Abstract |
Orally ingested botulinum toxin enters the circulatory system and eventually reaches the peripheral nerves, where it elicits a response of neurological dysfunction. In this study, we report the important findings concerning the mechanism of Clostridium botulinum type C progenitor toxin (C16S) endocytic mechanism. C16S toxin bound to high molecular weight proteins on the surface of human colon carcinoma HT-29 cells and was internalized, but not if the cells were pretreated with neuraminidase. Benzyl-GalNAc which inhibited O-glycosylation of glycoproteins also interfered in the toxin's ability to bind the cell surface. On the other hand, the toxin was internalized in spite of pretreatment of the cells with PPMP, an inhibitor of ganglioside synthesis. These results suggest that the glycoproteins, like mucin, fulfill the important roles of receptor and transporter of C16S toxin.
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Authors | Atsushi Nishikawa, Nobuo Uotsu, Hideyuki Arimitsu, Jae-Chul Lee, Yutaka Miura, Yukako Fujinaga, Hiroshi Nakada, Toshihiro Watanabe, Tohru Ohyama, Yoshiyuki Sakano, Keiji Oguma |
Journal | Biochemical and biophysical research communications
(Biochem Biophys Res Commun)
Vol. 319
Issue 2
Pg. 327-33
(Jun 25 2004)
ISSN: 0006-291X [Print] United States |
PMID | 15178410
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- Neuraminidase
- Botulinum Toxins
- botulinum toxin type C
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Topics |
- Botulinum Toxins
(metabolism)
- Glycosylation
- HT29 Cells
- Humans
- Microscopy, Fluorescence
- Neuraminidase
(pharmacology)
- Protein Binding
- Protein Transport
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