Pertussis toxin inhibits stimulated motility independently of the adenylate cyclase pathway in human melanoma cells
Autor: | Mary L. Stracke, Raouf Guirguis, Elliott Schiffmann, Lance A. Liotta |
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Rok vydání: | 1987 |
Předmět: |
Cholera Toxin
medicine.medical_specialty Autocrine Motility Factor Time Factors G protein Biophysics 8-Bromo Cyclic Adenosine Monophosphate Adenylate kinase Motility Biology Pertussis toxin medicine.disease_cause Biochemistry Cyclase chemistry.chemical_compound Cell Movement Internal medicine medicine Humans Virulence Factors Bordetella Melanoma Molecular Biology Forskolin Chemotactic Factors Deoxyadenosines Dose-Response Relationship Drug Chemotaxis Colforsin Cholera toxin Cell Biology Molecular biology Culture Media Endocrinology Pertussis Toxin chemistry Dideoxyadenosine Adenylate Cyclase Toxin Adenylyl Cyclases |
Zdroj: | Biochemical and Biophysical Research Communications. 146:339-345 |
ISSN: | 0006-291X |
DOI: | 10.1016/0006-291x(87)90730-3 |
Popis: | The human melanoma cell line, A2058, has previously been shown to respond to an autocrine motility factor (AMF). We have studied biochemical pathways that may be involved in the generation of such a motile reponse. Pertussis toxin (PT) caused a profound, rapid decrease in stimulated motility that was both dose and time-dependent. Preincubation of cells for 2 hr with as little as 1ng/ml of PT significantly inhibited motility. A concentration of PT (0.5 μg/ml) that completely eliminated migration after a 30 min. preincubation had a markedly reduced effect when added 1 hr after the start of the assay. In contrast, agents which selectively modulate or have a role in the adenylate cyclase pathway, e.g., cholera toxin, forskolin, the cAMP analogue 8-bromoadenosine 3′:5′-cyclic monophosphate and the cyclase inhibitor 2′,5′-dideoxyadenosine, all had negligible effect upon motility. These data are consistent with the presence of a receptor coupled to a PT sensitive G protein initiating motility independently of the adenylate cyclase system. |
Databáze: | OpenAIRE |
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