Regulation of cell motility via high and low affinity autocrine motility factor (AMF) receptor in human oral squamous carcinoma cells

Niinaka, Yasufumi; Haga, Akihiro; Negishi, Akihide; Yoshimasu, Hidemi; Raz, Avraham; Amagasa, Teruo

doi:10.1016/s1368-8375(01)00022-7

Cited by 16 publications

(15 citation statements)

References 19 publications

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“…However, cross-reaction is known in mammalian systems such as human, mouse, rat and rabbit. 3,4,22,23,29 Panels 5-8 of Figure 4 also suggest cross-linking between mouse AMF and human cells because morphological exchange was observed although GFP-fused AMFR did not respond.…”

Section: Discussionmentioning

confidence: 98%

“…Enhancement of locomotion was not recognized when over 100 pg/ml of AMF was added to the HT-1080 cell line, 5,24 and saturation may occur between the ligand and the receptor. 27,29 It was thought that such a large amount of an inactive mutant would be able to stimulate the cell locomotion. Therefore, we examined the dose-response effect of inactive mutants, but found that 100 pg/ml of S210D, T215S and H389F mutants were unable to stimulate HT-1080 cell motility (Figure 1(c)).…”

Section: Cell Motility-stimulating Activity Of Amf Mutantsmentioning

confidence: 99%

See 1 more Smart Citation

The Autocrine Motility Factor (AMF) and AMF-receptor Combination Needs Sugar Chain Recognition Ability and Interaction Using the C-terminal Region of AMF

Haga

Tanaka

Funasaka

et al. 2006

Journal of Molecular Biology

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Section: Discussionmentioning

confidence: 98%

Section: Cell Motility-stimulating Activity Of Amf Mutantsmentioning

confidence: 99%

The Autocrine Motility Factor (AMF) and AMF-receptor Combination Needs Sugar Chain Recognition Ability and Interaction Using the C-terminal Region of AMF

Haga

Tanaka

Funasaka

et al. 2006

Journal of Molecular Biology

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“…5, C-F). Therefore, in contrast to the limited, saturable number of PGI binding sites at neutral pH (23,40,58), the association of PGI with cell surface fibronectin fibrils at pH 5.0 is not saturable, potentially nonspecific, and apparently not mediated by the PGI receptor, AMF-R.…”

Section: Increased Cell Surface Fibrillar Binding Of Pgi Binding Atmentioning

confidence: 92%

Acid-induced Conformational Changes in Phosphoglucose Isomerase Result in Its Increased Cell Surface Association and Deposition on Fibronectin Fibrils

Amraei¹,

Jia²,

Reboul

et al. 2003

Journal of Biological Chemistry

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Phosphoglucose isomerase (PGI) is a glycolytic enzyme that exhibits extracellular cytokine activity as autocrine motility factor, neuroleukin, and maturation factor and that has been recently implicated as an autoantigen in rheumatoid arthritis. In contrast to its receptor-mediated endocytosis at neutral pH, addition of 25 g/ml of either Alexa 568-or FITC-conjugated PGI to NIH-3T3 cells at progressively acid pH results in its quantitatively increased association with cell surface fibrillar structures that is particularly evident at pH 5. A similar pH-dependent cell surface association of PGI is observed for first passage human chondrocytes obtained from osteoarthritic joints. At acid pH, PGI colocalizes with fibronectin fibrils, and this association occurs directly upon addition of PGI to the cells. In contrast to the receptor-mediated endocytosis of PGI, fibril association of 25 g/ml PGI at pH 5 is not competed with an excess (2 mg/ml) of unlabeled PGI. PGI binding at acid pH is therefore neither saturable nor mediated by its receptor. PGI is enzymatically active as a dimer and we show here by non-denaturing gel electrophoresis as well as by glutaraldehyde cross-linking that it exists at neutral pH in a tetrameric form. Increasingly acid pH results in the appearance of PGI monomers that correlates directly with its enhanced cell surface association. However, glutaraldehyde cross-linked PGI is endocytosed at neutral pH and still exhibits enhanced cell surface binding at pH 5. Circular dichroism analysis revealed pH-dependent changes in the near but not the far UV spectra indicating that the tertiary structure of the protein is specifically altered at pH 5. Conformational changes of PGI and exposure of the monomermonomer interface under acidic conditions, such as those encountered in the synovial fluid of arthritic joints, could therefore result in its deposition on the surface of joints and the induction of an autoimmune response.

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“…Ten microgram purified AMF expression vectors, [22][23][24] pBK-CMV-AMF and pBK-CMV were conjugated with TransIT -100 (PanVera Corp., Madison, WI) and dropped on HT-1080 monolayers, which were 70% confluent in 10 cm diameter dishes. After 4 hr, transfected cells were maintained with 10% FCS-DMEM containing 800 g/ml G-418.…”

Section: Cell Cultures and Gene Transfectionsmentioning

confidence: 99%

“…AMF activity is suppressible by monosaccharide, which is known as a PHI enzymic inhibitor, 17,[23][24][25][26] but it is unable to be used in vivo because of its cytotoxicity. However, immunological neutralization of external AMF can be achieved, as shown in Table III and Figure 5.…”

Section: The Apoptotic Effect Of Anti-amf Treatment On Tumor Cellsmentioning

confidence: 99%

Autocrine motility factor signaling induces tumor apoptotic resistance by regulations Apaf‐1 and Caspase‐9 apoptosome expression

Haga

Funasaka

Niinaka

et al. 2003

Intl Journal of Cancer

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Autocrine motility factor (AMF) is a cytokine that regulates locomotion and metastasis of tumor cells. It is well known that expression levels of AMF secretion and its receptor (AMF R) are closely related to tumor malignancy and rheumatoid arthritis. We have established that AMF signaling induced anti-apoptotic activity and that human fibrosarcoma HT-1080 line that secreted high levels of AMF were resistant to drug-induced apoptosis. These cells did not express the apoptotic protease activating factor-1 (Apaf-1) and Caspase-9 genes that encode for the proteins that form the "apoptosome" complex. The disappearance of the Apaf-1 and Caspase-9 gene was recovered by a cellular signaling inhibitor of protein kinase C, phosphatidylinositol 3-phosphate kinase and mitogen-activated protein kinase of the in vitro apoptosome Cancer is a disease in which down-regulation of apoptosis often occurs, and this often appears to compromise chemotherapy using anti-cancer drugs. It is well known that abnormal regulation of many mitochondria-related factors, such as Bcl-2, cytochrome c, Bax, Bik, Mn SOD, APAF-1 and Caspase-9, is observed in cancer cells. For example, the lack or loss of apoptotic proteinase activating factor-1 (Apaf-1) was observed in metastatic melanomas, which can contend with chemotherapy and are unable to execute the typical apoptotic programme in response to p53 activation. 1 Sensitivity to apoptosis induced by UV light dependent on its Apaf-1 deficiency level, 2 and over-expression of Apaf-1 induced etoposide-or paclitaxel-sensitive apoptosis, 3,4 have been reported in human leukemia cell lines. However, over-expression or experimental transduction of Apaf-1 and caspase-9 genes promoted the apoptotic sensitivities to radiation or the chemotherapeutic index of glioma cells. [5][6][7] Thus, the expression levels of Apaf-1 and caspase-9 in tumor cells seem to be important factors in determining the malignancy of the cells, and control of their expression may produce a therapeutic effect in clinical cancer treatments such as radiation and anti-cancer drugs. 8,9 Apaf-1 and caspase-9 are the core proteins of the "apoptosome" complex, which has an essential role in inducing mitochondrial programmed cell death. 10 It is necessary for the activation of pro-caspase-9 that cytochrome c and dATP interact with Apaf-1 as cofactors, and then the activated caspase-9 turns on the effector caspase-3 that then kills the cell by proteolysis. 11 Therefore, the apoptosome is a key molecular event of programmed cell death in several diseases that express an unusual apoptotic regulation, such as cancer. The function of the apoptosome is controlled by multiple molecules, transforming growth factor-beta up regulation via cytochrome c release, 12 heat shock protein 70 and 90 downregulation by binding to Apaf-1 and the formation of a cytosolic complex. [13][14][15] However, it is poorly understood at the molecular level why Apaf-1 and caspase-9 are decreased in malignant cells and how they regulate the function of the apoptosome. Ke...

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Regulation of cell motility via high and low affinity autocrine motility factor (AMF) receptor in human oral squamous carcinoma cells

Cited by 16 publications

References 19 publications

The Autocrine Motility Factor (AMF) and AMF-receptor Combination Needs Sugar Chain Recognition Ability and Interaction Using the C-terminal Region of AMF

The Autocrine Motility Factor (AMF) and AMF-receptor Combination Needs Sugar Chain Recognition Ability and Interaction Using the C-terminal Region of AMF

Acid-induced Conformational Changes in Phosphoglucose Isomerase Result in Its Increased Cell Surface Association and Deposition on Fibronectin Fibrils

Autocrine motility factor signaling induces tumor apoptotic resistance by regulations Apaf‐1 and Caspase‐9 apoptosome expression

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