lpa Induces C-met Redistribution Via Pkc δ In Hbepcmentioning

confidence: 99%

“…It is well established that many transmembrane receptors, such as EGF-R and c-Met, become internalized upon ligand stimulation [30][31][32][33]. It has been reported that upon HGF stimulation, c-Met is rapidly internalized via clathrin-coated vesicles and traffics through an early endosomal compartment, which is independent of the proteasome-mediated degradative pathway [34].…”

Section: Introductionmentioning

confidence: 99%

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Lysophosphatidic acid modulates c-Met redistribution and hepatocyte growth factor/c-Met signaling in human bronchial epithelial cells through PKC δ and E-cadherin

Zhao¹,

He²,

Stern³

et al. 2007

Cellular Signalling

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Previously we demonstrated that ligation of lysophosphatidic acid (LPA) to G protein-coupled LPA receptors induces transactivation of receptor tyrosine kinases (RTKs), such as platelet-derived growth factor receptor beta (PDGF-Rβ) and epidermal growth factor receptor (EGF-R), in primary cultures of human bronchial epithelial cells (HBEpCs). Here we examined the role of LPA on c-Met redistribution and modulation of hepatocyte growth factor ( These results demonstrate that LPA regulates c-Met function through PKC δ-and E-cadherin in HBEpCs, suggesting an alternate function of the cross-talk between G-protein coupled receptors (GPCRs) and RTKs in HBEpCs.

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Section: The Effect Of Lpa On Hgf / C-met-mediated C-met Internalizatsupporting

confidence: 92%

Section: Discussionmentioning

confidence: 63%

“…HGF induces c-Met endocytosis and intracellular traffic has been demonstrated in variety of cell types [33][34][35]. Here we examined the c-Met redistribution by LPA treatment in HBEpCs.…”

Section: Lpa Induces C-met Redistribution Via Pkc δ In Hbepcmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Lysophosphatidic acid modulates c-Met redistribution and hepatocyte growth factor/c-Met signaling in human bronchial epithelial cells through PKC δ and E-cadherin

Zhao¹,

He²,

Stern³

et al. 2007

Cellular Signalling

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“…tcHGF/SF is rapidly internalized and degraded. 41 The second phase is the productive phase (3 to 72 hours). It is characterized by an increase in the levels of scHGF/SF and active tcHGF/SF.…”

Section: Discussionmentioning

confidence: 99%

The processing and utilization of hepatocyte growth factor/scatter factor following partial hepatectomy in the rat

Pediaditakis

2001

Hepatology

130

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Hepatocyte growth factor/scatter factor (HGF/SF) is a pluripotent growth factor capable of acting as a motogen, a morphogen, and a mitogen. Originally, HGF/SF was found as a blood-borne mitogen for hepatocytes and has since been determined to be very important in liver repair. Previous studies have established that HGF/SF must be proteolytically cleaved to elicit its effects. After liver injury by toxins such as carbon tetrachloride or after surgical resection, partial hepatectomy (PHX), HGF/SF concentrations increase in the blood. The aims of this study were to examine (1) which form of HGF/SF is present in the normal liver, (2) which form is present in the regenerating liver after PHX, and (3)

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Glycosaminoglycans bind granulocyte-macrophage colony-stimulating factor and modulate its mitogenic activity and signaling in human osteoblastic cells

1998

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We recently demonstrated that granulocyte-macrophage colony-stimulating factor (GM-CSF) is an autocrine growth factor for human osteoblastic (hOB) cells. Since GM-CSF is a member of the heparin-binding factor family, we examined the interactions between GM-CSF and glycosaminoglycans (GAGs) present in the osteoblast microenvironment. Using a bioassay in which the mitogenic activity of recombinant human (rh) GM-CSF was measured after incubation in the presence of an hOB cell layer or extracellular matrix (ECM) produced by these cells, we showed that rhGM-CSF binds to GAG components present in the ECM and that the bound rhGM-CSF retains its ability to stimulate hOB cell proliferation. Heparan sulfate compounds on the hOB cell surface were also found to sequester GM-CSF. Moreover, treatment with sodium chlorate, an inhibitor of GAG sulfation, suppressed the mitogenic activity of rhGM-CSF on hOB cells. This inhibitory effect was rescued by a low dose of heparin. Heparin was also found to promote the effect of rhGM-CSF on hOB cell proliferation, allowing nonmitogenic high doses of rhGM-CSF to stimulate hOB cell growth. Western blot analysis showed that undersulfation of cellular GAGs by chlorate inhibited the increased tyrosine phosphorylation of proteins involved in GM-CSF signaling in cloned immortalized hOB cells. The data demonstrate that GM-CSF binds to proteoglycans on the hOB cell surface and in ECM produced by these cells and that the bound GM-CSF is biologically active. Furthermore, this study shows that cellular proteoglycans play an essential role in GM-CSF signaling and biological activity in hOBs.

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Internalization and degradation of hepatocyte growth factor in hepatocytes with down‐regulation of the receptor/c‐Met

Cited by 36 publications

References 28 publications

Lysophosphatidic acid modulates c-Met redistribution and hepatocyte growth factor/c-Met signaling in human bronchial epithelial cells through PKC δ and E-cadherin

Lysophosphatidic acid modulates c-Met redistribution and hepatocyte growth factor/c-Met signaling in human bronchial epithelial cells through PKC δ and E-cadherin

The processing and utilization of hepatocyte growth factor/scatter factor following partial hepatectomy in the rat

Glycosaminoglycans bind granulocyte-macrophage colony-stimulating factor and modulate its mitogenic activity and signaling in human osteoblastic cells

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