Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0043167 (pertussis)
 19,595 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The in vitro motility of B16-F1 melanoma cells is enhanced by incubation with a monoclonal antibody against gp78, previously characterized as a motility factor receptor. This antibody was used to study the relationship between motility stimulation in vitro and metastatic ability in vivo in the B16-F1 and K-1735 murine melanoma systems. While both high- and low-metastatic variants exhibited enhanced in vitro motility in response to the anti-gp78 monoclonal antibody, only the high-metastatic cells exhibited an increased metastatic ability. Surface immunofluorescence of low-metastatic cells was distributed more diffusely compared to a highly localized patching of gp78 on high-metastatic cells, suggesting that the directed endocytosis of gp78 to form a single leading edge is related to the metastatic ability of a cell, while fluorescence-activated cell sorter analysis revealed decreased gp78 surface expression in high-metastatic clones. Priming of cells by preventing internalization of gp78-antibody complexes by pertussis toxin resulted in a marked enhancement of pulmonary metastases by the treated cells which was directly correlated with decreased surface expression of gp78 following washout of pertussis toxin. These results suggest that cell motility induced by motility factor receptor occupancy may play a role in the process of metastasis and that the ligand-receptor complex internalization from the cell surface is involved in control of cell kinesis during metastasis.
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PMID:The relationship between motility factor receptor internalization and the lung colonization capacity of murine melanoma cells. 202 48

B16-F1 melanoma cells express augmented glycosylation of a Mr 78,000 (gp78) cell surface glycoprotein in response to cell shape modulation which is correlated to an increased metastatic ability in vivo and motility in vitro. A monoclonal antibody (mAb) directed against gp78 was used to study its surface distribution and possible function in cell locomotion. On motile cells, gp78 is localized by immunofluorescence to the leading lamella as well as to the trailing edge, suggesting shuffling of gp78 during cell migration. When bound to the cells the mAb induced locomotory activity similar to the effect of the cells' autocrine motility-like factor (AMLF). The enhanced motility induced by either anti-gp78 mAb or autocrine motility factor (AMF) were both inhibited by pertussis toxin, indicating that the 3F3A mAb induces cell kinesis via the same pertussis toxin-sensitive G protein pathway as has been described for other motility factors. The binding of anti-gp78 mAb to its ligand was inhibited (10-fold) by preincubation with B16-F1 AMLF containing conditioned media. Based on such functional properties, it was concluded that gp78 behaves as an AMF receptor of the B16-F1 melanoma cell.
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PMID:Identification of B16-F1 melanoma autocrine motility-like factor receptor. 215 51

We have previously shown that a protein-independent growing fibrosarcoma, Gc-4 PF has a high motile response to its cultured medium, which is associated with an increase in expression of gp78, a cell surface receptor for autocrine motility factor (AMF). Here we show that the cultured medium contains two motile activities, acidic and basic AMFs with regard to binding features on ion exchange chromatography. These two AMFs were purified by sequential DEAE anion exchange, CM cation exchange, and gel filtration chromatographies. However, both acidic and basic AMFs have a similar size of 55 kDa and 65 kDa under non-reducing and reducing conditions, respectively, with the same pI of 6.5. The stimulated motility of both AMFs was inhibited by the pertussis toxin (PT), but not by Streptomyces hyaluronidase. These two AMFs significantly stimulated the lung colonizing properties of the self-producing cells by 1.5-fold. These results suggest that both acidic and basic AMFs may correspond to the previously reported AMF and confirm directly that the AMF-gp78 signaling pathway is involved in cell motility associated with metastatic property.
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PMID:Differential purification of autocrine motility factor derived from a murine protein-free fibrosarcoma. 830 29

Autocrine motility factor (AMF) is a 55 kDa cytokine which is produced and secreted by cancer cells and which regulates cell motility via binding to its receptor, a 78 kDa cell surface glycoprotein (gp78-AMFR), and activating a pertussis toxin (PT)-sensitive G-protein. AMF purified from HT-1080 human fibrosarcoma cells stimulates the growth and motility of 3T3-A31-fibroblasts at a concentration of 0.1 ng/ml or less. The expression of total as well as cell surface gp78-AMFR is down-regulated in contact-inhibited A31-fibroblasts and AMF stimulates the healing of experimentally wounded, density-arrested A31 monolayer cultures. This is the first report of the paracrine and mitogenic actions of AMF and the results presented here show that AMF functions as a growth factor and suggest a possible role for its activity in normal tissue regeneration and tumor cell dissemination.
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PMID:Autocrine motility factor is a growth factor. 839 42