Please use this identifier to cite or link to this item:
|Title:||Pharmacology of pertussis toxin B-oligomer|
|Authors:||Wong, W.S.F. |
Protein kinase C
|Citation:||Wong, W.S.F., Rosoff, P.M. (1996). Pharmacology of pertussis toxin B-oligomer. Canadian Journal of Physiology and Pharmacology 74 (5) : 559-564. ScholarBank@NUS Repository. https://doi.org/10.1139/cjpp-74-5-559|
|Abstract:||Pertussis toxin (PTX) is a heterohexameric protein, which is divided into subunits A and B. The A-subunit (protomer) possesses adenine diphosphate (ADP) ribosyltransferase activity, and the B-oligomer confers cell surface binding specificity on the toxin. By virtue of the ADP-ribosylation activity in the A-subunit, PTX has become a very useful pharmacological tool for the identification of inhibitory guanine nucleotide binding (G(i)) proteins in the plasma membrane. However, the pharmacological properties of the PTX B-oligomer are largely unknown. In the course of identifying its binding site(s), PTX B-oligomer was recently found to elicit direct cellular responses in a variety of cell types. Several cell surface receptors with oligosaccharide side chains have been shown to be specifically bound by PTX B-oligomer. Moreover, occupation of these putative receptors by the B-oligomer alone can trigger phospholipase C and tyrosine kinase dependent signal transduction events. The impact of these B-oligomer-mediated rapid signaling responses on the subsequent ADP-ribosylation of G(i) protein by the A-subunit remains to be determined. These recent findings caution investigators not to attribute inhibitory effects of PTX solely to ADP-ribosylation of G(i) protein without first examining the cellular responses using PTX B-oligomer.|
|Source Title:||Canadian Journal of Physiology and Pharmacology|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
WEB OF SCIENCETM
checked on Mar 20, 2019
checked on Mar 15, 2019
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.