Abstract:
:The uptake mechanism of pertussis toxin (PT) in CHO and insulin-producing HIT-T15 cells was studied. By electron microscopy after direct labeling of the toxin with gold particles, PT was found to be taken up by receptor-mediated endocytosis. The presence of active pertussis toxin in the Golgi complex was shown by subcellular fractionation. The importance of the Golgi localization of pertussis toxin for the S1-dependent ADP-ribosylation of G-proteins was investigated employing Brefeldin A (BFA) treatment to disrupt Golgi structures. Treatment with Brefeldin A completely blocked the pertussis toxin mediated ADP-ribosylation of cellular G-proteins in CHO and HIT-T15 cells, whereas the BFA-resistant MDCK cells were not protected. A mutant CHO cell line (V24.1) exhibiting a temperature-sensitive Golgi complex could be protected when grown at restrictive conditions. These results strongly indicate that retrograde transport to the Golgi network is a necessary prerequisite for pertussis toxin mediated ADP-ribosylation of G-proteins and thus also for cellular intoxication.
journal_name
Eur J Cell Bioljournal_title
European journal of cell biologyauthors
el Bayâ A,Linnemann R,von Olleschik-Elbheim L,Robenek H,Schmidt MAsubject
Has Abstractpub_date
1997-05-01 00:00:00pages
40-8issue
1eissn
0171-9335issn
1618-1298journal_volume
73pub_type
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journal_title:European journal of cell biology
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journal_title:European journal of cell biology
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journal_title:European journal of cell biology
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journal_title:European journal of cell biology
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doi:
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journal_title:European journal of cell biology
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journal_title:European journal of cell biology
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journal_title:European journal of cell biology
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journal_title:European journal of cell biology
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