Pertussis toxin inhibits stimulated motility independently of the adenylate cyclase pathway in human melanoma cells

Stracke, Mary L.; Guirguis, Raouf; Liotta, Lance A.; Schiffmann, Elliott

doi:10.1016/0006-291x(87)90730-3

Cited by 86 publications

(43 citation statements)

References 16 publications

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“…The signaling pathway involves receptor phosphorylation, 4 and the inhibitory effect of pertussis toxin (PT) on the AMF-mediated cell motility suggests a regulatory role of G-binding protein. 26 It is also involved in the activation of phospholipases and the inositol cycle 27 with two downstream components, 12-lipoxygenases and protein kinase C. 28 Analysis of the protein kinase cascade(s) in the AMF-stimulated cell motility using specific kinase inhibitors reveals the involvement of protein kinase C and tyrosine kinase, but not kinase A, reiterating that the signaling is independent of the adenylate cyclase pathway. 29 Recently, AMF stimulation has been shown to result in stress-fiber formation, which is associated with activation of two family members of the Rholike GTPases, RhoA and Rac1, but not Cdc42 activation.…”

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confidence: 99%

Overexpression of autocrine motility factor in metastatic tumor cells: possible association with augmented expression of KIF3A and GDI-β

Yanagawa

Watanabe

Takeuchi

et al. 2004

Laboratory Investigation

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Autocrine motility factor (AMF), which is identical to phosphohexose isomerase (PHI)/glucose-6-phosphate isomerase (GPI) , a ubiquitous enzyme essential for glycolysis, neuroleukin (NLK), a neurotrophic growth factor, and maturation factor (MF) mediating the differentiation of human myeloid cells, enhances the motility and metastatic ability of tumor cells. AMF/PHI activity is elevated in the serum or urine in patients with malignant tumors. Here, we constructed an amf/phi/nlk/mf gene using adenovirus vector and transfected into two tumor cell lines. Overexpression of AMF/PHI/NLK/MF enhanced AMF secretion into the culture media in both tumor cell lines. However, upregulation of motility and metastatic ability was found only in metastatic fibrosarcoma cells expressing an AMF receptor, gp78, and was not found in gp78-undetectable osteosarcoma cells. Thus, not only serum AMF activity but also gp78-expression in tumor cells may be required for metastasis-related motility induction. With the use of microarray analyses, we detected two augmented genes, rho GDP dissociation inhibitor beta and kinesin motor 3A, as well as AMF itself. The RNA message and protein expression of these two molecules was confirmed to be upregulated, suggesting a possible association with AMF-induced signaling for cell motility and metastasis.

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confidence: 99%

Overexpression of autocrine motility factor in metastatic tumor cells: possible association with augmented expression of KIF3A and GDI-β

Yanagawa

Watanabe

Takeuchi

et al. 2004

Laboratory Investigation

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“…Production of this autocrine motility factor by a variety of cancer cell types is thought to provide a mechanism for tumor cells to initiate, sustain, and regulate their own motility, a critical feature of the metastatic cascade (2). The locomotory response to ATX was demonstrated to be sensitive to pretreatment of the cells with pertussis toxin, indicating that a G protein is involved in the signal transduction pathway (1,3). However, little else is known about how this complex protein interacts with tumor cells to stimulate locomotion.…”

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confidence: 99%

Stimulation of Tumor Cell Motility Linked to Phosphodiesterase Catalytic Site of Autotaxin

Lee

Clair

Mulvaney

et al. 1996

Journal of Biological Chemistry

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“…It is believed that the constitutive autocrine expression of AMF may confer metastatic capability on neoplastic cells [3], and AMF initiates cell motility by interacting with a cell surface receptor that is coupled to a pertussis toxin-sensitive G protein [7,16]. The receptor for AMF (AMFR), a 78 kDa cell surface glycoprotein (gp78), has been characterized [4,17], and the causal involvement of this protein in metastasis has been demonstrated both in vivo [17] and in vitro [4,10].…”

Section: Discussionmentioning

confidence: 99%

“…The predicted protein had the structural features of an integral membrane protein, consisting of a 111 amino-acid extracellular domain, a hydrophobic 25 amino-acid transmembrane domain and a 187 amino-acid cytoplasmic region [6]. Previous work showed that a number of cellular and biochemical events were involved in the process of AMF-AMFR interaction, including the activation of pertussis toxin-sensitive G protein [7], inositol phosphate production [8], stimulation of 12-1ipoxygenase [9], receptor phosphorylation [6] and ligand-receptor complex internalization [10]. Recently, it has been shown that the expression of AMFR (gp78) was down-regulated in normal cells by cell contact-inhibition, while in cancer cells it was constitutively expressed irrespective of cell density [l, 11, 12].…”

Section: Introductionmentioning

confidence: 99%

Differential expression of autocrine motility factor receptor (AMFR) mRNA in normal and cancer cells detected by in situ hybridization

Huangbaiqu

Avrahamraz

1995

Cell Res

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The receptor for autocrine motility factor (AMFR) is known to be involved in the process of AMF-mediated cell migration and metastasis. This paper describes the procedures of non-radioactive in situ hybridization (ISH) detection of AMFR mRNA in both paraffin-embedded surgical sections and cultured cells using either biotinylated oligonucleotide probes or digoxigenin-labeled RNA probes. The results showed that the AMFR mRNA was expressed at an enhanced level in hyperplastic and malignant tissues of breast and prostate cancer patient surgical specimens, indicating that the elevated AMFR expression was associated with the tissue malignancy. Moreover, AMFR mRNA was detected in both normal and carcinoma cells when cultured at a subconfluent density. However, AMFR expression was inhibited in confluent normal (3T3-A31 murine fibroblast and FHs738BL human bladder) cells while it continued to express in carcinoma (J82 human bladder) and metastatic (3T3-M murine fibroblast) cells irrespective of cell density. This suggested a cell-cell contact downregulation of AMFR mRNA expression in normal but not in cancer cells. The ISH data obtained in this study are closely consistent with the AMFR protein expression pattern previously reported, implying that the differential expression of AMFR gene may be regulated and controlled at the transcriptional level. 222In situ hybridization detection of AMFR mRNA

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Pertussis toxin inhibits stimulated motility independently of the adenylate cyclase pathway in human melanoma cells

Cited by 86 publications

References 16 publications

Overexpression of autocrine motility factor in metastatic tumor cells: possible association with augmented expression of KIF3A and GDI-β

Overexpression of autocrine motility factor in metastatic tumor cells: possible association with augmented expression of KIF3A and GDI-β

Stimulation of Tumor Cell Motility Linked to Phosphodiesterase Catalytic Site of Autotaxin

Differential expression of autocrine motility factor receptor (AMFR) mRNA in normal and cancer cells detected by in situ hybridization

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