Please use this identifier to cite or link to this item: https://doi.org/10.1139/cjpp-74-5-559
Title: Pharmacology of pertussis toxin B-oligomer
Authors: Wong, W.S.F. 
Rosoff, P.M.
Keywords: Calcium
Diacylglycerol
Inositol trisphosphate
Protein kinase C
Tyrosine phosphorylation
Issue Date: 1996
Source: 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
URI: http://scholarbank.nus.edu.sg/handle/10635/108078
ISSN: 00084212
DOI: 10.1139/cjpp-74-5-559
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