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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Backlund, P. S. Aksamit, R. R. Meade, B. D. Cantoni, G. L. Manclark, C. R. |
| Abstract | When WBC264-9C cells are preincubated with pertussis toxin, chemotaxis is inhibited and ADP-ribosylation of a membrane protein with a subunit Mr 41,000 is observed. Both the inhibition of chemotaxis and the ADP-ribosylation by pertussis toxin display a similar time lag, temperature dependence, and pertussis toxin-concentration dependence. Although the inhibition of chemotaxis and the ADP-ribosylation of the membrane protein are qualitatively correlated, nearly complete inhibition of chemotaxis occurs when there is only partial ADP-ribosylation of the membrane protein. Pertussis toxin-catalyzed ADP-ribosylation of the Mr 41,000 protein in WBC264-9C membranes is stimulated by GDP, GTP, and to a lesser extent by GMP; the nonhydrolyzable GTP analog guanosine 5'-[beta, gamma-imido]triphosphate has no effect. WBC264-9C membranes have a high-affinity GTPase activity, which is partially inhibited in membranes from pertussis toxin-treated cells. Neither GTPase activity nor adenylate cyclase activity in membranes from WBC264-9C cells is affected by fMet-Leu-Phe, an attractant for these cells. Our results suggest that a guanine nucleotide binding protein may be involved in chemotaxis, but they do not indicate an involvement of adenylate cyclase. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 9 |
| Volume Number | 82 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 1985-06-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Adenosine Diphosphate Ribose Metabolism Bacterial Toxins Pharmacology Chemotaxis Drug Effects Membrane Proteins Nucleoside Diphosphate Sugars Adenylate Cyclase Toxin Animals Cell Line GTP Phosphohydrolases Hybrid Cells Physiology Mice Molecular Weight N-Formylmethionine Leucyl-Phenylalanine Nerve Tissue Proteins Pertussis Toxin Virulence Factors, Bordetella Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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